data_9CFL
# 
_entry.id   9CFL 
# 
_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   9CFL         pdb_00009cfl 10.2210/pdb9cfl/pdb 
WWPDB D_1000285404 ?            ?                   
EMDB  EMD-45550    ?            ?                   
# 
_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                        9CFL 
_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           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of S. aureus TarGH in complex with ATP-gamma-S' 
_pdbx_database_related.db_id          EMD-45550 
_pdbx_database_related.content_type   '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 
'Li, F.K.K.'        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'                     34303.562 2 ?       ? ? ? 
2 polymer     man 'Teichoic acids export ATP-binding protein TagH' 29806.553 2 7.5.2.4 ? ? ? 
3 non-polymer syn 'Lauryl Maltose Neopentyl Glycol'                1005.188  3 ?       ? ? ? 
4 non-polymer syn 'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER'     523.247   2 ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                  24.305    2 ?       ? ? ? 
6 water       nat water                                            18.015    8 ?       ? ? ? 
# 
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 
;MGSSHHHHHHHHHHSSGLVPRGSGGSMSAIGTVFKEHVKNFYLIQRLAQFQVKIINHSNYLGVAWELINPVMQIMVYWMV
FGLGIRSNAPIHGVPFVYWLLVGISMWFFINQGILEGTKAITQKFNQVSKMNFPLSIIPTYIVTSRFYGHLGLLLLVIIA
CMFTGIYPSIHIIQLLIYVPFCFFLTASVTLLTSTLGVLVRDTQMLMQAILRILFYFSPILWLPKNHGISGLIHEMMKYN
PVYFIAESYRAAILYHEWYFMDHWKLMLYNFGIVAIFFAIGAYLHMKYRDQFADFL
;
;MGSSHHHHHHHHHHSSGLVPRGSGGSMSAIGTVFKEHVKNFYLIQRLAQFQVKIINHSNYLGVAWELINPVMQIMVYWMV
FGLGIRSNAPIHGVPFVYWLLVGISMWFFINQGILEGTKAITQKFNQVSKMNFPLSIIPTYIVTSRFYGHLGLLLLVIIA
CMFTGIYPSIHIIQLLIYVPFCFFLTASVTLLTSTLGVLVRDTQMLMQAILRILFYFSPILWLPKNHGISGLIHEMMKYN
PVYFIAESYRAAILYHEWYFMDHWKLMLYNFGIVAIFFAIGAYLHMKYRDQFADFL
;
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 'Lauryl Maltose Neopentyl Glycol'            AV0 
4 'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER' AGS 
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  GLY n 
1 25  GLY n 
1 26  SER n 
1 27  MET n 
1 28  SER n 
1 29  ALA n 
1 30  ILE n 
1 31  GLY n 
1 32  THR n 
1 33  VAL n 
1 34  PHE n 
1 35  LYS n 
1 36  GLU n 
1 37  HIS n 
1 38  VAL n 
1 39  LYS n 
1 40  ASN n 
1 41  PHE n 
1 42  TYR n 
1 43  LEU n 
1 44  ILE n 
1 45  GLN n 
1 46  ARG n 
1 47  LEU n 
1 48  ALA n 
1 49  GLN n 
1 50  PHE n 
1 51  GLN n 
1 52  VAL n 
1 53  LYS n 
1 54  ILE n 
1 55  ILE n 
1 56  ASN n 
1 57  HIS n 
1 58  SER n 
1 59  ASN n 
1 60  TYR n 
1 61  LEU n 
1 62  GLY n 
1 63  VAL n 
1 64  ALA n 
1 65  TRP n 
1 66  GLU n 
1 67  LEU n 
1 68  ILE n 
1 69  ASN n 
1 70  PRO n 
1 71  VAL n 
1 72  MET n 
1 73  GLN n 
1 74  ILE n 
1 75  MET n 
1 76  VAL n 
1 77  TYR n 
1 78  TRP n 
1 79  MET n 
1 80  VAL n 
1 81  PHE n 
1 82  GLY n 
1 83  LEU n 
1 84  GLY n 
1 85  ILE n 
1 86  ARG n 
1 87  SER n 
1 88  ASN n 
1 89  ALA n 
1 90  PRO n 
1 91  ILE n 
1 92  HIS n 
1 93  GLY n 
1 94  VAL n 
1 95  PRO n 
1 96  PHE n 
1 97  VAL n 
1 98  TYR n 
1 99  TRP n 
1 100 LEU n 
1 101 LEU n 
1 102 VAL n 
1 103 GLY n 
1 104 ILE n 
1 105 SER n 
1 106 MET n 
1 107 TRP n 
1 108 PHE n 
1 109 PHE n 
1 110 ILE n 
1 111 ASN n 
1 112 GLN n 
1 113 GLY n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 GLY n 
1 118 THR n 
1 119 LYS n 
1 120 ALA n 
1 121 ILE n 
1 122 THR n 
1 123 GLN n 
1 124 LYS n 
1 125 PHE n 
1 126 ASN n 
1 127 GLN n 
1 128 VAL n 
1 129 SER n 
1 130 LYS n 
1 131 MET n 
1 132 ASN n 
1 133 PHE n 
1 134 PRO n 
1 135 LEU n 
1 136 SER n 
1 137 ILE n 
1 138 ILE n 
1 139 PRO n 
1 140 THR n 
1 141 TYR n 
1 142 ILE n 
1 143 VAL n 
1 144 THR n 
1 145 SER n 
1 146 ARG n 
1 147 PHE n 
1 148 TYR n 
1 149 GLY n 
1 150 HIS n 
1 151 LEU n 
1 152 GLY n 
1 153 LEU n 
1 154 LEU n 
1 155 LEU n 
1 156 LEU n 
1 157 VAL n 
1 158 ILE n 
1 159 ILE n 
1 160 ALA n 
1 161 CYS n 
1 162 MET n 
1 163 PHE n 
1 164 THR n 
1 165 GLY n 
1 166 ILE n 
1 167 TYR n 
1 168 PRO n 
1 169 SER n 
1 170 ILE n 
1 171 HIS n 
1 172 ILE n 
1 173 ILE n 
1 174 GLN n 
1 175 LEU n 
1 176 LEU n 
1 177 ILE n 
1 178 TYR n 
1 179 VAL n 
1 180 PRO n 
1 181 PHE n 
1 182 CYS n 
1 183 PHE n 
1 184 PHE n 
1 185 LEU n 
1 186 THR n 
1 187 ALA n 
1 188 SER n 
1 189 VAL n 
1 190 THR n 
1 191 LEU n 
1 192 LEU n 
1 193 THR n 
1 194 SER n 
1 195 THR n 
1 196 LEU n 
1 197 GLY n 
1 198 VAL n 
1 199 LEU n 
1 200 VAL n 
1 201 ARG n 
1 202 ASP n 
1 203 THR n 
1 204 GLN n 
1 205 MET n 
1 206 LEU n 
1 207 MET n 
1 208 GLN n 
1 209 ALA n 
1 210 ILE n 
1 211 LEU n 
1 212 ARG n 
1 213 ILE n 
1 214 LEU n 
1 215 PHE n 
1 216 TYR n 
1 217 PHE n 
1 218 SER n 
1 219 PRO n 
1 220 ILE n 
1 221 LEU n 
1 222 TRP n 
1 223 LEU n 
1 224 PRO n 
1 225 LYS n 
1 226 ASN n 
1 227 HIS n 
1 228 GLY n 
1 229 ILE n 
1 230 SER n 
1 231 GLY n 
1 232 LEU n 
1 233 ILE n 
1 234 HIS n 
1 235 GLU n 
1 236 MET n 
1 237 MET n 
1 238 LYS n 
1 239 TYR n 
1 240 ASN n 
1 241 PRO n 
1 242 VAL n 
1 243 TYR n 
1 244 PHE n 
1 245 ILE n 
1 246 ALA n 
1 247 GLU n 
1 248 SER n 
1 249 TYR n 
1 250 ARG n 
1 251 ALA n 
1 252 ALA n 
1 253 ILE n 
1 254 LEU n 
1 255 TYR n 
1 256 HIS n 
1 257 GLU n 
1 258 TRP n 
1 259 TYR n 
1 260 PHE n 
1 261 MET n 
1 262 ASP n 
1 263 HIS n 
1 264 TRP n 
1 265 LYS n 
1 266 LEU n 
1 267 MET n 
1 268 LEU n 
1 269 TYR n 
1 270 ASN n 
1 271 PHE n 
1 272 GLY n 
1 273 ILE n 
1 274 VAL n 
1 275 ALA n 
1 276 ILE n 
1 277 PHE n 
1 278 PHE n 
1 279 ALA n 
1 280 ILE n 
1 281 GLY n 
1 282 ALA n 
1 283 TYR n 
1 284 LEU n 
1 285 HIS n 
1 286 MET n 
1 287 LYS n 
1 288 TYR n 
1 289 ARG n 
1 290 ASP n 
1 291 GLN n 
1 292 PHE n 
1 293 ALA n 
1 294 ASP n 
1 295 PHE n 
1 296 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' 1 296 ? ? 'tagG, SAUSA300_0625' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 264 ? ? 'tagH, SAUSA300_0624' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
AGS non-polymer         . 'PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER' 
;ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE); ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE
;
'C10 H16 N5 O12 P3 S' 523.247  
ALA 'L-peptide linking' y ALANINE                                      ? 'C3 H7 N O2'          89.093   
ARG 'L-peptide linking' y ARGININE                                     ? 'C6 H15 N4 O2 1'      175.209  
ASN 'L-peptide linking' y ASPARAGINE                                   ? 'C4 H8 N2 O3'         132.118  
ASP 'L-peptide linking' y 'ASPARTIC ACID'                              ? 'C4 H7 N O4'          133.103  
AV0 non-polymer         . 'Lauryl Maltose Neopentyl Glycol'            
;2,2-didecylpropane-1,3-bis-b-D-maltopyranoside; 2-decyl-2-{[(4-O-alpha-D-glucopyranosyl-beta-D-glucopyranosyl)oxy]methyl}dodecyl4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside
;
'C47 H88 O22'         1005.188 
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   -25 ?   ?   ?   A . n 
A 1 2   GLY 2   -24 ?   ?   ?   A . n 
A 1 3   SER 3   -23 ?   ?   ?   A . n 
A 1 4   SER 4   -22 ?   ?   ?   A . n 
A 1 5   HIS 5   -21 ?   ?   ?   A . n 
A 1 6   HIS 6   -20 ?   ?   ?   A . n 
A 1 7   HIS 7   -19 ?   ?   ?   A . n 
A 1 8   HIS 8   -18 ?   ?   ?   A . n 
A 1 9   HIS 9   -17 ?   ?   ?   A . n 
A 1 10  HIS 10  -16 ?   ?   ?   A . n 
A 1 11  HIS 11  -15 ?   ?   ?   A . n 
A 1 12  HIS 12  -14 ?   ?   ?   A . n 
A 1 13  HIS 13  -13 ?   ?   ?   A . n 
A 1 14  HIS 14  -12 ?   ?   ?   A . n 
A 1 15  SER 15  -11 ?   ?   ?   A . n 
A 1 16  SER 16  -10 ?   ?   ?   A . n 
A 1 17  GLY 17  -9  ?   ?   ?   A . n 
A 1 18  LEU 18  -8  ?   ?   ?   A . n 
A 1 19  VAL 19  -7  ?   ?   ?   A . n 
A 1 20  PRO 20  -6  ?   ?   ?   A . n 
A 1 21  ARG 21  -5  ?   ?   ?   A . n 
A 1 22  GLY 22  -4  ?   ?   ?   A . n 
A 1 23  SER 23  -3  ?   ?   ?   A . n 
A 1 24  GLY 24  -2  ?   ?   ?   A . n 
A 1 25  GLY 25  -1  ?   ?   ?   A . n 
A 1 26  SER 26  0   ?   ?   ?   A . n 
A 1 27  MET 27  1   1   MET MET A . n 
A 1 28  SER 28  2   2   SER SER A . n 
A 1 29  ALA 29  3   3   ALA ALA A . n 
A 1 30  ILE 30  4   4   ILE ILE A . n 
A 1 31  GLY 31  5   5   GLY GLY A . n 
A 1 32  THR 32  6   6   THR THR A . n 
A 1 33  VAL 33  7   7   VAL VAL A . n 
A 1 34  PHE 34  8   8   PHE PHE A . n 
A 1 35  LYS 35  9   9   LYS LYS A . n 
A 1 36  GLU 36  10  10  GLU GLU A . n 
A 1 37  HIS 37  11  11  HIS HIS A . n 
A 1 38  VAL 38  12  12  VAL VAL A . n 
A 1 39  LYS 39  13  13  LYS LYS A . n 
A 1 40  ASN 40  14  14  ASN ASN A . n 
A 1 41  PHE 41  15  15  PHE PHE A . n 
A 1 42  TYR 42  16  16  TYR TYR A . n 
A 1 43  LEU 43  17  17  LEU LEU A . n 
A 1 44  ILE 44  18  18  ILE ILE A . n 
A 1 45  GLN 45  19  19  GLN GLN A . n 
A 1 46  ARG 46  20  20  ARG ARG A . n 
A 1 47  LEU 47  21  21  LEU LEU A . n 
A 1 48  ALA 48  22  22  ALA ALA A . n 
A 1 49  GLN 49  23  23  GLN GLN A . n 
A 1 50  PHE 50  24  24  PHE PHE A . n 
A 1 51  GLN 51  25  25  GLN GLN A . n 
A 1 52  VAL 52  26  26  VAL VAL A . n 
A 1 53  LYS 53  27  27  LYS LYS A . n 
A 1 54  ILE 54  28  28  ILE ILE A . n 
A 1 55  ILE 55  29  29  ILE ILE A . n 
A 1 56  ASN 56  30  30  ASN ASN A . n 
A 1 57  HIS 57  31  31  HIS HIS A . n 
A 1 58  SER 58  32  32  SER SER A . n 
A 1 59  ASN 59  33  33  ASN ASN A . n 
A 1 60  TYR 60  34  34  TYR TYR A . n 
A 1 61  LEU 61  35  35  LEU LEU A . n 
A 1 62  GLY 62  36  36  GLY GLY A . n 
A 1 63  VAL 63  37  37  VAL VAL A . n 
A 1 64  ALA 64  38  38  ALA ALA A . n 
A 1 65  TRP 65  39  39  TRP TRP A . n 
A 1 66  GLU 66  40  40  GLU GLU A . n 
A 1 67  LEU 67  41  41  LEU LEU A . n 
A 1 68  ILE 68  42  42  ILE ILE A . n 
A 1 69  ASN 69  43  43  ASN ASN A . n 
A 1 70  PRO 70  44  44  PRO PRO A . n 
A 1 71  VAL 71  45  45  VAL VAL A . n 
A 1 72  MET 72  46  46  MET MET A . n 
A 1 73  GLN 73  47  47  GLN GLN A . n 
A 1 74  ILE 74  48  48  ILE ILE A . n 
A 1 75  MET 75  49  49  MET MET A . n 
A 1 76  VAL 76  50  50  VAL VAL A . n 
A 1 77  TYR 77  51  51  TYR TYR A . n 
A 1 78  TRP 78  52  52  TRP TRP A . n 
A 1 79  MET 79  53  53  MET MET A . n 
A 1 80  VAL 80  54  54  VAL VAL A . n 
A 1 81  PHE 81  55  55  PHE PHE A . n 
A 1 82  GLY 82  56  56  GLY GLY A . n 
A 1 83  LEU 83  57  57  LEU LEU A . n 
A 1 84  GLY 84  58  58  GLY GLY A . n 
A 1 85  ILE 85  59  59  ILE ILE A . n 
A 1 86  ARG 86  60  60  ARG ARG A . n 
A 1 87  SER 87  61  61  SER SER A . n 
A 1 88  ASN 88  62  62  ASN ASN A . n 
A 1 89  ALA 89  63  63  ALA ALA A . n 
A 1 90  PRO 90  64  64  PRO PRO A . n 
A 1 91  ILE 91  65  65  ILE ILE A . n 
A 1 92  HIS 92  66  66  HIS HIS A . n 
A 1 93  GLY 93  67  67  GLY GLY A . n 
A 1 94  VAL 94  68  68  VAL VAL A . n 
A 1 95  PRO 95  69  69  PRO PRO A . n 
A 1 96  PHE 96  70  70  PHE PHE A . n 
A 1 97  VAL 97  71  71  VAL VAL A . n 
A 1 98  TYR 98  72  72  TYR TYR A . n 
A 1 99  TRP 99  73  73  TRP TRP A . n 
A 1 100 LEU 100 74  74  LEU LEU A . n 
A 1 101 LEU 101 75  75  LEU LEU A . n 
A 1 102 VAL 102 76  76  VAL VAL A . n 
A 1 103 GLY 103 77  77  GLY GLY A . n 
A 1 104 ILE 104 78  78  ILE ILE A . n 
A 1 105 SER 105 79  79  SER SER A . n 
A 1 106 MET 106 80  80  MET MET A . n 
A 1 107 TRP 107 81  81  TRP TRP A . n 
A 1 108 PHE 108 82  82  PHE PHE A . n 
A 1 109 PHE 109 83  83  PHE PHE A . n 
A 1 110 ILE 110 84  84  ILE ILE A . n 
A 1 111 ASN 111 85  85  ASN ASN A . n 
A 1 112 GLN 112 86  86  GLN GLN A . n 
A 1 113 GLY 113 87  87  GLY GLY A . n 
A 1 114 ILE 114 88  88  ILE ILE A . n 
A 1 115 LEU 115 89  89  LEU LEU A . n 
A 1 116 GLU 116 90  90  GLU GLU A . n 
A 1 117 GLY 117 91  91  GLY GLY A . n 
A 1 118 THR 118 92  92  THR THR A . n 
A 1 119 LYS 119 93  93  LYS LYS A . n 
A 1 120 ALA 120 94  94  ALA ALA A . n 
A 1 121 ILE 121 95  95  ILE ILE A . n 
A 1 122 THR 122 96  96  THR THR A . n 
A 1 123 GLN 123 97  97  GLN GLN A . n 
A 1 124 LYS 124 98  98  LYS LYS A . n 
A 1 125 PHE 125 99  99  PHE PHE A . n 
A 1 126 ASN 126 100 100 ASN ASN A . n 
A 1 127 GLN 127 101 101 GLN GLN A . n 
A 1 128 VAL 128 102 102 VAL VAL A . n 
A 1 129 SER 129 103 103 SER SER A . n 
A 1 130 LYS 130 104 104 LYS LYS A . n 
A 1 131 MET 131 105 105 MET MET A . n 
A 1 132 ASN 132 106 106 ASN ASN A . n 
A 1 133 PHE 133 107 107 PHE PHE A . n 
A 1 134 PRO 134 108 108 PRO PRO A . n 
A 1 135 LEU 135 109 109 LEU LEU A . n 
A 1 136 SER 136 110 110 SER SER A . n 
A 1 137 ILE 137 111 111 ILE ILE A . n 
A 1 138 ILE 138 112 112 ILE ILE A . n 
A 1 139 PRO 139 113 113 PRO PRO A . n 
A 1 140 THR 140 114 114 THR THR A . n 
A 1 141 TYR 141 115 115 TYR TYR A . n 
A 1 142 ILE 142 116 116 ILE ILE A . n 
A 1 143 VAL 143 117 117 VAL VAL A . n 
A 1 144 THR 144 118 118 THR THR A . n 
A 1 145 SER 145 119 119 SER SER A . n 
A 1 146 ARG 146 120 120 ARG ARG A . n 
A 1 147 PHE 147 121 121 PHE PHE A . n 
A 1 148 TYR 148 122 122 TYR TYR A . n 
A 1 149 GLY 149 123 123 GLY GLY A . n 
A 1 150 HIS 150 124 124 HIS HIS A . n 
A 1 151 LEU 151 125 125 LEU LEU A . n 
A 1 152 GLY 152 126 126 GLY GLY A . n 
A 1 153 LEU 153 127 127 LEU LEU A . n 
A 1 154 LEU 154 128 128 LEU LEU A . n 
A 1 155 LEU 155 129 129 LEU LEU A . n 
A 1 156 LEU 156 130 130 LEU LEU A . n 
A 1 157 VAL 157 131 131 VAL VAL A . n 
A 1 158 ILE 158 132 132 ILE ILE A . n 
A 1 159 ILE 159 133 133 ILE ILE A . n 
A 1 160 ALA 160 134 134 ALA ALA A . n 
A 1 161 CYS 161 135 135 CYS CYS A . n 
A 1 162 MET 162 136 136 MET MET A . n 
A 1 163 PHE 163 137 137 PHE PHE A . n 
A 1 164 THR 164 138 138 THR THR A . n 
A 1 165 GLY 165 139 139 GLY GLY A . n 
A 1 166 ILE 166 140 140 ILE ILE A . n 
A 1 167 TYR 167 141 141 TYR TYR A . n 
A 1 168 PRO 168 142 142 PRO PRO A . n 
A 1 169 SER 169 143 143 SER SER A . n 
A 1 170 ILE 170 144 144 ILE ILE A . n 
A 1 171 HIS 171 145 145 HIS HIS A . n 
A 1 172 ILE 172 146 146 ILE ILE A . n 
A 1 173 ILE 173 147 147 ILE ILE A . n 
A 1 174 GLN 174 148 148 GLN GLN A . n 
A 1 175 LEU 175 149 149 LEU LEU A . n 
A 1 176 LEU 176 150 150 LEU LEU A . n 
A 1 177 ILE 177 151 151 ILE ILE A . n 
A 1 178 TYR 178 152 152 TYR TYR A . n 
A 1 179 VAL 179 153 153 VAL VAL A . n 
A 1 180 PRO 180 154 154 PRO PRO A . n 
A 1 181 PHE 181 155 155 PHE PHE A . n 
A 1 182 CYS 182 156 156 CYS CYS A . n 
A 1 183 PHE 183 157 157 PHE PHE A . n 
A 1 184 PHE 184 158 158 PHE PHE A . n 
A 1 185 LEU 185 159 159 LEU LEU A . n 
A 1 186 THR 186 160 160 THR THR A . n 
A 1 187 ALA 187 161 161 ALA ALA A . n 
A 1 188 SER 188 162 162 SER SER A . n 
A 1 189 VAL 189 163 163 VAL VAL A . n 
A 1 190 THR 190 164 164 THR THR A . n 
A 1 191 LEU 191 165 165 LEU LEU A . n 
A 1 192 LEU 192 166 166 LEU LEU A . n 
A 1 193 THR 193 167 167 THR THR A . n 
A 1 194 SER 194 168 168 SER SER A . n 
A 1 195 THR 195 169 169 THR THR A . n 
A 1 196 LEU 196 170 170 LEU LEU A . n 
A 1 197 GLY 197 171 171 GLY GLY A . n 
A 1 198 VAL 198 172 172 VAL VAL A . n 
A 1 199 LEU 199 173 173 LEU LEU A . n 
A 1 200 VAL 200 174 174 VAL VAL A . n 
A 1 201 ARG 201 175 175 ARG ARG A . n 
A 1 202 ASP 202 176 176 ASP ASP A . n 
A 1 203 THR 203 177 177 THR THR A . n 
A 1 204 GLN 204 178 178 GLN GLN A . n 
A 1 205 MET 205 179 179 MET MET A . n 
A 1 206 LEU 206 180 180 LEU LEU A . n 
A 1 207 MET 207 181 181 MET MET A . n 
A 1 208 GLN 208 182 182 GLN GLN A . n 
A 1 209 ALA 209 183 183 ALA ALA A . n 
A 1 210 ILE 210 184 184 ILE ILE A . n 
A 1 211 LEU 211 185 185 LEU LEU A . n 
A 1 212 ARG 212 186 186 ARG ARG A . n 
A 1 213 ILE 213 187 187 ILE ILE A . n 
A 1 214 LEU 214 188 188 LEU LEU A . n 
A 1 215 PHE 215 189 189 PHE PHE A . n 
A 1 216 TYR 216 190 190 TYR TYR A . n 
A 1 217 PHE 217 191 191 PHE PHE A . n 
A 1 218 SER 218 192 192 SER SER A . n 
A 1 219 PRO 219 193 193 PRO PRO A . n 
A 1 220 ILE 220 194 194 ILE ILE A . n 
A 1 221 LEU 221 195 195 LEU LEU A . n 
A 1 222 TRP 222 196 196 TRP TRP A . n 
A 1 223 LEU 223 197 197 LEU LEU A . n 
A 1 224 PRO 224 198 198 PRO PRO A . n 
A 1 225 LYS 225 199 199 LYS LYS A . n 
A 1 226 ASN 226 200 200 ASN ASN A . n 
A 1 227 HIS 227 201 201 HIS HIS A . n 
A 1 228 GLY 228 202 202 GLY GLY A . n 
A 1 229 ILE 229 203 203 ILE ILE A . n 
A 1 230 SER 230 204 204 SER SER A . n 
A 1 231 GLY 231 205 205 GLY GLY A . n 
A 1 232 LEU 232 206 206 LEU LEU A . n 
A 1 233 ILE 233 207 207 ILE ILE A . n 
A 1 234 HIS 234 208 208 HIS HIS A . n 
A 1 235 GLU 235 209 209 GLU GLU A . n 
A 1 236 MET 236 210 210 MET MET A . n 
A 1 237 MET 237 211 211 MET MET A . n 
A 1 238 LYS 238 212 212 LYS LYS A . n 
A 1 239 TYR 239 213 213 TYR TYR A . n 
A 1 240 ASN 240 214 214 ASN ASN A . n 
A 1 241 PRO 241 215 215 PRO PRO A . n 
A 1 242 VAL 242 216 216 VAL VAL A . n 
A 1 243 TYR 243 217 217 TYR TYR A . n 
A 1 244 PHE 244 218 218 PHE PHE A . n 
A 1 245 ILE 245 219 219 ILE ILE A . n 
A 1 246 ALA 246 220 220 ALA ALA A . n 
A 1 247 GLU 247 221 221 GLU GLU A . n 
A 1 248 SER 248 222 222 SER SER A . n 
A 1 249 TYR 249 223 223 TYR TYR A . n 
A 1 250 ARG 250 224 224 ARG ARG A . n 
A 1 251 ALA 251 225 225 ALA ALA A . n 
A 1 252 ALA 252 226 226 ALA ALA A . n 
A 1 253 ILE 253 227 227 ILE ILE A . n 
A 1 254 LEU 254 228 228 LEU LEU A . n 
A 1 255 TYR 255 229 229 TYR TYR A . n 
A 1 256 HIS 256 230 230 HIS HIS A . n 
A 1 257 GLU 257 231 231 GLU GLU A . n 
A 1 258 TRP 258 232 232 TRP TRP A . n 
A 1 259 TYR 259 233 233 TYR TYR A . n 
A 1 260 PHE 260 234 234 PHE PHE A . n 
A 1 261 MET 261 235 235 MET MET A . n 
A 1 262 ASP 262 236 236 ASP ASP A . n 
A 1 263 HIS 263 237 237 HIS HIS A . n 
A 1 264 TRP 264 238 238 TRP TRP A . n 
A 1 265 LYS 265 239 239 LYS LYS A . n 
A 1 266 LEU 266 240 240 LEU LEU A . n 
A 1 267 MET 267 241 241 MET MET A . n 
A 1 268 LEU 268 242 242 LEU LEU A . n 
A 1 269 TYR 269 243 243 TYR TYR A . n 
A 1 270 ASN 270 244 244 ASN ASN A . n 
A 1 271 PHE 271 245 245 PHE PHE A . n 
A 1 272 GLY 272 246 246 GLY GLY A . n 
A 1 273 ILE 273 247 247 ILE ILE A . n 
A 1 274 VAL 274 248 248 VAL VAL A . n 
A 1 275 ALA 275 249 249 ALA ALA A . n 
A 1 276 ILE 276 250 250 ILE ILE A . n 
A 1 277 PHE 277 251 251 PHE PHE A . n 
A 1 278 PHE 278 252 252 PHE PHE A . n 
A 1 279 ALA 279 253 253 ALA ALA A . n 
A 1 280 ILE 280 254 254 ILE ILE A . n 
A 1 281 GLY 281 255 255 GLY GLY A . n 
A 1 282 ALA 282 256 256 ALA ALA A . n 
A 1 283 TYR 283 257 257 TYR TYR A . n 
A 1 284 LEU 284 258 258 LEU LEU A . n 
A 1 285 HIS 285 259 259 HIS HIS A . n 
A 1 286 MET 286 260 260 MET MET A . n 
A 1 287 LYS 287 261 261 LYS LYS A . n 
A 1 288 TYR 288 262 262 TYR TYR A . n 
A 1 289 ARG 289 263 263 ARG ARG A . n 
A 1 290 ASP 290 264 264 ASP ASP A . n 
A 1 291 GLN 291 265 265 GLN GLN A . n 
A 1 292 PHE 292 266 266 PHE PHE A . n 
A 1 293 ALA 293 267 267 ALA ALA A . n 
A 1 294 ASP 294 268 268 ASP ASP A . n 
A 1 295 PHE 295 269 269 PHE PHE A . n 
A 1 296 LEU 296 270 270 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 1 1   MET 1   -25 ?   ?   ?   C . n 
C 1 2   GLY 2   -24 ?   ?   ?   C . n 
C 1 3   SER 3   -23 ?   ?   ?   C . n 
C 1 4   SER 4   -22 ?   ?   ?   C . n 
C 1 5   HIS 5   -21 ?   ?   ?   C . n 
C 1 6   HIS 6   -20 ?   ?   ?   C . n 
C 1 7   HIS 7   -19 ?   ?   ?   C . n 
C 1 8   HIS 8   -18 ?   ?   ?   C . n 
C 1 9   HIS 9   -17 ?   ?   ?   C . n 
C 1 10  HIS 10  -16 ?   ?   ?   C . n 
C 1 11  HIS 11  -15 ?   ?   ?   C . n 
C 1 12  HIS 12  -14 ?   ?   ?   C . n 
C 1 13  HIS 13  -13 ?   ?   ?   C . n 
C 1 14  HIS 14  -12 ?   ?   ?   C . n 
C 1 15  SER 15  -11 ?   ?   ?   C . n 
C 1 16  SER 16  -10 ?   ?   ?   C . n 
C 1 17  GLY 17  -9  ?   ?   ?   C . n 
C 1 18  LEU 18  -8  ?   ?   ?   C . n 
C 1 19  VAL 19  -7  ?   ?   ?   C . n 
C 1 20  PRO 20  -6  ?   ?   ?   C . n 
C 1 21  ARG 21  -5  ?   ?   ?   C . n 
C 1 22  GLY 22  -4  ?   ?   ?   C . n 
C 1 23  SER 23  -3  ?   ?   ?   C . n 
C 1 24  GLY 24  -2  ?   ?   ?   C . n 
C 1 25  GLY 25  -1  ?   ?   ?   C . n 
C 1 26  SER 26  0   ?   ?   ?   C . n 
C 1 27  MET 27  1   1   MET MET C . n 
C 1 28  SER 28  2   2   SER SER C . n 
C 1 29  ALA 29  3   3   ALA ALA C . n 
C 1 30  ILE 30  4   4   ILE ILE C . n 
C 1 31  GLY 31  5   5   GLY GLY C . n 
C 1 32  THR 32  6   6   THR THR C . n 
C 1 33  VAL 33  7   7   VAL VAL C . n 
C 1 34  PHE 34  8   8   PHE PHE C . n 
C 1 35  LYS 35  9   9   LYS LYS C . n 
C 1 36  GLU 36  10  10  GLU GLU C . n 
C 1 37  HIS 37  11  11  HIS HIS C . n 
C 1 38  VAL 38  12  12  VAL VAL C . n 
C 1 39  LYS 39  13  13  LYS LYS C . n 
C 1 40  ASN 40  14  14  ASN ASN C . n 
C 1 41  PHE 41  15  15  PHE PHE C . n 
C 1 42  TYR 42  16  16  TYR TYR C . n 
C 1 43  LEU 43  17  17  LEU LEU C . n 
C 1 44  ILE 44  18  18  ILE ILE C . n 
C 1 45  GLN 45  19  19  GLN GLN C . n 
C 1 46  ARG 46  20  20  ARG ARG C . n 
C 1 47  LEU 47  21  21  LEU LEU C . n 
C 1 48  ALA 48  22  22  ALA ALA C . n 
C 1 49  GLN 49  23  23  GLN GLN C . n 
C 1 50  PHE 50  24  24  PHE PHE C . n 
C 1 51  GLN 51  25  25  GLN GLN C . n 
C 1 52  VAL 52  26  26  VAL VAL C . n 
C 1 53  LYS 53  27  27  LYS LYS C . n 
C 1 54  ILE 54  28  28  ILE ILE C . n 
C 1 55  ILE 55  29  29  ILE ILE C . n 
C 1 56  ASN 56  30  30  ASN ASN C . n 
C 1 57  HIS 57  31  31  HIS HIS C . n 
C 1 58  SER 58  32  32  SER SER C . n 
C 1 59  ASN 59  33  33  ASN ASN C . n 
C 1 60  TYR 60  34  34  TYR TYR C . n 
C 1 61  LEU 61  35  35  LEU LEU C . n 
C 1 62  GLY 62  36  36  GLY GLY C . n 
C 1 63  VAL 63  37  37  VAL VAL C . n 
C 1 64  ALA 64  38  38  ALA ALA C . n 
C 1 65  TRP 65  39  39  TRP TRP C . n 
C 1 66  GLU 66  40  40  GLU GLU C . n 
C 1 67  LEU 67  41  41  LEU LEU C . n 
C 1 68  ILE 68  42  42  ILE ILE C . n 
C 1 69  ASN 69  43  43  ASN ASN C . n 
C 1 70  PRO 70  44  44  PRO PRO C . n 
C 1 71  VAL 71  45  45  VAL VAL C . n 
C 1 72  MET 72  46  46  MET MET C . n 
C 1 73  GLN 73  47  47  GLN GLN C . n 
C 1 74  ILE 74  48  48  ILE ILE C . n 
C 1 75  MET 75  49  49  MET MET C . n 
C 1 76  VAL 76  50  50  VAL VAL C . n 
C 1 77  TYR 77  51  51  TYR TYR C . n 
C 1 78  TRP 78  52  52  TRP TRP C . n 
C 1 79  MET 79  53  53  MET MET C . n 
C 1 80  VAL 80  54  54  VAL VAL C . n 
C 1 81  PHE 81  55  55  PHE PHE C . n 
C 1 82  GLY 82  56  56  GLY GLY C . n 
C 1 83  LEU 83  57  57  LEU LEU C . n 
C 1 84  GLY 84  58  58  GLY GLY C . n 
C 1 85  ILE 85  59  59  ILE ILE C . n 
C 1 86  ARG 86  60  60  ARG ARG C . n 
C 1 87  SER 87  61  61  SER SER C . n 
C 1 88  ASN 88  62  62  ASN ASN C . n 
C 1 89  ALA 89  63  63  ALA ALA C . n 
C 1 90  PRO 90  64  64  PRO PRO C . n 
C 1 91  ILE 91  65  65  ILE ILE C . n 
C 1 92  HIS 92  66  66  HIS HIS C . n 
C 1 93  GLY 93  67  67  GLY GLY C . n 
C 1 94  VAL 94  68  68  VAL VAL C . n 
C 1 95  PRO 95  69  69  PRO PRO C . n 
C 1 96  PHE 96  70  70  PHE PHE C . n 
C 1 97  VAL 97  71  71  VAL VAL C . n 
C 1 98  TYR 98  72  72  TYR TYR C . n 
C 1 99  TRP 99  73  73  TRP TRP C . n 
C 1 100 LEU 100 74  74  LEU LEU C . n 
C 1 101 LEU 101 75  75  LEU LEU C . n 
C 1 102 VAL 102 76  76  VAL VAL C . n 
C 1 103 GLY 103 77  77  GLY GLY C . n 
C 1 104 ILE 104 78  78  ILE ILE C . n 
C 1 105 SER 105 79  79  SER SER C . n 
C 1 106 MET 106 80  80  MET MET C . n 
C 1 107 TRP 107 81  81  TRP TRP C . n 
C 1 108 PHE 108 82  82  PHE PHE C . n 
C 1 109 PHE 109 83  83  PHE PHE C . n 
C 1 110 ILE 110 84  84  ILE ILE C . n 
C 1 111 ASN 111 85  85  ASN ASN C . n 
C 1 112 GLN 112 86  86  GLN GLN C . n 
C 1 113 GLY 113 87  87  GLY GLY C . n 
C 1 114 ILE 114 88  88  ILE ILE C . n 
C 1 115 LEU 115 89  89  LEU LEU C . n 
C 1 116 GLU 116 90  90  GLU GLU C . n 
C 1 117 GLY 117 91  91  GLY GLY C . n 
C 1 118 THR 118 92  92  THR THR C . n 
C 1 119 LYS 119 93  93  LYS LYS C . n 
C 1 120 ALA 120 94  94  ALA ALA C . n 
C 1 121 ILE 121 95  95  ILE ILE C . n 
C 1 122 THR 122 96  96  THR THR C . n 
C 1 123 GLN 123 97  97  GLN GLN C . n 
C 1 124 LYS 124 98  98  LYS LYS C . n 
C 1 125 PHE 125 99  99  PHE PHE C . n 
C 1 126 ASN 126 100 100 ASN ASN C . n 
C 1 127 GLN 127 101 101 GLN GLN C . n 
C 1 128 VAL 128 102 102 VAL VAL C . n 
C 1 129 SER 129 103 103 SER SER C . n 
C 1 130 LYS 130 104 104 LYS LYS C . n 
C 1 131 MET 131 105 105 MET MET C . n 
C 1 132 ASN 132 106 106 ASN ASN C . n 
C 1 133 PHE 133 107 107 PHE PHE C . n 
C 1 134 PRO 134 108 108 PRO PRO C . n 
C 1 135 LEU 135 109 109 LEU LEU C . n 
C 1 136 SER 136 110 110 SER SER C . n 
C 1 137 ILE 137 111 111 ILE ILE C . n 
C 1 138 ILE 138 112 112 ILE ILE C . n 
C 1 139 PRO 139 113 113 PRO PRO C . n 
C 1 140 THR 140 114 114 THR THR C . n 
C 1 141 TYR 141 115 115 TYR TYR C . n 
C 1 142 ILE 142 116 116 ILE ILE C . n 
C 1 143 VAL 143 117 117 VAL VAL C . n 
C 1 144 THR 144 118 118 THR THR C . n 
C 1 145 SER 145 119 119 SER SER C . n 
C 1 146 ARG 146 120 120 ARG ARG C . n 
C 1 147 PHE 147 121 121 PHE PHE C . n 
C 1 148 TYR 148 122 122 TYR TYR C . n 
C 1 149 GLY 149 123 123 GLY GLY C . n 
C 1 150 HIS 150 124 124 HIS HIS C . n 
C 1 151 LEU 151 125 125 LEU LEU C . n 
C 1 152 GLY 152 126 126 GLY GLY C . n 
C 1 153 LEU 153 127 127 LEU LEU C . n 
C 1 154 LEU 154 128 128 LEU LEU C . n 
C 1 155 LEU 155 129 129 LEU LEU C . n 
C 1 156 LEU 156 130 130 LEU LEU C . n 
C 1 157 VAL 157 131 131 VAL VAL C . n 
C 1 158 ILE 158 132 132 ILE ILE C . n 
C 1 159 ILE 159 133 133 ILE ILE C . n 
C 1 160 ALA 160 134 134 ALA ALA C . n 
C 1 161 CYS 161 135 135 CYS CYS C . n 
C 1 162 MET 162 136 136 MET MET C . n 
C 1 163 PHE 163 137 137 PHE PHE C . n 
C 1 164 THR 164 138 138 THR THR C . n 
C 1 165 GLY 165 139 139 GLY GLY C . n 
C 1 166 ILE 166 140 140 ILE ILE C . n 
C 1 167 TYR 167 141 141 TYR TYR C . n 
C 1 168 PRO 168 142 142 PRO PRO C . n 
C 1 169 SER 169 143 143 SER SER C . n 
C 1 170 ILE 170 144 144 ILE ILE C . n 
C 1 171 HIS 171 145 145 HIS HIS C . n 
C 1 172 ILE 172 146 146 ILE ILE C . n 
C 1 173 ILE 173 147 147 ILE ILE C . n 
C 1 174 GLN 174 148 148 GLN GLN C . n 
C 1 175 LEU 175 149 149 LEU LEU C . n 
C 1 176 LEU 176 150 150 LEU LEU C . n 
C 1 177 ILE 177 151 151 ILE ILE C . n 
C 1 178 TYR 178 152 152 TYR TYR C . n 
C 1 179 VAL 179 153 153 VAL VAL C . n 
C 1 180 PRO 180 154 154 PRO PRO C . n 
C 1 181 PHE 181 155 155 PHE PHE C . n 
C 1 182 CYS 182 156 156 CYS CYS C . n 
C 1 183 PHE 183 157 157 PHE PHE C . n 
C 1 184 PHE 184 158 158 PHE PHE C . n 
C 1 185 LEU 185 159 159 LEU LEU C . n 
C 1 186 THR 186 160 160 THR THR C . n 
C 1 187 ALA 187 161 161 ALA ALA C . n 
C 1 188 SER 188 162 162 SER SER C . n 
C 1 189 VAL 189 163 163 VAL VAL C . n 
C 1 190 THR 190 164 164 THR THR C . n 
C 1 191 LEU 191 165 165 LEU LEU C . n 
C 1 192 LEU 192 166 166 LEU LEU C . n 
C 1 193 THR 193 167 167 THR THR C . n 
C 1 194 SER 194 168 168 SER SER C . n 
C 1 195 THR 195 169 169 THR THR C . n 
C 1 196 LEU 196 170 170 LEU LEU C . n 
C 1 197 GLY 197 171 171 GLY GLY C . n 
C 1 198 VAL 198 172 172 VAL VAL C . n 
C 1 199 LEU 199 173 173 LEU LEU C . n 
C 1 200 VAL 200 174 174 VAL VAL C . n 
C 1 201 ARG 201 175 175 ARG ARG C . n 
C 1 202 ASP 202 176 176 ASP ASP C . n 
C 1 203 THR 203 177 177 THR THR C . n 
C 1 204 GLN 204 178 178 GLN GLN C . n 
C 1 205 MET 205 179 179 MET MET C . n 
C 1 206 LEU 206 180 180 LEU LEU C . n 
C 1 207 MET 207 181 181 MET MET C . n 
C 1 208 GLN 208 182 182 GLN GLN C . n 
C 1 209 ALA 209 183 183 ALA ALA C . n 
C 1 210 ILE 210 184 184 ILE ILE C . n 
C 1 211 LEU 211 185 185 LEU LEU C . n 
C 1 212 ARG 212 186 186 ARG ARG C . n 
C 1 213 ILE 213 187 187 ILE ILE C . n 
C 1 214 LEU 214 188 188 LEU LEU C . n 
C 1 215 PHE 215 189 189 PHE PHE C . n 
C 1 216 TYR 216 190 190 TYR TYR C . n 
C 1 217 PHE 217 191 191 PHE PHE C . n 
C 1 218 SER 218 192 192 SER SER C . n 
C 1 219 PRO 219 193 193 PRO PRO C . n 
C 1 220 ILE 220 194 194 ILE ILE C . n 
C 1 221 LEU 221 195 195 LEU LEU C . n 
C 1 222 TRP 222 196 196 TRP TRP C . n 
C 1 223 LEU 223 197 197 LEU LEU C . n 
C 1 224 PRO 224 198 198 PRO PRO C . n 
C 1 225 LYS 225 199 199 LYS LYS C . n 
C 1 226 ASN 226 200 200 ASN ASN C . n 
C 1 227 HIS 227 201 201 HIS HIS C . n 
C 1 228 GLY 228 202 202 GLY GLY C . n 
C 1 229 ILE 229 203 203 ILE ILE C . n 
C 1 230 SER 230 204 204 SER SER C . n 
C 1 231 GLY 231 205 205 GLY GLY C . n 
C 1 232 LEU 232 206 206 LEU LEU C . n 
C 1 233 ILE 233 207 207 ILE ILE C . n 
C 1 234 HIS 234 208 208 HIS HIS C . n 
C 1 235 GLU 235 209 209 GLU GLU C . n 
C 1 236 MET 236 210 210 MET MET C . n 
C 1 237 MET 237 211 211 MET MET C . n 
C 1 238 LYS 238 212 212 LYS LYS C . n 
C 1 239 TYR 239 213 213 TYR TYR C . n 
C 1 240 ASN 240 214 214 ASN ASN C . n 
C 1 241 PRO 241 215 215 PRO PRO C . n 
C 1 242 VAL 242 216 216 VAL VAL C . n 
C 1 243 TYR 243 217 217 TYR TYR C . n 
C 1 244 PHE 244 218 218 PHE PHE C . n 
C 1 245 ILE 245 219 219 ILE ILE C . n 
C 1 246 ALA 246 220 220 ALA ALA C . n 
C 1 247 GLU 247 221 221 GLU GLU C . n 
C 1 248 SER 248 222 222 SER SER C . n 
C 1 249 TYR 249 223 223 TYR TYR C . n 
C 1 250 ARG 250 224 224 ARG ARG C . n 
C 1 251 ALA 251 225 225 ALA ALA C . n 
C 1 252 ALA 252 226 226 ALA ALA C . n 
C 1 253 ILE 253 227 227 ILE ILE C . n 
C 1 254 LEU 254 228 228 LEU LEU C . n 
C 1 255 TYR 255 229 229 TYR TYR C . n 
C 1 256 HIS 256 230 230 HIS HIS C . n 
C 1 257 GLU 257 231 231 GLU GLU C . n 
C 1 258 TRP 258 232 232 TRP TRP C . n 
C 1 259 TYR 259 233 233 TYR TYR C . n 
C 1 260 PHE 260 234 234 PHE PHE C . n 
C 1 261 MET 261 235 235 MET MET C . n 
C 1 262 ASP 262 236 236 ASP ASP C . n 
C 1 263 HIS 263 237 237 HIS HIS C . n 
C 1 264 TRP 264 238 238 TRP TRP C . n 
C 1 265 LYS 265 239 239 LYS LYS C . n 
C 1 266 LEU 266 240 240 LEU LEU C . n 
C 1 267 MET 267 241 241 MET MET C . n 
C 1 268 LEU 268 242 242 LEU LEU C . n 
C 1 269 TYR 269 243 243 TYR TYR C . n 
C 1 270 ASN 270 244 244 ASN ASN C . n 
C 1 271 PHE 271 245 245 PHE PHE C . n 
C 1 272 GLY 272 246 246 GLY GLY C . n 
C 1 273 ILE 273 247 247 ILE ILE C . n 
C 1 274 VAL 274 248 248 VAL VAL C . n 
C 1 275 ALA 275 249 249 ALA ALA C . n 
C 1 276 ILE 276 250 250 ILE ILE C . n 
C 1 277 PHE 277 251 251 PHE PHE C . n 
C 1 278 PHE 278 252 252 PHE PHE C . n 
C 1 279 ALA 279 253 253 ALA ALA C . n 
C 1 280 ILE 280 254 254 ILE ILE C . n 
C 1 281 GLY 281 255 255 GLY GLY C . n 
C 1 282 ALA 282 256 256 ALA ALA C . n 
C 1 283 TYR 283 257 257 TYR TYR C . n 
C 1 284 LEU 284 258 258 LEU LEU C . n 
C 1 285 HIS 285 259 259 HIS HIS C . n 
C 1 286 MET 286 260 260 MET MET C . n 
C 1 287 LYS 287 261 261 LYS LYS C . n 
C 1 288 TYR 288 262 262 TYR TYR C . n 
C 1 289 ARG 289 263 263 ARG ARG C . n 
C 1 290 ASP 290 264 264 ASP ASP C . n 
C 1 291 GLN 291 265 265 GLN GLN C . n 
C 1 292 PHE 292 266 266 PHE PHE C . n 
C 1 293 ALA 293 267 267 ALA ALA C . n 
C 1 294 ASP 294 268 268 ASP ASP C . n 
C 1 295 PHE 295 269 269 PHE PHE C . n 
C 1 296 LEU 296 270 270 LEU LEU C . n 
D 2 1   MET 1   1   1   MET MET D . n 
D 2 2   ASN 2   2   2   ASN ASN D . n 
D 2 3   VAL 3   3   3   VAL VAL D . n 
D 2 4   SER 4   4   4   SER SER D . n 
D 2 5   VAL 5   5   5   VAL VAL D . n 
D 2 6   ASN 6   6   6   ASN ASN D . n 
D 2 7   ILE 7   7   7   ILE ILE D . n 
D 2 8   LYS 8   8   8   LYS LYS D . n 
D 2 9   ASN 9   9   9   ASN ASN D . n 
D 2 10  VAL 10  10  10  VAL VAL D . n 
D 2 11  THR 11  11  11  THR THR D . n 
D 2 12  LYS 12  12  12  LYS LYS D . n 
D 2 13  GLU 13  13  13  GLU GLU D . n 
D 2 14  TYR 14  14  14  TYR TYR D . n 
D 2 15  ARG 15  15  15  ARG ARG D . n 
D 2 16  ILE 16  16  16  ILE ILE D . n 
D 2 17  TYR 17  17  17  TYR TYR D . n 
D 2 18  ARG 18  18  18  ARG ARG D . n 
D 2 19  THR 19  19  19  THR THR D . n 
D 2 20  ASN 20  20  20  ASN ASN D . n 
D 2 21  LYS 21  21  21  LYS LYS D . n 
D 2 22  GLU 22  22  22  GLU GLU D . n 
D 2 23  ARG 23  23  23  ARG ARG D . n 
D 2 24  MET 24  24  24  MET MET D . n 
D 2 25  LYS 25  25  25  LYS LYS D . n 
D 2 26  ASP 26  26  26  ASP ASP D . n 
D 2 27  ALA 27  27  27  ALA ALA D . n 
D 2 28  LEU 28  28  28  LEU LEU D . n 
D 2 29  ILE 29  29  29  ILE ILE D . n 
D 2 30  PRO 30  30  30  PRO PRO D . n 
D 2 31  LYS 31  31  31  LYS LYS D . n 
D 2 32  HIS 32  32  32  HIS HIS D . n 
D 2 33  LYS 33  33  33  LYS LYS D . n 
D 2 34  ASN 34  34  34  ASN ASN D . n 
D 2 35  LYS 35  35  35  LYS LYS D . n 
D 2 36  THR 36  36  36  THR THR D . n 
D 2 37  PHE 37  37  37  PHE PHE D . n 
D 2 38  PHE 38  38  38  PHE PHE D . n 
D 2 39  ALA 39  39  39  ALA ALA D . n 
D 2 40  LEU 40  40  40  LEU LEU D . n 
D 2 41  ASP 41  41  41  ASP ASP D . n 
D 2 42  ASP 42  42  42  ASP ASP D . n 
D 2 43  ILE 43  43  43  ILE ILE D . n 
D 2 44  SER 44  44  44  SER SER D . n 
D 2 45  LEU 45  45  45  LEU LEU D . n 
D 2 46  LYS 46  46  46  LYS LYS D . n 
D 2 47  ALA 47  47  47  ALA ALA D . n 
D 2 48  TYR 48  48  48  TYR TYR D . n 
D 2 49  GLU 49  49  49  GLU GLU D . n 
D 2 50  GLY 50  50  50  GLY GLY D . n 
D 2 51  ASP 51  51  51  ASP ASP D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ILE 53  53  53  ILE ILE D . n 
D 2 54  GLY 54  54  54  GLY GLY D . n 
D 2 55  LEU 55  55  55  LEU LEU D . n 
D 2 56  VAL 56  56  56  VAL VAL D . n 
D 2 57  GLY 57  57  57  GLY GLY D . n 
D 2 58  ILE 58  58  58  ILE ILE D . n 
D 2 59  ASN 59  59  59  ASN ASN D . n 
D 2 60  GLY 60  60  60  GLY GLY D . n 
D 2 61  SER 61  61  61  SER SER D . n 
D 2 62  GLY 62  62  62  GLY GLY D . n 
D 2 63  LYS 63  63  63  LYS LYS D . n 
D 2 64  SER 64  64  64  SER SER D . n 
D 2 65  THR 65  65  65  THR THR D . n 
D 2 66  LEU 66  66  66  LEU LEU D . n 
D 2 67  SER 67  67  67  SER SER D . n 
D 2 68  ASN 68  68  68  ASN ASN D . n 
D 2 69  ILE 69  69  69  ILE ILE D . n 
D 2 70  ILE 70  70  70  ILE ILE D . n 
D 2 71  GLY 71  71  71  GLY GLY D . n 
D 2 72  GLY 72  72  72  GLY GLY D . n 
D 2 73  SER 73  73  73  SER SER D . n 
D 2 74  LEU 74  74  74  LEU LEU D . n 
D 2 75  SER 75  75  75  SER SER D . n 
D 2 76  PRO 76  76  76  PRO PRO D . n 
D 2 77  THR 77  77  77  THR THR D . n 
D 2 78  VAL 78  78  78  VAL VAL D . n 
D 2 79  GLY 79  79  79  GLY GLY D . n 
D 2 80  LYS 80  80  80  LYS LYS D . n 
D 2 81  VAL 81  81  81  VAL VAL D . n 
D 2 82  ASP 82  82  82  ASP ASP D . n 
D 2 83  ARG 83  83  83  ARG ARG D . n 
D 2 84  ASN 84  84  84  ASN ASN D . n 
D 2 85  GLY 85  85  85  GLY GLY D . n 
D 2 86  GLU 86  86  86  GLU GLU D . n 
D 2 87  VAL 87  87  87  VAL VAL D . n 
D 2 88  SER 88  88  88  SER SER D . n 
D 2 89  VAL 89  89  89  VAL VAL D . n 
D 2 90  ILE 90  90  90  ILE ILE D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  ILE 92  92  92  ILE ILE D . n 
D 2 93  SER 93  93  93  SER SER D . n 
D 2 94  ALA 94  94  94  ALA ALA D . n 
D 2 95  GLY 95  95  95  GLY GLY D . n 
D 2 96  LEU 96  96  96  LEU LEU D . n 
D 2 97  SER 97  97  97  SER SER D . n 
D 2 98  GLY 98  98  98  GLY GLY D . n 
D 2 99  GLN 99  99  99  GLN GLN D . n 
D 2 100 LEU 100 100 100 LEU LEU D . n 
D 2 101 THR 101 101 101 THR THR D . n 
D 2 102 GLY 102 102 102 GLY GLY D . n 
D 2 103 ILE 103 103 103 ILE ILE D . n 
D 2 104 GLU 104 104 104 GLU GLU D . n 
D 2 105 ASN 105 105 105 ASN ASN D . n 
D 2 106 ILE 106 106 106 ILE ILE D . n 
D 2 107 GLU 107 107 107 GLU GLU D . n 
D 2 108 PHE 108 108 108 PHE PHE D . n 
D 2 109 LYS 109 109 109 LYS LYS D . n 
D 2 110 MET 110 110 110 MET MET D . n 
D 2 111 LEU 111 111 111 LEU LEU D . n 
D 2 112 CYS 112 112 112 CYS CYS D . n 
D 2 113 MET 113 113 113 MET MET D . n 
D 2 114 GLY 114 114 114 GLY GLY D . n 
D 2 115 PHE 115 115 115 PHE PHE D . n 
D 2 116 LYS 116 116 116 LYS LYS D . n 
D 2 117 ARG 117 117 117 ARG ARG D . n 
D 2 118 LYS 118 118 118 LYS LYS D . n 
D 2 119 GLU 119 119 119 GLU GLU D . n 
D 2 120 ILE 120 120 120 ILE ILE D . n 
D 2 121 LYS 121 121 121 LYS LYS D . n 
D 2 122 ALA 122 122 122 ALA ALA D . n 
D 2 123 MET 123 123 123 MET MET D . n 
D 2 124 THR 124 124 124 THR THR D . n 
D 2 125 PRO 125 125 125 PRO PRO D . n 
D 2 126 LYS 126 126 126 LYS LYS D . n 
D 2 127 ILE 127 127 127 ILE ILE D . n 
D 2 128 ILE 128 128 128 ILE ILE D . n 
D 2 129 GLU 129 129 129 GLU GLU D . n 
D 2 130 PHE 130 130 130 PHE PHE D . n 
D 2 131 SER 131 131 131 SER SER D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 LEU 133 133 133 LEU LEU D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 GLU 135 135 135 GLU GLU D . n 
D 2 136 PHE 136 136 136 PHE PHE D . n 
D 2 137 ILE 137 137 137 ILE ILE D . n 
D 2 138 TYR 138 138 138 TYR TYR D . n 
D 2 139 GLN 139 139 139 GLN GLN D . n 
D 2 140 PRO 140 140 140 PRO PRO D . n 
D 2 141 VAL 141 141 141 VAL VAL D . n 
D 2 142 LYS 142 142 142 LYS LYS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 TYR 144 144 144 TYR TYR D . n 
D 2 145 SER 145 145 145 SER SER D . n 
D 2 146 SER 146 146 146 SER SER D . n 
D 2 147 GLY 147 147 147 GLY GLY D . n 
D 2 148 MET 148 148 148 MET MET D . n 
D 2 149 ARG 149 149 149 ARG ARG D . n 
D 2 150 ALA 150 150 150 ALA ALA D . n 
D 2 151 LYS 151 151 151 LYS LYS D . n 
D 2 152 LEU 152 152 152 LEU LEU D . n 
D 2 153 GLY 153 153 153 GLY GLY D . n 
D 2 154 PHE 154 154 154 PHE PHE D . n 
D 2 155 SER 155 155 155 SER SER D . n 
D 2 156 ILE 156 156 156 ILE ILE D . n 
D 2 157 ASN 157 157 157 ASN ASN D . n 
D 2 158 ILE 158 158 158 ILE ILE D . n 
D 2 159 THR 159 159 159 THR THR D . n 
D 2 160 VAL 160 160 160 VAL VAL D . n 
D 2 161 ASN 161 161 161 ASN ASN D . n 
D 2 162 PRO 162 162 162 PRO PRO D . n 
D 2 163 ASP 163 163 163 ASP ASP D . n 
D 2 164 ILE 164 164 164 ILE ILE D . n 
D 2 165 LEU 165 165 165 LEU LEU D . n 
D 2 166 VAL 166 166 166 VAL VAL D . n 
D 2 167 ILE 167 167 167 ILE ILE D . n 
D 2 168 ASP 168 168 168 ASP ASP D . n 
D 2 169 GLU 169 169 169 GLU GLU D . n 
D 2 170 ALA 170 170 170 ALA ALA D . n 
D 2 171 LEU 171 171 171 LEU LEU D . n 
D 2 172 SER 172 172 172 SER SER D . n 
D 2 173 VAL 173 173 173 VAL VAL D . n 
D 2 174 GLY 174 174 174 GLY GLY D . n 
D 2 175 ASP 175 175 175 ASP ASP D . n 
D 2 176 GLN 176 176 176 GLN GLN D . n 
D 2 177 THR 177 177 177 THR THR D . n 
D 2 178 PHE 178 178 178 PHE PHE D . n 
D 2 179 ALA 179 179 179 ALA ALA D . n 
D 2 180 GLN 180 180 180 GLN GLN D . n 
D 2 181 LYS 181 181 181 LYS LYS D . n 
D 2 182 CYS 182 182 182 CYS CYS D . n 
D 2 183 LEU 183 183 183 LEU LEU D . n 
D 2 184 ASP 184 184 184 ASP ASP D . n 
D 2 185 LYS 185 185 185 LYS LYS D . n 
D 2 186 ILE 186 186 186 ILE ILE D . n 
D 2 187 TYR 187 187 187 TYR TYR D . n 
D 2 188 GLU 188 188 188 GLU GLU D . n 
D 2 189 PHE 189 189 189 PHE PHE D . n 
D 2 190 LYS 190 190 190 LYS LYS D . n 
D 2 191 GLU 191 191 191 GLU GLU D . n 
D 2 192 GLN 192 192 192 GLN GLN D . n 
D 2 193 ASN 193 193 193 ASN ASN D . n 
D 2 194 LYS 194 194 194 LYS LYS D . n 
D 2 195 THR 195 195 195 THR THR D . n 
D 2 196 ILE 196 196 196 ILE ILE D . n 
D 2 197 PHE 197 197 197 PHE PHE D . n 
D 2 198 PHE 198 198 198 PHE PHE D . n 
D 2 199 VAL 199 199 199 VAL VAL D . n 
D 2 200 SER 200 200 200 SER SER D . n 
D 2 201 HIS 201 201 201 HIS HIS D . n 
D 2 202 ASN 202 202 202 ASN ASN D . n 
D 2 203 LEU 203 203 203 LEU LEU D . n 
D 2 204 GLY 204 204 204 GLY GLY D . n 
D 2 205 GLN 205 205 205 GLN GLN D . n 
D 2 206 VAL 206 206 206 VAL VAL D . n 
D 2 207 ARG 207 207 207 ARG ARG D . n 
D 2 208 GLN 208 208 208 GLN GLN D . n 
D 2 209 PHE 209 209 209 PHE PHE D . n 
D 2 210 CYS 210 210 210 CYS CYS D . n 
D 2 211 THR 211 211 211 THR THR D . n 
D 2 212 LYS 212 212 212 LYS LYS D . n 
D 2 213 ILE 213 213 213 ILE ILE D . n 
D 2 214 ALA 214 214 214 ALA ALA D . n 
D 2 215 TRP 215 215 215 TRP TRP D . n 
D 2 216 ILE 216 216 216 ILE ILE D . n 
D 2 217 GLU 217 217 217 GLU GLU D . n 
D 2 218 GLY 218 218 218 GLY GLY D . n 
D 2 219 GLY 219 219 219 GLY GLY D . n 
D 2 220 LYS 220 220 220 LYS LYS D . n 
D 2 221 LEU 221 221 221 LEU LEU D . n 
D 2 222 LYS 222 222 222 LYS LYS D . n 
D 2 223 ASP 223 223 223 ASP ASP D . n 
D 2 224 TYR 224 224 224 TYR TYR D . n 
D 2 225 GLY 225 225 225 GLY GLY D . n 
D 2 226 GLU 226 226 226 GLU GLU D . n 
D 2 227 LEU 227 227 227 LEU LEU D . n 
D 2 228 ASP 228 228 228 ASP ASP D . n 
D 2 229 ASP 229 229 229 ASP ASP D . n 
D 2 230 VAL 230 230 230 VAL VAL D . n 
D 2 231 LEU 231 231 231 LEU LEU D . n 
D 2 232 PRO 232 232 232 PRO PRO D . n 
D 2 233 LYS 233 233 233 LYS LYS D . n 
D 2 234 TYR 234 234 234 TYR TYR D . n 
D 2 235 GLU 235 235 235 GLU GLU D . n 
D 2 236 ALA 236 236 236 ALA ALA D . n 
D 2 237 PHE 237 237 237 PHE PHE D . n 
D 2 238 LEU 238 238 238 LEU LEU D . n 
D 2 239 ASN 239 239 239 ASN ASN D . n 
D 2 240 ASP 240 240 240 ASP ASP D . n 
D 2 241 PHE 241 241 241 PHE PHE D . n 
D 2 242 LYS 242 242 242 LYS LYS D . n 
D 2 243 LYS 243 243 243 LYS LYS D . n 
D 2 244 LYS 244 244 244 LYS LYS D . n 
D 2 245 SER 245 245 245 SER SER D . n 
D 2 246 LYS 246 246 246 LYS LYS D . n 
D 2 247 ALA 247 247 247 ALA ALA D . n 
D 2 248 GLU 248 248 248 GLU GLU D . n 
D 2 249 GLN 249 249 249 GLN GLN D . n 
D 2 250 LYS 250 250 250 LYS LYS D . n 
D 2 251 GLU 251 251 251 GLU GLU D . n 
D 2 252 PHE 252 252 252 PHE PHE D . n 
D 2 253 ARG 253 253 253 ARG ARG D . n 
D 2 254 ASN 254 254 254 ASN ASN D . n 
D 2 255 LYS 255 255 255 LYS LYS D . n 
D 2 256 LEU 256 256 256 LEU LEU D . n 
D 2 257 ASP 257 257 257 ASP ASP D . n 
D 2 258 GLU 258 258 258 GLU GLU D . n 
D 2 259 SER 259 259 259 SER SER D . n 
D 2 260 ARG 260 260 260 ARG ARG D . n 
D 2 261 PHE 261 261 261 PHE PHE D . n 
D 2 262 VAL 262 262 262 VAL VAL D . n 
D 2 263 ILE 263 263 263 ILE ILE D . n 
D 2 264 LYS 264 264 264 LYS LYS D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 AGS ? ? AGS ? ? 'SUBJECT OF INVESTIGATION' ? 
2 AV0 ? ? AV0 ? ? '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 AV0 1 301 302 AV0 AV0 A . 
F 3 AV0 1 302 303 AV0 AV0 A . 
G 4 AGS 1 301 301 AGS AGS B . 
H 5 MG  1 302 302 MG  MG  B . 
I 3 AV0 1 301 302 AV0 AV0 C . 
J 4 AGS 1 301 301 AGS AGS D . 
K 5 MG  1 302 302 MG  MG  D . 
L 6 HOH 1 401 403 HOH HOH B . 
L 6 HOH 2 402 402 HOH HOH B . 
L 6 HOH 3 403 401 HOH HOH B . 
L 6 HOH 4 404 404 HOH HOH B . 
M 6 HOH 1 401 403 HOH HOH D . 
M 6 HOH 2 402 402 HOH HOH D . 
M 6 HOH 3 403 401 HOH HOH D . 
M 6 HOH 4 404 404 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                     9CFL 
_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                         9CFL 
_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                   9CFL 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9CFL 
_struct.title                        'Cryo-EM structure of S. aureus TarGH in complex with ATP-gamma-S' 
_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        9CFL 
_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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M 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 9CFL A 27 ? 296 ? A0A0H2XIF1 1 ? 270 ? 1 270 
2 2 9CFL B 1  ? 264 ? Q2FJ01     1 ? 264 ? 1 264 
3 1 9CFL C 27 ? 296 ? A0A0H2XIF1 1 ? 270 ? 1 270 
4 2 9CFL D 1  ? 264 ? Q2FJ01     1 ? 264 ? 1 264 
# 
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 9CFL MET A 1  ? UNP A0A0H2XIF1 ? ? 'initiating methionine' -25 1  
1 9CFL GLY A 2  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -24 2  
1 9CFL SER A 3  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -23 3  
1 9CFL SER A 4  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -22 4  
1 9CFL HIS A 5  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -21 5  
1 9CFL HIS A 6  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -20 6  
1 9CFL HIS A 7  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -19 7  
1 9CFL HIS A 8  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -18 8  
1 9CFL HIS A 9  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -17 9  
1 9CFL HIS A 10 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -16 10 
1 9CFL HIS A 11 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -15 11 
1 9CFL HIS A 12 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -14 12 
1 9CFL HIS A 13 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -13 13 
1 9CFL HIS A 14 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -12 14 
1 9CFL SER A 15 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -11 15 
1 9CFL SER A 16 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -10 16 
1 9CFL GLY A 17 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -9  17 
1 9CFL LEU A 18 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -8  18 
1 9CFL VAL A 19 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -7  19 
1 9CFL PRO A 20 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -6  20 
1 9CFL ARG A 21 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -5  21 
1 9CFL GLY A 22 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -4  22 
1 9CFL SER A 23 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -3  23 
1 9CFL GLY A 24 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -2  24 
1 9CFL GLY A 25 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -1  25 
1 9CFL SER A 26 ? UNP A0A0H2XIF1 ? ? 'expression tag'        0   26 
3 9CFL MET C 1  ? UNP A0A0H2XIF1 ? ? 'initiating methionine' -25 27 
3 9CFL GLY C 2  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -24 28 
3 9CFL SER C 3  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -23 29 
3 9CFL SER C 4  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -22 30 
3 9CFL HIS C 5  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -21 31 
3 9CFL HIS C 6  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -20 32 
3 9CFL HIS C 7  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -19 33 
3 9CFL HIS C 8  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -18 34 
3 9CFL HIS C 9  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -17 35 
3 9CFL HIS C 10 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -16 36 
3 9CFL HIS C 11 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -15 37 
3 9CFL HIS C 12 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -14 38 
3 9CFL HIS C 13 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -13 39 
3 9CFL HIS C 14 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -12 40 
3 9CFL SER C 15 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -11 41 
3 9CFL SER C 16 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -10 42 
3 9CFL GLY C 17 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -9  43 
3 9CFL LEU C 18 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -8  44 
3 9CFL VAL C 19 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -7  45 
3 9CFL PRO C 20 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -6  46 
3 9CFL ARG C 21 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -5  47 
3 9CFL GLY C 22 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -4  48 
3 9CFL SER C 23 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -3  49 
3 9CFL GLY C 24 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -2  50 
3 9CFL GLY C 25 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -1  51 
3 9CFL SER C 26 ? UNP A0A0H2XIF1 ? ? 'expression tag'        0   52 
# 
_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,M 
# 
_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 27  ? LYS A 39  ? MET A 1   LYS A 13  1 ? 13 
HELX_P HELX_P2  AA2 ASN A 40  ? ASN A 56  ? ASN A 14  ASN A 30  1 ? 17 
HELX_P HELX_P3  AA3 LEU A 61  ? VAL A 63  ? LEU A 35  VAL A 37  5 ? 3  
HELX_P HELX_P4  AA4 ALA A 64  ? GLY A 82  ? ALA A 38  GLY A 56  1 ? 19 
HELX_P HELX_P5  AA5 PRO A 95  ? SER A 105 ? PRO A 69  SER A 79  1 ? 11 
HELX_P HELX_P6  AA6 MET A 106 ? LYS A 119 ? MET A 80  LYS A 93  1 ? 14 
HELX_P HELX_P7  AA7 LYS A 119 ? PHE A 125 ? LYS A 93  PHE A 99  1 ? 7  
HELX_P HELX_P8  AA8 PRO A 134 ? SER A 136 ? PRO A 108 SER A 110 5 ? 3  
HELX_P HELX_P9  AA9 ILE A 137 ? PHE A 163 ? ILE A 111 PHE A 137 1 ? 27 
HELX_P HELX_P10 AB1 SER A 169 ? ILE A 173 ? SER A 143 ILE A 147 5 ? 5  
HELX_P HELX_P11 AB2 GLN A 174 ? VAL A 200 ? GLN A 148 VAL A 174 1 ? 27 
HELX_P HELX_P12 AB3 ASP A 202 ? PHE A 217 ? ASP A 176 PHE A 191 1 ? 16 
HELX_P HELX_P13 AB4 LEU A 232 ? MET A 237 ? LEU A 206 MET A 211 1 ? 6  
HELX_P HELX_P14 AB5 ASN A 240 ? LEU A 254 ? ASN A 214 LEU A 228 1 ? 15 
HELX_P HELX_P15 AB6 HIS A 263 ? ARG A 289 ? HIS A 237 ARG A 263 1 ? 27 
HELX_P HELX_P16 AB7 GLN A 291 ? LEU A 296 ? GLN A 265 LEU A 270 1 ? 6  
HELX_P HELX_P17 AB8 THR B 19  ? ILE B 29  ? THR B 19  ILE B 29  1 ? 11 
HELX_P HELX_P18 AB9 GLY B 62  ? GLY B 71  ? GLY B 62  GLY B 71  1 ? 10 
HELX_P HELX_P19 AC1 THR B 101 ? GLY B 114 ? THR B 101 GLY B 114 1 ? 14 
HELX_P HELX_P20 AC2 LYS B 116 ? GLU B 132 ? LYS B 116 GLU B 132 1 ? 17 
HELX_P HELX_P21 AC3 LEU B 133 ? GLN B 139 ? LEU B 133 GLN B 139 5 ? 7  
HELX_P HELX_P22 AC4 PRO B 140 ? TYR B 144 ? PRO B 140 TYR B 144 5 ? 5  
HELX_P HELX_P23 AC5 SER B 145 ? ILE B 158 ? SER B 145 ILE B 158 1 ? 14 
HELX_P HELX_P24 AC6 ASP B 175 ? GLN B 192 ? ASP B 175 GLN B 192 1 ? 18 
HELX_P HELX_P25 AC7 ASN B 202 ? CYS B 210 ? ASN B 202 CYS B 210 1 ? 9  
HELX_P HELX_P26 AC8 LEU B 227 ? LYS B 243 ? LEU B 227 LYS B 243 1 ? 17 
HELX_P HELX_P27 AC9 SER B 245 ? ARG B 260 ? SER B 245 ARG B 260 1 ? 16 
HELX_P HELX_P28 AD1 SER C 28  ? LYS C 39  ? SER C 2   LYS C 13  1 ? 12 
HELX_P HELX_P29 AD2 ASN C 40  ? ASN C 56  ? ASN C 14  ASN C 30  1 ? 17 
HELX_P HELX_P30 AD3 LEU C 61  ? VAL C 63  ? LEU C 35  VAL C 37  5 ? 3  
HELX_P HELX_P31 AD4 ALA C 64  ? GLY C 82  ? ALA C 38  GLY C 56  1 ? 19 
HELX_P HELX_P32 AD5 PRO C 95  ? SER C 105 ? PRO C 69  SER C 79  1 ? 11 
HELX_P HELX_P33 AD6 MET C 106 ? LYS C 119 ? MET C 80  LYS C 93  1 ? 14 
HELX_P HELX_P34 AD7 LYS C 119 ? PHE C 125 ? LYS C 93  PHE C 99  1 ? 7  
HELX_P HELX_P35 AD8 PRO C 134 ? SER C 136 ? PRO C 108 SER C 110 5 ? 3  
HELX_P HELX_P36 AD9 ILE C 137 ? PHE C 163 ? ILE C 111 PHE C 137 1 ? 27 
HELX_P HELX_P37 AE1 SER C 169 ? ILE C 173 ? SER C 143 ILE C 147 5 ? 5  
HELX_P HELX_P38 AE2 GLN C 174 ? VAL C 200 ? GLN C 148 VAL C 174 1 ? 27 
HELX_P HELX_P39 AE3 ASP C 202 ? PHE C 217 ? ASP C 176 PHE C 191 1 ? 16 
HELX_P HELX_P40 AE4 LEU C 232 ? MET C 237 ? LEU C 206 MET C 211 1 ? 6  
HELX_P HELX_P41 AE5 ASN C 240 ? LEU C 254 ? ASN C 214 LEU C 228 1 ? 15 
HELX_P HELX_P42 AE6 HIS C 263 ? ARG C 289 ? HIS C 237 ARG C 263 1 ? 27 
HELX_P HELX_P43 AE7 GLN C 291 ? LEU C 296 ? GLN C 265 LEU C 270 1 ? 6  
HELX_P HELX_P44 AE8 THR D 19  ? ILE D 29  ? THR D 19  ILE D 29  1 ? 11 
HELX_P HELX_P45 AE9 GLY D 62  ? GLY D 71  ? GLY D 62  GLY D 71  1 ? 10 
HELX_P HELX_P46 AF1 THR D 101 ? GLY D 114 ? THR D 101 GLY D 114 1 ? 14 
HELX_P HELX_P47 AF2 LYS D 116 ? GLU D 132 ? LYS D 116 GLU D 132 1 ? 17 
HELX_P HELX_P48 AF3 LEU D 133 ? GLN D 139 ? LEU D 133 GLN D 139 5 ? 7  
HELX_P HELX_P49 AF4 PRO D 140 ? TYR D 144 ? PRO D 140 TYR D 144 5 ? 5  
HELX_P HELX_P50 AF5 SER D 145 ? ILE D 158 ? SER D 145 ILE D 158 1 ? 14 
HELX_P HELX_P51 AF6 ASP D 175 ? GLN D 192 ? ASP D 175 GLN D 192 1 ? 18 
HELX_P HELX_P52 AF7 ASN D 202 ? CYS D 210 ? ASN D 202 CYS D 210 1 ? 9  
HELX_P HELX_P53 AF8 LEU D 227 ? LYS D 243 ? LEU D 227 LYS D 243 1 ? 17 
HELX_P HELX_P54 AF9 SER D 245 ? ARG D 260 ? SER D 245 ARG D 260 1 ? 16 
# 
_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 H MG  . MG ? ? B SER 64  B MG  302 1_555 ? ? ? ? ? ? ? 2.602 ? ? 
metalc2  metalc ? ? G AGS .  O2G ? ? ? 1_555 H MG  . MG ? ? B AGS 301 B MG  302 1_555 ? ? ? ? ? ? ? 1.887 ? ? 
metalc3  metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  302 B HOH 401 1_555 ? ? ? ? ? ? ? 2.946 ? ? 
metalc4  metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  302 B HOH 402 1_555 ? ? ? ? ? ? ? 2.917 ? ? 
metalc5  metalc ? ? H MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? B MG  302 B HOH 404 1_555 ? ? ? ? ? ? ? 2.762 ? ? 
metalc6  metalc ? ? D SER 64 OG  ? ? ? 1_555 K MG  . MG ? ? D SER 64  D MG  302 1_555 ? ? ? ? ? ? ? 2.603 ? ? 
metalc7  metalc ? ? J AGS .  O2G ? ? ? 1_555 K MG  . MG ? ? D AGS 301 D MG  302 1_555 ? ? ? ? ? ? ? 1.887 ? ? 
metalc8  metalc ? ? K MG  .  MG  ? ? ? 1_555 M HOH . O  ? ? D MG  302 D HOH 401 1_555 ? ? ? ? ? ? ? 2.946 ? ? 
metalc9  metalc ? ? K MG  .  MG  ? ? ? 1_555 M HOH . O  ? ? D MG  302 D HOH 402 1_555 ? ? ? ? ? ? ? 2.917 ? ? 
metalc10 metalc ? ? K MG  .  MG  ? ? ? 1_555 M HOH . O  ? ? D MG  302 D HOH 404 1_555 ? ? ? ? ? ? ? 2.762 ? ? 
# 
_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 ? H MG . ? B MG 302 ? 1_555 O2G ? G AGS . ? B AGS 301 ? 1_555 114.2 ? 
2  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 401 ? 1_555 80.2  ? 
3  O2G ? G AGS .  ? B AGS 301 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 401 ? 1_555 90.9  ? 
4  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 402 ? 1_555 62.9  ? 
5  O2G ? G AGS .  ? B AGS 301 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 402 ? 1_555 93.8  ? 
6  O   ? L HOH .  ? B HOH 401 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 402 ? 1_555 141.3 ? 
7  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 404 ? 1_555 95.8  ? 
8  O2G ? G AGS .  ? B AGS 301 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 404 ? 1_555 145.8 ? 
9  O   ? L HOH .  ? B HOH 401 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 404 ? 1_555 111.0 ? 
10 O   ? L HOH .  ? B HOH 402 ? 1_555 MG ? H MG . ? B MG 302 ? 1_555 O   ? L HOH . ? B HOH 404 ? 1_555 85.3  ? 
11 OG  ? D SER 64 ? D SER 64  ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O2G ? J AGS . ? D AGS 301 ? 1_555 114.2 ? 
12 OG  ? D SER 64 ? D SER 64  ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 401 ? 1_555 80.2  ? 
13 O2G ? J AGS .  ? D AGS 301 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 401 ? 1_555 90.9  ? 
14 OG  ? D SER 64 ? D SER 64  ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 402 ? 1_555 62.8  ? 
15 O2G ? J AGS .  ? D AGS 301 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 402 ? 1_555 93.8  ? 
16 O   ? M HOH .  ? D HOH 401 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 402 ? 1_555 141.3 ? 
17 OG  ? D SER 64 ? D SER 64  ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 404 ? 1_555 95.7  ? 
18 O2G ? J AGS .  ? D AGS 301 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 404 ? 1_555 145.8 ? 
19 O   ? M HOH .  ? D HOH 401 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 404 ? 1_555 111.0 ? 
20 O   ? M HOH .  ? D HOH 402 ? 1_555 MG ? K MG . ? D MG 302 ? 1_555 O   ? M HOH . ? D HOH 404 ? 1_555 85.3  ? 
# 
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 3   ? ARG B 15  ? VAL B 3   ARG B 15  
AA1 3 LYS B 35  ? TYR B 48  ? LYS B 35  TYR B 48  
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 D 78  ? ARG D 83  ? VAL D 78  ARG D 83  
AA3 2 VAL D 3   ? ARG D 15  ? VAL D 3   ARG D 15  
AA3 3 LYS D 35  ? TYR D 48  ? LYS D 35  TYR D 48  
AA3 4 PHE D 261 ? ILE D 263 ? PHE D 261 ILE D 263 
AA4 1 VAL D 87  ? ILE D 90  ? VAL D 87  ILE D 90  
AA4 2 ILE D 164 ? ASP D 168 ? ILE D 164 ASP D 168 
AA4 3 THR D 195 ? VAL D 199 ? THR D 195 VAL D 199 
AA4 4 VAL D 52  ? VAL D 56  ? VAL D 52  VAL D 56  
AA4 5 LYS D 212 ? GLU D 217 ? LYS D 212 GLU D 217 
AA4 6 LYS D 220 ? GLU D 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 VAL B 5   ? N VAL B 5   O ALA B 47  ? O ALA B 47  
AA1 3 4 N THR B 36  ? N THR B 36  O VAL B 262 ? O VAL B 262 
AA2 1 2 N ILE B 90  ? N ILE B 90  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 LEU B 55  ? N LEU B 55  
AA2 4 5 N GLY B 54  ? N GLY B 54  O ALA B 214 ? O ALA B 214 
AA2 5 6 N TRP B 215 ? N TRP B 215 O ASP B 223 ? O ASP B 223 
AA3 1 2 O ASP D 82  ? O ASP D 82  N ASN D 6   ? N ASN D 6   
AA3 2 3 N VAL D 5   ? N VAL D 5   O ALA D 47  ? O ALA D 47  
AA3 3 4 N THR D 36  ? N THR D 36  O VAL D 262 ? O VAL D 262 
AA4 1 2 N ILE D 90  ? N ILE D 90  O VAL D 166 ? O VAL D 166 
AA4 2 3 N ILE D 167 ? N ILE D 167 O PHE D 197 ? O PHE D 197 
AA4 3 4 O PHE D 198 ? O PHE D 198 N LEU D 55  ? N LEU D 55  
AA4 4 5 N GLY D 54  ? N GLY D 54  O ALA D 214 ? O ALA D 214 
AA4 5 6 N TRP D 215 ? N TRP D 215 O ASP D 223 ? O ASP D 223 
# 
_pdbx_entry_details.entry_id                   9CFL 
_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 PRO A 198 ? ? -80.97 47.46 
2 1 PRO C 198 ? ? -80.96 47.46 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 263 ? ? 0.084 'SIDE CHAIN' 
2 1 ARG B 15  ? ? 0.208 'SIDE CHAIN' 
3 1 ARG B 23  ? ? 0.234 'SIDE CHAIN' 
4 1 ARG C 263 ? ? 0.084 'SIDE CHAIN' 
5 1 ARG D 15  ? ? 0.209 'SIDE CHAIN' 
6 1 ARG D 23  ? ? 0.234 'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CFL 
_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                    9CFL 
_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                  2.3 
_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               153452 
_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                        9CFL 
_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              9CFL 
_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                9CFL 
_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              9CFL 
_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 -25 ? A MET 1  
2  1 Y 1 A GLY -24 ? A GLY 2  
3  1 Y 1 A SER -23 ? A SER 3  
4  1 Y 1 A SER -22 ? A SER 4  
5  1 Y 1 A HIS -21 ? A HIS 5  
6  1 Y 1 A HIS -20 ? A HIS 6  
7  1 Y 1 A HIS -19 ? A HIS 7  
8  1 Y 1 A HIS -18 ? A HIS 8  
9  1 Y 1 A HIS -17 ? A HIS 9  
10 1 Y 1 A HIS -16 ? A HIS 10 
11 1 Y 1 A HIS -15 ? A HIS 11 
12 1 Y 1 A HIS -14 ? A HIS 12 
13 1 Y 1 A HIS -13 ? A HIS 13 
14 1 Y 1 A HIS -12 ? A HIS 14 
15 1 Y 1 A SER -11 ? A SER 15 
16 1 Y 1 A SER -10 ? A SER 16 
17 1 Y 1 A GLY -9  ? A GLY 17 
18 1 Y 1 A LEU -8  ? A LEU 18 
19 1 Y 1 A VAL -7  ? A VAL 19 
20 1 Y 1 A PRO -6  ? A PRO 20 
21 1 Y 1 A ARG -5  ? A ARG 21 
22 1 Y 1 A GLY -4  ? A GLY 22 
23 1 Y 1 A SER -3  ? A SER 23 
24 1 Y 1 A GLY -2  ? A GLY 24 
25 1 Y 1 A GLY -1  ? A GLY 25 
26 1 Y 1 A SER 0   ? A SER 26 
27 1 Y 1 C MET -25 ? C MET 1  
28 1 Y 1 C GLY -24 ? C GLY 2  
29 1 Y 1 C SER -23 ? C SER 3  
30 1 Y 1 C SER -22 ? C SER 4  
31 1 Y 1 C HIS -21 ? C HIS 5  
32 1 Y 1 C HIS -20 ? C HIS 6  
33 1 Y 1 C HIS -19 ? C HIS 7  
34 1 Y 1 C HIS -18 ? C HIS 8  
35 1 Y 1 C HIS -17 ? C HIS 9  
36 1 Y 1 C HIS -16 ? C HIS 10 
37 1 Y 1 C HIS -15 ? C HIS 11 
38 1 Y 1 C HIS -14 ? C HIS 12 
39 1 Y 1 C HIS -13 ? C HIS 13 
40 1 Y 1 C HIS -12 ? C HIS 14 
41 1 Y 1 C SER -11 ? C SER 15 
42 1 Y 1 C SER -10 ? C SER 16 
43 1 Y 1 C GLY -9  ? C GLY 17 
44 1 Y 1 C LEU -8  ? C LEU 18 
45 1 Y 1 C VAL -7  ? C VAL 19 
46 1 Y 1 C PRO -6  ? C PRO 20 
47 1 Y 1 C ARG -5  ? C ARG 21 
48 1 Y 1 C GLY -4  ? C GLY 22 
49 1 Y 1 C SER -3  ? C SER 23 
50 1 Y 1 C GLY -2  ? C GLY 24 
51 1 Y 1 C GLY -1  ? C GLY 25 
52 1 Y 1 C SER 0   ? C SER 26 
# 
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 
AGS PG     P  N N 1   
AGS S1G    S  N N 2   
AGS O2G    O  N N 3   
AGS O3G    O  N N 4   
AGS PB     P  N N 5   
AGS O1B    O  N N 6   
AGS O2B    O  N N 7   
AGS O3B    O  N N 8   
AGS PA     P  N N 9   
AGS O1A    O  N N 10  
AGS O2A    O  N N 11  
AGS O3A    O  N N 12  
AGS "O5'"  O  N N 13  
AGS "C5'"  C  N N 14  
AGS "C4'"  C  N R 15  
AGS "O4'"  O  N N 16  
AGS "C3'"  C  N S 17  
AGS "O3'"  O  N N 18  
AGS "C2'"  C  N R 19  
AGS "O2'"  O  N N 20  
AGS "C1'"  C  N R 21  
AGS N9     N  Y N 22  
AGS C8     C  Y N 23  
AGS N7     N  Y N 24  
AGS C5     C  Y N 25  
AGS C6     C  Y N 26  
AGS N6     N  N N 27  
AGS N1     N  Y N 28  
AGS C2     C  Y N 29  
AGS N3     N  Y N 30  
AGS C4     C  Y N 31  
AGS HOG2   H  N N 32  
AGS H21    H  N N 33  
AGS HOB2   H  N N 34  
AGS HOA2   H  N N 35  
AGS "H5'1" H  N N 36  
AGS "H5'2" H  N N 37  
AGS "H4'"  H  N N 38  
AGS "H3'"  H  N N 39  
AGS "HO3'" H  N N 40  
AGS "H2'"  H  N N 41  
AGS "HO2'" H  N N 42  
AGS "H1'"  H  N N 43  
AGS H8     H  N N 44  
AGS HN61   H  N N 45  
AGS HN62   H  N N 46  
AGS H2     H  N N 47  
ALA N      N  N N 48  
ALA CA     C  N S 49  
ALA C      C  N N 50  
ALA O      O  N N 51  
ALA CB     C  N N 52  
ALA OXT    O  N N 53  
ALA H      H  N N 54  
ALA H2     H  N N 55  
ALA HA     H  N N 56  
ALA HB1    H  N N 57  
ALA HB2    H  N N 58  
ALA HB3    H  N N 59  
ALA HXT    H  N N 60  
ARG N      N  N N 61  
ARG CA     C  N S 62  
ARG C      C  N N 63  
ARG O      O  N N 64  
ARG CB     C  N N 65  
ARG CG     C  N N 66  
ARG CD     C  N N 67  
ARG NE     N  N N 68  
ARG CZ     C  N N 69  
ARG NH1    N  N N 70  
ARG NH2    N  N N 71  
ARG OXT    O  N N 72  
ARG H      H  N N 73  
ARG H2     H  N N 74  
ARG HA     H  N N 75  
ARG HB2    H  N N 76  
ARG HB3    H  N N 77  
ARG HG2    H  N N 78  
ARG HG3    H  N N 79  
ARG HD2    H  N N 80  
ARG HD3    H  N N 81  
ARG HE     H  N N 82  
ARG HH11   H  N N 83  
ARG HH12   H  N N 84  
ARG HH21   H  N N 85  
ARG HH22   H  N N 86  
ARG HXT    H  N N 87  
ASN N      N  N N 88  
ASN CA     C  N S 89  
ASN C      C  N N 90  
ASN O      O  N N 91  
ASN CB     C  N N 92  
ASN CG     C  N N 93  
ASN OD1    O  N N 94  
ASN ND2    N  N N 95  
ASN OXT    O  N N 96  
ASN H      H  N N 97  
ASN H2     H  N N 98  
ASN HA     H  N N 99  
ASN HB2    H  N N 100 
ASN HB3    H  N N 101 
ASN HD21   H  N N 102 
ASN HD22   H  N N 103 
ASN HXT    H  N N 104 
ASP N      N  N N 105 
ASP CA     C  N S 106 
ASP C      C  N N 107 
ASP O      O  N N 108 
ASP CB     C  N N 109 
ASP CG     C  N N 110 
ASP OD1    O  N N 111 
ASP OD2    O  N N 112 
ASP OXT    O  N N 113 
ASP H      H  N N 114 
ASP H2     H  N N 115 
ASP HA     H  N N 116 
ASP HB2    H  N N 117 
ASP HB3    H  N N 118 
ASP HD2    H  N N 119 
ASP HXT    H  N N 120 
AV0 C1     C  N R 121 
AV0 O1     O  N N 122 
AV0 C2     C  N R 123 
AV0 O2     O  N N 124 
AV0 C3     C  N R 125 
AV0 O3     O  N N 126 
AV0 C4     C  N S 127 
AV0 O4     O  N N 128 
AV0 C5     C  N R 129 
AV0 O5     O  N N 130 
AV0 C6     C  N N 131 
AV0 O6     O  N N 132 
AV0 CAA    C  N N 133 
AV0 CAB    C  N N 134 
AV0 OAI    O  N N 135 
AV0 OAJ    O  N N 136 
AV0 OAL    O  N N 137 
AV0 OAN    O  N N 138 
AV0 OAP    O  N N 139 
AV0 OAQ    O  N N 140 
AV0 OAR    O  N N 141 
AV0 OAS    O  N N 142 
AV0 OAT    O  N N 143 
AV0 OAU    O  N N 144 
AV0 OAV    O  N N 145 
AV0 CAW    C  N N 146 
AV0 CAX    C  N N 147 
AV0 CAY    C  N N 148 
AV0 CAZ    C  N N 149 
AV0 CBA    C  N N 150 
AV0 CBB    C  N N 151 
AV0 CBC    C  N N 152 
AV0 CBD    C  N N 153 
AV0 CBE    C  N N 154 
AV0 CBF    C  N N 155 
AV0 CBG    C  N N 156 
AV0 CBH    C  N N 157 
AV0 CBI    C  N N 158 
AV0 CBJ    C  N N 159 
AV0 CBK    C  N N 160 
AV0 CBL    C  N N 161 
AV0 CBM    C  N N 162 
AV0 CBN    C  N N 163 
AV0 CBP    C  N N 164 
AV0 CBQ    C  N N 165 
AV0 CBR    C  N N 166 
AV0 CBS    C  N N 167 
AV0 CBT    C  N N 168 
AV0 OBV    O  N N 169 
AV0 OBX    O  N N 170 
AV0 OBY    O  N N 171 
AV0 OBZ    O  N N 172 
AV0 OCB    O  N N 173 
AV0 CCC    C  N R 174 
AV0 CCD    C  N R 175 
AV0 CCF    C  N R 176 
AV0 CCH    C  N R 177 
AV0 CCJ    C  N R 178 
AV0 CCL    C  N R 179 
AV0 CCM    C  N N 180 
AV0 CCN    C  N S 181 
AV0 CCO    C  N S 182 
AV0 CCQ    C  N S 183 
AV0 CCR    C  N R 184 
AV0 CCS    C  N R 185 
AV0 CCT    C  N S 186 
AV0 CCU    C  N S 187 
AV0 CCV    C  N R 188 
AV0 CCW    C  N R 189 
AV0 H1     H  N N 190 
AV0 H2     H  N N 191 
AV0 H3     H  N N 192 
AV0 H4     H  N N 193 
AV0 H5     H  N N 194 
AV0 H6     H  N N 195 
AV0 H7     H  N N 196 
AV0 H8     H  N N 197 
AV0 H9     H  N N 198 
AV0 H10    H  N N 199 
AV0 H11    H  N N 200 
AV0 H12    H  N N 201 
AV0 H13    H  N N 202 
AV0 H14    H  N N 203 
AV0 H15    H  N N 204 
AV0 H16    H  N N 205 
AV0 H17    H  N N 206 
AV0 H18    H  N N 207 
AV0 H19    H  N N 208 
AV0 H20    H  N N 209 
AV0 H21    H  N N 210 
AV0 H22    H  N N 211 
AV0 H23    H  N N 212 
AV0 H24    H  N N 213 
AV0 H25    H  N N 214 
AV0 H26    H  N N 215 
AV0 H27    H  N N 216 
AV0 H28    H  N N 217 
AV0 H29    H  N N 218 
AV0 H30    H  N N 219 
AV0 H31    H  N N 220 
AV0 H32    H  N N 221 
AV0 H33    H  N N 222 
AV0 H34    H  N N 223 
AV0 H35    H  N N 224 
AV0 H36    H  N N 225 
AV0 H37    H  N N 226 
AV0 H38    H  N N 227 
AV0 H39    H  N N 228 
AV0 H40    H  N N 229 
AV0 H41    H  N N 230 
AV0 H42    H  N N 231 
AV0 H43    H  N N 232 
AV0 H44    H  N N 233 
AV0 H45    H  N N 234 
AV0 H46    H  N N 235 
AV0 H47    H  N N 236 
AV0 H48    H  N N 237 
AV0 H49    H  N N 238 
AV0 H50    H  N N 239 
AV0 H51    H  N N 240 
AV0 H52    H  N N 241 
AV0 H53    H  N N 242 
AV0 H54    H  N N 243 
AV0 H55    H  N N 244 
AV0 H56    H  N N 245 
AV0 H57    H  N N 246 
AV0 H58    H  N N 247 
AV0 H59    H  N N 248 
AV0 H60    H  N N 249 
AV0 H61    H  N N 250 
AV0 H62    H  N N 251 
AV0 H63    H  N N 252 
AV0 H64    H  N N 253 
AV0 H65    H  N N 254 
AV0 H66    H  N N 255 
AV0 H67    H  N N 256 
AV0 H68    H  N N 257 
AV0 H69    H  N N 258 
AV0 H70    H  N N 259 
AV0 H71    H  N N 260 
AV0 H72    H  N N 261 
AV0 H73    H  N N 262 
AV0 H74    H  N N 263 
AV0 H75    H  N N 264 
AV0 H76    H  N N 265 
AV0 H77    H  N N 266 
AV0 H78    H  N N 267 
AV0 H79    H  N N 268 
AV0 H80    H  N N 269 
AV0 H81    H  N N 270 
AV0 H82    H  N N 271 
AV0 H83    H  N N 272 
AV0 H84    H  N N 273 
AV0 H85    H  N N 274 
AV0 H86    H  N N 275 
AV0 H87    H  N N 276 
AV0 H88    H  N N 277 
CYS N      N  N N 278 
CYS CA     C  N R 279 
CYS C      C  N N 280 
CYS O      O  N N 281 
CYS CB     C  N N 282 
CYS SG     S  N N 283 
CYS OXT    O  N N 284 
CYS H      H  N N 285 
CYS H2     H  N N 286 
CYS HA     H  N N 287 
CYS HB2    H  N N 288 
CYS HB3    H  N N 289 
CYS HG     H  N N 290 
CYS HXT    H  N N 291 
GLN N      N  N N 292 
GLN CA     C  N S 293 
GLN C      C  N N 294 
GLN O      O  N N 295 
GLN CB     C  N N 296 
GLN CG     C  N N 297 
GLN CD     C  N N 298 
GLN OE1    O  N N 299 
GLN NE2    N  N N 300 
GLN OXT    O  N N 301 
GLN H      H  N N 302 
GLN H2     H  N N 303 
GLN HA     H  N N 304 
GLN HB2    H  N N 305 
GLN HB3    H  N N 306 
GLN HG2    H  N N 307 
GLN HG3    H  N N 308 
GLN HE21   H  N N 309 
GLN HE22   H  N N 310 
GLN HXT    H  N N 311 
GLU N      N  N N 312 
GLU CA     C  N S 313 
GLU C      C  N N 314 
GLU O      O  N N 315 
GLU CB     C  N N 316 
GLU CG     C  N N 317 
GLU CD     C  N N 318 
GLU OE1    O  N N 319 
GLU OE2    O  N N 320 
GLU OXT    O  N N 321 
GLU H      H  N N 322 
GLU H2     H  N N 323 
GLU HA     H  N N 324 
GLU HB2    H  N N 325 
GLU HB3    H  N N 326 
GLU HG2    H  N N 327 
GLU HG3    H  N N 328 
GLU HE2    H  N N 329 
GLU HXT    H  N N 330 
GLY N      N  N N 331 
GLY CA     C  N N 332 
GLY C      C  N N 333 
GLY O      O  N N 334 
GLY OXT    O  N N 335 
GLY H      H  N N 336 
GLY H2     H  N N 337 
GLY HA2    H  N N 338 
GLY HA3    H  N N 339 
GLY HXT    H  N N 340 
HIS N      N  N N 341 
HIS CA     C  N S 342 
HIS C      C  N N 343 
HIS O      O  N N 344 
HIS CB     C  N N 345 
HIS CG     C  Y N 346 
HIS ND1    N  Y N 347 
HIS CD2    C  Y N 348 
HIS CE1    C  Y N 349 
HIS NE2    N  Y N 350 
HIS OXT    O  N N 351 
HIS H      H  N N 352 
HIS H2     H  N N 353 
HIS HA     H  N N 354 
HIS HB2    H  N N 355 
HIS HB3    H  N N 356 
HIS HD1    H  N N 357 
HIS HD2    H  N N 358 
HIS HE1    H  N N 359 
HIS HE2    H  N N 360 
HIS HXT    H  N N 361 
HOH O      O  N N 362 
HOH H1     H  N N 363 
HOH H2     H  N N 364 
ILE N      N  N N 365 
ILE CA     C  N S 366 
ILE C      C  N N 367 
ILE O      O  N N 368 
ILE CB     C  N S 369 
ILE CG1    C  N N 370 
ILE CG2    C  N N 371 
ILE CD1    C  N N 372 
ILE OXT    O  N N 373 
ILE H      H  N N 374 
ILE H2     H  N N 375 
ILE HA     H  N N 376 
ILE HB     H  N N 377 
ILE HG12   H  N N 378 
ILE HG13   H  N N 379 
ILE HG21   H  N N 380 
ILE HG22   H  N N 381 
ILE HG23   H  N N 382 
ILE HD11   H  N N 383 
ILE HD12   H  N N 384 
ILE HD13   H  N N 385 
ILE HXT    H  N N 386 
LEU N      N  N N 387 
LEU CA     C  N S 388 
LEU C      C  N N 389 
LEU O      O  N N 390 
LEU CB     C  N N 391 
LEU CG     C  N N 392 
LEU CD1    C  N N 393 
LEU CD2    C  N N 394 
LEU OXT    O  N N 395 
LEU H      H  N N 396 
LEU H2     H  N N 397 
LEU HA     H  N N 398 
LEU HB2    H  N N 399 
LEU HB3    H  N N 400 
LEU HG     H  N N 401 
LEU HD11   H  N N 402 
LEU HD12   H  N N 403 
LEU HD13   H  N N 404 
LEU HD21   H  N N 405 
LEU HD22   H  N N 406 
LEU HD23   H  N N 407 
LEU HXT    H  N N 408 
LYS N      N  N N 409 
LYS CA     C  N S 410 
LYS C      C  N N 411 
LYS O      O  N N 412 
LYS CB     C  N N 413 
LYS CG     C  N N 414 
LYS CD     C  N N 415 
LYS CE     C  N N 416 
LYS NZ     N  N N 417 
LYS OXT    O  N N 418 
LYS H      H  N N 419 
LYS H2     H  N N 420 
LYS HA     H  N N 421 
LYS HB2    H  N N 422 
LYS HB3    H  N N 423 
LYS HG2    H  N N 424 
LYS HG3    H  N N 425 
LYS HD2    H  N N 426 
LYS HD3    H  N N 427 
LYS HE2    H  N N 428 
LYS HE3    H  N N 429 
LYS HZ1    H  N N 430 
LYS HZ2    H  N N 431 
LYS HZ3    H  N N 432 
LYS HXT    H  N N 433 
MET N      N  N N 434 
MET CA     C  N S 435 
MET C      C  N N 436 
MET O      O  N N 437 
MET CB     C  N N 438 
MET CG     C  N N 439 
MET SD     S  N N 440 
MET CE     C  N N 441 
MET OXT    O  N N 442 
MET H      H  N N 443 
MET H2     H  N N 444 
MET HA     H  N N 445 
MET HB2    H  N N 446 
MET HB3    H  N N 447 
MET HG2    H  N N 448 
MET HG3    H  N N 449 
MET HE1    H  N N 450 
MET HE2    H  N N 451 
MET HE3    H  N N 452 
MET HXT    H  N N 453 
MG  MG     MG N N 454 
PHE N      N  N N 455 
PHE CA     C  N S 456 
PHE C      C  N N 457 
PHE O      O  N N 458 
PHE CB     C  N N 459 
PHE CG     C  Y N 460 
PHE CD1    C  Y N 461 
PHE CD2    C  Y N 462 
PHE CE1    C  Y N 463 
PHE CE2    C  Y N 464 
PHE CZ     C  Y N 465 
PHE OXT    O  N N 466 
PHE H      H  N N 467 
PHE H2     H  N N 468 
PHE HA     H  N N 469 
PHE HB2    H  N N 470 
PHE HB3    H  N N 471 
PHE HD1    H  N N 472 
PHE HD2    H  N N 473 
PHE HE1    H  N N 474 
PHE HE2    H  N N 475 
PHE HZ     H  N N 476 
PHE HXT    H  N N 477 
PRO N      N  N N 478 
PRO CA     C  N S 479 
PRO C      C  N N 480 
PRO O      O  N N 481 
PRO CB     C  N N 482 
PRO CG     C  N N 483 
PRO CD     C  N N 484 
PRO OXT    O  N N 485 
PRO H      H  N N 486 
PRO HA     H  N N 487 
PRO HB2    H  N N 488 
PRO HB3    H  N N 489 
PRO HG2    H  N N 490 
PRO HG3    H  N N 491 
PRO HD2    H  N N 492 
PRO HD3    H  N N 493 
PRO HXT    H  N N 494 
SER N      N  N N 495 
SER CA     C  N S 496 
SER C      C  N N 497 
SER O      O  N N 498 
SER CB     C  N N 499 
SER OG     O  N N 500 
SER OXT    O  N N 501 
SER H      H  N N 502 
SER H2     H  N N 503 
SER HA     H  N N 504 
SER HB2    H  N N 505 
SER HB3    H  N N 506 
SER HG     H  N N 507 
SER HXT    H  N N 508 
THR N      N  N N 509 
THR CA     C  N S 510 
THR C      C  N N 511 
THR O      O  N N 512 
THR CB     C  N R 513 
THR OG1    O  N N 514 
THR CG2    C  N N 515 
THR OXT    O  N N 516 
THR H      H  N N 517 
THR H2     H  N N 518 
THR HA     H  N N 519 
THR HB     H  N N 520 
THR HG1    H  N N 521 
THR HG21   H  N N 522 
THR HG22   H  N N 523 
THR HG23   H  N N 524 
THR HXT    H  N N 525 
TRP N      N  N N 526 
TRP CA     C  N S 527 
TRP C      C  N N 528 
TRP O      O  N N 529 
TRP CB     C  N N 530 
TRP CG     C  Y N 531 
TRP CD1    C  Y N 532 
TRP CD2    C  Y N 533 
TRP NE1    N  Y N 534 
TRP CE2    C  Y N 535 
TRP CE3    C  Y N 536 
TRP CZ2    C  Y N 537 
TRP CZ3    C  Y N 538 
TRP CH2    C  Y N 539 
TRP OXT    O  N N 540 
TRP H      H  N N 541 
TRP H2     H  N N 542 
TRP HA     H  N N 543 
TRP HB2    H  N N 544 
TRP HB3    H  N N 545 
TRP HD1    H  N N 546 
TRP HE1    H  N N 547 
TRP HE3    H  N N 548 
TRP HZ2    H  N N 549 
TRP HZ3    H  N N 550 
TRP HH2    H  N N 551 
TRP HXT    H  N N 552 
TYR N      N  N N 553 
TYR CA     C  N S 554 
TYR C      C  N N 555 
TYR O      O  N N 556 
TYR CB     C  N N 557 
TYR CG     C  Y N 558 
TYR CD1    C  Y N 559 
TYR CD2    C  Y N 560 
TYR CE1    C  Y N 561 
TYR CE2    C  Y N 562 
TYR CZ     C  Y N 563 
TYR OH     O  N N 564 
TYR OXT    O  N N 565 
TYR H      H  N N 566 
TYR H2     H  N N 567 
TYR HA     H  N N 568 
TYR HB2    H  N N 569 
TYR HB3    H  N N 570 
TYR HD1    H  N N 571 
TYR HD2    H  N N 572 
TYR HE1    H  N N 573 
TYR HE2    H  N N 574 
TYR HH     H  N N 575 
TYR HXT    H  N N 576 
VAL N      N  N N 577 
VAL CA     C  N S 578 
VAL C      C  N N 579 
VAL O      O  N N 580 
VAL CB     C  N N 581 
VAL CG1    C  N N 582 
VAL CG2    C  N N 583 
VAL OXT    O  N N 584 
VAL H      H  N N 585 
VAL H2     H  N N 586 
VAL HA     H  N N 587 
VAL HB     H  N N 588 
VAL HG11   H  N N 589 
VAL HG12   H  N N 590 
VAL HG13   H  N N 591 
VAL HG21   H  N N 592 
VAL HG22   H  N N 593 
VAL HG23   H  N N 594 
VAL HXT    H  N N 595 
# 
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 
AGS PG    S1G    doub N N 1   
AGS PG    O2G    sing N N 2   
AGS PG    O3G    sing N N 3   
AGS PG    O3B    sing N N 4   
AGS PB    O1B    doub N N 5   
AGS PB    O2B    sing N N 6   
AGS PB    O3B    sing N N 7   
AGS PB    O3A    sing N N 8   
AGS PA    O1A    doub N N 9   
AGS PA    O2A    sing N N 10  
AGS PA    O3A    sing N N 11  
AGS PA    "O5'"  sing N N 12  
AGS "O5'" "C5'"  sing N N 13  
AGS "C5'" "C4'"  sing N N 14  
AGS "C4'" "O4'"  sing N N 15  
AGS "C4'" "C3'"  sing N N 16  
AGS "O4'" "C1'"  sing N N 17  
AGS "C3'" "O3'"  sing N N 18  
AGS "C3'" "C2'"  sing N N 19  
AGS "C2'" "O2'"  sing N N 20  
AGS "C2'" "C1'"  sing N N 21  
AGS "C1'" N9     sing N N 22  
AGS N9    C8     sing Y N 23  
AGS N9    C4     sing Y N 24  
AGS C8    N7     doub Y N 25  
AGS N7    C5     sing Y N 26  
AGS C5    C6     sing Y N 27  
AGS C5    C4     doub Y N 28  
AGS C6    N6     sing N N 29  
AGS C6    N1     doub Y N 30  
AGS N1    C2     sing Y N 31  
AGS C2    N3     doub Y N 32  
AGS N3    C4     sing Y N 33  
AGS O2G   HOG2   sing N N 34  
AGS O3G   H21    sing N N 35  
AGS O2B   HOB2   sing N N 36  
AGS O2A   HOA2   sing N N 37  
AGS "C5'" "H5'1" sing N N 38  
AGS "C5'" "H5'2" sing N N 39  
AGS "C4'" "H4'"  sing N N 40  
AGS "C3'" "H3'"  sing N N 41  
AGS "O3'" "HO3'" sing N N 42  
AGS "C2'" "H2'"  sing N N 43  
AGS "O2'" "HO2'" sing N N 44  
AGS "C1'" "H1'"  sing N N 45  
AGS C8    H8     sing N N 46  
AGS N6    HN61   sing N N 47  
AGS N6    HN62   sing N N 48  
AGS C2    H2     sing N N 49  
ALA N     CA     sing N N 50  
ALA N     H      sing N N 51  
ALA N     H2     sing N N 52  
ALA CA    C      sing N N 53  
ALA CA    CB     sing N N 54  
ALA CA    HA     sing N N 55  
ALA C     O      doub N N 56  
ALA C     OXT    sing N N 57  
ALA CB    HB1    sing N N 58  
ALA CB    HB2    sing N N 59  
ALA CB    HB3    sing N N 60  
ALA OXT   HXT    sing N N 61  
ARG N     CA     sing N N 62  
ARG N     H      sing N N 63  
ARG N     H2     sing N N 64  
ARG CA    C      sing N N 65  
ARG CA    CB     sing N N 66  
ARG CA    HA     sing N N 67  
ARG C     O      doub N N 68  
ARG C     OXT    sing N N 69  
ARG CB    CG     sing N N 70  
ARG CB    HB2    sing N N 71  
ARG CB    HB3    sing N N 72  
ARG CG    CD     sing N N 73  
ARG CG    HG2    sing N N 74  
ARG CG    HG3    sing N N 75  
ARG CD    NE     sing N N 76  
ARG CD    HD2    sing N N 77  
ARG CD    HD3    sing N N 78  
ARG NE    CZ     sing N N 79  
ARG NE    HE     sing N N 80  
ARG CZ    NH1    sing N N 81  
ARG CZ    NH2    doub N N 82  
ARG NH1   HH11   sing N N 83  
ARG NH1   HH12   sing N N 84  
ARG NH2   HH21   sing N N 85  
ARG NH2   HH22   sing N N 86  
ARG OXT   HXT    sing N N 87  
ASN N     CA     sing N N 88  
ASN N     H      sing N N 89  
ASN N     H2     sing N N 90  
ASN CA    C      sing N N 91  
ASN CA    CB     sing N N 92  
ASN CA    HA     sing N N 93  
ASN C     O      doub N N 94  
ASN C     OXT    sing N N 95  
ASN CB    CG     sing N N 96  
ASN CB    HB2    sing N N 97  
ASN CB    HB3    sing N N 98  
ASN CG    OD1    doub N N 99  
ASN CG    ND2    sing N N 100 
ASN ND2   HD21   sing N N 101 
ASN ND2   HD22   sing N N 102 
ASN OXT   HXT    sing N N 103 
ASP N     CA     sing N N 104 
ASP N     H      sing N N 105 
ASP N     H2     sing N N 106 
ASP CA    C      sing N N 107 
ASP CA    CB     sing N N 108 
ASP CA    HA     sing N N 109 
ASP C     O      doub N N 110 
ASP C     OXT    sing N N 111 
ASP CB    CG     sing N N 112 
ASP CB    HB2    sing N N 113 
ASP CB    HB3    sing N N 114 
ASP CG    OD1    doub N N 115 
ASP CG    OD2    sing N N 116 
ASP OD2   HD2    sing N N 117 
ASP OXT   HXT    sing N N 118 
AV0 CAB   CAX    sing N N 119 
AV0 CAX   CAZ    sing N N 120 
AV0 CAA   CAW    sing N N 121 
AV0 CAZ   CBB    sing N N 122 
AV0 CAW   CAY    sing N N 123 
AV0 CBB   CBD    sing N N 124 
AV0 CAY   CBA    sing N N 125 
AV0 CBD   CBF    sing N N 126 
AV0 CBA   CBC    sing N N 127 
AV0 CBC   CBE    sing N N 128 
AV0 CBF   CBH    sing N N 129 
AV0 CBE   CBG    sing N N 130 
AV0 CBH   CBJ    sing N N 131 
AV0 OAJ   CBN    sing N N 132 
AV0 OAR   CCO    sing N N 133 
AV0 CBG   CBI    sing N N 134 
AV0 CBJ   CBL    sing N N 135 
AV0 CBL   CBR    sing N N 136 
AV0 CBP   OAL    sing N N 137 
AV0 CBP   CCF    sing N N 138 
AV0 CBN   CCD    sing N N 139 
AV0 CCO   CCD    sing N N 140 
AV0 CCO   CCU    sing N N 141 
AV0 CBI   CBK    sing N N 142 
AV0 OAT   CCU    sing N N 143 
AV0 CCD   OBZ    sing N N 144 
AV0 CCU   CCW    sing N N 145 
AV0 CBQ   CBK    sing N N 146 
AV0 CBQ   CCM    sing N N 147 
AV0 CCF   OBX    sing N N 148 
AV0 CCF   CCQ    sing N N 149 
AV0 CBR   CCM    sing N N 150 
AV0 CBT   CCM    sing N N 151 
AV0 CBT   OBV    sing N N 152 
AV0 OBX   CCJ    sing N N 153 
AV0 CCM   CBS    sing N N 154 
AV0 OBZ   CCS    sing N N 155 
AV0 OCB   CCQ    sing N N 156 
AV0 OCB   CCS    sing N N 157 
AV0 CCW   CCS    sing N N 158 
AV0 CCW   OAV    sing N N 159 
AV0 CCQ   CCH    sing N N 160 
AV0 CCJ   OBV    sing N N 161 
AV0 CCJ   CCL    sing N N 162 
AV0 CBS   O1     sing N N 163 
AV0 O1    C1     sing N N 164 
AV0 CCH   CCL    sing N N 165 
AV0 CCH   OAN    sing N N 166 
AV0 CCL   OAP    sing N N 167 
AV0 O2    C2     sing N N 168 
AV0 C1    C2     sing N N 169 
AV0 C1    O5     sing N N 170 
AV0 C2    C3     sing N N 171 
AV0 O5    C5     sing N N 172 
AV0 C3    O3     sing N N 173 
AV0 C3    C4     sing N N 174 
AV0 C5    C4     sing N N 175 
AV0 C5    C6     sing N N 176 
AV0 C4    O4     sing N N 177 
AV0 C6    O6     sing N N 178 
AV0 O4    CCR    sing N N 179 
AV0 CCR   OBY    sing N N 180 
AV0 CCR   CCV    sing N N 181 
AV0 OBY   CCC    sing N N 182 
AV0 OAU   CCV    sing N N 183 
AV0 CCV   CCT    sing N N 184 
AV0 CCC   CBM    sing N N 185 
AV0 CCC   CCN    sing N N 186 
AV0 CBM   OAI    sing N N 187 
AV0 CCT   CCN    sing N N 188 
AV0 CCT   OAS    sing N N 189 
AV0 CCN   OAQ    sing N N 190 
AV0 C1    H1     sing N N 191 
AV0 C2    H2     sing N N 192 
AV0 O2    H3     sing N N 193 
AV0 C3    H4     sing N N 194 
AV0 O3    H5     sing N N 195 
AV0 C4    H6     sing N N 196 
AV0 C5    H7     sing N N 197 
AV0 C6    H8     sing N N 198 
AV0 C6    H9     sing N N 199 
AV0 O6    H10    sing N N 200 
AV0 CAA   H11    sing N N 201 
AV0 CAA   H12    sing N N 202 
AV0 CAA   H13    sing N N 203 
AV0 CAB   H14    sing N N 204 
AV0 CAB   H15    sing N N 205 
AV0 CAB   H16    sing N N 206 
AV0 OAI   H17    sing N N 207 
AV0 OAJ   H18    sing N N 208 
AV0 OAL   H19    sing N N 209 
AV0 OAN   H20    sing N N 210 
AV0 OAP   H21    sing N N 211 
AV0 OAQ   H22    sing N N 212 
AV0 OAR   H23    sing N N 213 
AV0 OAS   H24    sing N N 214 
AV0 OAT   H25    sing N N 215 
AV0 OAU   H26    sing N N 216 
AV0 OAV   H27    sing N N 217 
AV0 CAW   H28    sing N N 218 
AV0 CAW   H29    sing N N 219 
AV0 CAX   H30    sing N N 220 
AV0 CAX   H31    sing N N 221 
AV0 CAY   H32    sing N N 222 
AV0 CAY   H33    sing N N 223 
AV0 CAZ   H34    sing N N 224 
AV0 CAZ   H35    sing N N 225 
AV0 CBA   H36    sing N N 226 
AV0 CBA   H37    sing N N 227 
AV0 CBB   H38    sing N N 228 
AV0 CBB   H39    sing N N 229 
AV0 CBC   H40    sing N N 230 
AV0 CBC   H41    sing N N 231 
AV0 CBD   H42    sing N N 232 
AV0 CBD   H43    sing N N 233 
AV0 CBE   H44    sing N N 234 
AV0 CBE   H45    sing N N 235 
AV0 CBF   H46    sing N N 236 
AV0 CBF   H47    sing N N 237 
AV0 CBG   H48    sing N N 238 
AV0 CBG   H49    sing N N 239 
AV0 CBH   H50    sing N N 240 
AV0 CBH   H51    sing N N 241 
AV0 CBI   H52    sing N N 242 
AV0 CBI   H53    sing N N 243 
AV0 CBJ   H54    sing N N 244 
AV0 CBJ   H55    sing N N 245 
AV0 CBK   H56    sing N N 246 
AV0 CBK   H57    sing N N 247 
AV0 CBL   H58    sing N N 248 
AV0 CBL   H59    sing N N 249 
AV0 CBM   H60    sing N N 250 
AV0 CBM   H61    sing N N 251 
AV0 CBN   H62    sing N N 252 
AV0 CBN   H63    sing N N 253 
AV0 CBP   H64    sing N N 254 
AV0 CBP   H65    sing N N 255 
AV0 CBQ   H66    sing N N 256 
AV0 CBQ   H67    sing N N 257 
AV0 CBR   H68    sing N N 258 
AV0 CBR   H69    sing N N 259 
AV0 CBS   H70    sing N N 260 
AV0 CBS   H71    sing N N 261 
AV0 CBT   H72    sing N N 262 
AV0 CBT   H73    sing N N 263 
AV0 CCC   H74    sing N N 264 
AV0 CCD   H75    sing N N 265 
AV0 CCF   H76    sing N N 266 
AV0 CCH   H77    sing N N 267 
AV0 CCJ   H78    sing N N 268 
AV0 CCL   H79    sing N N 269 
AV0 CCN   H80    sing N N 270 
AV0 CCO   H81    sing N N 271 
AV0 CCQ   H82    sing N N 272 
AV0 CCR   H83    sing N N 273 
AV0 CCS   H84    sing N N 274 
AV0 CCT   H85    sing N N 275 
AV0 CCU   H86    sing N N 276 
AV0 CCV   H87    sing N N 277 
AV0 CCW   H88    sing N N 278 
CYS N     CA     sing N N 279 
CYS N     H      sing N N 280 
CYS N     H2     sing N N 281 
CYS CA    C      sing N N 282 
CYS CA    CB     sing N N 283 
CYS CA    HA     sing N N 284 
CYS C     O      doub N N 285 
CYS C     OXT    sing N N 286 
CYS CB    SG     sing N N 287 
CYS CB    HB2    sing N N 288 
CYS CB    HB3    sing N N 289 
CYS SG    HG     sing N N 290 
CYS OXT   HXT    sing N N 291 
GLN N     CA     sing N N 292 
GLN N     H      sing N N 293 
GLN N     H2     sing N N 294 
GLN CA    C      sing N N 295 
GLN CA    CB     sing N N 296 
GLN CA    HA     sing N N 297 
GLN C     O      doub N N 298 
GLN C     OXT    sing N N 299 
GLN CB    CG     sing N N 300 
GLN CB    HB2    sing N N 301 
GLN CB    HB3    sing N N 302 
GLN CG    CD     sing N N 303 
GLN CG    HG2    sing N N 304 
GLN CG    HG3    sing N N 305 
GLN CD    OE1    doub N N 306 
GLN CD    NE2    sing N N 307 
GLN NE2   HE21   sing N N 308 
GLN NE2   HE22   sing N N 309 
GLN OXT   HXT    sing N N 310 
GLU N     CA     sing N N 311 
GLU N     H      sing N N 312 
GLU N     H2     sing N N 313 
GLU CA    C      sing N N 314 
GLU CA    CB     sing N N 315 
GLU CA    HA     sing N N 316 
GLU C     O      doub N N 317 
GLU C     OXT    sing N N 318 
GLU CB    CG     sing N N 319 
GLU CB    HB2    sing N N 320 
GLU CB    HB3    sing N N 321 
GLU CG    CD     sing N N 322 
GLU CG    HG2    sing N N 323 
GLU CG    HG3    sing N N 324 
GLU CD    OE1    doub N N 325 
GLU CD    OE2    sing N N 326 
GLU OE2   HE2    sing N N 327 
GLU OXT   HXT    sing N N 328 
GLY N     CA     sing N N 329 
GLY N     H      sing N N 330 
GLY N     H2     sing N N 331 
GLY CA    C      sing N N 332 
GLY CA    HA2    sing N N 333 
GLY CA    HA3    sing N N 334 
GLY C     O      doub N N 335 
GLY C     OXT    sing N N 336 
GLY OXT   HXT    sing N N 337 
HIS N     CA     sing N N 338 
HIS N     H      sing N N 339 
HIS N     H2     sing N N 340 
HIS CA    C      sing N N 341 
HIS CA    CB     sing N N 342 
HIS CA    HA     sing N N 343 
HIS C     O      doub N N 344 
HIS C     OXT    sing N N 345 
HIS CB    CG     sing N N 346 
HIS CB    HB2    sing N N 347 
HIS CB    HB3    sing N N 348 
HIS CG    ND1    sing Y N 349 
HIS CG    CD2    doub Y N 350 
HIS ND1   CE1    doub Y N 351 
HIS ND1   HD1    sing N N 352 
HIS CD2   NE2    sing Y N 353 
HIS CD2   HD2    sing N N 354 
HIS CE1   NE2    sing Y N 355 
HIS CE1   HE1    sing N N 356 
HIS NE2   HE2    sing N N 357 
HIS OXT   HXT    sing N N 358 
HOH O     H1     sing N N 359 
HOH O     H2     sing N N 360 
ILE N     CA     sing N N 361 
ILE N     H      sing N N 362 
ILE N     H2     sing N N 363 
ILE CA    C      sing N N 364 
ILE CA    CB     sing N N 365 
ILE CA    HA     sing N N 366 
ILE C     O      doub N N 367 
ILE C     OXT    sing N N 368 
ILE CB    CG1    sing N N 369 
ILE CB    CG2    sing N N 370 
ILE CB    HB     sing N N 371 
ILE CG1   CD1    sing N N 372 
ILE CG1   HG12   sing N N 373 
ILE CG1   HG13   sing N N 374 
ILE CG2   HG21   sing N N 375 
ILE CG2   HG22   sing N N 376 
ILE CG2   HG23   sing N N 377 
ILE CD1   HD11   sing N N 378 
ILE CD1   HD12   sing N N 379 
ILE CD1   HD13   sing N N 380 
ILE OXT   HXT    sing N N 381 
LEU N     CA     sing N N 382 
LEU N     H      sing N N 383 
LEU N     H2     sing N N 384 
LEU CA    C      sing N N 385 
LEU CA    CB     sing N N 386 
LEU CA    HA     sing N N 387 
LEU C     O      doub N N 388 
LEU C     OXT    sing N N 389 
LEU CB    CG     sing N N 390 
LEU CB    HB2    sing N N 391 
LEU CB    HB3    sing N N 392 
LEU CG    CD1    sing N N 393 
LEU CG    CD2    sing N N 394 
LEU CG    HG     sing N N 395 
LEU CD1   HD11   sing N N 396 
LEU CD1   HD12   sing N N 397 
LEU CD1   HD13   sing N N 398 
LEU CD2   HD21   sing N N 399 
LEU CD2   HD22   sing N N 400 
LEU CD2   HD23   sing N N 401 
LEU OXT   HXT    sing N N 402 
LYS N     CA     sing N N 403 
LYS N     H      sing N N 404 
LYS N     H2     sing N N 405 
LYS CA    C      sing N N 406 
LYS CA    CB     sing N N 407 
LYS CA    HA     sing N N 408 
LYS C     O      doub N N 409 
LYS C     OXT    sing N N 410 
LYS CB    CG     sing N N 411 
LYS CB    HB2    sing N N 412 
LYS CB    HB3    sing N N 413 
LYS CG    CD     sing N N 414 
LYS CG    HG2    sing N N 415 
LYS CG    HG3    sing N N 416 
LYS CD    CE     sing N N 417 
LYS CD    HD2    sing N N 418 
LYS CD    HD3    sing N N 419 
LYS CE    NZ     sing N N 420 
LYS CE    HE2    sing N N 421 
LYS CE    HE3    sing N N 422 
LYS NZ    HZ1    sing N N 423 
LYS NZ    HZ2    sing N N 424 
LYS NZ    HZ3    sing N N 425 
LYS OXT   HXT    sing N N 426 
MET N     CA     sing N N 427 
MET N     H      sing N N 428 
MET N     H2     sing N N 429 
MET CA    C      sing N N 430 
MET CA    CB     sing N N 431 
MET CA    HA     sing N N 432 
MET C     O      doub N N 433 
MET C     OXT    sing N N 434 
MET CB    CG     sing N N 435 
MET CB    HB2    sing N N 436 
MET CB    HB3    sing N N 437 
MET CG    SD     sing N N 438 
MET CG    HG2    sing N N 439 
MET CG    HG3    sing N N 440 
MET SD    CE     sing N N 441 
MET CE    HE1    sing N N 442 
MET CE    HE2    sing N N 443 
MET CE    HE3    sing N N 444 
MET OXT   HXT    sing N N 445 
PHE N     CA     sing N N 446 
PHE N     H      sing N N 447 
PHE N     H2     sing N N 448 
PHE CA    C      sing N N 449 
PHE CA    CB     sing N N 450 
PHE CA    HA     sing N N 451 
PHE C     O      doub N N 452 
PHE C     OXT    sing N N 453 
PHE CB    CG     sing N N 454 
PHE CB    HB2    sing N N 455 
PHE CB    HB3    sing N N 456 
PHE CG    CD1    doub Y N 457 
PHE CG    CD2    sing Y N 458 
PHE CD1   CE1    sing Y N 459 
PHE CD1   HD1    sing N N 460 
PHE CD2   CE2    doub Y N 461 
PHE CD2   HD2    sing N N 462 
PHE CE1   CZ     doub Y N 463 
PHE CE1   HE1    sing N N 464 
PHE CE2   CZ     sing Y N 465 
PHE CE2   HE2    sing N N 466 
PHE CZ    HZ     sing N N 467 
PHE OXT   HXT    sing N N 468 
PRO N     CA     sing N N 469 
PRO N     CD     sing N N 470 
PRO N     H      sing N N 471 
PRO CA    C      sing N N 472 
PRO CA    CB     sing N N 473 
PRO CA    HA     sing N N 474 
PRO C     O      doub N N 475 
PRO C     OXT    sing N N 476 
PRO CB    CG     sing N N 477 
PRO CB    HB2    sing N N 478 
PRO CB    HB3    sing N N 479 
PRO CG    CD     sing N N 480 
PRO CG    HG2    sing N N 481 
PRO CG    HG3    sing N N 482 
PRO CD    HD2    sing N N 483 
PRO CD    HD3    sing N N 484 
PRO OXT   HXT    sing N N 485 
SER N     CA     sing N N 486 
SER N     H      sing N N 487 
SER N     H2     sing N N 488 
SER CA    C      sing N N 489 
SER CA    CB     sing N N 490 
SER CA    HA     sing N N 491 
SER C     O      doub N N 492 
SER C     OXT    sing N N 493 
SER CB    OG     sing N N 494 
SER CB    HB2    sing N N 495 
SER CB    HB3    sing N N 496 
SER OG    HG     sing N N 497 
SER OXT   HXT    sing N N 498 
THR N     CA     sing N N 499 
THR N     H      sing N N 500 
THR N     H2     sing N N 501 
THR CA    C      sing N N 502 
THR CA    CB     sing N N 503 
THR CA    HA     sing N N 504 
THR C     O      doub N N 505 
THR C     OXT    sing N N 506 
THR CB    OG1    sing N N 507 
THR CB    CG2    sing N N 508 
THR CB    HB     sing N N 509 
THR OG1   HG1    sing N N 510 
THR CG2   HG21   sing N N 511 
THR CG2   HG22   sing N N 512 
THR CG2   HG23   sing N N 513 
THR OXT   HXT    sing N N 514 
TRP N     CA     sing N N 515 
TRP N     H      sing N N 516 
TRP N     H2     sing N N 517 
TRP CA    C      sing N N 518 
TRP CA    CB     sing N N 519 
TRP CA    HA     sing N N 520 
TRP C     O      doub N N 521 
TRP C     OXT    sing N N 522 
TRP CB    CG     sing N N 523 
TRP CB    HB2    sing N N 524 
TRP CB    HB3    sing N N 525 
TRP CG    CD1    doub Y N 526 
TRP CG    CD2    sing Y N 527 
TRP CD1   NE1    sing Y N 528 
TRP CD1   HD1    sing N N 529 
TRP CD2   CE2    doub Y N 530 
TRP CD2   CE3    sing Y N 531 
TRP NE1   CE2    sing Y N 532 
TRP NE1   HE1    sing N N 533 
TRP CE2   CZ2    sing Y N 534 
TRP CE3   CZ3    doub Y N 535 
TRP CE3   HE3    sing N N 536 
TRP CZ2   CH2    doub Y N 537 
TRP CZ2   HZ2    sing N N 538 
TRP CZ3   CH2    sing Y N 539 
TRP CZ3   HZ3    sing N N 540 
TRP CH2   HH2    sing N N 541 
TRP OXT   HXT    sing N N 542 
TYR N     CA     sing N N 543 
TYR N     H      sing N N 544 
TYR N     H2     sing N N 545 
TYR CA    C      sing N N 546 
TYR CA    CB     sing N N 547 
TYR CA    HA     sing N N 548 
TYR C     O      doub N N 549 
TYR C     OXT    sing N N 550 
TYR CB    CG     sing N N 551 
TYR CB    HB2    sing N N 552 
TYR CB    HB3    sing N N 553 
TYR CG    CD1    doub Y N 554 
TYR CG    CD2    sing Y N 555 
TYR CD1   CE1    sing Y N 556 
TYR CD1   HD1    sing N N 557 
TYR CD2   CE2    doub Y N 558 
TYR CD2   HD2    sing N N 559 
TYR CE1   CZ     doub Y N 560 
TYR CE1   HE1    sing N N 561 
TYR CE2   CZ     sing Y N 562 
TYR CE2   HE2    sing N N 563 
TYR CZ    OH     sing N N 564 
TYR OH    HH     sing N N 565 
TYR OXT   HXT    sing N N 566 
VAL N     CA     sing N N 567 
VAL N     H      sing N N 568 
VAL N     H2     sing N N 569 
VAL CA    C      sing N N 570 
VAL CA    CB     sing N N 571 
VAL CA    HA     sing N N 572 
VAL C     O      doub N N 573 
VAL C     OXT    sing N N 574 
VAL CB    CG1    sing N N 575 
VAL CB    CG2    sing N N 576 
VAL CB    HB     sing N N 577 
VAL CG1   HG11   sing N N 578 
VAL CG1   HG12   sing N N 579 
VAL CG1   HG13   sing N N 580 
VAL CG2   HG21   sing N N 581 
VAL CG2   HG22   sing N N 582 
VAL CG2   HG23   sing N N 583 
VAL OXT   HXT    sing N N 584 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-27 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CFL 
_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 ATP-gamma-S' 
# 
_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          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_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              'GATAN K3 BIOQUANTUM (6k 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 
'PARTICLE SELECTION'            ? 1  1 ? ? ?      ?            
'MODEL REFINEMENT'              ? 2  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 3  ? ? 1 ?      ?            
MASKING                         ? 4  ? ? ? ?      ?            
'CTF CORRECTION'                ? 5  1 ? ? ?      ?            
'LAYERLINE INDEXING'            ? 6  ? ? ? ?      ?            
'DIFFRACTION INDEXING'          ? 7  ? ? ? ?      ?            
'MODEL FITTING'                 ? 8  ? ? ? ?      ?            
OTHER                           ? 9  ? ? ? ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?      ?            
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ?      ?            
CLASSIFICATION                  ? 12 1 ? ? ?      ?            
RECONSTRUCTION                  ? 13 1 ? ? ?      ?            
'VOLUME SELECTION'              ? 14 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 15 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 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                    9CFL 
_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  
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 27  ? 158.540 110.110 139.540 1.00 59.80  ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 27  ? 159.913 110.548 139.740 1.00 61.27  ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 27  ? 160.411 111.310 138.511 1.00 60.53  ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 27  ? 161.260 112.194 138.620 1.00 59.19  ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 27  ? 160.848 109.364 140.058 1.00 61.77  ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 27  ? 161.001 108.276 138.979 1.00 61.27  ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 27  ? 159.546 107.767 138.035 1.00 75.19  ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 27  ? 158.631 106.814 139.254 1.00 60.38  ? 1   MET A CE    1 
ATOM   9    N  N     . SER A 1 28  ? 159.873 110.965 137.339 1.00 53.91  ? 2   SER A N     1 
ATOM   10   C  CA    . SER A 1 28  ? 160.174 111.721 136.130 1.00 47.92  ? 2   SER A CA    1 
ATOM   11   C  C     . SER A 1 28  ? 159.418 113.041 136.093 1.00 46.90  ? 2   SER A C     1 
ATOM   12   O  O     . SER A 1 28  ? 159.892 114.003 135.478 1.00 52.66  ? 2   SER A O     1 
ATOM   13   C  CB    . SER A 1 28  ? 159.842 110.887 134.892 1.00 53.91  ? 2   SER A CB    1 
ATOM   14   O  OG    . SER A 1 28  ? 160.685 111.228 133.807 1.00 55.75  ? 2   SER A OG    1 
ATOM   15   N  N     . ALA A 1 29  ? 158.251 113.096 136.741 1.00 44.23  ? 3   ALA A N     1 
ATOM   16   C  CA    . ALA A 1 29  ? 157.491 114.338 136.839 1.00 39.19  ? 3   ALA A CA    1 
ATOM   17   C  C     . ALA A 1 29  ? 158.236 115.380 137.663 1.00 43.20  ? 3   ALA A C     1 
ATOM   18   O  O     . ALA A 1 29  ? 158.248 116.569 137.313 1.00 45.84  ? 3   ALA A O     1 
ATOM   19   C  CB    . ALA A 1 29  ? 156.119 114.055 137.449 1.00 37.63  ? 3   ALA A CB    1 
ATOM   20   N  N     . ILE A 1 30  ? 158.865 114.940 138.759 1.00 43.16  ? 4   ILE A N     1 
ATOM   21   C  CA    . ILE A 1 30  ? 159.632 115.832 139.627 1.00 39.10  ? 4   ILE A CA    1 
ATOM   22   C  C     . ILE A 1 30  ? 160.815 116.418 138.874 1.00 39.72  ? 4   ILE A C     1 
ATOM   23   O  O     . ILE A 1 30  ? 161.052 117.631 138.904 1.00 47.33  ? 4   ILE A O     1 
ATOM   24   C  CB    . ILE A 1 30  ? 160.095 115.078 140.885 1.00 44.40  ? 4   ILE A CB    1 
ATOM   25   C  CG1   . ILE A 1 30  ? 158.892 114.479 141.605 1.00 42.36  ? 4   ILE A CG1   1 
ATOM   26   C  CG2   . ILE A 1 30  ? 160.897 115.993 141.805 1.00 39.85  ? 4   ILE A CG2   1 
ATOM   27   C  CD1   . ILE A 1 30  ? 158.015 115.511 142.206 1.00 43.55  ? 4   ILE A CD1   1 
ATOM   28   N  N     . GLY A 1 31  ? 161.555 115.561 138.165 1.00 38.30  ? 5   GLY A N     1 
ATOM   29   C  CA    . GLY A 1 31  ? 162.693 116.029 137.392 1.00 39.18  ? 5   GLY A CA    1 
ATOM   30   C  C     . GLY A 1 31  ? 162.291 116.919 136.233 1.00 39.99  ? 5   GLY A C     1 
ATOM   31   O  O     . GLY A 1 31  ? 162.986 117.886 135.917 1.00 44.09  ? 5   GLY A O     1 
ATOM   32   N  N     . THR A 1 32  ? 161.142 116.628 135.614 1.00 38.55  ? 6   THR A N     1 
ATOM   33   C  CA    . THR A 1 32  ? 160.659 117.445 134.504 1.00 37.21  ? 6   THR A CA    1 
ATOM   34   C  C     . THR A 1 32  ? 160.276 118.847 134.967 1.00 38.55  ? 6   THR A C     1 
ATOM   35   O  O     . THR A 1 32  ? 160.717 119.843 134.381 1.00 46.14  ? 6   THR A O     1 
ATOM   36   C  CB    . THR A 1 32  ? 159.472 116.764 133.825 1.00 40.02  ? 6   THR A CB    1 
ATOM   37   O  OG1   . THR A 1 32  ? 159.791 115.392 133.565 1.00 45.60  ? 6   THR A OG1   1 
ATOM   38   C  CG2   . THR A 1 32  ? 159.147 117.458 132.515 1.00 35.72  ? 6   THR A CG2   1 
ATOM   39   N  N     . VAL A 1 33  ? 159.476 118.941 136.036 1.00 36.04  ? 7   VAL A N     1 
ATOM   40   C  CA    . VAL A 1 33  ? 159.046 120.245 136.543 1.00 31.03  ? 7   VAL A CA    1 
ATOM   41   C  C     . VAL A 1 33  ? 160.235 121.018 137.112 1.00 33.98  ? 7   VAL A C     1 
ATOM   42   O  O     . VAL A 1 33  ? 160.363 122.235 136.900 1.00 39.09  ? 7   VAL A O     1 
ATOM   43   C  CB    . VAL A 1 33  ? 157.913 120.060 137.574 1.00 36.53  ? 7   VAL A CB    1 
ATOM   44   C  CG1   . VAL A 1 33  ? 157.566 121.366 138.275 1.00 35.46  ? 7   VAL A CG1   1 
ATOM   45   C  CG2   . VAL A 1 33  ? 156.678 119.491 136.894 1.00 30.18  ? 7   VAL A CG2   1 
ATOM   46   N  N     . PHE A 1 34  ? 161.159 120.312 137.776 1.00 37.35  ? 8   PHE A N     1 
ATOM   47   C  CA    . PHE A 1 34  ? 162.360 120.946 138.309 1.00 31.70  ? 8   PHE A CA    1 
ATOM   48   C  C     . PHE A 1 34  ? 163.253 121.491 137.199 1.00 36.23  ? 8   PHE A C     1 
ATOM   49   O  O     . PHE A 1 34  ? 163.776 122.606 137.313 1.00 45.55  ? 8   PHE A O     1 
ATOM   50   C  CB    . PHE A 1 34  ? 163.128 119.949 139.178 1.00 34.97  ? 8   PHE A CB    1 
ATOM   51   C  CG    . PHE A 1 34  ? 164.356 120.524 139.825 1.00 40.33  ? 8   PHE A CG    1 
ATOM   52   C  CD1   . PHE A 1 34  ? 164.246 121.383 140.908 1.00 39.97  ? 8   PHE A CD1   1 
ATOM   53   C  CD2   . PHE A 1 34  ? 165.620 120.199 139.356 1.00 38.62  ? 8   PHE A CD2   1 
ATOM   54   C  CE1   . PHE A 1 34  ? 165.374 121.912 141.508 1.00 40.61  ? 8   PHE A CE1   1 
ATOM   55   C  CE2   . PHE A 1 34  ? 166.752 120.725 139.952 1.00 40.75  ? 8   PHE A CE2   1 
ATOM   56   C  CZ    . PHE A 1 34  ? 166.628 121.582 141.030 1.00 38.53  ? 8   PHE A CZ    1 
ATOM   57   N  N     . LYS A 1 35  ? 163.411 120.744 136.099 1.00 38.90  ? 9   LYS A N     1 
ATOM   58   C  CA    . LYS A 1 35  ? 164.269 121.241 135.031 1.00 36.57  ? 9   LYS A CA    1 
ATOM   59   C  C     . LYS A 1 35  ? 163.604 122.392 134.280 1.00 40.49  ? 9   LYS A C     1 
ATOM   60   O  O     . LYS A 1 35  ? 164.282 123.362 133.922 1.00 44.24  ? 9   LYS A O     1 
ATOM   61   C  CB    . LYS A 1 35  ? 164.705 120.099 134.096 1.00 36.05  ? 9   LYS A CB    1 
ATOM   62   C  CG    . LYS A 1 35  ? 163.866 119.804 132.856 1.00 44.10  ? 9   LYS A CG    1 
ATOM   63   C  CD    . LYS A 1 35  ? 163.789 118.312 132.572 1.00 48.00  ? 9   LYS A CD    1 
ATOM   64   C  CE    . LYS A 1 35  ? 162.755 118.010 131.499 1.00 49.04  ? 9   LYS A CE    1 
ATOM   65   N  NZ    . LYS A 1 35  ? 162.580 116.548 131.296 1.00 46.55  ? 9   LYS A NZ    1 
ATOM   66   N  N     . GLU A 1 36  ? 162.271 122.357 134.113 1.00 37.35  ? 10  GLU A N     1 
ATOM   67   C  CA    . GLU A 1 36  ? 161.587 123.484 133.477 1.00 37.26  ? 10  GLU A CA    1 
ATOM   68   C  C     . GLU A 1 36  ? 161.609 124.724 134.361 1.00 38.78  ? 10  GLU A C     1 
ATOM   69   O  O     . GLU A 1 36  ? 161.480 125.849 133.866 1.00 47.60  ? 10  GLU A O     1 
ATOM   70   C  CB    . GLU A 1 36  ? 160.144 123.127 133.118 1.00 36.15  ? 10  GLU A CB    1 
ATOM   71   C  CG    . GLU A 1 36  ? 159.977 122.007 132.112 1.00 42.45  ? 10  GLU A CG    1 
ATOM   72   C  CD    . GLU A 1 36  ? 158.548 121.884 131.622 1.00 47.65  ? 10  GLU A CD    1 
ATOM   73   O  OE1   . GLU A 1 36  ? 158.332 121.927 130.393 1.00 51.29  ? 10  GLU A OE1   1 
ATOM   74   O  OE2   . GLU A 1 36  ? 157.640 121.756 132.468 1.00 42.94  ? 10  GLU A OE2   1 
ATOM   75   N  N     . HIS A 1 37  ? 161.772 124.543 135.671 1.00 34.67  ? 11  HIS A N     1 
ATOM   76   C  CA    . HIS A 1 37  ? 161.919 125.708 136.534 1.00 30.63  ? 11  HIS A CA    1 
ATOM   77   C  C     . HIS A 1 37  ? 163.358 126.215 136.568 1.00 32.71  ? 11  HIS A C     1 
ATOM   78   O  O     . HIS A 1 37  ? 163.587 127.411 136.783 1.00 39.12  ? 11  HIS A O     1 
ATOM   79   C  CB    . HIS A 1 37  ? 161.412 125.386 137.935 1.00 26.14  ? 11  HIS A CB    1 
ATOM   80   C  CG    . HIS A 1 37  ? 159.941 125.595 138.094 1.00 23.44  ? 11  HIS A CG    1 
ATOM   81   N  ND1   . HIS A 1 37  ? 159.011 124.659 137.701 1.00 30.50  ? 11  HIS A ND1   1 
ATOM   82   C  CD2   . HIS A 1 37  ? 159.237 126.640 138.588 1.00 30.35  ? 11  HIS A CD2   1 
ATOM   83   C  CE1   . HIS A 1 37  ? 157.798 125.115 137.952 1.00 27.25  ? 11  HIS A CE1   1 
ATOM   84   N  NE2   . HIS A 1 37  ? 157.907 126.315 138.491 1.00 30.16  ? 11  HIS A NE2   1 
ATOM   85   N  N     . VAL A 1 38  ? 164.347 125.340 136.356 1.00 38.17  ? 12  VAL A N     1 
ATOM   86   C  CA    . VAL A 1 38  ? 165.722 125.827 136.478 1.00 33.27  ? 12  VAL A CA    1 
ATOM   87   C  C     . VAL A 1 38  ? 166.331 126.337 135.171 1.00 39.19  ? 12  VAL A C     1 
ATOM   88   O  O     . VAL A 1 38  ? 167.308 127.093 135.234 1.00 45.40  ? 12  VAL A O     1 
ATOM   89   C  CB    . VAL A 1 38  ? 166.686 124.794 137.093 1.00 40.04  ? 12  VAL A CB    1 
ATOM   90   C  CG1   . VAL A 1 38  ? 166.235 124.393 138.492 1.00 35.10  ? 12  VAL A CG1   1 
ATOM   91   C  CG2   . VAL A 1 38  ? 166.862 123.591 136.192 1.00 42.71  ? 12  VAL A CG2   1 
ATOM   92   N  N     . LYS A 1 39  ? 165.817 125.979 133.986 1.00 37.11  ? 13  LYS A N     1 
ATOM   93   C  CA    . LYS A 1 39  ? 166.367 126.682 132.819 1.00 39.60  ? 13  LYS A CA    1 
ATOM   94   C  C     . LYS A 1 39  ? 165.544 127.895 132.403 1.00 41.03  ? 13  LYS A C     1 
ATOM   95   O  O     . LYS A 1 39  ? 165.843 128.492 131.364 1.00 47.49  ? 13  LYS A O     1 
ATOM   96   C  CB    . LYS A 1 39  ? 166.548 125.798 131.569 1.00 44.69  ? 13  LYS A CB    1 
ATOM   97   C  CG    . LYS A 1 39  ? 165.789 124.522 131.468 1.00 45.46  ? 13  LYS A CG    1 
ATOM   98   C  CD    . LYS A 1 39  ? 165.973 123.845 130.124 1.00 47.27  ? 13  LYS A CD    1 
ATOM   99   C  CE    . LYS A 1 39  ? 165.344 122.460 130.125 1.00 48.35  ? 13  LYS A CE    1 
ATOM   100  N  NZ    . LYS A 1 39  ? 163.867 122.520 130.337 1.00 44.14  ? 13  LYS A NZ    1 
ATOM   101  N  N     . ASN A 1 40  ? 164.523 128.276 133.165 1.00 37.54  ? 14  ASN A N     1 
ATOM   102  C  CA    . ASN A 1 40  ? 163.654 129.385 132.787 1.00 33.30  ? 14  ASN A CA    1 
ATOM   103  C  C     . ASN A 1 40  ? 163.521 130.390 133.919 1.00 32.92  ? 14  ASN A C     1 
ATOM   104  O  O     . ASN A 1 40  ? 162.467 131.002 134.104 1.00 41.61  ? 14  ASN A O     1 
ATOM   105  C  CB    . ASN A 1 40  ? 162.281 128.878 132.353 1.00 32.69  ? 14  ASN A CB    1 
ATOM   106  C  CG    . ASN A 1 40  ? 162.362 127.884 131.216 1.00 33.88  ? 14  ASN A CG    1 
ATOM   107  O  OD1   . ASN A 1 40  ? 162.548 128.261 130.062 1.00 41.02  ? 14  ASN A OD1   1 
ATOM   108  N  ND2   . ASN A 1 40  ? 162.223 126.605 131.536 1.00 33.88  ? 14  ASN A ND2   1 
ATOM   109  N  N     . PHE A 1 41  ? 164.602 130.592 134.676 1.00 33.86  ? 15  PHE A N     1 
ATOM   110  C  CA    . PHE A 1 41  ? 164.577 131.504 135.819 1.00 32.81  ? 15  PHE A CA    1 
ATOM   111  C  C     . PHE A 1 41  ? 164.433 132.959 135.372 1.00 34.43  ? 15  PHE A C     1 
ATOM   112  O  O     . PHE A 1 41  ? 163.622 133.719 135.926 1.00 36.37  ? 15  PHE A O     1 
ATOM   113  C  CB    . PHE A 1 41  ? 165.846 131.289 136.647 1.00 35.92  ? 15  PHE A CB    1 
ATOM   114  C  CG    . PHE A 1 41  ? 165.911 132.107 137.900 1.00 38.76  ? 15  PHE A CG    1 
ATOM   115  C  CD1   . PHE A 1 41  ? 165.061 131.845 138.963 1.00 38.26  ? 15  PHE A CD1   1 
ATOM   116  C  CD2   . PHE A 1 41  ? 166.861 133.106 138.036 1.00 38.57  ? 15  PHE A CD2   1 
ATOM   117  C  CE1   . PHE A 1 41  ? 165.131 132.593 140.124 1.00 35.18  ? 15  PHE A CE1   1 
ATOM   118  C  CE2   . PHE A 1 41  ? 166.940 133.855 139.195 1.00 39.03  ? 15  PHE A CE2   1 
ATOM   119  C  CZ    . PHE A 1 41  ? 166.074 133.598 140.239 1.00 37.10  ? 15  PHE A CZ    1 
ATOM   120  N  N     . TYR A 1 42  ? 165.192 133.351 134.342 1.00 31.11  ? 16  TYR A N     1 
ATOM   121  C  CA    . TYR A 1 42  ? 165.072 134.696 133.783 1.00 32.28  ? 16  TYR A CA    1 
ATOM   122  C  C     . TYR A 1 42  ? 163.711 134.906 133.131 1.00 25.63  ? 16  TYR A C     1 
ATOM   123  O  O     . TYR A 1 42  ? 163.140 136.001 133.211 1.00 38.47  ? 16  TYR A O     1 
ATOM   124  C  CB    . TYR A 1 42  ? 166.193 134.948 132.772 1.00 28.18  ? 16  TYR A CB    1 
ATOM   125  C  CG    . TYR A 1 42  ? 165.986 136.195 131.941 1.00 33.63  ? 16  TYR A CG    1 
ATOM   126  C  CD1   . TYR A 1 42  ? 166.108 137.457 132.510 1.00 33.90  ? 16  TYR A CD1   1 
ATOM   127  C  CD2   . TYR A 1 42  ? 165.656 136.112 130.592 1.00 36.74  ? 16  TYR A CD2   1 
ATOM   128  C  CE1   . TYR A 1 42  ? 165.913 138.600 131.761 1.00 34.09  ? 16  TYR A CE1   1 
ATOM   129  C  CE2   . TYR A 1 42  ? 165.456 137.253 129.836 1.00 35.60  ? 16  TYR A CE2   1 
ATOM   130  C  CZ    . TYR A 1 42  ? 165.588 138.492 130.427 1.00 38.37  ? 16  TYR A CZ    1 
ATOM   131  O  OH    . TYR A 1 42  ? 165.394 139.630 129.682 1.00 43.83  ? 16  TYR A OH    1 
ATOM   132  N  N     . LEU A 1 43  ? 163.185 133.865 132.477 1.00 26.64  ? 17  LEU A N     1 
ATOM   133  C  CA    . LEU A 1 43  ? 161.858 133.934 131.873 1.00 26.79  ? 17  LEU A CA    1 
ATOM   134  C  C     . LEU A 1 43  ? 160.777 134.138 132.927 1.00 25.88  ? 17  LEU A C     1 
ATOM   135  O  O     . LEU A 1 43  ? 159.861 134.945 132.731 1.00 35.37  ? 17  LEU A O     1 
ATOM   136  C  CB    . LEU A 1 43  ? 161.590 132.663 131.066 1.00 27.25  ? 17  LEU A CB    1 
ATOM   137  C  CG    . LEU A 1 43  ? 160.243 132.520 130.357 1.00 24.39  ? 17  LEU A CG    1 
ATOM   138  C  CD1   . LEU A 1 43  ? 159.990 133.686 129.425 1.00 24.74  ? 17  LEU A CD1   1 
ATOM   139  C  CD2   . LEU A 1 43  ? 160.186 131.211 129.596 1.00 27.02  ? 17  LEU A CD2   1 
ATOM   140  N  N     . ILE A 1 44  ? 160.896 133.439 134.062 1.00 19.25  ? 18  ILE A N     1 
ATOM   141  C  CA    . ILE A 1 44  ? 159.953 133.595 135.170 1.00 24.39  ? 18  ILE A CA    1 
ATOM   142  C  C     . ILE A 1 44  ? 160.007 135.015 135.725 1.00 22.03  ? 18  ILE A C     1 
ATOM   143  O  O     . ILE A 1 44  ? 158.966 135.653 135.934 1.00 32.38  ? 18  ILE A O     1 
ATOM   144  C  CB    . ILE A 1 44  ? 160.235 132.542 136.262 1.00 33.34  ? 18  ILE A CB    1 
ATOM   145  C  CG1   . ILE A 1 44  ? 159.705 131.172 135.841 1.00 31.40  ? 18  ILE A CG1   1 
ATOM   146  C  CG2   . ILE A 1 44  ? 159.618 132.932 137.600 1.00 22.64  ? 18  ILE A CG2   1 
ATOM   147  C  CD1   . ILE A 1 44  ? 160.376 130.017 136.553 1.00 22.91  ? 18  ILE A CD1   1 
ATOM   148  N  N     . GLN A 1 45  ? 161.223 135.546 135.918 1.00 29.14  ? 19  GLN A N     1 
ATOM   149  C  CA    . GLN A 1 45  ? 161.375 136.895 136.469 1.00 31.94  ? 19  GLN A CA    1 
ATOM   150  C  C     . GLN A 1 45  ? 160.821 137.963 135.526 1.00 30.86  ? 19  GLN A C     1 
ATOM   151  O  O     . GLN A 1 45  ? 160.114 138.885 135.958 1.00 34.84  ? 19  GLN A O     1 
ATOM   152  C  CB    . GLN A 1 45  ? 162.846 137.177 136.773 1.00 32.26  ? 19  GLN A CB    1 
ATOM   153  C  CG    . GLN A 1 45  ? 163.398 136.430 137.964 1.00 30.81  ? 19  GLN A CG    1 
ATOM   154  C  CD    . GLN A 1 45  ? 164.910 136.396 137.959 1.00 44.19  ? 19  GLN A CD    1 
ATOM   155  O  OE1   . GLN A 1 45  ? 165.526 135.831 137.057 1.00 44.36  ? 19  GLN A OE1   1 
ATOM   156  N  NE2   . GLN A 1 45  ? 165.519 136.999 138.973 1.00 40.58  ? 19  GLN A NE2   1 
ATOM   157  N  N     . ARG A 1 46  ? 161.111 137.840 134.228 1.00 25.44  ? 20  ARG A N     1 
ATOM   158  C  CA    . ARG A 1 46  ? 160.666 138.848 133.270 1.00 24.65  ? 20  ARG A CA    1 
ATOM   159  C  C     . ARG A 1 46  ? 159.158 138.786 133.046 1.00 22.49  ? 20  ARG A C     1 
ATOM   160  O  O     . ARG A 1 46  ? 158.502 139.830 132.927 1.00 32.55  ? 20  ARG A O     1 
ATOM   161  C  CB    . ARG A 1 46  ? 161.422 138.681 131.952 1.00 25.01  ? 20  ARG A CB    1 
ATOM   162  C  CG    . ARG A 1 46  ? 161.585 139.968 131.167 1.00 30.94  ? 20  ARG A CG    1 
ATOM   163  C  CD    . ARG A 1 46  ? 162.266 141.052 131.978 1.00 29.78  ? 20  ARG A CD    1 
ATOM   164  N  NE    . ARG A 1 46  ? 162.406 142.279 131.205 1.00 32.08  ? 20  ARG A NE    1 
ATOM   165  C  CZ    . ARG A 1 46  ? 161.546 143.288 131.243 1.00 34.11  ? 20  ARG A CZ    1 
ATOM   166  N  NH1   . ARG A 1 46  ? 160.476 143.256 132.019 1.00 36.88  ? 20  ARG A NH1   1 
ATOM   167  N  NH2   . ARG A 1 46  ? 161.765 144.354 130.479 1.00 31.35  ? 20  ARG A NH2   1 
ATOM   168  N  N     . LEU A 1 47  ? 158.584 137.578 133.010 1.00 19.23  ? 21  LEU A N     1 
ATOM   169  C  CA    . LEU A 1 47  ? 157.136 137.459 132.874 1.00 23.02  ? 21  LEU A CA    1 
ATOM   170  C  C     . LEU A 1 47  ? 156.416 137.941 134.131 1.00 22.89  ? 21  LEU A C     1 
ATOM   171  O  O     . LEU A 1 47  ? 155.316 138.497 134.042 1.00 29.07  ? 21  LEU A O     1 
ATOM   172  C  CB    . LEU A 1 47  ? 156.752 136.016 132.544 1.00 26.07  ? 21  LEU A CB    1 
ATOM   173  C  CG    . LEU A 1 47  ? 157.040 135.483 131.133 1.00 27.39  ? 21  LEU A CG    1 
ATOM   174  C  CD1   . LEU A 1 47  ? 156.168 134.275 130.821 1.00 22.43  ? 21  LEU A CD1   1 
ATOM   175  C  CD2   . LEU A 1 47  ? 156.886 136.552 130.063 1.00 25.74  ? 21  LEU A CD2   1 
ATOM   176  N  N     . ALA A 1 48  ? 157.029 137.757 135.308 1.00 21.70  ? 22  ALA A N     1 
ATOM   177  C  CA    . ALA A 1 48  ? 156.452 138.290 136.539 1.00 21.14  ? 22  ALA A CA    1 
ATOM   178  C  C     . ALA A 1 48  ? 156.472 139.814 136.550 1.00 21.41  ? 22  ALA A C     1 
ATOM   179  O  O     . ALA A 1 48  ? 155.509 140.451 136.998 1.00 37.58  ? 22  ALA A O     1 
ATOM   180  C  CB    . ALA A 1 48  ? 157.202 137.737 137.748 1.00 23.22  ? 22  ALA A CB    1 
ATOM   181  N  N     . GLN A 1 49  ? 157.562 140.414 136.055 1.00 25.94  ? 23  GLN A N     1 
ATOM   182  C  CA    . GLN A 1 49  ? 157.629 141.869 135.930 1.00 22.46  ? 23  GLN A CA    1 
ATOM   183  C  C     . GLN A 1 49  ? 156.581 142.395 134.955 1.00 28.13  ? 23  GLN A C     1 
ATOM   184  O  O     . GLN A 1 49  ? 155.936 143.422 135.214 1.00 34.98  ? 23  GLN A O     1 
ATOM   185  C  CB    . GLN A 1 49  ? 159.028 142.291 135.483 1.00 25.63  ? 23  GLN A CB    1 
ATOM   186  C  CG    . GLN A 1 49  ? 160.080 142.230 136.570 1.00 28.40  ? 23  GLN A CG    1 
ATOM   187  C  CD    . GLN A 1 49  ? 161.486 142.294 136.016 1.00 33.86  ? 23  GLN A CD    1 
ATOM   188  O  OE1   . GLN A 1 49  ? 162.165 141.276 135.887 1.00 37.82  ? 23  GLN A OE1   1 
ATOM   189  N  NE2   . GLN A 1 49  ? 161.931 143.496 135.678 1.00 33.82  ? 23  GLN A NE2   1 
ATOM   190  N  N     . PHE A 1 50  ? 156.385 141.687 133.837 1.00 26.21  ? 24  PHE A N     1 
ATOM   191  C  CA    . PHE A 1 50  ? 155.354 142.070 132.877 1.00 16.02  ? 24  PHE A CA    1 
ATOM   192  C  C     . PHE A 1 50  ? 153.956 141.941 133.469 1.00 23.75  ? 24  PHE A C     1 
ATOM   193  O  O     . PHE A 1 50  ? 153.084 142.767 133.189 1.00 33.55  ? 24  PHE A O     1 
ATOM   194  C  CB    . PHE A 1 50  ? 155.476 141.228 131.610 1.00 23.72  ? 24  PHE A CB    1 
ATOM   195  C  CG    . PHE A 1 50  ? 156.475 141.759 130.631 1.00 28.20  ? 24  PHE A CG    1 
ATOM   196  C  CD1   . PHE A 1 50  ? 156.481 143.103 130.295 1.00 27.94  ? 24  PHE A CD1   1 
ATOM   197  C  CD2   . PHE A 1 50  ? 157.414 140.922 130.055 1.00 27.63  ? 24  PHE A CD2   1 
ATOM   198  C  CE1   . PHE A 1 50  ? 157.403 143.601 129.396 1.00 24.31  ? 24  PHE A CE1   1 
ATOM   199  C  CE2   . PHE A 1 50  ? 158.339 141.414 129.157 1.00 29.98  ? 24  PHE A CE2   1 
ATOM   200  C  CZ    . PHE A 1 50  ? 158.332 142.755 128.827 1.00 24.82  ? 24  PHE A CZ    1 
ATOM   201  N  N     . GLN A 1 51  ? 153.725 140.916 134.295 1.00 22.27  ? 25  GLN A N     1 
ATOM   202  C  CA    . GLN A 1 51  ? 152.424 140.758 134.943 1.00 21.13  ? 25  GLN A CA    1 
ATOM   203  C  C     . GLN A 1 51  ? 152.160 141.875 135.949 1.00 24.47  ? 25  GLN A C     1 
ATOM   204  O  O     . GLN A 1 51  ? 151.028 142.372 136.052 1.00 34.28  ? 25  GLN A O     1 
ATOM   205  C  CB    . GLN A 1 51  ? 152.341 139.386 135.616 1.00 25.82  ? 25  GLN A CB    1 
ATOM   206  C  CG    . GLN A 1 51  ? 151.017 139.092 136.306 1.00 29.01  ? 25  GLN A CG    1 
ATOM   207  C  CD    . GLN A 1 51  ? 149.876 138.865 135.331 1.00 33.44  ? 25  GLN A CD    1 
ATOM   208  O  OE1   . GLN A 1 51  ? 150.091 138.551 134.161 1.00 39.29  ? 25  GLN A OE1   1 
ATOM   209  N  NE2   . GLN A 1 51  ? 148.651 139.021 135.814 1.00 33.05  ? 25  GLN A NE2   1 
ATOM   210  N  N     . VAL A 1 52  ? 153.201 142.285 136.686 1.00 29.28  ? 26  VAL A N     1 
ATOM   211  C  CA    . VAL A 1 52  ? 153.098 143.423 137.603 1.00 26.29  ? 26  VAL A CA    1 
ATOM   212  C  C     . VAL A 1 52  ? 152.743 144.697 136.841 1.00 29.12  ? 26  VAL A C     1 
ATOM   213  O  O     . VAL A 1 52  ? 151.873 145.469 137.265 1.00 38.82  ? 26  VAL A O     1 
ATOM   214  C  CB    . VAL A 1 52  ? 154.409 143.580 138.402 1.00 27.81  ? 26  VAL A CB    1 
ATOM   215  C  CG1   . VAL A 1 52  ? 154.479 144.929 139.105 1.00 30.59  ? 26  VAL A CG1   1 
ATOM   216  C  CG2   . VAL A 1 52  ? 154.538 142.479 139.417 1.00 22.89  ? 26  VAL A CG2   1 
ATOM   217  N  N     . LYS A 1 53  ? 153.378 144.914 135.686 1.00 35.49  ? 27  LYS A N     1 
ATOM   218  C  CA    . LYS A 1 53  ? 153.046 146.084 134.873 1.00 25.33  ? 27  LYS A CA    1 
ATOM   219  C  C     . LYS A 1 53  ? 151.649 145.982 134.259 1.00 31.12  ? 27  LYS A C     1 
ATOM   220  O  O     . LYS A 1 53  ? 150.997 147.006 134.026 1.00 35.66  ? 27  LYS A O     1 
ATOM   221  C  CB    . LYS A 1 53  ? 154.096 146.282 133.781 1.00 30.02  ? 27  LYS A CB    1 
ATOM   222  C  CG    . LYS A 1 53  ? 155.492 146.544 134.313 1.00 37.05  ? 27  LYS A CG    1 
ATOM   223  C  CD    . LYS A 1 53  ? 156.514 146.569 133.194 1.00 37.78  ? 27  LYS A CD    1 
ATOM   224  C  CE    . LYS A 1 53  ? 156.171 147.624 132.164 1.00 36.98  ? 27  LYS A CE    1 
ATOM   225  N  NZ    . LYS A 1 53  ? 156.125 148.991 132.752 1.00 40.46  ? 27  LYS A NZ    1 
ATOM   226  N  N     . ILE A 1 54  ? 151.181 144.763 133.978 1.00 39.46  ? 28  ILE A N     1 
ATOM   227  C  CA    . ILE A 1 54  ? 149.868 144.586 133.358 1.00 27.93  ? 28  ILE A CA    1 
ATOM   228  C  C     . ILE A 1 54  ? 148.752 144.903 134.351 1.00 26.46  ? 28  ILE A C     1 
ATOM   229  O  O     . ILE A 1 54  ? 147.815 145.645 134.033 1.00 39.53  ? 28  ILE A O     1 
ATOM   230  C  CB    . ILE A 1 54  ? 149.739 143.164 132.772 1.00 28.42  ? 28  ILE A CB    1 
ATOM   231  C  CG1   . ILE A 1 54  ? 150.381 143.098 131.387 1.00 25.46  ? 28  ILE A CG1   1 
ATOM   232  C  CG2   . ILE A 1 54  ? 148.285 142.727 132.649 1.00 24.08  ? 28  ILE A CG2   1 
ATOM   233  C  CD1   . ILE A 1 54  ? 150.778 141.701 130.964 1.00 25.66  ? 28  ILE A CD1   1 
ATOM   234  N  N     . ILE A 1 55  ? 148.844 144.377 135.580 1.00 29.07  ? 29  ILE A N     1 
ATOM   235  C  CA    . ILE A 1 55  ? 147.750 144.574 136.535 1.00 30.91  ? 29  ILE A CA    1 
ATOM   236  C  C     . ILE A 1 55  ? 147.718 145.961 137.161 1.00 32.53  ? 29  ILE A C     1 
ATOM   237  O  O     . ILE A 1 55  ? 146.740 146.293 137.843 1.00 34.39  ? 29  ILE A O     1 
ATOM   238  C  CB    . ILE A 1 55  ? 147.765 143.521 137.664 1.00 28.72  ? 29  ILE A CB    1 
ATOM   239  C  CG1   . ILE A 1 55  ? 148.811 143.866 138.727 1.00 31.56  ? 29  ILE A CG1   1 
ATOM   240  C  CG2   . ILE A 1 55  ? 147.934 142.121 137.104 1.00 33.71  ? 29  ILE A CG2   1 
ATOM   241  C  CD1   . ILE A 1 55  ? 148.496 143.301 140.088 1.00 34.92  ? 29  ILE A CD1   1 
ATOM   242  N  N     . ASN A 1 56  ? 148.742 146.792 136.948 1.00 32.88  ? 30  ASN A N     1 
ATOM   243  C  CA    . ASN A 1 56  ? 148.781 148.130 137.531 1.00 31.86  ? 30  ASN A CA    1 
ATOM   244  C  C     . ASN A 1 56  ? 148.859 149.220 136.467 1.00 37.30  ? 30  ASN A C     1 
ATOM   245  O  O     . ASN A 1 56  ? 149.370 150.309 136.746 1.00 36.19  ? 30  ASN A O     1 
ATOM   246  C  CB    . ASN A 1 56  ? 149.964 148.267 138.494 1.00 32.85  ? 30  ASN A CB    1 
ATOM   247  C  CG    . ASN A 1 56  ? 149.732 147.560 139.812 1.00 36.78  ? 30  ASN A CG    1 
ATOM   248  O  OD1   . ASN A 1 56  ? 148.831 147.913 140.569 1.00 40.27  ? 30  ASN A OD1   1 
ATOM   249  N  ND2   . ASN A 1 56  ? 150.551 146.554 140.093 1.00 32.50  ? 30  ASN A ND2   1 
ATOM   250  N  N     . HIS A 1 57  ? 148.366 148.950 135.254 1.00 44.81  ? 31  HIS A N     1 
ATOM   251  C  CA    . HIS A 1 57  ? 148.652 149.827 134.121 1.00 41.25  ? 31  HIS A CA    1 
ATOM   252  C  C     . HIS A 1 57  ? 147.851 151.124 134.176 1.00 45.12  ? 31  HIS A C     1 
ATOM   253  O  O     . HIS A 1 57  ? 148.391 152.201 133.897 1.00 47.12  ? 31  HIS A O     1 
ATOM   254  C  CB    . HIS A 1 57  ? 148.383 149.094 132.809 1.00 36.69  ? 31  HIS A CB    1 
ATOM   255  C  CG    . HIS A 1 57  ? 148.471 149.974 131.602 1.00 42.76  ? 31  HIS A CG    1 
ATOM   256  N  ND1   . HIS A 1 57  ? 149.610 150.678 131.278 1.00 45.34  ? 31  HIS A ND1   1 
ATOM   257  C  CD2   . HIS A 1 57  ? 147.561 150.271 130.646 1.00 38.20  ? 31  HIS A CD2   1 
ATOM   258  C  CE1   . HIS A 1 57  ? 149.399 151.368 130.172 1.00 39.37  ? 31  HIS A CE1   1 
ATOM   259  N  NE2   . HIS A 1 57  ? 148.163 151.137 129.768 1.00 43.61  ? 31  HIS A NE2   1 
ATOM   260  N  N     . SER A 1 58  ? 146.567 151.049 134.526 1.00 40.00  ? 32  SER A N     1 
ATOM   261  C  CA    . SER A 1 58  ? 145.716 152.231 134.480 1.00 34.43  ? 32  SER A CA    1 
ATOM   262  C  C     . SER A 1 58  ? 145.768 153.061 135.755 1.00 41.32  ? 32  SER A C     1 
ATOM   263  O  O     . SER A 1 58  ? 145.122 154.112 135.813 1.00 46.20  ? 32  SER A O     1 
ATOM   264  C  CB    . SER A 1 58  ? 144.269 151.828 134.191 1.00 40.88  ? 32  SER A CB    1 
ATOM   265  O  OG    . SER A 1 58  ? 144.159 151.207 132.923 1.00 46.89  ? 32  SER A OG    1 
ATOM   266  N  N     . ASN A 1 59  ? 146.508 152.621 136.768 1.00 40.19  ? 33  ASN A N     1 
ATOM   267  C  CA    . ASN A 1 59  ? 146.620 153.382 138.004 1.00 29.60  ? 33  ASN A CA    1 
ATOM   268  C  C     . ASN A 1 59  ? 147.502 154.607 137.797 1.00 37.58  ? 33  ASN A C     1 
ATOM   269  O  O     . ASN A 1 59  ? 148.492 154.555 137.060 1.00 39.96  ? 33  ASN A O     1 
ATOM   270  C  CB    . ASN A 1 59  ? 147.189 152.506 139.117 1.00 34.38  ? 33  ASN A CB    1 
ATOM   271  C  CG    . ASN A 1 59  ? 146.269 151.364 139.487 1.00 36.71  ? 33  ASN A CG    1 
ATOM   272  O  OD1   . ASN A 1 59  ? 145.059 151.440 139.289 1.00 46.48  ? 33  ASN A OD1   1 
ATOM   273  N  ND2   . ASN A 1 59  ? 146.837 150.300 140.037 1.00 35.68  ? 33  ASN A ND2   1 
ATOM   274  N  N     . TYR A 1 60  ? 147.129 155.717 138.439 1.00 47.30  ? 34  TYR A N     1 
ATOM   275  C  CA    . TYR A 1 60  ? 147.967 156.911 138.409 1.00 37.78  ? 34  TYR A CA    1 
ATOM   276  C  C     . TYR A 1 60  ? 149.258 156.694 139.187 1.00 45.51  ? 34  TYR A C     1 
ATOM   277  O  O     . TYR A 1 60  ? 150.325 157.167 138.780 1.00 50.55  ? 34  TYR A O     1 
ATOM   278  C  CB    . TYR A 1 60  ? 147.202 158.109 138.971 1.00 43.02  ? 34  TYR A CB    1 
ATOM   279  C  CG    . TYR A 1 60  ? 146.337 158.821 137.956 1.00 47.99  ? 34  TYR A CG    1 
ATOM   280  C  CD1   . TYR A 1 60  ? 144.993 158.497 137.810 1.00 43.48  ? 34  TYR A CD1   1 
ATOM   281  C  CD2   . TYR A 1 60  ? 146.864 159.819 137.145 1.00 48.05  ? 34  TYR A CD2   1 
ATOM   282  C  CE1   . TYR A 1 60  ? 144.199 159.146 136.883 1.00 43.40  ? 34  TYR A CE1   1 
ATOM   283  C  CE2   . TYR A 1 60  ? 146.080 160.473 136.215 1.00 47.38  ? 34  TYR A CE2   1 
ATOM   284  C  CZ    . TYR A 1 60  ? 144.749 160.133 136.089 1.00 51.49  ? 34  TYR A CZ    1 
ATOM   285  O  OH    . TYR A 1 60  ? 143.964 160.782 135.165 1.00 49.98  ? 34  TYR A OH    1 
ATOM   286  N  N     . LEU A 1 61  ? 149.183 155.974 140.304 1.00 47.60  ? 35  LEU A N     1 
ATOM   287  C  CA    . LEU A 1 61  ? 150.353 155.695 141.124 1.00 41.16  ? 35  LEU A CA    1 
ATOM   288  C  C     . LEU A 1 61  ? 151.183 154.531 140.600 1.00 39.88  ? 35  LEU A C     1 
ATOM   289  O  O     . LEU A 1 61  ? 152.286 154.304 141.108 1.00 48.90  ? 35  LEU A O     1 
ATOM   290  C  CB    . LEU A 1 61  ? 149.925 155.429 142.570 1.00 41.64  ? 35  LEU A CB    1 
ATOM   291  C  CG    . LEU A 1 61  ? 149.079 156.533 143.213 1.00 40.76  ? 35  LEU A CG    1 
ATOM   292  C  CD1   . LEU A 1 61  ? 148.646 156.149 144.617 1.00 43.99  ? 35  LEU A CD1   1 
ATOM   293  C  CD2   . LEU A 1 61  ? 149.832 157.853 143.226 1.00 39.59  ? 35  LEU A CD2   1 
ATOM   294  N  N     . GLY A 1 62  ? 150.690 153.796 139.607 1.00 36.69  ? 36  GLY A N     1 
ATOM   295  C  CA    . GLY A 1 62  ? 151.501 152.781 138.958 1.00 33.28  ? 36  GLY A CA    1 
ATOM   296  C  C     . GLY A 1 62  ? 151.624 151.518 139.784 1.00 36.74  ? 36  GLY A C     1 
ATOM   297  O  O     . GLY A 1 62  ? 150.654 151.026 140.370 1.00 42.16  ? 36  GLY A O     1 
ATOM   298  N  N     . VAL A 1 63  ? 152.846 150.981 139.834 1.00 44.29  ? 37  VAL A N     1 
ATOM   299  C  CA    . VAL A 1 63  ? 153.112 149.748 140.568 1.00 36.35  ? 37  VAL A CA    1 
ATOM   300  C  C     . VAL A 1 63  ? 153.351 149.982 142.050 1.00 40.64  ? 37  VAL A C     1 
ATOM   301  O  O     . VAL A 1 63  ? 153.708 149.041 142.766 1.00 44.14  ? 37  VAL A O     1 
ATOM   302  C  CB    . VAL A 1 63  ? 154.320 149.004 139.966 1.00 34.58  ? 37  VAL A CB    1 
ATOM   303  C  CG1   . VAL A 1 63  ? 154.050 148.647 138.514 1.00 34.99  ? 37  VAL A CG1   1 
ATOM   304  C  CG2   . VAL A 1 63  ? 155.579 149.846 140.090 1.00 33.87  ? 37  VAL A CG2   1 
ATOM   305  N  N     . ALA A 1 64  ? 153.163 151.213 142.531 1.00 41.90  ? 38  ALA A N     1 
ATOM   306  C  CA    . ALA A 1 64  ? 153.269 151.488 143.957 1.00 36.41  ? 38  ALA A CA    1 
ATOM   307  C  C     . ALA A 1 64  ? 152.076 150.958 144.740 1.00 41.38  ? 38  ALA A C     1 
ATOM   308  O  O     . ALA A 1 64  ? 152.148 150.886 145.969 1.00 44.48  ? 38  ALA A O     1 
ATOM   309  C  CB    . ALA A 1 64  ? 153.418 152.991 144.194 1.00 32.31  ? 38  ALA A CB    1 
ATOM   310  N  N     . TRP A 1 65  ? 150.986 150.584 144.062 1.00 39.02  ? 39  TRP A N     1 
ATOM   311  C  CA    . TRP A 1 65  ? 149.808 150.085 144.763 1.00 34.62  ? 39  TRP A CA    1 
ATOM   312  C  C     . TRP A 1 65  ? 150.048 148.717 145.385 1.00 39.09  ? 39  TRP A C     1 
ATOM   313  O  O     . TRP A 1 65  ? 149.430 148.395 146.408 1.00 45.85  ? 39  TRP A O     1 
ATOM   314  C  CB    . TRP A 1 65  ? 148.610 150.046 143.819 1.00 41.53  ? 39  TRP A CB    1 
ATOM   315  C  CG    . TRP A 1 65  ? 147.795 151.283 143.926 1.00 40.61  ? 39  TRP A CG    1 
ATOM   316  C  CD1   . TRP A 1 65  ? 147.703 152.286 143.010 1.00 33.47  ? 39  TRP A CD1   1 
ATOM   317  C  CD2   . TRP A 1 65  ? 146.981 151.673 145.035 1.00 43.00  ? 39  TRP A CD2   1 
ATOM   318  N  NE1   . TRP A 1 65  ? 146.870 153.271 143.472 1.00 39.41  ? 39  TRP A NE1   1 
ATOM   319  C  CE2   . TRP A 1 65  ? 146.412 152.919 144.715 1.00 42.40  ? 39  TRP A CE2   1 
ATOM   320  C  CE3   . TRP A 1 65  ? 146.673 151.087 146.268 1.00 41.32  ? 39  TRP A CE3   1 
ATOM   321  C  CZ2   . TRP A 1 65  ? 145.551 153.588 145.579 1.00 39.92  ? 39  TRP A CZ2   1 
ATOM   322  C  CZ3   . TRP A 1 65  ? 145.815 151.750 147.119 1.00 42.31  ? 39  TRP A CZ3   1 
ATOM   323  C  CH2   . TRP A 1 65  ? 145.267 152.988 146.773 1.00 38.87  ? 39  TRP A CH2   1 
ATOM   324  N  N     . GLU A 1 66  ? 150.988 147.942 144.824 1.00 41.80  ? 40  GLU A N     1 
ATOM   325  C  CA    . GLU A 1 66  ? 151.407 146.671 145.412 1.00 45.25  ? 40  GLU A CA    1 
ATOM   326  C  C     . GLU A 1 66  ? 152.046 146.858 146.783 1.00 42.40  ? 40  GLU A C     1 
ATOM   327  O  O     . GLU A 1 66  ? 152.106 145.913 147.577 1.00 47.07  ? 40  GLU A O     1 
ATOM   328  C  CB    . GLU A 1 66  ? 152.390 145.965 144.475 1.00 42.88  ? 40  GLU A CB    1 
ATOM   329  C  CG    . GLU A 1 66  ? 151.771 145.420 143.200 1.00 44.72  ? 40  GLU A CG    1 
ATOM   330  C  CD    . GLU A 1 66  ? 152.148 143.973 142.938 1.00 55.44  ? 40  GLU A CD    1 
ATOM   331  O  OE1   . GLU A 1 66  ? 151.351 143.258 142.295 1.00 54.09  ? 40  GLU A OE1   1 
ATOM   332  O  OE2   . GLU A 1 66  ? 153.239 143.550 143.375 1.00 48.67  ? 40  GLU A OE2   1 
ATOM   333  N  N     . LEU A 1 67  ? 152.545 148.058 147.064 1.00 37.31  ? 41  LEU A N     1 
ATOM   334  C  CA    . LEU A 1 67  ? 153.046 148.474 148.363 1.00 32.84  ? 41  LEU A CA    1 
ATOM   335  C  C     . LEU A 1 67  ? 151.993 149.192 149.198 1.00 37.76  ? 41  LEU A C     1 
ATOM   336  O  O     . LEU A 1 67  ? 151.923 148.982 150.411 1.00 41.65  ? 41  LEU A O     1 
ATOM   337  C  CB    . LEU A 1 67  ? 154.250 149.393 148.152 1.00 38.62  ? 41  LEU A CB    1 
ATOM   338  C  CG    . LEU A 1 67  ? 155.543 149.196 148.928 1.00 44.22  ? 41  LEU A CG    1 
ATOM   339  C  CD1   . LEU A 1 67  ? 156.133 147.832 148.635 1.00 42.98  ? 41  LEU A CD1   1 
ATOM   340  C  CD2   . LEU A 1 67  ? 156.505 150.283 148.493 1.00 46.33  ? 41  LEU A CD2   1 
ATOM   341  N  N     . ILE A 1 68  ? 151.167 150.028 148.561 1.00 39.47  ? 42  ILE A N     1 
ATOM   342  C  CA    . ILE A 1 68  ? 150.254 150.906 149.294 1.00 38.24  ? 42  ILE A CA    1 
ATOM   343  C  C     . ILE A 1 68  ? 149.075 150.122 149.867 1.00 39.13  ? 42  ILE A C     1 
ATOM   344  O  O     . ILE A 1 68  ? 148.698 150.315 151.031 1.00 46.41  ? 42  ILE A O     1 
ATOM   345  C  CB    . ILE A 1 68  ? 149.792 152.066 148.389 1.00 36.18  ? 42  ILE A CB    1 
ATOM   346  C  CG1   . ILE A 1 68  ? 150.953 153.020 148.112 1.00 38.41  ? 42  ILE A CG1   1 
ATOM   347  C  CG2   . ILE A 1 68  ? 148.669 152.865 149.031 1.00 37.06  ? 42  ILE A CG2   1 
ATOM   348  C  CD1   . ILE A 1 68  ? 150.687 153.993 146.989 1.00 39.58  ? 42  ILE A CD1   1 
ATOM   349  N  N     . ASN A 1 69  ? 148.474 149.233 149.067 1.00 39.95  ? 43  ASN A N     1 
ATOM   350  C  CA    . ASN A 1 69  ? 147.297 148.485 149.518 1.00 38.36  ? 43  ASN A CA    1 
ATOM   351  C  C     . ASN A 1 69  ? 147.561 147.541 150.699 1.00 37.65  ? 43  ASN A C     1 
ATOM   352  O  O     . ASN A 1 69  ? 146.728 147.523 151.629 1.00 44.42  ? 43  ASN A O     1 
ATOM   353  C  CB    . ASN A 1 69  ? 146.665 147.769 148.313 1.00 37.86  ? 43  ASN A CB    1 
ATOM   354  C  CG    . ASN A 1 69  ? 145.545 146.828 148.707 1.00 46.27  ? 43  ASN A CG    1 
ATOM   355  O  OD1   . ASN A 1 69  ? 145.697 145.609 148.647 1.00 42.91  ? 43  ASN A OD1   1 
ATOM   356  N  ND2   . ASN A 1 69  ? 144.412 147.389 149.111 1.00 47.93  ? 43  ASN A ND2   1 
ATOM   357  N  N     . PRO A 1 70  ? 148.656 146.747 150.749 1.00 40.81  ? 44  PRO A N     1 
ATOM   358  C  CA    . PRO A 1 70  ? 148.952 146.032 152.003 1.00 37.16  ? 44  PRO A CA    1 
ATOM   359  C  C     . PRO A 1 70  ? 149.199 146.932 153.200 1.00 35.79  ? 44  PRO A C     1 
ATOM   360  O  O     . PRO A 1 70  ? 148.833 146.541 154.307 1.00 45.14  ? 44  PRO A O     1 
ATOM   361  C  CB    . PRO A 1 70  ? 150.204 145.218 151.653 1.00 32.94  ? 44  PRO A CB    1 
ATOM   362  C  CG    . PRO A 1 70  ? 150.077 144.974 150.229 1.00 34.85  ? 44  PRO A CG    1 
ATOM   363  C  CD    . PRO A 1 70  ? 149.568 146.263 149.687 1.00 37.20  ? 44  PRO A CD    1 
ATOM   364  N  N     . VAL A 1 71  ? 149.775 148.124 153.014 1.00 34.72  ? 45  VAL A N     1 
ATOM   365  C  CA    . VAL A 1 71  ? 150.026 149.032 154.136 1.00 36.53  ? 45  VAL A CA    1 
ATOM   366  C  C     . VAL A 1 71  ? 148.710 149.547 154.719 1.00 34.08  ? 45  VAL A C     1 
ATOM   367  O  O     . VAL A 1 71  ? 148.538 149.616 155.945 1.00 39.84  ? 45  VAL A O     1 
ATOM   368  C  CB    . VAL A 1 71  ? 150.958 150.175 153.682 1.00 37.95  ? 45  VAL A CB    1 
ATOM   369  C  CG1   . VAL A 1 71  ? 150.842 151.409 154.576 1.00 33.93  ? 45  VAL A CG1   1 
ATOM   370  C  CG2   . VAL A 1 71  ? 152.397 149.691 153.645 1.00 35.32  ? 45  VAL A CG2   1 
ATOM   371  N  N     . MET A 1 72  ? 147.751 149.877 153.849 1.00 37.68  ? 46  MET A N     1 
ATOM   372  C  CA    . MET A 1 72  ? 146.423 150.287 154.299 1.00 33.26  ? 46  MET A CA    1 
ATOM   373  C  C     . MET A 1 72  ? 145.701 149.155 155.020 1.00 38.59  ? 46  MET A C     1 
ATOM   374  O  O     . MET A 1 72  ? 145.059 149.381 156.057 1.00 41.60  ? 46  MET A O     1 
ATOM   375  C  CB    . MET A 1 72  ? 145.600 150.768 153.108 1.00 35.44  ? 46  MET A CB    1 
ATOM   376  C  CG    . MET A 1 72  ? 145.538 152.271 152.952 1.00 38.38  ? 46  MET A CG    1 
ATOM   377  S  SD    . MET A 1 72  ? 145.443 152.719 151.215 1.00 56.93  ? 46  MET A SD    1 
ATOM   378  C  CE    . MET A 1 72  ? 143.938 151.869 150.764 1.00 45.73  ? 46  MET A CE    1 
ATOM   379  N  N     . GLN A 1 73  ? 145.818 147.927 154.499 1.00 37.81  ? 47  GLN A N     1 
ATOM   380  C  CA    . GLN A 1 73  ? 145.230 146.777 155.184 1.00 27.52  ? 47  GLN A CA    1 
ATOM   381  C  C     . GLN A 1 73  ? 145.902 146.520 156.532 1.00 26.10  ? 47  GLN A C     1 
ATOM   382  O  O     . GLN A 1 73  ? 145.241 146.113 157.493 1.00 35.52  ? 47  GLN A O     1 
ATOM   383  C  CB    . GLN A 1 73  ? 145.307 145.544 154.287 1.00 34.33  ? 47  GLN A CB    1 
ATOM   384  C  CG    . GLN A 1 73  ? 144.379 145.618 153.088 1.00 38.02  ? 47  GLN A CG    1 
ATOM   385  C  CD    . GLN A 1 73  ? 144.355 144.341 152.283 1.00 38.96  ? 47  GLN A CD    1 
ATOM   386  O  OE1   . GLN A 1 73  ? 144.659 144.339 151.093 1.00 43.98  ? 47  GLN A OE1   1 
ATOM   387  N  NE2   . GLN A 1 73  ? 143.993 143.241 152.930 1.00 41.76  ? 47  GLN A NE2   1 
ATOM   388  N  N     . ILE A 1 74  ? 147.211 146.781 156.622 1.00 29.42  ? 48  ILE A N     1 
ATOM   389  C  CA    . ILE A 1 74  ? 147.951 146.673 157.879 1.00 29.81  ? 48  ILE A CA    1 
ATOM   390  C  C     . ILE A 1 74  ? 147.426 147.675 158.900 1.00 27.40  ? 48  ILE A C     1 
ATOM   391  O  O     . ILE A 1 74  ? 147.254 147.347 160.082 1.00 31.69  ? 48  ILE A O     1 
ATOM   392  C  CB    . ILE A 1 74  ? 149.459 146.866 157.611 1.00 40.67  ? 48  ILE A CB    1 
ATOM   393  C  CG1   . ILE A 1 74  ? 150.079 145.579 157.088 1.00 32.42  ? 48  ILE A CG1   1 
ATOM   394  C  CG2   . ILE A 1 74  ? 150.214 147.329 158.850 1.00 36.66  ? 48  ILE A CG2   1 
ATOM   395  C  CD1   . ILE A 1 74  ? 151.394 145.775 156.372 1.00 35.81  ? 48  ILE A CD1   1 
ATOM   396  N  N     . MET A 1 75  ? 147.157 148.907 158.455 1.00 35.94  ? 49  MET A N     1 
ATOM   397  C  CA    . MET A 1 75  ? 146.588 149.924 159.341 1.00 34.74  ? 49  MET A CA    1 
ATOM   398  C  C     . MET A 1 75  ? 145.202 149.524 159.835 1.00 34.35  ? 49  MET A C     1 
ATOM   399  O  O     . MET A 1 75  ? 144.876 149.729 161.013 1.00 39.17  ? 49  MET A O     1 
ATOM   400  C  CB    . MET A 1 75  ? 146.532 151.277 158.631 1.00 34.54  ? 49  MET A CB    1 
ATOM   401  C  CG    . MET A 1 75  ? 147.890 151.849 158.270 1.00 38.04  ? 49  MET A CG    1 
ATOM   402  S  SD    . MET A 1 75  ? 147.840 152.951 156.844 1.00 64.83  ? 49  MET A SD    1 
ATOM   403  C  CE    . MET A 1 75  ? 146.449 153.997 157.263 1.00 42.98  ? 49  MET A CE    1 
ATOM   404  N  N     . VAL A 1 76  ? 144.389 148.926 158.956 1.00 34.77  ? 50  VAL A N     1 
ATOM   405  C  CA    . VAL A 1 76  ? 143.066 148.436 159.358 1.00 33.54  ? 50  VAL A CA    1 
ATOM   406  C  C     . VAL A 1 76  ? 143.193 147.323 160.398 1.00 33.38  ? 50  VAL A C     1 
ATOM   407  O  O     . VAL A 1 76  ? 142.506 147.329 161.431 1.00 37.14  ? 50  VAL A O     1 
ATOM   408  C  CB    . VAL A 1 76  ? 142.272 147.966 158.125 1.00 33.28  ? 50  VAL A CB    1 
ATOM   409  C  CG1   . VAL A 1 76  ? 140.955 147.324 158.537 1.00 31.01  ? 50  VAL A CG1   1 
ATOM   410  C  CG2   . VAL A 1 76  ? 142.017 149.123 157.192 1.00 33.17  ? 50  VAL A CG2   1 
ATOM   411  N  N     . TYR A 1 77  ? 144.100 146.371 160.155 1.00 30.42  ? 51  TYR A N     1 
ATOM   412  C  CA    . TYR A 1 77  ? 144.258 145.234 161.059 1.00 20.17  ? 51  TYR A CA    1 
ATOM   413  C  C     . TYR A 1 77  ? 144.852 145.655 162.399 1.00 23.44  ? 51  TYR A C     1 
ATOM   414  O  O     . TYR A 1 77  ? 144.552 145.046 163.430 1.00 33.01  ? 51  TYR A O     1 
ATOM   415  C  CB    . TYR A 1 77  ? 145.116 144.152 160.403 1.00 27.63  ? 51  TYR A CB    1 
ATOM   416  C  CG    . TYR A 1 77  ? 144.370 143.304 159.395 1.00 31.30  ? 51  TYR A CG    1 
ATOM   417  C  CD1   . TYR A 1 77  ? 143.136 142.749 159.704 1.00 30.17  ? 51  TYR A CD1   1 
ATOM   418  C  CD2   . TYR A 1 77  ? 144.900 143.058 158.134 1.00 28.80  ? 51  TYR A CD2   1 
ATOM   419  C  CE1   . TYR A 1 77  ? 142.451 141.975 158.788 1.00 25.99  ? 51  TYR A CE1   1 
ATOM   420  C  CE2   . TYR A 1 77  ? 144.221 142.289 157.209 1.00 34.50  ? 51  TYR A CE2   1 
ATOM   421  C  CZ    . TYR A 1 77  ? 142.998 141.750 157.543 1.00 34.91  ? 51  TYR A CZ    1 
ATOM   422  O  OH    . TYR A 1 77  ? 142.321 140.980 156.627 1.00 37.90  ? 51  TYR A OH    1 
ATOM   423  N  N     . TRP A 1 78  ? 145.684 146.699 162.412 1.00 29.39  ? 52  TRP A N     1 
ATOM   424  C  CA    . TRP A 1 78  ? 146.215 147.179 163.683 1.00 30.89  ? 52  TRP A CA    1 
ATOM   425  C  C     . TRP A 1 78  ? 145.170 147.986 164.444 1.00 34.71  ? 52  TRP A C     1 
ATOM   426  O  O     . TRP A 1 78  ? 145.143 147.959 165.680 1.00 36.71  ? 52  TRP A O     1 
ATOM   427  C  CB    . TRP A 1 78  ? 147.496 147.992 163.461 1.00 29.90  ? 52  TRP A CB    1 
ATOM   428  C  CG    . TRP A 1 78  ? 147.874 148.907 164.605 1.00 32.16  ? 52  TRP A CG    1 
ATOM   429  C  CD1   . TRP A 1 78  ? 148.729 148.618 165.626 1.00 29.52  ? 52  TRP A CD1   1 
ATOM   430  C  CD2   . TRP A 1 78  ? 147.475 150.273 164.795 1.00 40.37  ? 52  TRP A CD2   1 
ATOM   431  N  NE1   . TRP A 1 78  ? 148.848 149.695 166.466 1.00 32.63  ? 52  TRP A NE1   1 
ATOM   432  C  CE2   . TRP A 1 78  ? 148.090 150.725 165.978 1.00 43.14  ? 52  TRP A CE2   1 
ATOM   433  C  CE3   . TRP A 1 78  ? 146.630 151.143 164.100 1.00 39.96  ? 52  TRP A CE3   1 
ATOM   434  C  CZ2   . TRP A 1 78  ? 147.899 152.013 166.473 1.00 40.11  ? 52  TRP A CZ2   1 
ATOM   435  C  CZ3   . TRP A 1 78  ? 146.442 152.420 164.593 1.00 40.65  ? 52  TRP A CZ3   1 
ATOM   436  C  CH2   . TRP A 1 78  ? 147.075 152.844 165.766 1.00 43.88  ? 52  TRP A CH2   1 
ATOM   437  N  N     . MET A 1 79  ? 144.312 148.723 163.726 1.00 32.86  ? 53  MET A N     1 
ATOM   438  C  CA    . MET A 1 79  ? 143.223 149.435 164.388 1.00 33.22  ? 53  MET A CA    1 
ATOM   439  C  C     . MET A 1 79  ? 142.226 148.468 165.010 1.00 34.51  ? 53  MET A C     1 
ATOM   440  O  O     . MET A 1 79  ? 141.666 148.741 166.077 1.00 39.03  ? 53  MET A O     1 
ATOM   441  C  CB    . MET A 1 79  ? 142.511 150.360 163.401 1.00 38.86  ? 53  MET A CB    1 
ATOM   442  C  CG    . MET A 1 79  ? 143.117 151.745 163.287 1.00 44.55  ? 53  MET A CG    1 
ATOM   443  S  SD    . MET A 1 79  ? 142.184 152.824 162.185 1.00 58.75  ? 53  MET A SD    1 
ATOM   444  C  CE    . MET A 1 79  ? 142.211 151.875 160.669 1.00 39.10  ? 53  MET A CE    1 
ATOM   445  N  N     . VAL A 1 80  ? 141.996 147.328 164.363 1.00 33.27  ? 54  VAL A N     1 
ATOM   446  C  CA    . VAL A 1 80  ? 140.998 146.388 164.866 1.00 29.61  ? 54  VAL A CA    1 
ATOM   447  C  C     . VAL A 1 80  ? 141.599 145.459 165.915 1.00 27.67  ? 54  VAL A C     1 
ATOM   448  O  O     . VAL A 1 80  ? 141.159 145.433 167.069 1.00 35.64  ? 54  VAL A O     1 
ATOM   449  C  CB    . VAL A 1 80  ? 140.371 145.604 163.702 1.00 31.43  ? 54  VAL A CB    1 
ATOM   450  C  CG1   . VAL A 1 80  ? 139.445 144.521 164.229 1.00 27.81  ? 54  VAL A CG1   1 
ATOM   451  C  CG2   . VAL A 1 80  ? 139.626 146.561 162.804 1.00 34.74  ? 54  VAL A CG2   1 
ATOM   452  N  N     . PHE A 1 81  ? 142.615 144.689 165.535 1.00 30.28  ? 55  PHE A N     1 
ATOM   453  C  CA    . PHE A 1 81  ? 143.143 143.636 166.389 1.00 27.97  ? 55  PHE A CA    1 
ATOM   454  C  C     . PHE A 1 81  ? 144.175 144.132 167.392 1.00 28.78  ? 55  PHE A C     1 
ATOM   455  O  O     . PHE A 1 81  ? 144.559 143.371 168.286 1.00 39.65  ? 55  PHE A O     1 
ATOM   456  C  CB    . PHE A 1 81  ? 143.745 142.521 165.524 1.00 28.53  ? 55  PHE A CB    1 
ATOM   457  C  CG    . PHE A 1 81  ? 142.732 141.809 164.670 1.00 27.26  ? 55  PHE A CG    1 
ATOM   458  C  CD1   . PHE A 1 81  ? 142.451 142.250 163.384 1.00 31.38  ? 55  PHE A CD1   1 
ATOM   459  C  CD2   . PHE A 1 81  ? 142.046 140.711 165.160 1.00 20.96  ? 55  PHE A CD2   1 
ATOM   460  C  CE1   . PHE A 1 81  ? 141.510 141.604 162.605 1.00 28.77  ? 55  PHE A CE1   1 
ATOM   461  C  CE2   . PHE A 1 81  ? 141.105 140.062 164.384 1.00 26.62  ? 55  PHE A CE2   1 
ATOM   462  C  CZ    . PHE A 1 81  ? 140.839 140.507 163.106 1.00 28.30  ? 55  PHE A CZ    1 
ATOM   463  N  N     . GLY A 1 82  ? 144.634 145.374 167.270 1.00 34.29  ? 56  GLY A N     1 
ATOM   464  C  CA    . GLY A 1 82  ? 145.558 145.926 168.240 1.00 27.57  ? 56  GLY A CA    1 
ATOM   465  C  C     . GLY A 1 82  ? 144.908 146.803 169.285 1.00 35.31  ? 56  GLY A C     1 
ATOM   466  O  O     . GLY A 1 82  ? 145.124 146.614 170.485 1.00 46.43  ? 56  GLY A O     1 
ATOM   467  N  N     . LEU A 1 83  ? 144.098 147.762 168.842 1.00 38.39  ? 57  LEU A N     1 
ATOM   468  C  CA    . LEU A 1 83  ? 143.441 148.694 169.748 1.00 37.88  ? 57  LEU A CA    1 
ATOM   469  C  C     . LEU A 1 83  ? 142.131 148.138 170.293 1.00 43.62  ? 57  LEU A C     1 
ATOM   470  O  O     . LEU A 1 83  ? 141.824 148.312 171.475 1.00 48.57  ? 57  LEU A O     1 
ATOM   471  C  CB    . LEU A 1 83  ? 143.182 150.024 169.037 1.00 40.65  ? 57  LEU A CB    1 
ATOM   472  C  CG    . LEU A 1 83  ? 144.318 151.042 169.010 1.00 45.85  ? 57  LEU A CG    1 
ATOM   473  C  CD1   . LEU A 1 83  ? 144.226 151.872 167.748 1.00 44.35  ? 57  LEU A CD1   1 
ATOM   474  C  CD2   . LEU A 1 83  ? 144.271 151.928 170.241 1.00 42.20  ? 57  LEU A CD2   1 
ATOM   475  N  N     . GLY A 1 84  ? 141.349 147.475 169.441 1.00 44.36  ? 58  GLY A N     1 
ATOM   476  C  CA    . GLY A 1 84  ? 140.040 147.011 169.868 1.00 42.69  ? 58  GLY A CA    1 
ATOM   477  C  C     . GLY A 1 84  ? 140.096 145.764 170.729 1.00 47.05  ? 58  GLY A C     1 
ATOM   478  O  O     . GLY A 1 84  ? 139.236 145.558 171.589 1.00 56.60  ? 58  GLY A O     1 
ATOM   479  N  N     . ILE A 1 85  ? 141.101 144.920 170.518 1.00 39.91  ? 59  ILE A N     1 
ATOM   480  C  CA    . ILE A 1 85  ? 141.157 143.631 171.202 1.00 42.93  ? 59  ILE A CA    1 
ATOM   481  C  C     . ILE A 1 85  ? 142.042 143.692 172.440 1.00 47.31  ? 59  ILE A C     1 
ATOM   482  O  O     . ILE A 1 85  ? 141.624 143.300 173.533 1.00 50.39  ? 59  ILE A O     1 
ATOM   483  C  CB    . ILE A 1 85  ? 141.617 142.532 170.218 1.00 44.09  ? 59  ILE A CB    1 
ATOM   484  C  CG1   . ILE A 1 85  ? 140.493 142.231 169.218 1.00 40.98  ? 59  ILE A CG1   1 
ATOM   485  C  CG2   . ILE A 1 85  ? 142.068 141.275 170.973 1.00 41.56  ? 59  ILE A CG2   1 
ATOM   486  C  CD1   . ILE A 1 85  ? 140.621 140.917 168.480 1.00 41.98  ? 59  ILE A CD1   1 
ATOM   487  N  N     . ARG A 1 86  ? 143.270 144.194 172.308 1.00 42.42  ? 60  ARG A N     1 
ATOM   488  C  CA    . ARG A 1 86  ? 144.218 144.181 173.415 1.00 39.14  ? 60  ARG A CA    1 
ATOM   489  C  C     . ARG A 1 86  ? 144.721 145.567 173.798 1.00 41.97  ? 60  ARG A C     1 
ATOM   490  O  O     . ARG A 1 86  ? 145.631 145.663 174.632 1.00 43.94  ? 60  ARG A O     1 
ATOM   491  C  CB    . ARG A 1 86  ? 145.403 143.271 173.084 1.00 42.52  ? 60  ARG A CB    1 
ATOM   492  C  CG    . ARG A 1 86  ? 146.153 143.655 171.830 1.00 37.99  ? 60  ARG A CG    1 
ATOM   493  C  CD    . ARG A 1 86  ? 147.274 142.678 171.564 1.00 33.02  ? 60  ARG A CD    1 
ATOM   494  N  NE    . ARG A 1 86  ? 148.294 142.717 172.604 1.00 35.64  ? 60  ARG A NE    1 
ATOM   495  C  CZ    . ARG A 1 86  ? 148.598 141.697 173.392 1.00 38.35  ? 60  ARG A CZ    1 
ATOM   496  N  NH1   . ARG A 1 86  ? 147.980 140.533 173.284 1.00 45.06  ? 60  ARG A NH1   1 
ATOM   497  N  NH2   . ARG A 1 86  ? 149.544 141.848 174.314 1.00 36.90  ? 60  ARG A NH2   1 
ATOM   498  N  N     . SER A 1 87  ? 144.136 146.631 173.229 1.00 44.15  ? 61  SER A N     1 
ATOM   499  C  CA    . SER A 1 87  ? 144.467 148.039 173.511 1.00 44.82  ? 61  SER A CA    1 
ATOM   500  C  C     . SER A 1 87  ? 145.950 148.346 173.299 1.00 46.58  ? 61  SER A C     1 
ATOM   501  O  O     . SER A 1 87  ? 146.567 149.057 174.097 1.00 46.99  ? 61  SER A O     1 
ATOM   502  C  CB    . SER A 1 87  ? 144.022 148.463 174.917 1.00 47.28  ? 61  SER A CB    1 
ATOM   503  O  OG    . SER A 1 87  ? 144.708 147.762 175.940 1.00 51.41  ? 61  SER A OG    1 
ATOM   504  N  N     . ASN A 1 88  ? 146.512 147.793 172.212 1.00 46.87  ? 62  ASN A N     1 
ATOM   505  C  CA    . ASN A 1 88  ? 147.901 148.010 171.775 1.00 41.64  ? 62  ASN A CA    1 
ATOM   506  C  C     . ASN A 1 88  ? 148.913 147.607 172.847 1.00 41.45  ? 62  ASN A C     1 
ATOM   507  O  O     . ASN A 1 88  ? 149.929 148.274 173.050 1.00 47.25  ? 62  ASN A O     1 
ATOM   508  C  CB    . ASN A 1 88  ? 148.126 149.458 171.323 1.00 41.66  ? 62  ASN A CB    1 
ATOM   509  C  CG    . ASN A 1 88  ? 149.178 149.575 170.239 1.00 47.01  ? 62  ASN A CG    1 
ATOM   510  O  OD1   . ASN A 1 88  ? 149.464 148.614 169.528 1.00 50.76  ? 62  ASN A OD1   1 
ATOM   511  N  ND2   . ASN A 1 88  ? 149.759 150.760 170.106 1.00 47.85  ? 62  ASN A ND2   1 
ATOM   512  N  N     . ALA A 1 89  ? 148.629 146.511 173.544 1.00 41.63  ? 63  ALA A N     1 
ATOM   513  C  CA    . ALA A 1 89  ? 149.537 146.006 174.563 1.00 39.30  ? 63  ALA A CA    1 
ATOM   514  C  C     . ALA A 1 89  ? 150.746 145.338 173.907 1.00 49.04  ? 63  ALA A C     1 
ATOM   515  O  O     . ALA A 1 89  ? 150.608 144.707 172.856 1.00 47.83  ? 63  ALA A O     1 
ATOM   516  C  CB    . ALA A 1 89  ? 148.822 145.012 175.474 1.00 37.69  ? 63  ALA A CB    1 
ATOM   517  N  N     . PRO A 1 90  ? 151.936 145.478 174.491 1.00 51.25  ? 64  PRO A N     1 
ATOM   518  C  CA    . PRO A 1 90  ? 153.123 144.839 173.913 1.00 42.34  ? 64  PRO A CA    1 
ATOM   519  C  C     . PRO A 1 90  ? 153.089 143.324 174.049 1.00 42.72  ? 64  PRO A C     1 
ATOM   520  O  O     . PRO A 1 90  ? 152.476 142.760 174.958 1.00 44.48  ? 64  PRO A O     1 
ATOM   521  C  CB    . PRO A 1 90  ? 154.282 145.437 174.720 1.00 42.91  ? 64  PRO A CB    1 
ATOM   522  C  CG    . PRO A 1 90  ? 153.719 146.651 175.380 1.00 44.41  ? 64  PRO A CG    1 
ATOM   523  C  CD    . PRO A 1 90  ? 152.283 146.346 175.628 1.00 41.20  ? 64  PRO A CD    1 
ATOM   524  N  N     . ILE A 1 91  ? 153.769 142.663 173.114 1.00 44.63  ? 65  ILE A N     1 
ATOM   525  C  CA    . ILE A 1 91  ? 153.898 141.211 173.100 1.00 41.79  ? 65  ILE A CA    1 
ATOM   526  C  C     . ILE A 1 91  ? 155.381 140.872 173.123 1.00 43.97  ? 65  ILE A C     1 
ATOM   527  O  O     . ILE A 1 91  ? 156.124 141.290 172.225 1.00 47.54  ? 65  ILE A O     1 
ATOM   528  C  CB    . ILE A 1 91  ? 153.223 140.577 171.871 1.00 37.43  ? 65  ILE A CB    1 
ATOM   529  C  CG1   . ILE A 1 91  ? 151.719 140.858 171.880 1.00 43.70  ? 65  ILE A CG1   1 
ATOM   530  C  CG2   . ILE A 1 91  ? 153.494 139.079 171.836 1.00 41.60  ? 65  ILE A CG2   1 
ATOM   531  C  CD1   . ILE A 1 91  ? 150.925 140.090 170.843 1.00 40.49  ? 65  ILE A CD1   1 
ATOM   532  N  N     . HIS A 1 92  ? 155.802 140.122 174.152 1.00 52.46  ? 66  HIS A N     1 
ATOM   533  C  CA    . HIS A 1 92  ? 157.166 139.592 174.307 1.00 54.73  ? 66  HIS A CA    1 
ATOM   534  C  C     . HIS A 1 92  ? 158.216 140.702 174.336 1.00 55.75  ? 66  HIS A C     1 
ATOM   535  O  O     . HIS A 1 92  ? 159.324 140.554 173.819 1.00 57.63  ? 66  HIS A O     1 
ATOM   536  C  CB    . HIS A 1 92  ? 157.493 138.564 173.217 1.00 55.36  ? 66  HIS A CB    1 
ATOM   537  C  CG    . HIS A 1 92  ? 156.841 137.231 173.419 1.00 57.84  ? 66  HIS A CG    1 
ATOM   538  N  ND1   . HIS A 1 92  ? 155.525 137.094 173.805 1.00 59.81  ? 66  HIS A ND1   1 
ATOM   539  C  CD2   . HIS A 1 92  ? 157.323 135.974 173.278 1.00 58.13  ? 66  HIS A CD2   1 
ATOM   540  C  CE1   . HIS A 1 92  ? 155.226 135.811 173.899 1.00 58.98  ? 66  HIS A CE1   1 
ATOM   541  N  NE2   . HIS A 1 92  ? 156.300 135.110 173.583 1.00 61.00  ? 66  HIS A NE2   1 
ATOM   542  N  N     . GLY A 1 93  ? 157.862 141.830 174.949 1.00 49.15  ? 67  GLY A N     1 
ATOM   543  C  CA    . GLY A 1 93  ? 158.766 142.961 175.015 1.00 47.58  ? 67  GLY A CA    1 
ATOM   544  C  C     . GLY A 1 93  ? 158.830 143.809 173.766 1.00 48.30  ? 67  GLY A C     1 
ATOM   545  O  O     . GLY A 1 93  ? 159.615 144.760 173.719 1.00 55.48  ? 67  GLY A O     1 
ATOM   546  N  N     . VAL A 1 94  ? 158.035 143.494 172.756 1.00 41.25  ? 68  VAL A N     1 
ATOM   547  C  CA    . VAL A 1 94  ? 157.981 144.238 171.500 1.00 40.28  ? 68  VAL A CA    1 
ATOM   548  C  C     . VAL A 1 94  ? 156.625 144.925 171.433 1.00 44.88  ? 68  VAL A C     1 
ATOM   549  O  O     . VAL A 1 94  ? 155.620 144.312 171.808 1.00 46.74  ? 68  VAL A O     1 
ATOM   550  C  CB    . VAL A 1 94  ? 158.185 143.311 170.283 1.00 39.73  ? 68  VAL A CB    1 
ATOM   551  C  CG1   . VAL A 1 94  ? 158.278 144.104 168.987 1.00 39.27  ? 68  VAL A CG1   1 
ATOM   552  C  CG2   . VAL A 1 94  ? 159.424 142.449 170.471 1.00 42.48  ? 68  VAL A CG2   1 
ATOM   553  N  N     . PRO A 1 95  ? 156.552 146.192 171.013 1.00 41.39  ? 69  PRO A N     1 
ATOM   554  C  CA    . PRO A 1 95  ? 155.245 146.822 170.781 1.00 40.98  ? 69  PRO A CA    1 
ATOM   555  C  C     . PRO A 1 95  ? 154.474 146.122 169.670 1.00 38.47  ? 69  PRO A C     1 
ATOM   556  O  O     . PRO A 1 95  ? 155.061 145.514 168.773 1.00 42.16  ? 69  PRO A O     1 
ATOM   557  C  CB    . PRO A 1 95  ? 155.604 148.264 170.398 1.00 37.28  ? 69  PRO A CB    1 
ATOM   558  C  CG    . PRO A 1 95  ? 157.077 148.261 170.135 1.00 35.73  ? 69  PRO A CG    1 
ATOM   559  C  CD    . PRO A 1 95  ? 157.648 147.172 170.970 1.00 33.37  ? 69  PRO A CD    1 
ATOM   560  N  N     . PHE A 1 96  ? 153.139 146.204 169.755 1.00 40.41  ? 70  PHE A N     1 
ATOM   561  C  CA    . PHE A 1 96  ? 152.273 145.355 168.940 1.00 33.79  ? 70  PHE A CA    1 
ATOM   562  C  C     . PHE A 1 96  ? 152.329 145.706 167.460 1.00 28.02  ? 70  PHE A C     1 
ATOM   563  O  O     . PHE A 1 96  ? 152.105 144.830 166.616 1.00 29.35  ? 70  PHE A O     1 
ATOM   564  C  CB    . PHE A 1 96  ? 150.823 145.436 169.431 1.00 34.38  ? 70  PHE A CB    1 
ATOM   565  C  CG    . PHE A 1 96  ? 149.899 144.465 168.741 1.00 34.06  ? 70  PHE A CG    1 
ATOM   566  C  CD1   . PHE A 1 96  ? 149.877 143.133 169.115 1.00 33.07  ? 70  PHE A CD1   1 
ATOM   567  C  CD2   . PHE A 1 96  ? 149.075 144.877 167.700 1.00 27.07  ? 70  PHE A CD2   1 
ATOM   568  C  CE1   . PHE A 1 96  ? 149.043 142.234 168.479 1.00 30.78  ? 70  PHE A CE1   1 
ATOM   569  C  CE2   . PHE A 1 96  ? 148.252 143.975 167.053 1.00 25.61  ? 70  PHE A CE2   1 
ATOM   570  C  CZ    . PHE A 1 96  ? 148.231 142.656 167.449 1.00 26.00  ? 70  PHE A CZ    1 
ATOM   571  N  N     . VAL A 1 97  ? 152.604 146.970 167.126 1.00 32.93  ? 71  VAL A N     1 
ATOM   572  C  CA    . VAL A 1 97  ? 152.582 147.398 165.728 1.00 31.32  ? 71  VAL A CA    1 
ATOM   573  C  C     . VAL A 1 97  ? 153.710 146.730 164.942 1.00 35.42  ? 71  VAL A C     1 
ATOM   574  O  O     . VAL A 1 97  ? 153.494 146.210 163.843 1.00 36.57  ? 71  VAL A O     1 
ATOM   575  C  CB    . VAL A 1 97  ? 152.615 148.939 165.635 1.00 37.51  ? 71  VAL A CB    1 
ATOM   576  C  CG1   . VAL A 1 97  ? 153.661 149.543 166.564 1.00 32.13  ? 71  VAL A CG1   1 
ATOM   577  C  CG2   . VAL A 1 97  ? 152.832 149.403 164.200 1.00 31.70  ? 71  VAL A CG2   1 
ATOM   578  N  N     . TYR A 1 98  ? 154.902 146.641 165.535 1.00 34.26  ? 72  TYR A N     1 
ATOM   579  C  CA    . TYR A 1 98  ? 156.020 145.996 164.851 1.00 34.84  ? 72  TYR A CA    1 
ATOM   580  C  C     . TYR A 1 98  ? 155.911 144.476 164.893 1.00 38.16  ? 72  TYR A C     1 
ATOM   581  O  O     . TYR A 1 98  ? 156.339 143.804 163.949 1.00 39.81  ? 72  TYR A O     1 
ATOM   582  C  CB    . TYR A 1 98  ? 157.336 146.479 165.457 1.00 32.49  ? 72  TYR A CB    1 
ATOM   583  C  CG    . TYR A 1 98  ? 157.456 147.982 165.404 1.00 34.38  ? 72  TYR A CG    1 
ATOM   584  C  CD1   . TYR A 1 98  ? 157.791 148.628 164.220 1.00 36.36  ? 72  TYR A CD1   1 
ATOM   585  C  CD2   . TYR A 1 98  ? 157.202 148.758 166.528 1.00 39.60  ? 72  TYR A CD2   1 
ATOM   586  C  CE1   . TYR A 1 98  ? 157.885 150.005 164.160 1.00 34.39  ? 72  TYR A CE1   1 
ATOM   587  C  CE2   . TYR A 1 98  ? 157.289 150.134 166.477 1.00 37.18  ? 72  TYR A CE2   1 
ATOM   588  C  CZ    . TYR A 1 98  ? 157.629 150.751 165.291 1.00 35.81  ? 72  TYR A CZ    1 
ATOM   589  O  OH    . TYR A 1 98  ? 157.725 152.121 165.243 1.00 41.36  ? 72  TYR A OH    1 
ATOM   590  N  N     . TRP A 1 99  ? 155.331 143.930 165.968 1.00 32.01  ? 73  TRP A N     1 
ATOM   591  C  CA    . TRP A 1 99  ? 155.055 142.497 166.061 1.00 16.88  ? 73  TRP A CA    1 
ATOM   592  C  C     . TRP A 1 99  ? 154.098 142.047 164.961 1.00 26.18  ? 73  TRP A C     1 
ATOM   593  O  O     . TRP A 1 99  ? 154.363 141.070 164.246 1.00 34.06  ? 73  TRP A O     1 
ATOM   594  C  CB    . TRP A 1 99  ? 154.481 142.201 167.448 1.00 23.83  ? 73  TRP A CB    1 
ATOM   595  C  CG    . TRP A 1 99  ? 154.147 140.772 167.758 1.00 30.43  ? 73  TRP A CG    1 
ATOM   596  C  CD1   . TRP A 1 99  ? 154.956 139.853 168.354 1.00 27.71  ? 73  TRP A CD1   1 
ATOM   597  C  CD2   . TRP A 1 99  ? 152.895 140.113 167.527 1.00 28.00  ? 73  TRP A CD2   1 
ATOM   598  N  NE1   . TRP A 1 99  ? 154.294 138.658 168.495 1.00 17.68  ? 73  TRP A NE1   1 
ATOM   599  C  CE2   . TRP A 1 99  ? 153.026 138.792 167.993 1.00 26.78  ? 73  TRP A CE2   1 
ATOM   600  C  CE3   . TRP A 1 99  ? 151.682 140.509 166.958 1.00 25.46  ? 73  TRP A CE3   1 
ATOM   601  C  CZ2   . TRP A 1 99  ? 151.985 137.868 167.918 1.00 23.94  ? 73  TRP A CZ2   1 
ATOM   602  C  CZ3   . TRP A 1 99  ? 150.655 139.587 166.876 1.00 21.32  ? 73  TRP A CZ3   1 
ATOM   603  C  CH2   . TRP A 1 99  ? 150.813 138.283 167.352 1.00 20.45  ? 73  TRP A CH2   1 
ATOM   604  N  N     . LEU A 1 100 ? 152.995 142.781 164.789 1.00 24.14  ? 74  LEU A N     1 
ATOM   605  C  CA    . LEU A 1 100 ? 152.059 142.507 163.706 1.00 26.03  ? 74  LEU A CA    1 
ATOM   606  C  C     . LEU A 1 100 ? 152.690 142.781 162.346 1.00 27.88  ? 74  LEU A C     1 
ATOM   607  O  O     . LEU A 1 100 ? 152.448 142.036 161.392 1.00 34.48  ? 74  LEU A O     1 
ATOM   608  C  CB    . LEU A 1 100 ? 150.790 143.340 163.892 1.00 28.30  ? 74  LEU A CB    1 
ATOM   609  C  CG    . LEU A 1 100 ? 149.743 143.333 162.773 1.00 26.27  ? 74  LEU A CG    1 
ATOM   610  C  CD1   . LEU A 1 100 ? 148.869 142.097 162.843 1.00 25.97  ? 74  LEU A CD1   1 
ATOM   611  C  CD2   . LEU A 1 100 ? 148.897 144.587 162.825 1.00 25.05  ? 74  LEU A CD2   1 
ATOM   612  N  N     . LEU A 1 101 ? 153.522 143.826 162.257 1.00 26.78  ? 75  LEU A N     1 
ATOM   613  C  CA    . LEU A 1 101 ? 154.158 144.222 161.004 1.00 25.40  ? 75  LEU A CA    1 
ATOM   614  C  C     . LEU A 1 101 ? 155.084 143.136 160.472 1.00 25.01  ? 75  LEU A C     1 
ATOM   615  O  O     . LEU A 1 101 ? 155.064 142.820 159.277 1.00 29.01  ? 75  LEU A O     1 
ATOM   616  C  CB    . LEU A 1 101 ? 154.930 145.523 161.230 1.00 30.87  ? 75  LEU A CB    1 
ATOM   617  C  CG    . LEU A 1 101 ? 155.022 146.611 160.163 1.00 30.69  ? 75  LEU A CG    1 
ATOM   618  C  CD1   . LEU A 1 101 ? 153.823 146.596 159.245 1.00 23.78  ? 75  LEU A CD1   1 
ATOM   619  C  CD2   . LEU A 1 101 ? 155.166 147.966 160.833 1.00 28.06  ? 75  LEU A CD2   1 
ATOM   620  N  N     . VAL A 1 102 ? 155.838 142.470 161.346 1.00 30.99  ? 76  VAL A N     1 
ATOM   621  C  CA    . VAL A 1 102 ? 156.717 141.357 160.878 1.00 27.77  ? 76  VAL A CA    1 
ATOM   622  C  C     . VAL A 1 102 ? 155.858 140.127 160.542 1.00 26.29  ? 76  VAL A C     1 
ATOM   623  O  O     . VAL A 1 102 ? 156.111 139.513 159.493 1.00 37.46  ? 76  VAL A O     1 
ATOM   624  C  CB    . VAL A 1 102 ? 157.847 141.041 161.876 1.00 27.98  ? 76  VAL A CB    1 
ATOM   625  C  CG1   . VAL A 1 102 ? 158.677 139.844 161.443 1.00 27.14  ? 76  VAL A CG1   1 
ATOM   626  C  CG2   . VAL A 1 102 ? 158.741 142.251 162.099 1.00 28.51  ? 76  VAL A CG2   1 
ATOM   627  N  N     . GLY A 1 103 ? 154.879 139.794 161.383 1.00 32.99  ? 77  GLY A N     1 
ATOM   628  C  CA    . GLY A 1 103 ? 153.984 138.642 161.158 1.00 23.22  ? 77  GLY A CA    1 
ATOM   629  C  C     . GLY A 1 103 ? 153.102 138.712 159.924 1.00 20.97  ? 77  GLY A C     1 
ATOM   630  O  O     . GLY A 1 103 ? 152.900 137.662 159.314 1.00 32.92  ? 77  GLY A O     1 
ATOM   631  N  N     . ILE A 1 104 ? 152.535 139.867 159.591 1.00 33.53  ? 78  ILE A N     1 
ATOM   632  C  CA    . ILE A 1 104 ? 151.572 139.992 158.451 1.00 27.63  ? 78  ILE A CA    1 
ATOM   633  C  C     . ILE A 1 104 ? 152.307 140.264 157.130 1.00 37.22  ? 78  ILE A C     1 
ATOM   634  O  O     . ILE A 1 104 ? 151.638 140.282 156.083 1.00 45.50  ? 78  ILE A O     1 
ATOM   635  C  CB    . ILE A 1 104 ? 150.531 141.086 158.754 1.00 25.34  ? 78  ILE A CB    1 
ATOM   636  C  CG1   . ILE A 1 104 ? 149.219 140.854 158.000 1.00 26.18  ? 78  ILE A CG1   1 
ATOM   637  C  CG2   . ILE A 1 104 ? 151.104 142.479 158.494 1.00 28.45  ? 78  ILE A CG2   1 
ATOM   638  C  CD1   . ILE A 1 104 ? 147.983 141.314 158.745 1.00 30.92  ? 78  ILE A CD1   1 
ATOM   639  N  N     . SER A 1 105 ? 153.627 140.425 157.150 1.00 34.92  ? 79  SER A N     1 
ATOM   640  C  CA    . SER A 1 105 ? 154.346 140.844 155.918 1.00 32.43  ? 79  SER A CA    1 
ATOM   641  C  C     . SER A 1 105 ? 154.198 139.816 154.788 1.00 32.99  ? 79  SER A C     1 
ATOM   642  O  O     . SER A 1 105 ? 154.031 140.242 153.632 1.00 38.29  ? 79  SER A O     1 
ATOM   643  C  CB    . SER A 1 105 ? 155.801 141.112 156.215 1.00 35.74  ? 79  SER A CB    1 
ATOM   644  O  OG    . SER A 1 105 ? 156.369 140.059 156.979 1.00 40.64  ? 79  SER A OG    1 
ATOM   645  N  N     . MET A 1 106 ? 154.287 138.522 155.090 1.00 37.02  ? 80  MET A N     1 
ATOM   646  C  CA    . MET A 1 106 ? 154.223 137.470 154.039 1.00 29.08  ? 80  MET A CA    1 
ATOM   647  C  C     . MET A 1 106 ? 152.775 137.081 153.716 1.00 32.27  ? 80  MET A C     1 
ATOM   648  O  O     . MET A 1 106 ? 152.580 136.456 152.671 1.00 36.17  ? 80  MET A O     1 
ATOM   649  C  CB    . MET A 1 106 ? 155.019 136.240 154.484 1.00 23.60  ? 80  MET A CB    1 
ATOM   650  C  CG    . MET A 1 106 ? 154.252 135.287 155.372 1.00 31.22  ? 80  MET A CG    1 
ATOM   651  S  SD    . MET A 1 106 ? 153.976 135.877 157.053 1.00 52.92  ? 80  MET A SD    1 
ATOM   652  C  CE    . MET A 1 106 ? 155.618 136.398 157.563 1.00 28.67  ? 80  MET A CE    1 
ATOM   653  N  N     . TRP A 1 107 ? 151.805 137.504 154.525 1.00 29.14  ? 81  TRP A N     1 
ATOM   654  C  CA    . TRP A 1 107 ? 150.400 137.059 154.352 1.00 27.68  ? 81  TRP A CA    1 
ATOM   655  C  C     . TRP A 1 107 ? 149.832 137.513 153.017 1.00 20.61  ? 81  TRP A C     1 
ATOM   656  O  O     . TRP A 1 107 ? 149.265 136.685 152.291 1.00 33.32  ? 81  TRP A O     1 
ATOM   657  C  CB    . TRP A 1 107 ? 149.510 137.592 155.482 1.00 29.80  ? 81  TRP A CB    1 
ATOM   658  C  CG    . TRP A 1 107 ? 148.053 137.432 155.142 1.00 26.40  ? 81  TRP A CG    1 
ATOM   659  C  CD1   . TRP A 1 107 ? 147.138 138.418 154.928 1.00 19.85  ? 81  TRP A CD1   1 
ATOM   660  C  CD2   . TRP A 1 107 ? 147.367 136.185 154.899 1.00 25.36  ? 81  TRP A CD2   1 
ATOM   661  N  NE1   . TRP A 1 107 ? 145.930 137.875 154.589 1.00 25.86  ? 81  TRP A NE1   1 
ATOM   662  C  CE2   . TRP A 1 107 ? 146.039 136.510 154.557 1.00 22.28  ? 81  TRP A CE2   1 
ATOM   663  C  CE3   . TRP A 1 107 ? 147.742 134.837 154.938 1.00 19.27  ? 81  TRP A CE3   1 
ATOM   664  C  CZ2   . TRP A 1 107 ? 145.090 135.536 154.263 1.00 25.91  ? 81  TRP A CZ2   1 
ATOM   665  C  CZ3   . TRP A 1 107 ? 146.803 133.875 154.645 1.00 24.85  ? 81  TRP A CZ3   1 
ATOM   666  C  CH2   . TRP A 1 107 ? 145.499 134.223 154.301 1.00 24.35  ? 81  TRP A CH2   1 
ATOM   667  N  N     . PHE A 1 108 ? 149.955 138.796 152.725 1.00 23.00  ? 82  PHE A N     1 
ATOM   668  C  CA    . PHE A 1 108 ? 149.362 139.342 151.507 1.00 22.58  ? 82  PHE A CA    1 
ATOM   669  C  C     . PHE A 1 108 ? 149.915 138.653 150.267 1.00 28.46  ? 82  PHE A C     1 
ATOM   670  O  O     . PHE A 1 108 ? 149.166 138.360 149.327 1.00 38.15  ? 82  PHE A O     1 
ATOM   671  C  CB    . PHE A 1 108 ? 149.599 140.851 151.441 1.00 27.29  ? 82  PHE A CB    1 
ATOM   672  C  CG    . PHE A 1 108 ? 149.084 141.595 152.640 1.00 35.25  ? 82  PHE A CG    1 
ATOM   673  C  CD1   . PHE A 1 108 ? 147.722 141.778 152.827 1.00 26.46  ? 82  PHE A CD1   1 
ATOM   674  C  CD2   . PHE A 1 108 ? 149.962 142.109 153.583 1.00 31.26  ? 82  PHE A CD2   1 
ATOM   675  C  CE1   . PHE A 1 108 ? 147.244 142.458 153.932 1.00 21.41  ? 82  PHE A CE1   1 
ATOM   676  C  CE2   . PHE A 1 108 ? 149.490 142.792 154.690 1.00 35.13  ? 82  PHE A CE2   1 
ATOM   677  C  CZ    . PHE A 1 108 ? 148.130 142.967 154.864 1.00 28.98  ? 82  PHE A CZ    1 
ATOM   678  N  N     . PHE A 1 109 ? 151.212 138.333 150.281 1.00 29.21  ? 83  PHE A N     1 
ATOM   679  C  CA    . PHE A 1 109 ? 151.821 137.573 149.194 1.00 21.76  ? 83  PHE A CA    1 
ATOM   680  C  C     . PHE A 1 109 ? 151.242 136.167 149.101 1.00 24.52  ? 83  PHE A C     1 
ATOM   681  O  O     . PHE A 1 109 ? 150.931 135.696 148.005 1.00 28.06  ? 83  PHE A O     1 
ATOM   682  C  CB    . PHE A 1 109 ? 153.336 137.516 149.387 1.00 26.58  ? 83  PHE A CB    1 
ATOM   683  C  CG    . PHE A 1 109 ? 153.999 136.338 148.724 1.00 26.86  ? 83  PHE A CG    1 
ATOM   684  C  CD1   . PHE A 1 109 ? 154.079 136.248 147.340 1.00 19.14  ? 83  PHE A CD1   1 
ATOM   685  C  CD2   . PHE A 1 109 ? 154.558 135.325 149.489 1.00 21.43  ? 83  PHE A CD2   1 
ATOM   686  C  CE1   . PHE A 1 109 ? 154.687 135.165 146.737 1.00 22.71  ? 83  PHE A CE1   1 
ATOM   687  C  CE2   . PHE A 1 109 ? 155.169 134.241 148.889 1.00 19.16  ? 83  PHE A CE2   1 
ATOM   688  C  CZ    . PHE A 1 109 ? 155.234 134.162 147.512 1.00 23.29  ? 83  PHE A CZ    1 
ATOM   689  N  N     . ILE A 1 110 ? 151.093 135.487 150.244 1.00 22.19  ? 84  ILE A N     1 
ATOM   690  C  CA    . ILE A 1 110 ? 150.589 134.112 150.258 1.00 24.08  ? 84  ILE A CA    1 
ATOM   691  C  C     . ILE A 1 110 ? 149.150 134.068 149.760 1.00 29.21  ? 84  ILE A C     1 
ATOM   692  O  O     . ILE A 1 110 ? 148.801 133.267 148.882 1.00 37.85  ? 84  ILE A O     1 
ATOM   693  C  CB    . ILE A 1 110 ? 150.715 133.514 151.673 1.00 28.89  ? 84  ILE A CB    1 
ATOM   694  C  CG1   . ILE A 1 110 ? 152.180 133.251 152.021 1.00 25.66  ? 84  ILE A CG1   1 
ATOM   695  C  CG2   . ILE A 1 110 ? 149.898 132.234 151.809 1.00 23.17  ? 84  ILE A CG2   1 
ATOM   696  C  CD1   . ILE A 1 110 ? 152.384 132.757 153.434 1.00 26.18  ? 84  ILE A CD1   1 
ATOM   697  N  N     . ASN A 1 111 ? 148.317 134.977 150.273 1.00 26.59  ? 85  ASN A N     1 
ATOM   698  C  CA    . ASN A 1 111 ? 146.909 135.044 149.897 1.00 27.24  ? 85  ASN A CA    1 
ATOM   699  C  C     . ASN A 1 111 ? 146.739 135.395 148.424 1.00 27.82  ? 85  ASN A C     1 
ATOM   700  O  O     . ASN A 1 111 ? 145.997 134.721 147.700 1.00 32.30  ? 85  ASN A O     1 
ATOM   701  C  CB    . ASN A 1 111 ? 146.199 136.068 150.784 1.00 23.42  ? 85  ASN A CB    1 
ATOM   702  C  CG    . ASN A 1 111 ? 144.702 136.077 150.588 1.00 29.72  ? 85  ASN A CG    1 
ATOM   703  O  OD1   . ASN A 1 111 ? 144.031 135.070 150.797 1.00 35.58  ? 85  ASN A OD1   1 
ATOM   704  N  ND2   . ASN A 1 111 ? 144.166 137.222 150.190 1.00 28.36  ? 85  ASN A ND2   1 
ATOM   705  N  N     . GLN A 1 112 ? 147.467 136.412 147.949 1.00 28.17  ? 86  GLN A N     1 
ATOM   706  C  CA    . GLN A 1 112 ? 147.324 136.848 146.565 1.00 24.95  ? 86  GLN A CA    1 
ATOM   707  C  C     . GLN A 1 112 ? 147.907 135.832 145.590 1.00 29.97  ? 86  GLN A C     1 
ATOM   708  O  O     . GLN A 1 112 ? 147.330 135.598 144.524 1.00 35.76  ? 86  GLN A O     1 
ATOM   709  C  CB    . GLN A 1 112 ? 147.981 138.215 146.394 1.00 29.90  ? 86  GLN A CB    1 
ATOM   710  C  CG    . GLN A 1 112 ? 147.011 139.375 146.504 1.00 36.87  ? 86  GLN A CG    1 
ATOM   711  C  CD    . GLN A 1 112 ? 147.710 140.718 146.534 1.00 44.18  ? 86  GLN A CD    1 
ATOM   712  O  OE1   . GLN A 1 112 ? 148.938 140.791 146.568 1.00 40.86  ? 86  GLN A OE1   1 
ATOM   713  N  NE2   . GLN A 1 112 ? 146.930 141.791 146.519 1.00 38.08  ? 86  GLN A NE2   1 
ATOM   714  N  N     . GLY A 1 113 ? 149.032 135.201 145.943 1.00 30.84  ? 87  GLY A N     1 
ATOM   715  C  CA    . GLY A 1 113 ? 149.619 134.199 145.072 1.00 25.26  ? 87  GLY A CA    1 
ATOM   716  C  C     . GLY A 1 113 ? 148.786 132.938 144.970 1.00 32.26  ? 87  GLY A C     1 
ATOM   717  O  O     . GLY A 1 113 ? 148.630 132.379 143.882 1.00 40.36  ? 87  GLY A O     1 
ATOM   718  N  N     . ILE A 1 114 ? 148.227 132.480 146.096 1.00 28.16  ? 88  ILE A N     1 
ATOM   719  C  CA    . ILE A 1 114 ? 147.375 131.295 146.070 1.00 23.02  ? 88  ILE A CA    1 
ATOM   720  C  C     . ILE A 1 114 ? 146.058 131.594 145.354 1.00 28.59  ? 88  ILE A C     1 
ATOM   721  O  O     . ILE A 1 114 ? 145.556 130.760 144.590 1.00 38.34  ? 88  ILE A O     1 
ATOM   722  C  CB    . ILE A 1 114 ? 147.178 130.762 147.505 1.00 29.76  ? 88  ILE A CB    1 
ATOM   723  C  CG1   . ILE A 1 114 ? 148.482 130.134 148.004 1.00 25.45  ? 88  ILE A CG1   1 
ATOM   724  C  CG2   . ILE A 1 114 ? 146.064 129.725 147.587 1.00 23.61  ? 88  ILE A CG2   1 
ATOM   725  C  CD1   . ILE A 1 114 ? 148.423 129.604 149.417 1.00 33.72  ? 88  ILE A CD1   1 
ATOM   726  N  N     . LEU A 1 115 ? 145.508 132.801 145.537 1.00 31.48  ? 89  LEU A N     1 
ATOM   727  C  CA    . LEU A 1 115 ? 144.260 133.159 144.864 1.00 31.46  ? 89  LEU A CA    1 
ATOM   728  C  C     . LEU A 1 115 ? 144.451 133.317 143.358 1.00 32.33  ? 89  LEU A C     1 
ATOM   729  O  O     . LEU A 1 115 ? 143.685 132.757 142.566 1.00 33.15  ? 89  LEU A O     1 
ATOM   730  C  CB    . LEU A 1 115 ? 143.694 134.447 145.462 1.00 31.29  ? 89  LEU A CB    1 
ATOM   731  C  CG    . LEU A 1 115 ? 142.785 134.321 146.683 1.00 36.49  ? 89  LEU A CG    1 
ATOM   732  C  CD1   . LEU A 1 115 ? 142.291 135.687 147.133 1.00 34.69  ? 89  LEU A CD1   1 
ATOM   733  C  CD2   . LEU A 1 115 ? 141.619 133.387 146.402 1.00 34.33  ? 89  LEU A CD2   1 
ATOM   734  N  N     . GLU A 1 116 ? 145.468 134.074 142.941 1.00 35.38  ? 90  GLU A N     1 
ATOM   735  C  CA    . GLU A 1 116 ? 145.644 134.376 141.527 1.00 31.97  ? 90  GLU A CA    1 
ATOM   736  C  C     . GLU A 1 116 ? 146.257 133.220 140.753 1.00 33.14  ? 90  GLU A C     1 
ATOM   737  O  O     . GLU A 1 116 ? 145.926 133.027 139.579 1.00 43.69  ? 90  GLU A O     1 
ATOM   738  C  CB    . GLU A 1 116 ? 146.508 135.626 141.364 1.00 33.87  ? 90  GLU A CB    1 
ATOM   739  C  CG    . GLU A 1 116 ? 145.725 136.919 141.429 1.00 35.00  ? 90  GLU A CG    1 
ATOM   740  C  CD    . GLU A 1 116 ? 146.416 137.972 142.266 1.00 46.51  ? 90  GLU A CD    1 
ATOM   741  O  OE1   . GLU A 1 116 ? 145.789 138.479 143.220 1.00 47.50  ? 90  GLU A OE1   1 
ATOM   742  O  OE2   . GLU A 1 116 ? 147.584 138.294 141.971 1.00 45.66  ? 90  GLU A OE2   1 
ATOM   743  N  N     . GLY A 1 117 ? 147.153 132.454 141.370 1.00 23.85  ? 91  GLY A N     1 
ATOM   744  C  CA    . GLY A 1 117 ? 147.783 131.380 140.638 1.00 28.59  ? 91  GLY A CA    1 
ATOM   745  C  C     . GLY A 1 117 ? 147.026 130.074 140.609 1.00 29.32  ? 91  GLY A C     1 
ATOM   746  O  O     . GLY A 1 117 ? 147.434 129.162 139.885 1.00 40.61  ? 91  GLY A O     1 
ATOM   747  N  N     . THR A 1 118 ? 145.955 129.948 141.397 1.00 31.38  ? 92  THR A N     1 
ATOM   748  C  CA    . THR A 1 118 ? 145.050 128.813 141.244 1.00 29.65  ? 92  THR A CA    1 
ATOM   749  C  C     . THR A 1 118 ? 144.343 128.872 139.896 1.00 32.89  ? 92  THR A C     1 
ATOM   750  O  O     . THR A 1 118 ? 144.122 127.841 139.249 1.00 40.60  ? 92  THR A O     1 
ATOM   751  C  CB    . THR A 1 118 ? 144.038 128.795 142.395 1.00 32.28  ? 92  THR A CB    1 
ATOM   752  O  OG1   . THR A 1 118 ? 144.739 128.773 143.643 1.00 37.11  ? 92  THR A OG1   1 
ATOM   753  C  CG2   . THR A 1 118 ? 143.126 127.576 142.326 1.00 33.13  ? 92  THR A CG2   1 
ATOM   754  N  N     . LYS A 1 119 ? 144.011 130.075 139.439 1.00 34.18  ? 93  LYS A N     1 
ATOM   755  C  CA    . LYS A 1 119 ? 143.347 130.268 138.162 1.00 37.07  ? 93  LYS A CA    1 
ATOM   756  C  C     . LYS A 1 119 ? 144.313 130.667 137.053 1.00 32.38  ? 93  LYS A C     1 
ATOM   757  O  O     . LYS A 1 119 ? 143.863 131.130 136.005 1.00 37.61  ? 93  LYS A O     1 
ATOM   758  C  CB    . LYS A 1 119 ? 142.242 131.314 138.302 1.00 39.22  ? 93  LYS A CB    1 
ATOM   759  C  CG    . LYS A 1 119 ? 142.675 132.567 139.032 1.00 31.85  ? 93  LYS A CG    1 
ATOM   760  C  CD    . LYS A 1 119 ? 141.585 133.620 139.022 1.00 40.29  ? 93  LYS A CD    1 
ATOM   761  C  CE    . LYS A 1 119 ? 140.829 133.635 140.337 1.00 36.17  ? 93  LYS A CE    1 
ATOM   762  N  NZ    . LYS A 1 119 ? 139.398 133.994 140.152 1.00 43.84  ? 93  LYS A NZ    1 
ATOM   763  N  N     . ALA A 1 120 ? 145.623 130.489 137.261 1.00 33.22  ? 94  ALA A N     1 
ATOM   764  C  CA    . ALA A 1 120 ? 146.619 131.013 136.326 1.00 30.86  ? 94  ALA A CA    1 
ATOM   765  C  C     . ALA A 1 120 ? 146.584 130.282 134.989 1.00 39.99  ? 94  ALA A C     1 
ATOM   766  O  O     . ALA A 1 120 ? 146.613 130.911 133.924 1.00 42.01  ? 94  ALA A O     1 
ATOM   767  C  CB    . ALA A 1 120 ? 148.014 130.924 136.943 1.00 23.75  ? 94  ALA A CB    1 
ATOM   768  N  N     . ILE A 1 121 ? 146.506 128.951 135.023 1.00 37.90  ? 95  ILE A N     1 
ATOM   769  C  CA    . ILE A 1 121 ? 146.406 128.180 133.788 1.00 31.84  ? 95  ILE A CA    1 
ATOM   770  C  C     . ILE A 1 121 ? 145.014 128.336 133.175 1.00 30.49  ? 95  ILE A C     1 
ATOM   771  O  O     . ILE A 1 121 ? 144.827 128.153 131.969 1.00 41.57  ? 95  ILE A O     1 
ATOM   772  C  CB    . ILE A 1 121 ? 146.773 126.706 134.060 1.00 35.93  ? 95  ILE A CB    1 
ATOM   773  C  CG1   . ILE A 1 121 ? 148.061 126.624 134.882 1.00 35.27  ? 95  ILE A CG1   1 
ATOM   774  C  CG2   . ILE A 1 121 ? 146.980 125.918 132.766 1.00 37.68  ? 95  ILE A CG2   1 
ATOM   775  C  CD1   . ILE A 1 121 ? 148.517 125.211 135.183 1.00 33.83  ? 95  ILE A CD1   1 
ATOM   776  N  N     . THR A 1 122 ? 144.022 128.717 133.984 1.00 36.71  ? 96  THR A N     1 
ATOM   777  C  CA    . THR A 1 122 ? 142.675 128.914 133.455 1.00 39.61  ? 96  THR A CA    1 
ATOM   778  C  C     . THR A 1 122 ? 142.588 130.125 132.526 1.00 37.60  ? 96  THR A C     1 
ATOM   779  O  O     . THR A 1 122 ? 141.859 130.083 131.529 1.00 46.58  ? 96  THR A O     1 
ATOM   780  C  CB    . THR A 1 122 ? 141.672 129.044 134.603 1.00 38.53  ? 96  THR A CB    1 
ATOM   781  O  OG1   . THR A 1 122 ? 141.998 128.097 135.627 1.00 49.99  ? 96  THR A OG1   1 
ATOM   782  C  CG2   . THR A 1 122 ? 140.264 128.772 134.116 1.00 38.49  ? 96  THR A CG2   1 
ATOM   783  N  N     . GLN A 1 123 ? 143.331 131.198 132.806 1.00 38.61  ? 97  GLN A N     1 
ATOM   784  C  CA    . GLN A 1 123 ? 143.298 132.376 131.948 1.00 43.63  ? 97  GLN A CA    1 
ATOM   785  C  C     . GLN A 1 123 ? 144.593 132.616 131.184 1.00 39.51  ? 97  GLN A C     1 
ATOM   786  O  O     . GLN A 1 123 ? 144.680 133.605 130.451 1.00 48.91  ? 97  GLN A O     1 
ATOM   787  C  CB    . GLN A 1 123 ? 142.959 133.639 132.754 1.00 47.67  ? 97  GLN A CB    1 
ATOM   788  C  CG    . GLN A 1 123 ? 143.556 133.691 134.136 1.00 40.18  ? 97  GLN A CG    1 
ATOM   789  C  CD    . GLN A 1 123 ? 143.083 134.879 134.946 1.00 50.39  ? 97  GLN A CD    1 
ATOM   790  O  OE1   . GLN A 1 123 ? 142.179 134.760 135.773 1.00 47.72  ? 97  GLN A OE1   1 
ATOM   791  N  NE2   . GLN A 1 123 ? 143.698 136.034 134.719 1.00 49.27  ? 97  GLN A NE2   1 
ATOM   792  N  N     . LYS A 1 124 ? 145.599 131.753 131.324 1.00 40.86  ? 98  LYS A N     1 
ATOM   793  C  CA    . LYS A 1 124 ? 146.867 131.970 130.644 1.00 38.12  ? 98  LYS A CA    1 
ATOM   794  C  C     . LYS A 1 124 ? 147.300 130.826 129.738 1.00 44.83  ? 98  LYS A C     1 
ATOM   795  O  O     . LYS A 1 124 ? 148.360 130.931 129.113 1.00 49.09  ? 98  LYS A O     1 
ATOM   796  C  CB    . LYS A 1 124 ? 147.976 132.248 131.669 1.00 42.16  ? 98  LYS A CB    1 
ATOM   797  C  CG    . LYS A 1 124 ? 148.205 133.722 131.944 1.00 41.32  ? 98  LYS A CG    1 
ATOM   798  C  CD    . LYS A 1 124 ? 147.601 134.132 133.274 1.00 50.54  ? 98  LYS A CD    1 
ATOM   799  C  CE    . LYS A 1 124 ? 147.833 135.602 133.557 1.00 44.52  ? 98  LYS A CE    1 
ATOM   800  N  NZ    . LYS A 1 124 ? 147.576 136.439 132.356 1.00 47.17  ? 98  LYS A NZ    1 
ATOM   801  N  N     . PHE A 1 125 ? 146.527 129.741 129.645 1.00 44.29  ? 99  PHE A N     1 
ATOM   802  C  CA    . PHE A 1 125 ? 146.937 128.618 128.803 1.00 43.06  ? 99  PHE A CA    1 
ATOM   803  C  C     . PHE A 1 125 ? 146.764 128.936 127.325 1.00 46.96  ? 99  PHE A C     1 
ATOM   804  O  O     . PHE A 1 125 ? 147.603 128.550 126.504 1.00 50.22  ? 99  PHE A O     1 
ATOM   805  C  CB    . PHE A 1 125 ? 146.149 127.360 129.172 1.00 40.54  ? 99  PHE A CB    1 
ATOM   806  C  CG    . PHE A 1 125 ? 146.379 126.194 128.252 1.00 42.80  ? 99  PHE A CG    1 
ATOM   807  C  CD1   . PHE A 1 125 ? 147.556 125.465 128.317 1.00 42.29  ? 99  PHE A CD1   1 
ATOM   808  C  CD2   . PHE A 1 125 ? 145.408 125.815 127.335 1.00 43.10  ? 99  PHE A CD2   1 
ATOM   809  C  CE1   . PHE A 1 125 ? 147.766 124.388 127.473 1.00 42.21  ? 99  PHE A CE1   1 
ATOM   810  C  CE2   . PHE A 1 125 ? 145.614 124.743 126.490 1.00 44.78  ? 99  PHE A CE2   1 
ATOM   811  C  CZ    . PHE A 1 125 ? 146.794 124.028 126.560 1.00 40.01  ? 99  PHE A CZ    1 
ATOM   812  N  N     . ASN A 1 126 ? 145.686 129.642 126.970 1.00 49.03  ? 100 ASN A N     1 
ATOM   813  C  CA    . ASN A 1 126 ? 145.334 129.829 125.565 1.00 48.17  ? 100 ASN A CA    1 
ATOM   814  C  C     . ASN A 1 126 ? 146.291 130.774 124.849 1.00 51.85  ? 100 ASN A C     1 
ATOM   815  O  O     . ASN A 1 126 ? 146.426 130.699 123.623 1.00 55.49  ? 100 ASN A O     1 
ATOM   816  C  CB    . ASN A 1 126 ? 143.901 130.345 125.451 1.00 47.85  ? 100 ASN A CB    1 
ATOM   817  C  CG    . ASN A 1 126 ? 142.915 129.247 125.122 1.00 53.50  ? 100 ASN A CG    1 
ATOM   818  O  OD1   . ASN A 1 126 ? 143.095 128.505 124.157 1.00 54.79  ? 100 ASN A OD1   1 
ATOM   819  N  ND2   . ASN A 1 126 ? 141.865 129.134 125.927 1.00 53.13  ? 100 ASN A ND2   1 
ATOM   820  N  N     . GLN A 1 127 ? 146.961 131.659 125.583 1.00 52.78  ? 101 GLN A N     1 
ATOM   821  C  CA    . GLN A 1 127 ? 147.911 132.568 124.960 1.00 50.68  ? 101 GLN A CA    1 
ATOM   822  C  C     . GLN A 1 127 ? 149.282 131.941 124.745 1.00 51.58  ? 101 GLN A C     1 
ATOM   823  O  O     . GLN A 1 127 ? 150.116 132.547 124.064 1.00 54.08  ? 101 GLN A O     1 
ATOM   824  C  CB    . GLN A 1 127 ? 148.050 133.841 125.799 1.00 53.33  ? 101 GLN A CB    1 
ATOM   825  C  CG    . GLN A 1 127 ? 148.681 133.629 127.161 1.00 53.38  ? 101 GLN A CG    1 
ATOM   826  C  CD    . GLN A 1 127 ? 148.660 134.883 128.012 1.00 58.56  ? 101 GLN A CD    1 
ATOM   827  O  OE1   . GLN A 1 127 ? 149.706 135.383 128.427 1.00 57.63  ? 101 GLN A OE1   1 
ATOM   828  N  NE2   . GLN A 1 127 ? 147.465 135.399 128.277 1.00 54.34  ? 101 GLN A NE2   1 
ATOM   829  N  N     . VAL A 1 128 ? 149.542 130.757 125.302 1.00 51.40  ? 102 VAL A N     1 
ATOM   830  C  CA    . VAL A 1 128 ? 150.829 130.087 125.130 1.00 53.81  ? 102 VAL A CA    1 
ATOM   831  C  C     . VAL A 1 128 ? 150.621 128.654 124.655 1.00 54.16  ? 102 VAL A C     1 
ATOM   832  O  O     . VAL A 1 128 ? 151.564 127.855 124.655 1.00 57.35  ? 102 VAL A O     1 
ATOM   833  C  CB    . VAL A 1 128 ? 151.656 130.099 126.431 1.00 53.56  ? 102 VAL A CB    1 
ATOM   834  C  CG1   . VAL A 1 128 ? 152.085 131.513 126.806 1.00 50.22  ? 102 VAL A CG1   1 
ATOM   835  C  CG2   . VAL A 1 128 ? 150.884 129.439 127.562 1.00 50.15  ? 102 VAL A CG2   1 
ATOM   836  N  N     . SER A 1 129 ? 149.388 128.315 124.261 1.00 50.67  ? 103 SER A N     1 
ATOM   837  C  CA    . SER A 1 129 ? 149.086 126.938 123.872 1.00 51.57  ? 103 SER A CA    1 
ATOM   838  C  C     . SER A 1 129 ? 149.731 126.575 122.541 1.00 55.93  ? 103 SER A C     1 
ATOM   839  O  O     . SER A 1 129 ? 150.233 125.458 122.370 1.00 55.15  ? 103 SER A O     1 
ATOM   840  C  CB    . SER A 1 129 ? 147.574 126.725 123.803 1.00 49.55  ? 103 SER A CB    1 
ATOM   841  O  OG    . SER A 1 129 ? 146.960 127.685 122.964 1.00 57.85  ? 103 SER A OG    1 
ATOM   842  N  N     . LYS A 1 130 ? 149.731 127.503 121.587 1.00 48.72  ? 104 LYS A N     1 
ATOM   843  C  CA    . LYS A 1 130 ? 150.308 127.243 120.275 1.00 49.70  ? 104 LYS A CA    1 
ATOM   844  C  C     . LYS A 1 130 ? 151.806 127.504 120.217 1.00 54.84  ? 104 LYS A C     1 
ATOM   845  O  O     . LYS A 1 130 ? 152.419 127.261 119.172 1.00 58.59  ? 104 LYS A O     1 
ATOM   846  C  CB    . LYS A 1 130 ? 149.586 128.076 119.214 1.00 47.50  ? 104 LYS A CB    1 
ATOM   847  C  CG    . LYS A 1 130 ? 148.212 127.534 118.860 1.00 46.64  ? 104 LYS A CG    1 
ATOM   848  C  CD    . LYS A 1 130 ? 147.264 128.633 118.423 1.00 53.40  ? 104 LYS A CD    1 
ATOM   849  C  CE    . LYS A 1 130 ? 146.022 128.047 117.773 1.00 53.88  ? 104 LYS A CE    1 
ATOM   850  N  NZ    . LYS A 1 130 ? 144.874 127.985 118.719 1.00 52.81  ? 104 LYS A NZ    1 
ATOM   851  N  N     . MET A 1 131 ? 152.407 127.987 121.299 1.00 54.80  ? 105 MET A N     1 
ATOM   852  C  CA    . MET A 1 131 ? 153.849 128.161 121.385 1.00 51.11  ? 105 MET A CA    1 
ATOM   853  C  C     . MET A 1 131 ? 154.448 127.047 122.230 1.00 56.26  ? 105 MET A C     1 
ATOM   854  O  O     . MET A 1 131 ? 153.803 126.537 123.150 1.00 57.32  ? 105 MET A O     1 
ATOM   855  C  CB    . MET A 1 131 ? 154.210 129.517 121.992 1.00 51.74  ? 105 MET A CB    1 
ATOM   856  C  CG    . MET A 1 131 ? 153.448 130.695 121.419 1.00 56.71  ? 105 MET A CG    1 
ATOM   857  S  SD    . MET A 1 131 ? 153.032 131.898 122.693 1.00 66.83  ? 105 MET A SD    1 
ATOM   858  C  CE    . MET A 1 131 ? 152.921 133.399 121.728 1.00 52.89  ? 105 MET A CE    1 
ATOM   859  N  N     . ASN A 1 132 ? 155.685 126.669 121.912 1.00 66.15  ? 106 ASN A N     1 
ATOM   860  C  CA    . ASN A 1 132 ? 156.399 125.692 122.723 1.00 62.91  ? 106 ASN A CA    1 
ATOM   861  C  C     . ASN A 1 132 ? 156.856 126.352 124.017 1.00 63.66  ? 106 ASN A C     1 
ATOM   862  O  O     . ASN A 1 132 ? 157.899 127.013 124.055 1.00 59.31  ? 106 ASN A O     1 
ATOM   863  C  CB    . ASN A 1 132 ? 157.587 125.109 121.956 1.00 59.77  ? 106 ASN A CB    1 
ATOM   864  C  CG    . ASN A 1 132 ? 157.562 123.594 121.912 1.00 62.68  ? 106 ASN A CG    1 
ATOM   865  O  OD1   . ASN A 1 132 ? 156.496 122.982 121.856 1.00 59.94  ? 106 ASN A OD1   1 
ATOM   866  N  ND2   . ASN A 1 132 ? 158.739 122.981 121.936 1.00 62.91  ? 106 ASN A ND2   1 
ATOM   867  N  N     . PHE A 1 133 ? 156.073 126.179 125.080 1.00 50.46  ? 107 PHE A N     1 
ATOM   868  C  CA    . PHE A 1 133 ? 156.266 126.896 126.326 1.00 47.34  ? 107 PHE A CA    1 
ATOM   869  C  C     . PHE A 1 133 ? 156.337 125.916 127.489 1.00 49.79  ? 107 PHE A C     1 
ATOM   870  O  O     . PHE A 1 133 ? 155.607 124.917 127.503 1.00 49.01  ? 107 PHE A O     1 
ATOM   871  C  CB    . PHE A 1 133 ? 155.113 127.889 126.545 1.00 44.36  ? 107 PHE A CB    1 
ATOM   872  C  CG    . PHE A 1 133 ? 155.365 128.892 127.631 1.00 45.21  ? 107 PHE A CG    1 
ATOM   873  C  CD1   . PHE A 1 133 ? 156.116 130.030 127.379 1.00 47.41  ? 107 PHE A CD1   1 
ATOM   874  C  CD2   . PHE A 1 133 ? 154.838 128.706 128.899 1.00 40.66  ? 107 PHE A CD2   1 
ATOM   875  C  CE1   . PHE A 1 133 ? 156.344 130.960 128.376 1.00 44.69  ? 107 PHE A CE1   1 
ATOM   876  C  CE2   . PHE A 1 133 ? 155.063 129.631 129.900 1.00 41.26  ? 107 PHE A CE2   1 
ATOM   877  C  CZ    . PHE A 1 133 ? 155.817 130.759 129.638 1.00 45.55  ? 107 PHE A CZ    1 
ATOM   878  N  N     . PRO A 1 134 ? 157.213 126.163 128.475 1.00 52.89  ? 108 PRO A N     1 
ATOM   879  C  CA    . PRO A 1 134 ? 157.193 125.347 129.699 1.00 45.42  ? 108 PRO A CA    1 
ATOM   880  C  C     . PRO A 1 134 ? 155.980 125.669 130.557 1.00 41.23  ? 108 PRO A C     1 
ATOM   881  O  O     . PRO A 1 134 ? 155.922 126.722 131.197 1.00 48.12  ? 108 PRO A O     1 
ATOM   882  C  CB    . PRO A 1 134 ? 158.506 125.721 130.398 1.00 38.04  ? 108 PRO A CB    1 
ATOM   883  C  CG    . PRO A 1 134 ? 158.889 127.045 129.830 1.00 35.79  ? 108 PRO A CG    1 
ATOM   884  C  CD    . PRO A 1 134 ? 158.358 127.090 128.434 1.00 37.36  ? 108 PRO A CD    1 
ATOM   885  N  N     . LEU A 1 135 ? 155.006 124.757 130.586 1.00 28.92  ? 109 LEU A N     1 
ATOM   886  C  CA    . LEU A 1 135 ? 153.693 125.092 131.126 1.00 29.59  ? 109 LEU A CA    1 
ATOM   887  C  C     . LEU A 1 135 ? 153.675 125.120 132.650 1.00 36.95  ? 109 LEU A C     1 
ATOM   888  O  O     . LEU A 1 135 ? 152.750 125.688 133.241 1.00 41.92  ? 109 LEU A O     1 
ATOM   889  C  CB    . LEU A 1 135 ? 152.648 124.104 130.607 1.00 35.10  ? 109 LEU A CB    1 
ATOM   890  C  CG    . LEU A 1 135 ? 152.091 124.386 129.212 1.00 41.91  ? 109 LEU A CG    1 
ATOM   891  C  CD1   . LEU A 1 135 ? 151.461 123.136 128.619 1.00 38.89  ? 109 LEU A CD1   1 
ATOM   892  C  CD2   . LEU A 1 135 ? 151.095 125.529 129.251 1.00 42.31  ? 109 LEU A CD2   1 
ATOM   893  N  N     . SER A 1 136 ? 154.674 124.527 133.304 1.00 34.00  ? 110 SER A N     1 
ATOM   894  C  CA    . SER A 1 136 ? 154.653 124.446 134.759 1.00 25.33  ? 110 SER A CA    1 
ATOM   895  C  C     . SER A 1 136 ? 155.119 125.727 135.439 1.00 31.42  ? 110 SER A C     1 
ATOM   896  O  O     . SER A 1 136 ? 155.008 125.828 136.664 1.00 42.08  ? 110 SER A O     1 
ATOM   897  C  CB    . SER A 1 136 ? 155.509 123.268 135.234 1.00 27.91  ? 110 SER A CB    1 
ATOM   898  O  OG    . SER A 1 136 ? 156.800 123.300 134.656 1.00 30.36  ? 110 SER A OG    1 
ATOM   899  N  N     . ILE A 1 137 ? 155.628 126.709 134.685 1.00 35.34  ? 111 ILE A N     1 
ATOM   900  C  CA    . ILE A 1 137 ? 156.150 127.932 135.285 1.00 26.45  ? 111 ILE A CA    1 
ATOM   901  C  C     . ILE A 1 137 ? 155.146 129.076 135.273 1.00 28.26  ? 111 ILE A C     1 
ATOM   902  O  O     . ILE A 1 137 ? 155.456 130.157 135.795 1.00 43.73  ? 111 ILE A O     1 
ATOM   903  C  CB    . ILE A 1 137 ? 157.451 128.383 134.585 1.00 30.24  ? 111 ILE A CB    1 
ATOM   904  C  CG1   . ILE A 1 137 ? 157.147 129.016 133.224 1.00 31.48  ? 111 ILE A CG1   1 
ATOM   905  C  CG2   . ILE A 1 137 ? 158.408 127.216 134.439 1.00 22.52  ? 111 ILE A CG2   1 
ATOM   906  C  CD1   . ILE A 1 137 ? 158.331 129.706 132.594 1.00 31.88  ? 111 ILE A CD1   1 
ATOM   907  N  N     . ILE A 1 138 ? 153.965 128.881 134.692 1.00 24.43  ? 112 ILE A N     1 
ATOM   908  C  CA    . ILE A 1 138 ? 152.911 129.900 134.675 1.00 25.35  ? 112 ILE A CA    1 
ATOM   909  C  C     . ILE A 1 138 ? 152.428 130.252 136.089 1.00 26.62  ? 112 ILE A C     1 
ATOM   910  O  O     . ILE A 1 138 ? 152.446 131.454 136.431 1.00 35.53  ? 112 ILE A O     1 
ATOM   911  C  CB    . ILE A 1 138 ? 151.757 129.486 133.736 1.00 28.95  ? 112 ILE A CB    1 
ATOM   912  C  CG1   . ILE A 1 138 ? 152.243 129.407 132.288 1.00 34.49  ? 112 ILE A CG1   1 
ATOM   913  C  CG2   . ILE A 1 138 ? 150.582 130.442 133.859 1.00 29.36  ? 112 ILE A CG2   1 
ATOM   914  C  CD1   . ILE A 1 138 ? 151.303 128.664 131.373 1.00 30.50  ? 112 ILE A CD1   1 
ATOM   915  N  N     . PRO A 1 139 ? 152.045 129.298 136.973 1.00 34.38  ? 113 PRO A N     1 
ATOM   916  C  CA    . PRO A 1 139 ? 151.725 129.722 138.347 1.00 27.41  ? 113 PRO A CA    1 
ATOM   917  C  C     . PRO A 1 139 ? 152.929 130.231 139.121 1.00 25.78  ? 113 PRO A C     1 
ATOM   918  O  O     . PRO A 1 139 ? 152.761 131.043 140.037 1.00 36.12  ? 113 PRO A O     1 
ATOM   919  C  CB    . PRO A 1 139 ? 151.143 128.449 138.973 1.00 29.84  ? 113 PRO A CB    1 
ATOM   920  C  CG    . PRO A 1 139 ? 151.801 127.370 138.274 1.00 24.07  ? 113 PRO A CG    1 
ATOM   921  C  CD    . PRO A 1 139 ? 151.839 127.831 136.864 1.00 27.64  ? 113 PRO A CD    1 
ATOM   922  N  N     . THR A 1 140 ? 154.142 129.814 138.746 1.00 20.63  ? 114 THR A N     1 
ATOM   923  C  CA    . THR A 1 140 ? 155.341 130.287 139.429 1.00 21.67  ? 114 THR A CA    1 
ATOM   924  C  C     . THR A 1 140 ? 155.604 131.765 139.153 1.00 26.57  ? 114 THR A C     1 
ATOM   925  O  O     . THR A 1 140 ? 155.954 132.516 140.071 1.00 33.94  ? 114 THR A O     1 
ATOM   926  C  CB    . THR A 1 140 ? 156.543 129.436 139.022 1.00 26.57  ? 114 THR A CB    1 
ATOM   927  O  OG1   . THR A 1 140 ? 156.162 128.056 139.009 1.00 36.80  ? 114 THR A OG1   1 
ATOM   928  C  CG2   . THR A 1 140 ? 157.686 129.622 140.007 1.00 26.53  ? 114 THR A CG2   1 
ATOM   929  N  N     . TYR A 1 141 ? 155.425 132.216 137.906 1.00 26.98  ? 115 TYR A N     1 
ATOM   930  C  CA    . TYR A 1 141 ? 155.621 133.642 137.648 1.00 24.64  ? 115 TYR A CA    1 
ATOM   931  C  C     . TYR A 1 141 ? 154.445 134.465 138.161 1.00 28.72  ? 115 TYR A C     1 
ATOM   932  O  O     . TYR A 1 141 ? 154.638 135.626 138.556 1.00 38.64  ? 115 TYR A O     1 
ATOM   933  C  CB    . TYR A 1 141 ? 155.924 133.900 136.156 1.00 28.43  ? 115 TYR A CB    1 
ATOM   934  C  CG    . TYR A 1 141 ? 154.771 134.159 135.189 1.00 28.83  ? 115 TYR A CG    1 
ATOM   935  C  CD1   . TYR A 1 141 ? 154.213 135.431 135.030 1.00 28.29  ? 115 TYR A CD1   1 
ATOM   936  C  CD2   . TYR A 1 141 ? 154.304 133.145 134.372 1.00 27.02  ? 115 TYR A CD2   1 
ATOM   937  C  CE1   . TYR A 1 141 ? 153.183 135.655 134.138 1.00 31.31  ? 115 TYR A CE1   1 
ATOM   938  C  CE2   . TYR A 1 141 ? 153.277 133.360 133.474 1.00 25.58  ? 115 TYR A CE2   1 
ATOM   939  C  CZ    . TYR A 1 141 ? 152.723 134.615 133.360 1.00 33.33  ? 115 TYR A CZ    1 
ATOM   940  O  OH    . TYR A 1 141 ? 151.705 134.828 132.463 1.00 39.98  ? 115 TYR A OH    1 
ATOM   941  N  N     . ILE A 1 142 ? 153.238 133.879 138.200 1.00 26.68  ? 116 ILE A N     1 
ATOM   942  C  CA    . ILE A 1 142 ? 152.116 134.566 138.847 1.00 23.75  ? 116 ILE A CA    1 
ATOM   943  C  C     . ILE A 1 142 ? 152.386 134.756 140.345 1.00 29.54  ? 116 ILE A C     1 
ATOM   944  O  O     . ILE A 1 142 ? 152.071 135.807 140.919 1.00 40.92  ? 116 ILE A O     1 
ATOM   945  C  CB    . ILE A 1 142 ? 150.800 133.807 138.572 1.00 32.42  ? 116 ILE A CB    1 
ATOM   946  C  CG1   . ILE A 1 142 ? 150.436 133.904 137.089 1.00 29.80  ? 116 ILE A CG1   1 
ATOM   947  C  CG2   . ILE A 1 142 ? 149.644 134.356 139.390 1.00 31.02  ? 116 ILE A CG2   1 
ATOM   948  C  CD1   . ILE A 1 142 ? 150.127 135.307 136.612 1.00 26.26  ? 116 ILE A CD1   1 
ATOM   949  N  N     . VAL A 1 143 ? 153.025 133.771 140.984 1.00 25.48  ? 117 VAL A N     1 
ATOM   950  C  CA    . VAL A 1 143 ? 153.413 133.898 142.390 1.00 23.35  ? 117 VAL A CA    1 
ATOM   951  C  C     . VAL A 1 143 ? 154.550 134.913 142.560 1.00 20.93  ? 117 VAL A C     1 
ATOM   952  O  O     . VAL A 1 143 ? 154.548 135.719 143.504 1.00 38.38  ? 117 VAL A O     1 
ATOM   953  C  CB    . VAL A 1 143 ? 153.770 132.503 142.949 1.00 30.28  ? 117 VAL A CB    1 
ATOM   954  C  CG1   . VAL A 1 143 ? 154.654 132.575 144.187 1.00 24.19  ? 117 VAL A CG1   1 
ATOM   955  C  CG2   . VAL A 1 143 ? 152.502 131.725 143.269 1.00 23.83  ? 117 VAL A CG2   1 
ATOM   956  N  N     . THR A 1 144 ? 155.519 134.917 141.635 1.00 11.75  ? 118 THR A N     1 
ATOM   957  C  CA    . THR A 1 144 ? 156.663 135.829 141.728 1.00 27.74  ? 118 THR A CA    1 
ATOM   958  C  C     . THR A 1 144 ? 156.253 137.292 141.560 1.00 25.33  ? 118 THR A C     1 
ATOM   959  O  O     . THR A 1 144 ? 156.895 138.192 142.136 1.00 35.77  ? 118 THR A O     1 
ATOM   960  C  CB    . THR A 1 144 ? 157.715 135.451 140.682 1.00 23.04  ? 118 THR A CB    1 
ATOM   961  O  OG1   . THR A 1 144 ? 157.743 134.028 140.522 1.00 29.66  ? 118 THR A OG1   1 
ATOM   962  C  CG2   . THR A 1 144 ? 159.095 135.929 141.104 1.00 23.40  ? 118 THR A CG2   1 
ATOM   963  N  N     . SER A 1 145 ? 155.176 137.540 140.803 1.00 22.48  ? 119 SER A N     1 
ATOM   964  C  CA    . SER A 1 145 ? 154.647 138.896 140.657 1.00 19.68  ? 119 SER A CA    1 
ATOM   965  C  C     . SER A 1 145 ? 154.157 139.474 141.987 1.00 31.40  ? 119 SER A C     1 
ATOM   966  O  O     . SER A 1 145 ? 154.173 140.694 142.183 1.00 37.16  ? 119 SER A O     1 
ATOM   967  C  CB    . SER A 1 145 ? 153.522 138.904 139.620 1.00 19.15  ? 119 SER A CB    1 
ATOM   968  O  OG    . SER A 1 145 ? 152.494 137.996 139.969 1.00 29.01  ? 119 SER A OG    1 
ATOM   969  N  N     . ARG A 1 146 ? 153.725 138.619 142.914 1.00 29.42  ? 120 ARG A N     1 
ATOM   970  C  CA    . ARG A 1 146 ? 153.401 139.059 144.268 1.00 17.86  ? 120 ARG A CA    1 
ATOM   971  C  C     . ARG A 1 146 ? 154.603 138.995 145.202 1.00 25.37  ? 120 ARG A C     1 
ATOM   972  O  O     . ARG A 1 146 ? 154.660 139.735 146.200 1.00 36.04  ? 120 ARG A O     1 
ATOM   973  C  CB    . ARG A 1 146 ? 152.257 138.212 144.832 1.00 29.21  ? 120 ARG A CB    1 
ATOM   974  C  CG    . ARG A 1 146 ? 150.946 138.337 144.066 1.00 27.71  ? 120 ARG A CG    1 
ATOM   975  C  CD    . ARG A 1 146 ? 150.583 139.794 143.822 1.00 30.41  ? 120 ARG A CD    1 
ATOM   976  N  NE    . ARG A 1 146 ? 149.275 139.944 143.198 1.00 32.29  ? 120 ARG A NE    1 
ATOM   977  C  CZ    . ARG A 1 146 ? 148.587 141.077 143.167 1.00 36.12  ? 120 ARG A CZ    1 
ATOM   978  N  NH1   . ARG A 1 146 ? 149.060 142.188 143.707 1.00 34.69  ? 120 ARG A NH1   1 
ATOM   979  N  NH2   . ARG A 1 146 ? 147.394 141.097 142.580 1.00 31.06  ? 120 ARG A NH2   1 
ATOM   980  N  N     . PHE A 1 147 ? 155.564 138.122 144.887 1.00 26.60  ? 121 PHE A N     1 
ATOM   981  C  CA    . PHE A 1 147 ? 156.784 138.019 145.682 1.00 15.91  ? 121 PHE A CA    1 
ATOM   982  C  C     . PHE A 1 147 ? 157.622 139.291 145.616 1.00 21.87  ? 121 PHE A C     1 
ATOM   983  O  O     . PHE A 1 147 ? 158.330 139.612 146.581 1.00 36.88  ? 121 PHE A O     1 
ATOM   984  C  CB    . PHE A 1 147 ? 157.607 136.821 145.219 1.00 22.57  ? 121 PHE A CB    1 
ATOM   985  C  CG    . PHE A 1 147 ? 158.736 136.469 146.139 1.00 27.54  ? 121 PHE A CG    1 
ATOM   986  C  CD1   . PHE A 1 147 ? 158.491 136.137 147.462 1.00 24.83  ? 121 PHE A CD1   1 
ATOM   987  C  CD2   . PHE A 1 147 ? 160.044 136.468 145.680 1.00 26.66  ? 121 PHE A CD2   1 
ATOM   988  C  CE1   . PHE A 1 147 ? 159.530 135.812 148.311 1.00 27.42  ? 121 PHE A CE1   1 
ATOM   989  C  CE2   . PHE A 1 147 ? 161.088 136.142 146.524 1.00 25.72  ? 121 PHE A CE2   1 
ATOM   990  C  CZ    . PHE A 1 147 ? 160.829 135.814 147.839 1.00 27.65  ? 121 PHE A CZ    1 
ATOM   991  N  N     . TYR A 1 148 ? 157.560 140.016 144.492 1.00 24.66  ? 122 TYR A N     1 
ATOM   992  C  CA    . TYR A 1 148 ? 158.246 141.310 144.391 1.00 27.06  ? 122 TYR A CA    1 
ATOM   993  C  C     . TYR A 1 148 ? 157.727 142.307 145.430 1.00 31.29  ? 122 TYR A C     1 
ATOM   994  O  O     . TYR A 1 148 ? 158.510 142.964 146.140 1.00 26.77  ? 122 TYR A O     1 
ATOM   995  C  CB    . TYR A 1 148 ? 158.074 141.887 142.987 1.00 28.04  ? 122 TYR A CB    1 
ATOM   996  C  CG    . TYR A 1 148 ? 158.886 141.204 141.916 1.00 33.64  ? 122 TYR A CG    1 
ATOM   997  C  CD1   . TYR A 1 148 ? 160.207 140.841 142.145 1.00 30.17  ? 122 TYR A CD1   1 
ATOM   998  C  CD2   . TYR A 1 148 ? 158.334 140.931 140.669 1.00 29.44  ? 122 TYR A CD2   1 
ATOM   999  C  CE1   . TYR A 1 148 ? 160.954 140.217 141.164 1.00 30.04  ? 122 TYR A CE1   1 
ATOM   1000 C  CE2   . TYR A 1 148 ? 159.072 140.308 139.684 1.00 26.44  ? 122 TYR A CE2   1 
ATOM   1001 C  CZ    . TYR A 1 148 ? 160.382 139.955 139.937 1.00 26.78  ? 122 TYR A CZ    1 
ATOM   1002 O  OH    . TYR A 1 148 ? 161.123 139.336 138.961 1.00 36.66  ? 122 TYR A OH    1 
ATOM   1003 N  N     . GLY A 1 149 ? 156.400 142.419 145.539 1.00 27.75  ? 123 GLY A N     1 
ATOM   1004 C  CA    . GLY A 1 149 ? 155.812 143.296 146.536 1.00 18.09  ? 123 GLY A CA    1 
ATOM   1005 C  C     . GLY A 1 149 ? 156.059 142.820 147.953 1.00 27.98  ? 123 GLY A C     1 
ATOM   1006 O  O     . GLY A 1 149 ? 156.184 143.632 148.875 1.00 39.83  ? 123 GLY A O     1 
ATOM   1007 N  N     . HIS A 1 150 ? 156.140 141.496 148.143 1.00 26.46  ? 124 HIS A N     1 
ATOM   1008 C  CA    . HIS A 1 150 ? 156.510 140.952 149.450 1.00 23.47  ? 124 HIS A CA    1 
ATOM   1009 C  C     . HIS A 1 150 ? 157.919 141.371 149.858 1.00 30.05  ? 124 HIS A C     1 
ATOM   1010 O  O     . HIS A 1 150 ? 158.157 141.731 151.016 1.00 33.32  ? 124 HIS A O     1 
ATOM   1011 C  CB    . HIS A 1 150 ? 156.412 139.430 149.443 1.00 22.99  ? 124 HIS A CB    1 
ATOM   1012 C  CG    . HIS A 1 150 ? 157.059 138.784 150.629 1.00 29.34  ? 124 HIS A CG    1 
ATOM   1013 N  ND1   . HIS A 1 150 ? 156.763 139.145 151.926 1.00 28.84  ? 124 HIS A ND1   1 
ATOM   1014 C  CD2   . HIS A 1 150 ? 157.999 137.815 150.715 1.00 30.52  ? 124 HIS A CD2   1 
ATOM   1015 C  CE1   . HIS A 1 150 ? 157.486 138.420 152.759 1.00 28.68  ? 124 HIS A CE1   1 
ATOM   1016 N  NE2   . HIS A 1 150 ? 158.245 137.604 152.050 1.00 31.06  ? 124 HIS A NE2   1 
ATOM   1017 N  N     . LEU A 1 151 ? 158.868 141.317 148.916 1.00 30.71  ? 125 LEU A N     1 
ATOM   1018 C  CA    . LEU A 1 151 ? 160.243 141.719 149.212 1.00 28.11  ? 125 LEU A CA    1 
ATOM   1019 C  C     . LEU A 1 151 ? 160.335 143.208 149.535 1.00 30.95  ? 125 LEU A C     1 
ATOM   1020 O  O     . LEU A 1 151 ? 161.049 143.606 150.471 1.00 38.33  ? 125 LEU A O     1 
ATOM   1021 C  CB    . LEU A 1 151 ? 161.159 141.372 148.039 1.00 34.40  ? 125 LEU A CB    1 
ATOM   1022 C  CG    . LEU A 1 151 ? 161.431 139.890 147.777 1.00 33.63  ? 125 LEU A CG    1 
ATOM   1023 C  CD1   . LEU A 1 151 ? 162.157 139.714 146.454 1.00 32.71  ? 125 LEU A CD1   1 
ATOM   1024 C  CD2   . LEU A 1 151 ? 162.219 139.268 148.917 1.00 31.50  ? 125 LEU A CD2   1 
ATOM   1025 N  N     . GLY A 1 152 ? 159.604 144.040 148.782 1.00 28.73  ? 126 GLY A N     1 
ATOM   1026 C  CA    . GLY A 1 152 ? 159.580 145.469 149.080 1.00 23.47  ? 126 GLY A CA    1 
ATOM   1027 C  C     . GLY A 1 152 ? 158.972 145.785 150.437 1.00 27.27  ? 126 GLY A C     1 
ATOM   1028 O  O     . GLY A 1 152 ? 159.499 146.612 151.196 1.00 31.34  ? 126 GLY A O     1 
ATOM   1029 N  N     . LEU A 1 153 ? 157.867 145.106 150.770 1.00 30.75  ? 127 LEU A N     1 
ATOM   1030 C  CA    . LEU A 1 153 ? 157.226 145.293 152.067 1.00 26.13  ? 127 LEU A CA    1 
ATOM   1031 C  C     . LEU A 1 153 ? 158.121 144.824 153.209 1.00 31.49  ? 127 LEU A C     1 
ATOM   1032 O  O     . LEU A 1 153 ? 158.166 145.463 154.263 1.00 37.99  ? 127 LEU A O     1 
ATOM   1033 C  CB    . LEU A 1 153 ? 155.886 144.555 152.097 1.00 30.44  ? 127 LEU A CB    1 
ATOM   1034 C  CG    . LEU A 1 153 ? 155.059 144.635 153.383 1.00 34.38  ? 127 LEU A CG    1 
ATOM   1035 C  CD1   . LEU A 1 153 ? 154.812 146.080 153.786 1.00 28.11  ? 127 LEU A CD1   1 
ATOM   1036 C  CD2   . LEU A 1 153 ? 153.747 143.888 153.225 1.00 28.13  ? 127 LEU A CD2   1 
ATOM   1037 N  N     . LEU A 1 154 ? 158.848 143.719 153.014 1.00 36.11  ? 128 LEU A N     1 
ATOM   1038 C  CA    . LEU A 1 154 ? 159.744 143.219 154.055 1.00 31.64  ? 128 LEU A CA    1 
ATOM   1039 C  C     . LEU A 1 154 ? 160.914 144.168 154.294 1.00 31.10  ? 128 LEU A C     1 
ATOM   1040 O  O     . LEU A 1 154 ? 161.334 144.369 155.444 1.00 35.82  ? 128 LEU A O     1 
ATOM   1041 C  CB    . LEU A 1 154 ? 160.247 141.824 153.684 1.00 32.20  ? 128 LEU A CB    1 
ATOM   1042 C  CG    . LEU A 1 154 ? 161.129 141.116 154.714 1.00 32.33  ? 128 LEU A CG    1 
ATOM   1043 C  CD1   . LEU A 1 154 ? 160.362 140.873 156.001 1.00 31.74  ? 128 LEU A CD1   1 
ATOM   1044 C  CD2   . LEU A 1 154 ? 161.663 139.813 154.152 1.00 33.72  ? 128 LEU A CD2   1 
ATOM   1045 N  N     . LEU A 1 155 ? 161.447 144.766 153.220 1.00 33.80  ? 129 LEU A N     1 
ATOM   1046 C  CA    . LEU A 1 155 ? 162.495 145.775 153.377 1.00 37.27  ? 129 LEU A CA    1 
ATOM   1047 C  C     . LEU A 1 155 ? 161.986 146.998 154.138 1.00 41.53  ? 129 LEU A C     1 
ATOM   1048 O  O     . LEU A 1 155 ? 162.678 147.516 155.030 1.00 40.76  ? 129 LEU A O     1 
ATOM   1049 C  CB    . LEU A 1 155 ? 163.040 146.182 152.009 1.00 39.97  ? 129 LEU A CB    1 
ATOM   1050 C  CG    . LEU A 1 155 ? 164.212 147.166 152.020 1.00 42.41  ? 129 LEU A CG    1 
ATOM   1051 C  CD1   . LEU A 1 155 ? 165.477 146.493 152.530 1.00 34.76  ? 129 LEU A CD1   1 
ATOM   1052 C  CD2   . LEU A 1 155 ? 164.434 147.751 150.636 1.00 39.55  ? 129 LEU A CD2   1 
ATOM   1053 N  N     . LEU A 1 156 ? 160.763 147.450 153.826 1.00 39.34  ? 130 LEU A N     1 
ATOM   1054 C  CA    . LEU A 1 156 ? 160.185 148.571 154.568 1.00 31.31  ? 130 LEU A CA    1 
ATOM   1055 C  C     . LEU A 1 156 ? 159.906 148.211 156.023 1.00 35.53  ? 130 LEU A C     1 
ATOM   1056 O  O     . LEU A 1 156 ? 160.019 149.064 156.907 1.00 40.17  ? 130 LEU A O     1 
ATOM   1057 C  CB    . LEU A 1 156 ? 158.902 149.056 153.905 1.00 38.48  ? 130 LEU A CB    1 
ATOM   1058 C  CG    . LEU A 1 156 ? 159.019 149.760 152.563 1.00 41.50  ? 130 LEU A CG    1 
ATOM   1059 C  CD1   . LEU A 1 156 ? 157.646 149.816 151.962 1.00 43.05  ? 130 LEU A CD1   1 
ATOM   1060 C  CD2   . LEU A 1 156 ? 159.596 151.152 152.731 1.00 37.47  ? 130 LEU A CD2   1 
ATOM   1061 N  N     . VAL A 1 157 ? 159.535 146.956 156.288 1.00 37.76  ? 131 VAL A N     1 
ATOM   1062 C  CA    . VAL A 1 157 ? 159.265 146.514 157.654 1.00 32.75  ? 131 VAL A CA    1 
ATOM   1063 C  C     . VAL A 1 157 ? 160.550 146.505 158.481 1.00 35.03  ? 131 VAL A C     1 
ATOM   1064 O  O     . VAL A 1 157 ? 160.558 146.940 159.641 1.00 35.83  ? 131 VAL A O     1 
ATOM   1065 C  CB    . VAL A 1 157 ? 158.568 145.137 157.625 1.00 35.85  ? 131 VAL A CB    1 
ATOM   1066 C  CG1   . VAL A 1 157 ? 158.760 144.365 158.923 1.00 34.50  ? 131 VAL A CG1   1 
ATOM   1067 C  CG2   . VAL A 1 157 ? 157.084 145.305 157.342 1.00 28.09  ? 131 VAL A CG2   1 
ATOM   1068 N  N     . ILE A 1 158 ? 161.659 146.050 157.886 1.00 40.14  ? 132 ILE A N     1 
ATOM   1069 C  CA    . ILE A 1 158 ? 162.952 146.066 158.576 1.00 38.32  ? 132 ILE A CA    1 
ATOM   1070 C  C     . ILE A 1 158 ? 163.415 147.502 158.836 1.00 42.51  ? 132 ILE A C     1 
ATOM   1071 O  O     . ILE A 1 158 ? 163.908 147.827 159.930 1.00 44.54  ? 132 ILE A O     1 
ATOM   1072 C  CB    . ILE A 1 158 ? 163.985 145.255 157.767 1.00 40.60  ? 132 ILE A CB    1 
ATOM   1073 C  CG1   . ILE A 1 158 ? 163.618 143.770 157.790 1.00 41.80  ? 132 ILE A CG1   1 
ATOM   1074 C  CG2   . ILE A 1 158 ? 165.395 145.438 158.307 1.00 38.29  ? 132 ILE A CG2   1 
ATOM   1075 C  CD1   . ILE A 1 158 ? 164.412 142.926 156.823 1.00 37.43  ? 132 ILE A CD1   1 
ATOM   1076 N  N     . ILE A 1 159 ? 163.218 148.393 157.856 1.00 42.99  ? 133 ILE A N     1 
ATOM   1077 C  CA    . ILE A 1 159 ? 163.589 149.800 158.030 1.00 37.84  ? 133 ILE A CA    1 
ATOM   1078 C  C     . ILE A 1 159 ? 162.717 150.471 159.097 1.00 41.55  ? 133 ILE A C     1 
ATOM   1079 O  O     . ILE A 1 159 ? 163.204 151.275 159.903 1.00 45.08  ? 133 ILE A O     1 
ATOM   1080 C  CB    . ILE A 1 159 ? 163.525 150.526 156.669 1.00 43.55  ? 133 ILE A CB    1 
ATOM   1081 C  CG1   . ILE A 1 159 ? 164.684 150.071 155.781 1.00 43.31  ? 133 ILE A CG1   1 
ATOM   1082 C  CG2   . ILE A 1 159 ? 163.572 152.044 156.813 1.00 44.19  ? 133 ILE A CG2   1 
ATOM   1083 C  CD1   . ILE A 1 159 ? 164.488 150.380 154.319 1.00 45.69  ? 133 ILE A CD1   1 
ATOM   1084 N  N     . ALA A 1 160 ? 161.430 150.115 159.154 1.00 40.41  ? 134 ALA A N     1 
ATOM   1085 C  CA    . ALA A 1 160 ? 160.547 150.669 160.177 1.00 38.83  ? 134 ALA A CA    1 
ATOM   1086 C  C     . ALA A 1 160 ? 160.885 150.128 161.562 1.00 43.05  ? 134 ALA A C     1 
ATOM   1087 O  O     . ALA A 1 160 ? 160.726 150.832 162.566 1.00 52.10  ? 134 ALA A O     1 
ATOM   1088 C  CB    . ALA A 1 160 ? 159.089 150.370 159.830 1.00 38.19  ? 134 ALA A CB    1 
ATOM   1089 N  N     . CYS A 1 161 ? 161.346 148.877 161.638 1.00 49.44  ? 135 CYS A N     1 
ATOM   1090 C  CA    . CYS A 1 161 ? 161.802 148.325 162.908 1.00 44.30  ? 135 CYS A CA    1 
ATOM   1091 C  C     . CYS A 1 161 ? 163.112 148.948 163.369 1.00 49.95  ? 135 CYS A C     1 
ATOM   1092 O  O     . CYS A 1 161 ? 163.392 148.947 164.572 1.00 51.07  ? 135 CYS A O     1 
ATOM   1093 C  CB    . CYS A 1 161 ? 161.960 146.807 162.803 1.00 42.42  ? 135 CYS A CB    1 
ATOM   1094 S  SG    . CYS A 1 161 ? 160.410 145.881 162.852 1.00 60.69  ? 135 CYS A SG    1 
ATOM   1095 N  N     . MET A 1 162 ? 163.924 149.461 162.435 1.00 56.96  ? 136 MET A N     1 
ATOM   1096 C  CA    . MET A 1 162 ? 165.127 150.207 162.807 1.00 53.14  ? 136 MET A CA    1 
ATOM   1097 C  C     . MET A 1 162 ? 164.819 151.481 163.590 1.00 56.08  ? 136 MET A C     1 
ATOM   1098 O  O     . MET A 1 162 ? 165.651 151.916 164.392 1.00 59.07  ? 136 MET A O     1 
ATOM   1099 C  CB    . MET A 1 162 ? 165.928 150.598 161.564 1.00 53.06  ? 136 MET A CB    1 
ATOM   1100 C  CG    . MET A 1 162 ? 167.108 149.716 161.217 1.00 48.28  ? 136 MET A CG    1 
ATOM   1101 S  SD    . MET A 1 162 ? 167.350 149.714 159.430 1.00 65.30  ? 136 MET A SD    1 
ATOM   1102 C  CE    . MET A 1 162 ? 168.753 148.619 159.256 1.00 55.96  ? 136 MET A CE    1 
ATOM   1103 N  N     . PHE A 1 163 ? 163.649 152.086 163.378 1.00 57.53  ? 137 PHE A N     1 
ATOM   1104 C  CA    . PHE A 1 163 ? 163.320 153.392 163.941 1.00 55.68  ? 137 PHE A CA    1 
ATOM   1105 C  C     . PHE A 1 163 ? 162.950 153.348 165.419 1.00 58.51  ? 137 PHE A C     1 
ATOM   1106 O  O     . PHE A 1 163 ? 162.829 154.410 166.038 1.00 62.68  ? 137 PHE A O     1 
ATOM   1107 C  CB    . PHE A 1 163 ? 162.173 154.025 163.149 1.00 57.28  ? 137 PHE A CB    1 
ATOM   1108 C  CG    . PHE A 1 163 ? 162.627 154.893 162.011 1.00 59.13  ? 137 PHE A CG    1 
ATOM   1109 C  CD1   . PHE A 1 163 ? 163.416 154.372 160.995 1.00 60.05  ? 137 PHE A CD1   1 
ATOM   1110 C  CD2   . PHE A 1 163 ? 162.265 156.231 161.955 1.00 59.49  ? 137 PHE A CD2   1 
ATOM   1111 C  CE1   . PHE A 1 163 ? 163.836 155.168 159.945 1.00 60.96  ? 137 PHE A CE1   1 
ATOM   1112 C  CE2   . PHE A 1 163 ? 162.682 157.034 160.907 1.00 60.49  ? 137 PHE A CE2   1 
ATOM   1113 C  CZ    . PHE A 1 163 ? 163.469 156.501 159.901 1.00 60.82  ? 137 PHE A CZ    1 
ATOM   1114 N  N     . THR A 1 164 ? 162.758 152.163 165.998 1.00 56.72  ? 138 THR A N     1 
ATOM   1115 C  CA    . THR A 1 164 ? 162.458 152.028 167.416 1.00 56.55  ? 138 THR A CA    1 
ATOM   1116 C  C     . THR A 1 164 ? 163.684 151.713 168.259 1.00 58.12  ? 138 THR A C     1 
ATOM   1117 O  O     . THR A 1 164 ? 163.815 152.251 169.363 1.00 61.78  ? 138 THR A O     1 
ATOM   1118 C  CB    . THR A 1 164 ? 161.413 150.921 167.628 1.00 55.18  ? 138 THR A CB    1 
ATOM   1119 O  OG1   . THR A 1 164 ? 160.340 151.112 166.705 1.00 56.44  ? 138 THR A OG1   1 
ATOM   1120 C  CG2   . THR A 1 164 ? 160.846 150.951 169.041 1.00 55.07  ? 138 THR A CG2   1 
ATOM   1121 N  N     . GLY A 1 165 ? 164.596 150.894 167.747 1.00 49.87  ? 139 GLY A N     1 
ATOM   1122 C  CA    . GLY A 1 165 ? 165.711 150.369 168.511 1.00 50.55  ? 139 GLY A CA    1 
ATOM   1123 C  C     . GLY A 1 165 ? 165.978 148.908 168.245 1.00 51.93  ? 139 GLY A C     1 
ATOM   1124 O  O     . GLY A 1 165 ? 166.921 148.349 168.822 1.00 58.83  ? 139 GLY A O     1 
ATOM   1125 N  N     . ILE A 1 166 ? 165.177 148.267 167.397 1.00 44.15  ? 140 ILE A N     1 
ATOM   1126 C  CA    . ILE A 1 166 ? 165.389 146.883 166.995 1.00 45.66  ? 140 ILE A CA    1 
ATOM   1127 C  C     . ILE A 1 166 ? 166.248 146.923 165.736 1.00 43.32  ? 140 ILE A C     1 
ATOM   1128 O  O     . ILE A 1 166 ? 165.759 147.206 164.642 1.00 47.95  ? 140 ILE A O     1 
ATOM   1129 C  CB    . ILE A 1 166 ? 164.065 146.155 166.762 1.00 46.04  ? 140 ILE A CB    1 
ATOM   1130 C  CG1   . ILE A 1 166 ? 163.099 146.435 167.915 1.00 45.37  ? 140 ILE A CG1   1 
ATOM   1131 C  CG2   . ILE A 1 166 ? 164.298 144.664 166.603 1.00 44.97  ? 140 ILE A CG2   1 
ATOM   1132 C  CD1   . ILE A 1 166 ? 161.696 145.933 167.679 1.00 45.42  ? 140 ILE A CD1   1 
ATOM   1133 N  N     . TYR A 1 167 ? 167.531 146.645 165.895 1.00 47.34  ? 141 TYR A N     1 
ATOM   1134 C  CA    . TYR A 1 167 ? 168.477 146.700 164.799 1.00 47.96  ? 141 TYR A CA    1 
ATOM   1135 C  C     . TYR A 1 167 ? 168.840 145.292 164.339 1.00 50.49  ? 141 TYR A C     1 
ATOM   1136 O  O     . TYR A 1 167 ? 168.779 144.347 165.132 1.00 53.07  ? 141 TYR A O     1 
ATOM   1137 C  CB    . TYR A 1 167 ? 169.744 147.455 165.223 1.00 46.54  ? 141 TYR A CB    1 
ATOM   1138 C  CG    . TYR A 1 167 ? 169.479 148.896 165.589 1.00 48.59  ? 141 TYR A CG    1 
ATOM   1139 C  CD1   . TYR A 1 167 ? 169.135 149.826 164.616 1.00 48.39  ? 141 TYR A CD1   1 
ATOM   1140 C  CD2   . TYR A 1 167 ? 169.554 149.323 166.910 1.00 50.01  ? 141 TYR A CD2   1 
ATOM   1141 C  CE1   . TYR A 1 167 ? 168.886 151.145 164.946 1.00 51.37  ? 141 TYR A CE1   1 
ATOM   1142 C  CE2   . TYR A 1 167 ? 169.305 150.639 167.249 1.00 48.85  ? 141 TYR A CE2   1 
ATOM   1143 C  CZ    . TYR A 1 167 ? 168.971 151.545 166.263 1.00 53.41  ? 141 TYR A CZ    1 
ATOM   1144 O  OH    . TYR A 1 167 ? 168.724 152.856 166.597 1.00 54.74  ? 141 TYR A OH    1 
ATOM   1145 N  N     . PRO A 1 168 ? 169.183 145.111 163.049 1.00 41.33  ? 142 PRO A N     1 
ATOM   1146 C  CA    . PRO A 1 168 ? 169.579 143.782 162.562 1.00 37.90  ? 142 PRO A CA    1 
ATOM   1147 C  C     . PRO A 1 168 ? 170.846 143.240 163.202 1.00 42.55  ? 142 PRO A C     1 
ATOM   1148 O  O     . PRO A 1 168 ? 171.923 143.835 163.097 1.00 48.31  ? 142 PRO A O     1 
ATOM   1149 C  CB    . PRO A 1 168 ? 169.778 144.007 161.059 1.00 35.96  ? 142 PRO A CB    1 
ATOM   1150 C  CG    . PRO A 1 168 ? 168.920 145.167 160.740 1.00 39.80  ? 142 PRO A CG    1 
ATOM   1151 C  CD    . PRO A 1 168 ? 168.981 146.058 161.939 1.00 40.95  ? 142 PRO A CD    1 
ATOM   1152 N  N     . SER A 1 169 ? 170.707 142.110 163.885 1.00 39.08  ? 143 SER A N     1 
ATOM   1153 C  CA    . SER A 1 169 ? 171.825 141.389 164.468 1.00 38.20  ? 143 SER A CA    1 
ATOM   1154 C  C     . SER A 1 169 ? 172.305 140.325 163.484 1.00 36.42  ? 143 SER A C     1 
ATOM   1155 O  O     . SER A 1 169 ? 171.956 140.336 162.301 1.00 38.43  ? 143 SER A O     1 
ATOM   1156 C  CB    . SER A 1 169 ? 171.423 140.791 165.815 1.00 39.24  ? 143 SER A CB    1 
ATOM   1157 O  OG    . SER A 1 169 ? 170.336 139.896 165.674 1.00 38.08  ? 143 SER A OG    1 
ATOM   1158 N  N     . ILE A 1 170 ? 173.125 139.390 163.970 1.00 41.44  ? 144 ILE A N     1 
ATOM   1159 C  CA    . ILE A 1 170 ? 173.582 138.276 163.148 1.00 35.43  ? 144 ILE A CA    1 
ATOM   1160 C  C     . ILE A 1 170 ? 172.449 137.288 162.858 1.00 30.40  ? 144 ILE A C     1 
ATOM   1161 O  O     . ILE A 1 170 ? 172.540 136.503 161.911 1.00 38.21  ? 144 ILE A O     1 
ATOM   1162 C  CB    . ILE A 1 170 ? 174.790 137.602 163.842 1.00 37.03  ? 144 ILE A CB    1 
ATOM   1163 C  CG1   . ILE A 1 170 ? 175.582 136.698 162.886 1.00 35.37  ? 144 ILE A CG1   1 
ATOM   1164 C  CG2   . ILE A 1 170 ? 174.349 136.825 165.075 1.00 33.22  ? 144 ILE A CG2   1 
ATOM   1165 C  CD1   . ILE A 1 170 ? 175.836 137.299 161.516 1.00 34.38  ? 144 ILE A CD1   1 
ATOM   1166 N  N     . HIS A 1 171 ? 171.352 137.342 163.616 1.00 37.89  ? 145 HIS A N     1 
ATOM   1167 C  CA    . HIS A 1 171 ? 170.245 136.412 163.438 1.00 35.38  ? 145 HIS A CA    1 
ATOM   1168 C  C     . HIS A 1 171 ? 169.391 136.711 162.211 1.00 29.80  ? 145 HIS A C     1 
ATOM   1169 O  O     . HIS A 1 171 ? 168.496 135.920 161.901 1.00 40.48  ? 145 HIS A O     1 
ATOM   1170 C  CB    . HIS A 1 171 ? 169.364 136.416 164.687 1.00 28.83  ? 145 HIS A CB    1 
ATOM   1171 C  CG    . HIS A 1 171 ? 170.114 136.141 165.952 1.00 30.34  ? 145 HIS A CG    1 
ATOM   1172 N  ND1   . HIS A 1 171 ? 170.764 137.128 166.661 1.00 34.86  ? 145 HIS A ND1   1 
ATOM   1173 C  CD2   . HIS A 1 171 ? 170.321 134.991 166.635 1.00 31.78  ? 145 HIS A CD2   1 
ATOM   1174 C  CE1   . HIS A 1 171 ? 171.338 136.598 167.726 1.00 36.76  ? 145 HIS A CE1   1 
ATOM   1175 N  NE2   . HIS A 1 171 ? 171.084 135.302 167.733 1.00 31.56  ? 145 HIS A NE2   1 
ATOM   1176 N  N     . ILE A 1 172 ? 169.635 137.820 161.507 1.00 33.15  ? 146 ILE A N     1 
ATOM   1177 C  CA    . ILE A 1 172 ? 168.805 138.180 160.363 1.00 36.42  ? 146 ILE A CA    1 
ATOM   1178 C  C     . ILE A 1 172 ? 169.186 137.436 159.088 1.00 35.66  ? 146 ILE A C     1 
ATOM   1179 O  O     . ILE A 1 172 ? 168.430 137.481 158.110 1.00 42.92  ? 146 ILE A O     1 
ATOM   1180 C  CB    . ILE A 1 172 ? 168.841 139.711 160.156 1.00 37.24  ? 146 ILE A CB    1 
ATOM   1181 C  CG1   . ILE A 1 172 ? 167.514 140.209 159.564 1.00 36.33  ? 146 ILE A CG1   1 
ATOM   1182 C  CG2   . ILE A 1 172 ? 170.036 140.127 159.307 1.00 33.45  ? 146 ILE A CG2   1 
ATOM   1183 C  CD1   . ILE A 1 172 ? 167.144 141.616 159.950 1.00 38.98  ? 146 ILE A CD1   1 
ATOM   1184 N  N     . ILE A 1 173 ? 170.307 136.706 159.070 1.00 34.41  ? 147 ILE A N     1 
ATOM   1185 C  CA    . ILE A 1 173 ? 170.644 135.923 157.882 1.00 34.13  ? 147 ILE A CA    1 
ATOM   1186 C  C     . ILE A 1 173 ? 169.825 134.643 157.761 1.00 37.61  ? 147 ILE A C     1 
ATOM   1187 O  O     . ILE A 1 173 ? 169.970 133.919 156.771 1.00 41.04  ? 147 ILE A O     1 
ATOM   1188 C  CB    . ILE A 1 173 ? 172.181 135.710 157.789 1.00 37.60  ? 147 ILE A CB    1 
ATOM   1189 C  CG1   . ILE A 1 173 ? 172.889 135.068 159.017 1.00 32.44  ? 147 ILE A CG1   1 
ATOM   1190 C  CG2   . ILE A 1 173 ? 172.873 137.023 157.439 1.00 42.89  ? 147 ILE A CG2   1 
ATOM   1191 C  CD1   . ILE A 1 173 ? 172.476 133.702 159.575 1.00 33.79  ? 147 ILE A CD1   1 
ATOM   1192 N  N     . GLN A 1 174 ? 168.972 134.349 158.747 1.00 38.02  ? 148 GLN A N     1 
ATOM   1193 C  CA    . GLN A 1 174 ? 167.985 133.284 158.622 1.00 29.96  ? 148 GLN A CA    1 
ATOM   1194 C  C     . GLN A 1 174 ? 166.883 133.627 157.626 1.00 27.37  ? 148 GLN A C     1 
ATOM   1195 O  O     . GLN A 1 174 ? 166.142 132.730 157.208 1.00 38.68  ? 148 GLN A O     1 
ATOM   1196 C  CB    . GLN A 1 174 ? 167.360 132.989 159.982 1.00 29.60  ? 148 GLN A CB    1 
ATOM   1197 C  CG    . GLN A 1 174 ? 168.336 132.684 161.092 1.00 33.08  ? 148 GLN A CG    1 
ATOM   1198 C  CD    . GLN A 1 174 ? 167.645 132.547 162.433 1.00 35.53  ? 148 GLN A CD    1 
ATOM   1199 O  OE1   . GLN A 1 174 ? 167.106 131.492 162.760 1.00 36.90  ? 148 GLN A OE1   1 
ATOM   1200 N  NE2   . GLN A 1 174 ? 167.649 133.619 163.213 1.00 33.75  ? 148 GLN A NE2   1 
ATOM   1201 N  N     . LEU A 1 175 ? 166.753 134.904 157.248 1.00 28.83  ? 149 LEU A N     1 
ATOM   1202 C  CA    . LEU A 1 175 ? 165.797 135.291 156.218 1.00 29.56  ? 149 LEU A CA    1 
ATOM   1203 C  C     . LEU A 1 175 ? 166.159 134.694 154.864 1.00 32.35  ? 149 LEU A C     1 
ATOM   1204 O  O     . LEU A 1 175 ? 165.264 134.390 154.071 1.00 43.34  ? 149 LEU A O     1 
ATOM   1205 C  CB    . LEU A 1 175 ? 165.709 136.815 156.130 1.00 32.29  ? 149 LEU A CB    1 
ATOM   1206 C  CG    . LEU A 1 175 ? 164.956 137.533 157.254 1.00 34.65  ? 149 LEU A CG    1 
ATOM   1207 C  CD1   . LEU A 1 175 ? 164.688 138.982 156.881 1.00 30.03  ? 149 LEU A CD1   1 
ATOM   1208 C  CD2   . LEU A 1 175 ? 163.655 136.820 157.603 1.00 29.50  ? 149 LEU A CD2   1 
ATOM   1209 N  N     . LEU A 1 176 ? 167.452 134.445 154.622 1.00 34.52  ? 150 LEU A N     1 
ATOM   1210 C  CA    . LEU A 1 176 ? 167.902 133.768 153.408 1.00 35.01  ? 150 LEU A CA    1 
ATOM   1211 C  C     . LEU A 1 176 ? 167.414 132.325 153.320 1.00 36.26  ? 150 LEU A C     1 
ATOM   1212 O  O     . LEU A 1 176 ? 167.436 131.741 152.232 1.00 41.82  ? 150 LEU A O     1 
ATOM   1213 C  CB    . LEU A 1 176 ? 169.429 133.798 153.331 1.00 38.63  ? 150 LEU A CB    1 
ATOM   1214 C  CG    . LEU A 1 176 ? 170.088 135.151 153.062 1.00 37.79  ? 150 LEU A CG    1 
ATOM   1215 C  CD1   . LEU A 1 176 ? 171.591 134.991 152.927 1.00 37.60  ? 150 LEU A CD1   1 
ATOM   1216 C  CD2   . LEU A 1 176 ? 169.505 135.799 151.819 1.00 36.62  ? 150 LEU A CD2   1 
ATOM   1217 N  N     . ILE A 1 177 ? 166.994 131.736 154.434 1.00 37.76  ? 151 ILE A N     1 
ATOM   1218 C  CA    . ILE A 1 177 ? 166.323 130.446 154.439 1.00 36.59  ? 151 ILE A CA    1 
ATOM   1219 C  C     . ILE A 1 177 ? 164.807 130.608 154.463 1.00 34.54  ? 151 ILE A C     1 
ATOM   1220 O  O     . ILE A 1 177 ? 164.090 129.895 153.760 1.00 38.04  ? 151 ILE A O     1 
ATOM   1221 C  CB    . ILE A 1 177 ? 166.819 129.610 155.641 1.00 35.05  ? 151 ILE A CB    1 
ATOM   1222 C  CG1   . ILE A 1 177 ? 168.339 129.430 155.572 1.00 39.61  ? 151 ILE A CG1   1 
ATOM   1223 C  CG2   . ILE A 1 177 ? 166.109 128.260 155.721 1.00 34.52  ? 151 ILE A CG2   1 
ATOM   1224 C  CD1   . ILE A 1 177 ? 168.806 128.436 154.524 1.00 40.86  ? 151 ILE A CD1   1 
ATOM   1225 N  N     . TYR A 1 178 ? 164.310 131.580 155.231 1.00 30.28  ? 152 TYR A N     1 
ATOM   1226 C  CA    . TYR A 1 178 ? 162.882 131.631 155.535 1.00 26.79  ? 152 TYR A CA    1 
ATOM   1227 C  C     . TYR A 1 178 ? 162.057 132.280 154.425 1.00 26.81  ? 152 TYR A C     1 
ATOM   1228 O  O     . TYR A 1 178 ? 160.948 131.818 154.139 1.00 38.23  ? 152 TYR A O     1 
ATOM   1229 C  CB    . TYR A 1 178 ? 162.663 132.350 156.867 1.00 32.50  ? 152 TYR A CB    1 
ATOM   1230 C  CG    . TYR A 1 178 ? 163.211 131.586 158.054 1.00 25.07  ? 152 TYR A CG    1 
ATOM   1231 C  CD1   . TYR A 1 178 ? 163.294 130.197 158.032 1.00 31.29  ? 152 TYR A CD1   1 
ATOM   1232 C  CD2   . TYR A 1 178 ? 163.649 132.250 159.192 1.00 27.22  ? 152 TYR A CD2   1 
ATOM   1233 C  CE1   . TYR A 1 178 ? 163.794 129.493 159.109 1.00 29.92  ? 152 TYR A CE1   1 
ATOM   1234 C  CE2   . TYR A 1 178 ? 164.147 131.550 160.277 1.00 27.94  ? 152 TYR A CE2   1 
ATOM   1235 C  CZ    . TYR A 1 178 ? 164.221 130.175 160.227 1.00 33.48  ? 152 TYR A CZ    1 
ATOM   1236 O  OH    . TYR A 1 178 ? 164.719 129.479 161.302 1.00 43.26  ? 152 TYR A OH    1 
ATOM   1237 N  N     . VAL A 1 179 ? 162.549 133.366 153.814 1.00 30.43  ? 153 VAL A N     1 
ATOM   1238 C  CA    . VAL A 1 179 ? 161.832 133.973 152.684 1.00 36.47  ? 153 VAL A CA    1 
ATOM   1239 C  C     . VAL A 1 179 ? 161.775 133.064 151.452 1.00 30.56  ? 153 VAL A C     1 
ATOM   1240 O  O     . VAL A 1 179 ? 160.692 132.958 150.844 1.00 39.84  ? 153 VAL A O     1 
ATOM   1241 C  CB    . VAL A 1 179 ? 162.400 135.374 152.387 1.00 34.41  ? 153 VAL A CB    1 
ATOM   1242 C  CG1   . VAL A 1 179 ? 161.513 136.123 151.411 1.00 34.49  ? 153 VAL A CG1   1 
ATOM   1243 C  CG2   . VAL A 1 179 ? 162.564 136.172 153.672 1.00 21.99  ? 153 VAL A CG2   1 
ATOM   1244 N  N     . PRO A 1 180 ? 162.871 132.392 151.019 1.00 38.84  ? 154 PRO A N     1 
ATOM   1245 C  CA    . PRO A 1 180 ? 162.698 131.372 149.968 1.00 32.38  ? 154 PRO A CA    1 
ATOM   1246 C  C     . PRO A 1 180 ? 161.792 130.222 150.358 1.00 30.20  ? 154 PRO A C     1 
ATOM   1247 O  O     . PRO A 1 180 ? 161.140 129.657 149.475 1.00 36.80  ? 154 PRO A O     1 
ATOM   1248 C  CB    . PRO A 1 180 ? 164.130 130.889 149.709 1.00 24.84  ? 154 PRO A CB    1 
ATOM   1249 C  CG    . PRO A 1 180 ? 164.952 132.028 150.033 1.00 29.17  ? 154 PRO A CG    1 
ATOM   1250 C  CD    . PRO A 1 180 ? 164.321 132.592 151.254 1.00 29.03  ? 154 PRO A CD    1 
ATOM   1251 N  N     . PHE A 1 181 ? 161.722 129.864 151.644 1.00 26.49  ? 155 PHE A N     1 
ATOM   1252 C  CA    . PHE A 1 181 ? 160.785 128.828 152.069 1.00 25.53  ? 155 PHE A CA    1 
ATOM   1253 C  C     . PHE A 1 181 ? 159.339 129.265 151.864 1.00 28.93  ? 155 PHE A C     1 
ATOM   1254 O  O     . PHE A 1 181 ? 158.496 128.459 151.452 1.00 32.35  ? 155 PHE A O     1 
ATOM   1255 C  CB    . PHE A 1 181 ? 161.009 128.456 153.535 1.00 24.01  ? 155 PHE A CB    1 
ATOM   1256 C  CG    . PHE A 1 181 ? 159.931 127.574 154.083 1.00 35.51  ? 155 PHE A CG    1 
ATOM   1257 C  CD1   . PHE A 1 181 ? 159.858 126.248 153.697 1.00 33.03  ? 155 PHE A CD1   1 
ATOM   1258 C  CD2   . PHE A 1 181 ? 158.961 128.075 154.943 1.00 38.35  ? 155 PHE A CD2   1 
ATOM   1259 C  CE1   . PHE A 1 181 ? 158.860 125.435 154.172 1.00 31.80  ? 155 PHE A CE1   1 
ATOM   1260 C  CE2   . PHE A 1 181 ? 157.953 127.266 155.404 1.00 37.23  ? 155 PHE A CE2   1 
ATOM   1261 C  CZ    . PHE A 1 181 ? 157.905 125.948 155.021 1.00 35.30  ? 155 PHE A CZ    1 
ATOM   1262 N  N     . CYS A 1 182 ? 159.029 130.525 152.184 1.00 29.14  ? 156 CYS A N     1 
ATOM   1263 C  CA    . CYS A 1 182 ? 157.686 131.054 151.965 1.00 28.82  ? 156 CYS A CA    1 
ATOM   1264 C  C     . CYS A 1 182 ? 157.341 131.078 150.482 1.00 24.77  ? 156 CYS A C     1 
ATOM   1265 O  O     . CYS A 1 182 ? 156.227 130.693 150.086 1.00 32.38  ? 156 CYS A O     1 
ATOM   1266 C  CB    . CYS A 1 182 ? 157.580 132.454 152.572 1.00 32.74  ? 156 CYS A CB    1 
ATOM   1267 S  SG    . CYS A 1 182 ? 155.951 133.215 152.478 1.00 51.08  ? 156 CYS A SG    1 
ATOM   1268 N  N     . PHE A 1 183 ? 158.309 131.484 149.646 1.00 26.91  ? 157 PHE A N     1 
ATOM   1269 C  CA    . PHE A 1 183 ? 158.114 131.451 148.197 1.00 25.16  ? 157 PHE A CA    1 
ATOM   1270 C  C     . PHE A 1 183 ? 157.880 130.029 147.689 1.00 26.22  ? 157 PHE A C     1 
ATOM   1271 O  O     . PHE A 1 183 ? 157.000 129.802 146.852 1.00 31.98  ? 157 PHE A O     1 
ATOM   1272 C  CB    . PHE A 1 183 ? 159.316 132.077 147.487 1.00 22.73  ? 157 PHE A CB    1 
ATOM   1273 C  CG    . PHE A 1 183 ? 159.199 132.076 145.987 1.00 21.97  ? 157 PHE A CG    1 
ATOM   1274 C  CD1   . PHE A 1 183 ? 158.382 132.993 145.345 1.00 28.35  ? 157 PHE A CD1   1 
ATOM   1275 C  CD2   . PHE A 1 183 ? 159.897 131.154 145.220 1.00 25.40  ? 157 PHE A CD2   1 
ATOM   1276 C  CE1   . PHE A 1 183 ? 158.267 132.993 143.968 1.00 25.63  ? 157 PHE A CE1   1 
ATOM   1277 C  CE2   . PHE A 1 183 ? 159.781 131.146 143.844 1.00 29.21  ? 157 PHE A CE2   1 
ATOM   1278 C  CZ    . PHE A 1 183 ? 158.965 132.069 143.218 1.00 27.59  ? 157 PHE A CZ    1 
ATOM   1279 N  N     . PHE A 1 184 ? 158.640 129.058 148.203 1.00 31.59  ? 158 PHE A N     1 
ATOM   1280 C  CA    . PHE A 1 184 ? 158.537 127.687 147.712 1.00 22.21  ? 158 PHE A CA    1 
ATOM   1281 C  C     . PHE A 1 184 ? 157.254 127.013 148.185 1.00 27.58  ? 158 PHE A C     1 
ATOM   1282 O  O     . PHE A 1 184 ? 156.672 126.207 147.450 1.00 34.16  ? 158 PHE A O     1 
ATOM   1283 C  CB    . PHE A 1 184 ? 159.764 126.884 148.142 1.00 25.91  ? 158 PHE A CB    1 
ATOM   1284 C  CG    . PHE A 1 184 ? 161.013 127.239 147.385 1.00 34.88  ? 158 PHE A CG    1 
ATOM   1285 C  CD1   . PHE A 1 184 ? 160.940 127.700 146.079 1.00 34.60  ? 158 PHE A CD1   1 
ATOM   1286 C  CD2   . PHE A 1 184 ? 162.261 127.109 147.976 1.00 36.91  ? 158 PHE A CD2   1 
ATOM   1287 C  CE1   . PHE A 1 184 ? 162.086 128.030 145.379 1.00 35.12  ? 158 PHE A CE1   1 
ATOM   1288 C  CE2   . PHE A 1 184 ? 163.411 127.439 147.283 1.00 36.53  ? 158 PHE A CE2   1 
ATOM   1289 C  CZ    . PHE A 1 184 ? 163.322 127.899 145.982 1.00 34.35  ? 158 PHE A CZ    1 
ATOM   1290 N  N     . LEU A 1 185 ? 156.798 127.333 149.402 1.00 27.45  ? 159 LEU A N     1 
ATOM   1291 C  CA    . LEU A 1 185 ? 155.504 126.844 149.876 1.00 26.62  ? 159 LEU A CA    1 
ATOM   1292 C  C     . LEU A 1 185 ? 154.366 127.371 149.015 1.00 23.39  ? 159 LEU A C     1 
ATOM   1293 O  O     . LEU A 1 185 ? 153.486 126.603 148.592 1.00 35.70  ? 159 LEU A O     1 
ATOM   1294 C  CB    . LEU A 1 185 ? 155.283 127.246 151.336 1.00 29.88  ? 159 LEU A CB    1 
ATOM   1295 C  CG    . LEU A 1 185 ? 153.875 126.933 151.866 1.00 36.42  ? 159 LEU A CG    1 
ATOM   1296 C  CD1   . LEU A 1 185 ? 153.779 125.548 152.487 1.00 29.52  ? 159 LEU A CD1   1 
ATOM   1297 C  CD2   . LEU A 1 185 ? 153.382 127.996 152.830 1.00 32.78  ? 159 LEU A CD2   1 
ATOM   1298 N  N     . THR A 1 186 ? 154.379 128.684 148.737 1.00 26.32  ? 160 THR A N     1 
ATOM   1299 C  CA    . THR A 1 186 ? 153.346 129.276 147.890 1.00 29.93  ? 160 THR A CA    1 
ATOM   1300 C  C     . THR A 1 186 ? 153.388 128.699 146.479 1.00 22.31  ? 160 THR A C     1 
ATOM   1301 O  O     . THR A 1 186 ? 152.341 128.388 145.903 1.00 25.99  ? 160 THR A O     1 
ATOM   1302 C  CB    . THR A 1 186 ? 153.500 130.798 147.858 1.00 29.80  ? 160 THR A CB    1 
ATOM   1303 O  OG1   . THR A 1 186 ? 153.795 131.276 149.175 1.00 37.36  ? 160 THR A OG1   1 
ATOM   1304 C  CG2   . THR A 1 186 ? 152.221 131.456 147.367 1.00 17.05  ? 160 THR A CG2   1 
ATOM   1305 N  N     . ALA A 1 187 ? 154.592 128.480 145.942 1.00 26.27  ? 161 ALA A N     1 
ATOM   1306 C  CA    . ALA A 1 187 ? 154.735 127.941 144.593 1.00 23.37  ? 161 ALA A CA    1 
ATOM   1307 C  C     . ALA A 1 187 ? 154.278 126.486 144.503 1.00 29.83  ? 161 ALA A C     1 
ATOM   1308 O  O     . ALA A 1 187 ? 153.663 126.095 143.509 1.00 38.25  ? 161 ALA A O     1 
ATOM   1309 C  CB    . ALA A 1 187 ? 156.184 128.080 144.130 1.00 21.94  ? 161 ALA A CB    1 
ATOM   1310 N  N     . SER A 1 188 ? 154.547 125.675 145.532 1.00 26.72  ? 162 SER A N     1 
ATOM   1311 C  CA    . SER A 1 188 ? 154.134 124.272 145.504 1.00 23.34  ? 162 SER A CA    1 
ATOM   1312 C  C     . SER A 1 188 ? 152.620 124.129 145.643 1.00 28.75  ? 162 SER A C     1 
ATOM   1313 O  O     . SER A 1 188 ? 151.986 123.349 144.908 1.00 41.81  ? 162 SER A O     1 
ATOM   1314 C  CB    . SER A 1 188 ? 154.849 123.498 146.611 1.00 27.50  ? 162 SER A CB    1 
ATOM   1315 O  OG    . SER A 1 188 ? 156.253 123.647 146.509 1.00 43.87  ? 162 SER A OG    1 
ATOM   1316 N  N     . VAL A 1 189 ? 152.026 124.881 146.582 1.00 31.21  ? 163 VAL A N     1 
ATOM   1317 C  CA    . VAL A 1 189 ? 150.572 124.884 146.748 1.00 31.84  ? 163 VAL A CA    1 
ATOM   1318 C  C     . VAL A 1 189 ? 149.894 125.393 145.481 1.00 27.99  ? 163 VAL A C     1 
ATOM   1319 O  O     . VAL A 1 189 ? 148.889 124.832 145.024 1.00 36.22  ? 163 VAL A O     1 
ATOM   1320 C  CB    . VAL A 1 189 ? 150.186 125.719 147.986 1.00 28.76  ? 163 VAL A CB    1 
ATOM   1321 C  CG1   . VAL A 1 189 ? 148.686 125.970 148.049 1.00 26.26  ? 163 VAL A CG1   1 
ATOM   1322 C  CG2   . VAL A 1 189 ? 150.653 125.028 149.254 1.00 27.44  ? 163 VAL A CG2   1 
ATOM   1323 N  N     . THR A 1 190 ? 150.477 126.419 144.862 1.00 32.74  ? 164 THR A N     1 
ATOM   1324 C  CA    . THR A 1 190 ? 149.933 126.988 143.638 1.00 29.51  ? 164 THR A CA    1 
ATOM   1325 C  C     . THR A 1 190 ? 150.066 126.028 142.457 1.00 31.24  ? 164 THR A C     1 
ATOM   1326 O  O     . THR A 1 190 ? 149.168 125.955 141.612 1.00 36.35  ? 164 THR A O     1 
ATOM   1327 C  CB    . THR A 1 190 ? 150.642 128.310 143.367 1.00 26.02  ? 164 THR A CB    1 
ATOM   1328 O  OG1   . THR A 1 190 ? 150.636 129.098 144.563 1.00 40.78  ? 164 THR A OG1   1 
ATOM   1329 C  CG2   . THR A 1 190 ? 149.932 129.066 142.342 1.00 33.18  ? 164 THR A CG2   1 
ATOM   1330 N  N     . LEU A 1 191 ? 151.168 125.271 142.399 1.00 29.34  ? 165 LEU A N     1 
ATOM   1331 C  CA    . LEU A 1 191 ? 151.361 124.282 141.342 1.00 25.04  ? 165 LEU A CA    1 
ATOM   1332 C  C     . LEU A 1 191 ? 150.337 123.159 141.436 1.00 34.07  ? 165 LEU A C     1 
ATOM   1333 O  O     . LEU A 1 191 ? 149.846 122.672 140.410 1.00 37.42  ? 165 LEU A O     1 
ATOM   1334 C  CB    . LEU A 1 191 ? 152.785 123.723 141.407 1.00 25.26  ? 165 LEU A CB    1 
ATOM   1335 C  CG    . LEU A 1 191 ? 153.136 122.492 140.566 1.00 28.92  ? 165 LEU A CG    1 
ATOM   1336 C  CD1   . LEU A 1 191 ? 153.282 122.855 139.096 1.00 25.30  ? 165 LEU A CD1   1 
ATOM   1337 C  CD2   . LEU A 1 191 ? 154.398 121.823 141.085 1.00 24.20  ? 165 LEU A CD2   1 
ATOM   1338 N  N     . LEU A 1 192 ? 149.999 122.733 142.657 1.00 37.15  ? 166 LEU A N     1 
ATOM   1339 C  CA    . LEU A 1 192 ? 148.924 121.749 142.796 1.00 25.05  ? 166 LEU A CA    1 
ATOM   1340 C  C     . LEU A 1 192 ? 147.562 122.350 142.444 1.00 30.23  ? 166 LEU A C     1 
ATOM   1341 O  O     . LEU A 1 192 ? 146.793 121.766 141.663 1.00 32.75  ? 166 LEU A O     1 
ATOM   1342 C  CB    . LEU A 1 192 ? 148.903 121.173 144.212 1.00 30.87  ? 166 LEU A CB    1 
ATOM   1343 C  CG    . LEU A 1 192 ? 147.753 120.197 144.492 1.00 31.99  ? 166 LEU A CG    1 
ATOM   1344 C  CD1   . LEU A 1 192 ? 147.814 118.983 143.575 1.00 32.51  ? 166 LEU A CD1   1 
ATOM   1345 C  CD2   . LEU A 1 192 ? 147.741 119.764 145.942 1.00 29.83  ? 166 LEU A CD2   1 
ATOM   1346 N  N     . THR A 1 193 ? 147.250 123.528 142.996 1.00 34.13  ? 167 THR A N     1 
ATOM   1347 C  CA    . THR A 1 193 ? 145.900 124.064 142.875 1.00 22.73  ? 167 THR A CA    1 
ATOM   1348 C  C     . THR A 1 193 ? 145.596 124.617 141.489 1.00 29.07  ? 167 THR A C     1 
ATOM   1349 O  O     . THR A 1 193 ? 144.421 124.706 141.135 1.00 32.70  ? 167 THR A O     1 
ATOM   1350 C  CB    . THR A 1 193 ? 145.648 125.151 143.922 1.00 30.79  ? 167 THR A CB    1 
ATOM   1351 O  OG1   . THR A 1 193 ? 146.697 126.123 143.876 1.00 33.30  ? 167 THR A OG1   1 
ATOM   1352 C  CG2   . THR A 1 193 ? 145.570 124.545 145.315 1.00 28.22  ? 167 THR A CG2   1 
ATOM   1353 N  N     . SER A 1 194 ? 146.609 124.965 140.690 1.00 34.99  ? 168 SER A N     1 
ATOM   1354 C  CA    . SER A 1 194 ? 146.342 125.405 139.323 1.00 25.46  ? 168 SER A CA    1 
ATOM   1355 C  C     . SER A 1 194 ? 145.848 124.252 138.455 1.00 27.96  ? 168 SER A C     1 
ATOM   1356 O  O     . SER A 1 194 ? 144.864 124.398 137.717 1.00 38.71  ? 168 SER A O     1 
ATOM   1357 C  CB    . SER A 1 194 ? 147.595 126.043 138.725 1.00 24.83  ? 168 SER A CB    1 
ATOM   1358 O  OG    . SER A 1 194 ? 148.636 125.096 138.578 1.00 33.86  ? 168 SER A OG    1 
ATOM   1359 N  N     . THR A 1 195 ? 146.463 123.077 138.553 1.00 27.29  ? 169 THR A N     1 
ATOM   1360 C  CA    . THR A 1 195 ? 146.017 121.886 137.803 1.00 26.80  ? 169 THR A CA    1 
ATOM   1361 C  C     . THR A 1 195 ? 144.646 121.430 138.253 1.00 26.69  ? 169 THR A C     1 
ATOM   1362 O  O     . THR A 1 195 ? 143.842 121.109 137.400 1.00 34.50  ? 169 THR A O     1 
ATOM   1363 C  CB    . THR A 1 195 ? 147.072 120.777 137.887 1.00 33.88  ? 169 THR A CB    1 
ATOM   1364 O  OG1   . THR A 1 195 ? 148.179 121.288 137.159 1.00 39.31  ? 169 THR A OG1   1 
ATOM   1365 C  CG2   . THR A 1 195 ? 146.613 119.477 137.254 1.00 26.19  ? 169 THR A CG2   1 
ATOM   1366 N  N     . LEU A 1 196 ? 144.385 121.397 139.544 1.00 32.15  ? 170 LEU A N     1 
ATOM   1367 C  CA    . LEU A 1 196 ? 143.071 121.016 140.116 1.00 28.94  ? 170 LEU A CA    1 
ATOM   1368 C  C     . LEU A 1 196 ? 142.001 122.016 139.654 1.00 24.98  ? 170 LEU A C     1 
ATOM   1369 O  O     . LEU A 1 196 ? 140.934 121.567 139.331 1.00 27.32  ? 170 LEU A O     1 
ATOM   1370 C  CB    . LEU A 1 196 ? 143.162 120.910 141.639 1.00 31.85  ? 170 LEU A CB    1 
ATOM   1371 C  CG    . LEU A 1 196 ? 143.784 119.647 142.228 1.00 31.63  ? 170 LEU A CG    1 
ATOM   1372 C  CD1   . LEU A 1 196 ? 143.597 119.730 143.724 1.00 32.06  ? 170 LEU A CD1   1 
ATOM   1373 C  CD2   . LEU A 1 196 ? 143.137 118.407 141.668 1.00 26.66  ? 170 LEU A CD2   1 
ATOM   1374 N  N     . GLY A 1 197 ? 142.288 123.306 139.593 1.00 29.33  ? 171 GLY A N     1 
ATOM   1375 C  CA    . GLY A 1 197 ? 141.347 124.315 139.086 1.00 30.47  ? 171 GLY A CA    1 
ATOM   1376 C  C     . GLY A 1 197 ? 140.981 124.126 137.643 1.00 31.27  ? 171 GLY A C     1 
ATOM   1377 O  O     . GLY A 1 197 ? 139.845 124.419 137.304 1.00 40.75  ? 171 GLY A O     1 
ATOM   1378 N  N     . VAL A 1 198 ? 141.917 123.781 136.783 1.00 35.27  ? 172 VAL A N     1 
ATOM   1379 C  CA    . VAL A 1 198 ? 141.553 123.442 135.380 1.00 35.37  ? 172 VAL A CA    1 
ATOM   1380 C  C     . VAL A 1 198 ? 140.663 122.188 135.293 1.00 33.37  ? 172 VAL A C     1 
ATOM   1381 O  O     . VAL A 1 198 ? 139.687 122.229 134.585 1.00 35.74  ? 172 VAL A O     1 
ATOM   1382 C  CB    . VAL A 1 198 ? 142.891 123.267 134.623 1.00 31.78  ? 172 VAL A CB    1 
ATOM   1383 C  CG1   . VAL A 1 198 ? 142.698 122.690 133.230 1.00 35.97  ? 172 VAL A CG1   1 
ATOM   1384 C  CG2   . VAL A 1 198 ? 143.679 124.560 134.552 1.00 35.90  ? 172 VAL A CG2   1 
ATOM   1385 N  N     . LEU A 1 199 ? 140.987 121.118 135.997 1.00 34.55  ? 173 LEU A N     1 
ATOM   1386 C  CA    . LEU A 1 199 ? 140.154 119.901 136.012 1.00 28.23  ? 173 LEU A CA    1 
ATOM   1387 C  C     . LEU A 1 199 ? 138.792 120.121 136.681 1.00 36.54  ? 173 LEU A C     1 
ATOM   1388 O  O     . LEU A 1 199 ? 137.819 119.673 136.089 1.00 41.70  ? 173 LEU A O     1 
ATOM   1389 C  CB    . LEU A 1 199 ? 140.984 118.830 136.716 1.00 31.53  ? 173 LEU A CB    1 
ATOM   1390 C  CG    . LEU A 1 199 ? 142.358 118.499 136.132 1.00 33.83  ? 173 LEU A CG    1 
ATOM   1391 C  CD1   . LEU A 1 199 ? 143.088 117.614 137.116 1.00 38.92  ? 173 LEU A CD1   1 
ATOM   1392 C  CD2   . LEU A 1 199 ? 142.230 117.795 134.812 1.00 34.59  ? 173 LEU A CD2   1 
ATOM   1393 N  N     . VAL A 1 200 ? 138.724 120.784 137.838 1.00 36.70  ? 174 VAL A N     1 
ATOM   1394 C  CA    . VAL A 1 200 ? 137.437 121.131 138.509 1.00 27.72  ? 174 VAL A CA    1 
ATOM   1395 C  C     . VAL A 1 200 ? 137.496 122.620 138.851 1.00 30.83  ? 174 VAL A C     1 
ATOM   1396 O  O     . VAL A 1 200 ? 138.226 122.951 139.733 1.00 44.51  ? 174 VAL A O     1 
ATOM   1397 C  CB    . VAL A 1 200 ? 137.126 120.234 139.733 1.00 32.45  ? 174 VAL A CB    1 
ATOM   1398 C  CG1   . VAL A 1 200 ? 135.758 120.499 140.337 1.00 31.26  ? 174 VAL A CG1   1 
ATOM   1399 C  CG2   . VAL A 1 200 ? 137.289 118.755 139.417 1.00 34.72  ? 174 VAL A CG2   1 
ATOM   1400 N  N     . ARG A 1 201 ? 136.645 123.436 138.268 1.00 33.25  ? 175 ARG A N     1 
ATOM   1401 C  CA    . ARG A 1 201 ? 136.579 124.903 138.505 1.00 36.01  ? 175 ARG A CA    1 
ATOM   1402 C  C     . ARG A 1 201 ? 136.108 125.168 139.940 1.00 37.21  ? 175 ARG A C     1 
ATOM   1403 O  O     . ARG A 1 201 ? 136.418 126.249 140.420 1.00 42.68  ? 175 ARG A O     1 
ATOM   1404 C  CB    . ARG A 1 201 ? 135.811 125.610 137.379 1.00 35.99  ? 175 ARG A CB    1 
ATOM   1405 C  CG    . ARG A 1 201 ? 136.194 127.055 137.096 1.00 33.19  ? 175 ARG A CG    1 
ATOM   1406 C  CD    . ARG A 1 201 ? 137.415 127.274 136.217 1.00 37.11  ? 175 ARG A CD    1 
ATOM   1407 N  NE    . ARG A 1 201 ? 137.980 126.059 135.624 1.00 42.13  ? 175 ARG A NE    1 
ATOM   1408 C  CZ    . ARG A 1 201 ? 137.885 125.706 134.356 1.00 40.81  ? 175 ARG A CZ    1 
ATOM   1409 N  NH1   . ARG A 1 201 ? 137.490 126.577 133.455 1.00 34.84  ? 175 ARG A NH1   1 
ATOM   1410 N  NH2   . ARG A 1 201 ? 138.175 124.477 133.993 1.00 39.73  ? 175 ARG A NH2   1 
ATOM   1411 N  N     . ASP A 1 202 ? 135.369 124.246 140.550 1.00 36.49  ? 176 ASP A N     1 
ATOM   1412 C  CA    . ASP A 1 202 ? 134.778 124.380 141.909 1.00 32.91  ? 176 ASP A CA    1 
ATOM   1413 C  C     . ASP A 1 202 ? 135.920 124.576 142.908 1.00 37.12  ? 176 ASP A C     1 
ATOM   1414 O  O     . ASP A 1 202 ? 135.694 125.267 143.863 1.00 49.78  ? 176 ASP A O     1 
ATOM   1415 C  CB    . ASP A 1 202 ? 133.847 123.203 142.138 1.00 39.13  ? 176 ASP A CB    1 
ATOM   1416 C  CG    . ASP A 1 202 ? 132.885 122.882 141.007 1.00 38.59  ? 176 ASP A CG    1 
ATOM   1417 O  OD1   . ASP A 1 202 ? 133.355 122.708 139.871 1.00 37.01  ? 176 ASP A OD1   1 
ATOM   1418 O  OD2   . ASP A 1 202 ? 131.681 122.796 141.277 1.00 39.31  ? 176 ASP A OD2   1 
ATOM   1419 N  N     . THR A 1 203 ? 137.055 123.922 142.733 1.00 41.01  ? 177 THR A N     1 
ATOM   1420 C  CA    . THR A 1 203 ? 138.285 124.045 143.532 1.00 39.34  ? 177 THR A CA    1 
ATOM   1421 C  C     . THR A 1 203 ? 138.704 125.483 143.787 1.00 37.81  ? 177 THR A C     1 
ATOM   1422 O  O     . THR A 1 203 ? 139.055 125.759 144.916 1.00 47.78  ? 177 THR A O     1 
ATOM   1423 C  CB    . THR A 1 203 ? 139.320 123.238 142.742 1.00 39.89  ? 177 THR A CB    1 
ATOM   1424 O  OG1   . THR A 1 203 ? 139.129 121.890 143.155 1.00 39.76  ? 177 THR A OG1   1 
ATOM   1425 C  CG2   . THR A 1 203 ? 140.749 123.678 143.011 1.00 43.26  ? 177 THR A CG2   1 
ATOM   1426 N  N     . GLN A 1 204 ? 138.675 126.365 142.806 1.00 29.54  ? 178 GLN A N     1 
ATOM   1427 C  CA    . GLN A 1 204 ? 138.953 127.804 142.979 1.00 37.94  ? 178 GLN A CA    1 
ATOM   1428 C  C     . GLN A 1 204 ? 137.959 128.472 143.941 1.00 38.48  ? 178 GLN A C     1 
ATOM   1429 O  O     . GLN A 1 204 ? 138.349 129.466 144.538 1.00 46.50  ? 178 GLN A O     1 
ATOM   1430 C  CB    . GLN A 1 204 ? 138.864 128.424 141.586 1.00 40.86  ? 178 GLN A CB    1 
ATOM   1431 C  CG    . GLN A 1 204 ? 139.664 127.721 140.496 1.00 42.32  ? 178 GLN A CG    1 
ATOM   1432 C  CD    . GLN A 1 204 ? 139.683 128.504 139.203 1.00 45.02  ? 178 GLN A CD    1 
ATOM   1433 O  OE1   . GLN A 1 204 ? 138.975 129.503 139.052 1.00 48.54  ? 178 GLN A OE1   1 
ATOM   1434 N  NE2   . GLN A 1 204 ? 140.484 128.062 138.248 1.00 43.48  ? 178 GLN A NE2   1 
ATOM   1435 N  N     . MET A 1 205 ? 136.707 128.039 144.020 1.00 48.83  ? 179 MET A N     1 
ATOM   1436 C  CA    . MET A 1 205 ? 135.711 128.490 144.984 1.00 40.73  ? 179 MET A CA    1 
ATOM   1437 C  C     . MET A 1 205 ? 136.044 128.037 146.402 1.00 43.04  ? 179 MET A C     1 
ATOM   1438 O  O     . MET A 1 205 ? 135.706 128.734 147.364 1.00 49.28  ? 179 MET A O     1 
ATOM   1439 C  CB    . MET A 1 205 ? 134.329 127.980 144.578 1.00 46.00  ? 179 MET A CB    1 
ATOM   1440 C  CG    . MET A 1 205 ? 133.784 128.571 143.286 1.00 43.98  ? 179 MET A CG    1 
ATOM   1441 S  SD    . MET A 1 205 ? 133.690 130.370 143.300 1.00 60.96  ? 179 MET A SD    1 
ATOM   1442 C  CE    . MET A 1 205 ? 132.575 130.643 144.673 1.00 46.85  ? 179 MET A CE    1 
ATOM   1443 N  N     . LEU A 1 206 ? 136.688 126.873 146.542 1.00 45.28  ? 180 LEU A N     1 
ATOM   1444 C  CA    . LEU A 1 206 ? 137.080 126.375 147.865 1.00 41.82  ? 180 LEU A CA    1 
ATOM   1445 C  C     . LEU A 1 206 ? 138.171 127.238 148.506 1.00 41.37  ? 180 LEU A C     1 
ATOM   1446 O  O     . LEU A 1 206 ? 138.267 127.321 149.746 1.00 42.97  ? 180 LEU A O     1 
ATOM   1447 C  CB    . LEU A 1 206 ? 137.565 124.928 147.749 1.00 45.74  ? 180 LEU A CB    1 
ATOM   1448 C  CG    . LEU A 1 206 ? 137.061 123.827 148.683 1.00 46.78  ? 180 LEU A CG    1 
ATOM   1449 C  CD1   . LEU A 1 206 ? 135.568 123.626 148.554 1.00 46.04  ? 180 LEU A CD1   1 
ATOM   1450 C  CD2   . LEU A 1 206 ? 137.802 122.529 148.413 1.00 44.58  ? 180 LEU A CD2   1 
ATOM   1451 N  N     . MET A 1 207 ? 139.024 127.859 147.673 1.00 39.61  ? 181 MET A N     1 
ATOM   1452 C  CA    . MET A 1 207 ? 140.196 128.576 148.197 1.00 41.72  ? 181 MET A CA    1 
ATOM   1453 C  C     . MET A 1 207 ? 139.841 129.777 149.075 1.00 45.28  ? 181 MET A C     1 
ATOM   1454 O  O     . MET A 1 207 ? 140.638 130.143 149.946 1.00 50.50  ? 181 MET A O     1 
ATOM   1455 C  CB    . MET A 1 207 ? 141.130 129.049 147.074 1.00 48.25  ? 181 MET A CB    1 
ATOM   1456 C  CG    . MET A 1 207 ? 141.532 128.030 146.015 1.00 44.89  ? 181 MET A CG    1 
ATOM   1457 S  SD    . MET A 1 207 ? 142.280 126.447 146.500 1.00 58.93  ? 181 MET A SD    1 
ATOM   1458 C  CE    . MET A 1 207 ? 143.392 126.877 147.843 1.00 46.95  ? 181 MET A CE    1 
ATOM   1459 N  N     . GLN A 1 208 ? 138.667 130.393 148.874 1.00 40.85  ? 182 GLN A N     1 
ATOM   1460 C  CA    . GLN A 1 208 ? 138.257 131.520 149.716 1.00 42.86  ? 182 GLN A CA    1 
ATOM   1461 C  C     . GLN A 1 208 ? 138.073 131.116 151.175 1.00 44.70  ? 182 GLN A C     1 
ATOM   1462 O  O     . GLN A 1 208 ? 138.515 131.833 152.077 1.00 47.44  ? 182 GLN A O     1 
ATOM   1463 C  CB    . GLN A 1 208 ? 136.973 132.156 149.183 1.00 50.88  ? 182 GLN A CB    1 
ATOM   1464 C  CG    . GLN A 1 208 ? 137.175 133.178 148.078 1.00 53.16  ? 182 GLN A CG    1 
ATOM   1465 C  CD    . GLN A 1 208 ? 137.182 132.563 146.705 1.00 57.83  ? 182 GLN A CD    1 
ATOM   1466 O  OE1   . GLN A 1 208 ? 138.086 131.808 146.368 1.00 54.40  ? 182 GLN A OE1   1 
ATOM   1467 N  NE2   . GLN A 1 208 ? 136.170 132.875 145.905 1.00 55.61  ? 182 GLN A NE2   1 
ATOM   1468 N  N     . ALA A 1 209 ? 137.437 129.974 151.430 1.00 46.75  ? 183 ALA A N     1 
ATOM   1469 C  CA    . ALA A 1 209 ? 137.301 129.517 152.809 1.00 42.35  ? 183 ALA A CA    1 
ATOM   1470 C  C     . ALA A 1 209 ? 138.615 128.964 153.347 1.00 39.77  ? 183 ALA A C     1 
ATOM   1471 O  O     . ALA A 1 209 ? 138.928 129.145 154.537 1.00 45.46  ? 183 ALA A O     1 
ATOM   1472 C  CB    . ALA A 1 209 ? 136.195 128.468 152.913 1.00 43.14  ? 183 ALA A CB    1 
ATOM   1473 N  N     . ILE A 1 210 ? 139.395 128.301 152.477 1.00 33.81  ? 184 ILE A N     1 
ATOM   1474 C  CA    . ILE A 1 210 ? 140.665 127.709 152.908 1.00 40.47  ? 184 ILE A CA    1 
ATOM   1475 C  C     . ILE A 1 210 ? 141.646 128.789 153.371 1.00 37.07  ? 184 ILE A C     1 
ATOM   1476 O  O     . ILE A 1 210 ? 142.308 128.646 154.409 1.00 29.06  ? 184 ILE A O     1 
ATOM   1477 C  CB    . ILE A 1 210 ? 141.249 126.837 151.778 1.00 42.36  ? 184 ILE A CB    1 
ATOM   1478 C  CG1   . ILE A 1 210 ? 140.392 125.586 151.585 1.00 36.21  ? 184 ILE A CG1   1 
ATOM   1479 C  CG2   . ILE A 1 210 ? 142.688 126.428 152.069 1.00 36.92  ? 184 ILE A CG2   1 
ATOM   1480 C  CD1   . ILE A 1 210 ? 140.799 124.741 150.403 1.00 38.90  ? 184 ILE A CD1   1 
ATOM   1481 N  N     . LEU A 1 211 ? 141.707 129.912 152.649 1.00 37.42  ? 185 LEU A N     1 
ATOM   1482 C  CA    . LEU A 1 211 ? 142.652 130.963 153.012 1.00 38.37  ? 185 LEU A CA    1 
ATOM   1483 C  C     . LEU A 1 211 ? 142.230 131.716 154.270 1.00 31.58  ? 185 LEU A C     1 
ATOM   1484 O  O     . LEU A 1 211 ? 143.091 132.190 155.015 1.00 37.76  ? 185 LEU A O     1 
ATOM   1485 C  CB    . LEU A 1 211 ? 142.839 131.921 151.839 1.00 37.97  ? 185 LEU A CB    1 
ATOM   1486 C  CG    . LEU A 1 211 ? 143.859 131.391 150.828 1.00 34.57  ? 185 LEU A CG    1 
ATOM   1487 C  CD1   . LEU A 1 211 ? 143.653 132.016 149.469 1.00 37.06  ? 185 LEU A CD1   1 
ATOM   1488 C  CD2   . LEU A 1 211 ? 145.277 131.625 151.322 1.00 30.49  ? 185 LEU A CD2   1 
ATOM   1489 N  N     . ARG A 1 212 ? 140.927 131.815 154.546 1.00 31.35  ? 186 ARG A N     1 
ATOM   1490 C  CA    . ARG A 1 212 ? 140.496 132.415 155.808 1.00 30.36  ? 186 ARG A CA    1 
ATOM   1491 C  C     . ARG A 1 212 ? 140.806 131.501 156.987 1.00 32.58  ? 186 ARG A C     1 
ATOM   1492 O  O     . ARG A 1 212 ? 141.133 131.983 158.084 1.00 29.68  ? 186 ARG A O     1 
ATOM   1493 C  CB    . ARG A 1 212 ? 139.007 132.747 155.754 1.00 38.86  ? 186 ARG A CB    1 
ATOM   1494 C  CG    . ARG A 1 212 ? 138.665 133.753 154.680 1.00 35.96  ? 186 ARG A CG    1 
ATOM   1495 C  CD    . ARG A 1 212 ? 137.665 134.789 155.140 1.00 37.31  ? 186 ARG A CD    1 
ATOM   1496 N  NE    . ARG A 1 212 ? 137.949 136.102 154.571 1.00 42.17  ? 186 ARG A NE    1 
ATOM   1497 C  CZ    . ARG A 1 212 ? 137.629 136.481 153.341 1.00 43.68  ? 186 ARG A CZ    1 
ATOM   1498 N  NH1   . ARG A 1 212 ? 136.992 135.672 152.510 1.00 39.14  ? 186 ARG A NH1   1 
ATOM   1499 N  NH2   . ARG A 1 212 ? 137.952 137.705 152.934 1.00 42.66  ? 186 ARG A NH2   1 
ATOM   1500 N  N     . ILE A 1 213 ? 140.706 130.180 156.772 1.00 40.42  ? 187 ILE A N     1 
ATOM   1501 C  CA    . ILE A 1 213 ? 141.163 129.208 157.770 1.00 27.63  ? 187 ILE A CA    1 
ATOM   1502 C  C     . ILE A 1 213 ? 142.651 129.397 158.052 1.00 35.67  ? 187 ILE A C     1 
ATOM   1503 O  O     . ILE A 1 213 ? 143.086 129.424 159.210 1.00 38.39  ? 187 ILE A O     1 
ATOM   1504 C  CB    . ILE A 1 213 ? 140.852 127.773 157.297 1.00 37.32  ? 187 ILE A CB    1 
ATOM   1505 C  CG1   . ILE A 1 213 ? 139.372 127.452 157.494 1.00 38.05  ? 187 ILE A CG1   1 
ATOM   1506 C  CG2   . ILE A 1 213 ? 141.714 126.737 158.025 1.00 38.10  ? 187 ILE A CG2   1 
ATOM   1507 C  CD1   . ILE A 1 213 ? 138.994 126.014 157.196 1.00 32.93  ? 187 ILE A CD1   1 
ATOM   1508 N  N     . LEU A 1 214 ? 143.447 129.568 156.992 1.00 41.02  ? 188 LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 214 ? 144.886 129.767 157.167 1.00 29.67  ? 188 LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 214 ? 145.214 131.118 157.800 1.00 28.81  ? 188 LEU A C     1 
ATOM   1511 O  O     . LEU A 1 214 ? 146.236 131.250 158.482 1.00 31.74  ? 188 LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 214 ? 145.605 129.628 155.825 1.00 30.43  ? 188 LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 214 ? 145.521 128.271 155.124 1.00 31.89  ? 188 LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 214 ? 146.373 128.269 153.868 1.00 32.62  ? 188 LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 214 ? 145.924 127.142 156.057 1.00 26.32  ? 188 LEU A CD2   1 
ATOM   1516 N  N     . PHE A 1 215 ? 144.369 132.129 157.585 1.00 34.62  ? 189 PHE A N     1 
ATOM   1517 C  CA    . PHE A 1 215 ? 144.640 133.456 158.129 1.00 16.67  ? 189 PHE A CA    1 
ATOM   1518 C  C     . PHE A 1 215 ? 144.334 133.526 159.618 1.00 28.66  ? 189 PHE A C     1 
ATOM   1519 O  O     . PHE A 1 215 ? 145.193 133.913 160.419 1.00 28.11  ? 189 PHE A O     1 
ATOM   1520 C  CB    . PHE A 1 215 ? 143.824 134.509 157.385 1.00 21.59  ? 189 PHE A CB    1 
ATOM   1521 C  CG    . PHE A 1 215 ? 144.105 135.919 157.825 1.00 29.35  ? 189 PHE A CG    1 
ATOM   1522 C  CD1   . PHE A 1 215 ? 145.407 136.390 157.902 1.00 31.22  ? 189 PHE A CD1   1 
ATOM   1523 C  CD2   . PHE A 1 215 ? 143.067 136.774 158.163 1.00 24.34  ? 189 PHE A CD2   1 
ATOM   1524 C  CE1   . PHE A 1 215 ? 145.669 137.688 158.299 1.00 23.63  ? 189 PHE A CE1   1 
ATOM   1525 C  CE2   . PHE A 1 215 ? 143.323 138.072 158.564 1.00 25.91  ? 189 PHE A CE2   1 
ATOM   1526 C  CZ    . PHE A 1 215 ? 144.626 138.528 158.631 1.00 17.63  ? 189 PHE A CZ    1 
ATOM   1527 N  N     . TYR A 1 216 ? 143.107 133.175 160.008 1.00 34.34  ? 190 TYR A N     1 
ATOM   1528 C  CA    . TYR A 1 216 ? 142.692 133.426 161.385 1.00 22.48  ? 190 TYR A CA    1 
ATOM   1529 C  C     . TYR A 1 216 ? 143.279 132.414 162.363 1.00 23.12  ? 190 TYR A C     1 
ATOM   1530 O  O     . TYR A 1 216 ? 143.543 132.753 163.521 1.00 29.36  ? 190 TYR A O     1 
ATOM   1531 C  CB    . TYR A 1 216 ? 141.172 133.432 161.479 1.00 24.92  ? 190 TYR A CB    1 
ATOM   1532 C  CG    . TYR A 1 216 ? 140.507 134.637 160.865 1.00 28.25  ? 190 TYR A CG    1 
ATOM   1533 C  CD1   . TYR A 1 216 ? 140.715 135.910 161.382 1.00 24.86  ? 190 TYR A CD1   1 
ATOM   1534 C  CD2   . TYR A 1 216 ? 139.662 134.500 159.774 1.00 28.76  ? 190 TYR A CD2   1 
ATOM   1535 C  CE1   . TYR A 1 216 ? 140.099 137.014 160.821 1.00 27.84  ? 190 TYR A CE1   1 
ATOM   1536 C  CE2   . TYR A 1 216 ? 139.046 135.592 159.208 1.00 30.07  ? 190 TYR A CE2   1 
ATOM   1537 C  CZ    . TYR A 1 216 ? 139.266 136.846 159.734 1.00 28.48  ? 190 TYR A CZ    1 
ATOM   1538 O  OH    . TYR A 1 216 ? 138.647 137.932 159.166 1.00 33.81  ? 190 TYR A OH    1 
ATOM   1539 N  N     . PHE A 1 217 ? 143.483 131.172 161.927 1.00 32.63  ? 191 PHE A N     1 
ATOM   1540 C  CA    . PHE A 1 217 ? 144.093 130.159 162.782 1.00 36.51  ? 191 PHE A CA    1 
ATOM   1541 C  C     . PHE A 1 217 ? 145.611 130.218 162.676 1.00 37.71  ? 191 PHE A C     1 
ATOM   1542 O  O     . PHE A 1 217 ? 146.250 129.259 162.232 1.00 44.66  ? 191 PHE A O     1 
ATOM   1543 C  CB    . PHE A 1 217 ? 143.581 128.766 162.412 1.00 38.70  ? 191 PHE A CB    1 
ATOM   1544 C  CG    . PHE A 1 217 ? 143.486 127.826 163.576 1.00 42.70  ? 191 PHE A CG    1 
ATOM   1545 C  CD1   . PHE A 1 217 ? 142.893 128.227 164.762 1.00 44.68  ? 191 PHE A CD1   1 
ATOM   1546 C  CD2   . PHE A 1 217 ? 143.994 126.538 163.485 1.00 47.19  ? 191 PHE A CD2   1 
ATOM   1547 C  CE1   . PHE A 1 217 ? 142.806 127.360 165.838 1.00 47.64  ? 191 PHE A CE1   1 
ATOM   1548 C  CE2   . PHE A 1 217 ? 143.911 125.666 164.556 1.00 44.56  ? 191 PHE A CE2   1 
ATOM   1549 C  CZ    . PHE A 1 217 ? 143.315 126.079 165.734 1.00 47.43  ? 191 PHE A CZ    1 
ATOM   1550 N  N     . SER A 1 218 ? 146.180 131.334 163.125 1.00 32.64  ? 192 SER A N     1 
ATOM   1551 C  CA    . SER A 1 218 ? 147.633 131.558 162.983 1.00 24.31  ? 192 SER A CA    1 
ATOM   1552 C  C     . SER A 1 218 ? 148.076 132.548 164.068 1.00 32.82  ? 192 SER A C     1 
ATOM   1553 O  O     . SER A 1 218 ? 147.202 133.096 164.757 1.00 34.50  ? 192 SER A O     1 
ATOM   1554 C  CB    . SER A 1 218 ? 147.927 132.069 161.595 1.00 23.76  ? 192 SER A CB    1 
ATOM   1555 O  OG    . SER A 1 218 ? 147.522 133.422 161.459 1.00 34.71  ? 192 SER A OG    1 
ATOM   1556 N  N     . PRO A 1 219 ? 149.388 132.824 164.231 1.00 38.15  ? 193 PRO A N     1 
ATOM   1557 C  CA    . PRO A 1 219 ? 149.917 133.760 165.257 1.00 29.44  ? 193 PRO A CA    1 
ATOM   1558 C  C     . PRO A 1 219 ? 150.032 135.188 164.726 1.00 29.75  ? 193 PRO A C     1 
ATOM   1559 O  O     . PRO A 1 219 ? 150.665 135.992 165.433 1.00 40.81  ? 193 PRO A O     1 
ATOM   1560 C  CB    . PRO A 1 219 ? 151.220 133.084 165.656 1.00 34.41  ? 193 PRO A CB    1 
ATOM   1561 C  CG    . PRO A 1 219 ? 151.742 132.582 164.327 1.00 23.31  ? 193 PRO A CG    1 
ATOM   1562 C  CD    . PRO A 1 219 ? 150.543 132.161 163.541 1.00 30.60  ? 193 PRO A CD    1 
ATOM   1563 N  N     . ILE A 1 220 ? 149.588 135.473 163.503 1.00 24.63  ? 194 ILE A N     1 
ATOM   1564 C  CA    . ILE A 1 220 ? 149.731 136.820 162.869 1.00 26.78  ? 194 ILE A CA    1 
ATOM   1565 C  C     . ILE A 1 220 ? 148.988 137.948 163.617 1.00 37.12  ? 194 ILE A C     1 
ATOM   1566 O  O     . ILE A 1 220 ? 149.617 139.014 163.759 1.00 41.54  ? 194 ILE A O     1 
ATOM   1567 C  CB    . ILE A 1 220 ? 149.237 136.750 161.410 1.00 34.72  ? 194 ILE A CB    1 
ATOM   1568 C  CG1   . ILE A 1 220 ? 150.077 135.808 160.557 1.00 33.20  ? 194 ILE A CG1   1 
ATOM   1569 C  CG2   . ILE A 1 220 ? 149.137 138.139 160.779 1.00 24.53  ? 194 ILE A CG2   1 
ATOM   1570 C  CD1   . ILE A 1 220 ? 149.670 135.797 159.096 1.00 33.37  ? 194 ILE A CD1   1 
ATOM   1571 N  N     . LEU A 1 221 ? 147.758 137.750 164.115 1.00 29.80  ? 195 LEU A N     1 
ATOM   1572 C  CA    . LEU A 1 221 ? 146.952 138.866 164.699 1.00 29.32  ? 195 LEU A CA    1 
ATOM   1573 C  C     . LEU A 1 221 ? 146.829 138.731 166.214 1.00 30.40  ? 195 LEU A C     1 
ATOM   1574 O  O     . LEU A 1 221 ? 146.479 139.731 166.859 1.00 41.71  ? 195 LEU A O     1 
ATOM   1575 C  CB    . LEU A 1 221 ? 145.554 138.866 164.081 1.00 32.10  ? 195 LEU A CB    1 
ATOM   1576 C  CG    . LEU A 1 221 ? 145.441 138.976 162.559 1.00 27.67  ? 195 LEU A CG    1 
ATOM   1577 C  CD1   . LEU A 1 221 ? 144.055 138.474 162.200 1.00 30.05  ? 195 LEU A CD1   1 
ATOM   1578 C  CD2   . LEU A 1 221 ? 145.602 140.418 162.120 1.00 27.95  ? 195 LEU A CD2   1 
ATOM   1579 N  N     . TRP A 1 222 ? 147.126 137.559 166.753 1.00 27.02  ? 196 TRP A N     1 
ATOM   1580 C  CA    . TRP A 1 222 ? 146.925 137.246 168.160 1.00 25.46  ? 196 TRP A CA    1 
ATOM   1581 C  C     . TRP A 1 222 ? 147.764 136.041 168.552 1.00 33.01  ? 196 TRP A C     1 
ATOM   1582 O  O     . TRP A 1 222 ? 148.179 135.244 167.710 1.00 41.25  ? 196 TRP A O     1 
ATOM   1583 C  CB    . TRP A 1 222 ? 145.439 137.005 168.468 1.00 31.33  ? 196 TRP A CB    1 
ATOM   1584 C  CG    . TRP A 1 222 ? 144.706 136.162 167.446 1.00 30.18  ? 196 TRP A CG    1 
ATOM   1585 C  CD1   . TRP A 1 222 ? 145.155 135.033 166.823 1.00 28.49  ? 196 TRP A CD1   1 
ATOM   1586 C  CD2   . TRP A 1 222 ? 143.384 136.392 166.946 1.00 32.82  ? 196 TRP A CD2   1 
ATOM   1587 N  NE1   . TRP A 1 222 ? 144.203 134.556 165.960 1.00 28.29  ? 196 TRP A NE1   1 
ATOM   1588 C  CE2   . TRP A 1 222 ? 143.104 135.370 166.019 1.00 29.39  ? 196 TRP A CE2   1 
ATOM   1589 C  CE3   . TRP A 1 222 ? 142.409 137.363 167.194 1.00 31.94  ? 196 TRP A CE3   1 
ATOM   1590 C  CZ2   . TRP A 1 222 ? 141.891 135.291 165.340 1.00 32.65  ? 196 TRP A CZ2   1 
ATOM   1591 C  CZ3   . TRP A 1 222 ? 141.206 137.282 166.520 1.00 31.82  ? 196 TRP A CZ3   1 
ATOM   1592 C  CH2   . TRP A 1 222 ? 140.958 136.255 165.603 1.00 27.86  ? 196 TRP A CH2   1 
ATOM   1593 N  N     . LEU A 1 223 ? 148.007 135.927 169.851 1.00 55.74  ? 197 LEU A N     1 
ATOM   1594 C  CA    . LEU A 1 223 ? 148.640 134.750 170.441 1.00 51.86  ? 197 LEU A CA    1 
ATOM   1595 C  C     . LEU A 1 223 ? 147.682 134.171 171.469 1.00 60.62  ? 197 LEU A C     1 
ATOM   1596 O  O     . LEU A 1 223 ? 147.364 134.853 172.462 1.00 66.82  ? 197 LEU A O     1 
ATOM   1597 C  CB    . LEU A 1 223 ? 149.973 135.110 171.095 1.00 51.53  ? 197 LEU A CB    1 
ATOM   1598 C  CG    . LEU A 1 223 ? 151.235 135.060 170.233 1.00 57.23  ? 197 LEU A CG    1 
ATOM   1599 C  CD1   . LEU A 1 223 ? 152.442 135.479 171.055 1.00 58.18  ? 197 LEU A CD1   1 
ATOM   1600 C  CD2   . LEU A 1 223 ? 151.442 133.676 169.639 1.00 58.01  ? 197 LEU A CD2   1 
ATOM   1601 N  N     . PRO A 1 224 ? 147.189 132.941 171.296 1.00 70.55  ? 198 PRO A N     1 
ATOM   1602 C  CA    . PRO A 1 224 ? 146.248 132.380 172.278 1.00 72.03  ? 198 PRO A CA    1 
ATOM   1603 C  C     . PRO A 1 224 ? 146.913 131.804 173.522 1.00 75.30  ? 198 PRO A C     1 
ATOM   1604 O  O     . PRO A 1 224 ? 146.586 130.692 173.947 1.00 78.52  ? 198 PRO A O     1 
ATOM   1605 C  CB    . PRO A 1 224 ? 145.526 131.283 171.481 1.00 73.20  ? 198 PRO A CB    1 
ATOM   1606 C  CG    . PRO A 1 224 ? 145.842 131.565 170.036 1.00 71.41  ? 198 PRO A CG    1 
ATOM   1607 C  CD    . PRO A 1 224 ? 147.208 132.156 170.054 1.00 71.78  ? 198 PRO A CD    1 
ATOM   1608 N  N     . LYS A 1 225 ? 147.840 132.550 174.117 1.00 81.20  ? 199 LYS A N     1 
ATOM   1609 C  CA    . LYS A 1 225 ? 148.472 132.199 175.382 1.00 80.68  ? 199 LYS A CA    1 
ATOM   1610 C  C     . LYS A 1 225 ? 147.999 133.066 176.534 1.00 80.94  ? 199 LYS A C     1 
ATOM   1611 O  O     . LYS A 1 225 ? 147.795 132.561 177.640 1.00 82.62  ? 199 LYS A O     1 
ATOM   1612 C  CB    . LYS A 1 225 ? 149.998 132.315 175.260 1.00 82.80  ? 199 LYS A CB    1 
ATOM   1613 C  CG    . LYS A 1 225 ? 150.691 131.092 174.676 1.00 84.33  ? 199 LYS A CG    1 
ATOM   1614 C  CD    . LYS A 1 225 ? 150.194 129.808 175.314 1.00 84.35  ? 199 LYS A CD    1 
ATOM   1615 C  CE    . LYS A 1 225 ? 151.342 128.873 175.659 1.00 83.04  ? 199 LYS A CE    1 
ATOM   1616 N  NZ    . LYS A 1 225 ? 151.005 127.990 176.810 1.00 80.72  ? 199 LYS A NZ    1 
ATOM   1617 N  N     . ASN A 1 226 ? 147.817 134.362 176.294 1.00 79.81  ? 200 ASN A N     1 
ATOM   1618 C  CA    . ASN A 1 226 ? 147.314 135.288 177.297 1.00 82.30  ? 200 ASN A CA    1 
ATOM   1619 C  C     . ASN A 1 226 ? 145.816 135.538 177.176 1.00 82.05  ? 200 ASN A C     1 
ATOM   1620 O  O     . ASN A 1 226 ? 145.286 136.385 177.904 1.00 79.79  ? 200 ASN A O     1 
ATOM   1621 C  CB    . ASN A 1 226 ? 148.063 136.621 177.202 1.00 80.83  ? 200 ASN A CB    1 
ATOM   1622 C  CG    . ASN A 1 226 ? 148.201 137.113 175.773 1.00 80.88  ? 200 ASN A CG    1 
ATOM   1623 O  OD1   . ASN A 1 226 ? 148.826 136.460 174.937 1.00 80.06  ? 200 ASN A OD1   1 
ATOM   1624 N  ND2   . ASN A 1 226 ? 147.620 138.272 175.488 1.00 79.37  ? 200 ASN A ND2   1 
ATOM   1625 N  N     . HIS A 1 227 ? 145.128 134.833 176.280 1.00 80.71  ? 201 HIS A N     1 
ATOM   1626 C  CA    . HIS A 1 227 ? 143.702 135.036 176.053 1.00 80.45  ? 201 HIS A CA    1 
ATOM   1627 C  C     . HIS A 1 227 ? 142.855 133.838 176.452 1.00 82.25  ? 201 HIS A C     1 
ATOM   1628 O  O     . HIS A 1 227 ? 141.931 133.985 177.261 1.00 78.97  ? 201 HIS A O     1 
ATOM   1629 C  CB    . HIS A 1 227 ? 143.448 135.380 174.577 1.00 78.91  ? 201 HIS A CB    1 
ATOM   1630 C  CG    . HIS A 1 227 ? 143.972 136.720 174.164 1.00 80.18  ? 201 HIS A CG    1 
ATOM   1631 N  ND1   . HIS A 1 227 ? 144.144 137.759 175.052 1.00 78.96  ? 201 HIS A ND1   1 
ATOM   1632 C  CD2   . HIS A 1 227 ? 144.359 137.192 172.955 1.00 80.09  ? 201 HIS A CD2   1 
ATOM   1633 C  CE1   . HIS A 1 227 ? 144.610 138.814 174.409 1.00 78.40  ? 201 HIS A CE1   1 
ATOM   1634 N  NE2   . HIS A 1 227 ? 144.752 138.495 173.135 1.00 79.66  ? 201 HIS A NE2   1 
ATOM   1635 N  N     . GLY A 1 228 ? 143.135 132.658 175.916 1.00 90.77  ? 202 GLY A N     1 
ATOM   1636 C  CA    . GLY A 1 228 ? 142.266 131.508 176.094 1.00 87.84  ? 202 GLY A CA    1 
ATOM   1637 C  C     . GLY A 1 228 ? 143.014 130.196 176.193 1.00 88.12  ? 202 GLY A C     1 
ATOM   1638 O  O     . GLY A 1 228 ? 144.069 130.110 176.829 1.00 88.18  ? 202 GLY A O     1 
ATOM   1639 N  N     . ILE A 1 229 ? 142.455 129.165 175.556 1.00 91.18  ? 203 ILE A N     1 
ATOM   1640 C  CA    . ILE A 1 229 ? 142.951 127.803 175.716 1.00 90.86  ? 203 ILE A CA    1 
ATOM   1641 C  C     . ILE A 1 229 ? 144.194 127.602 174.859 1.00 89.82  ? 203 ILE A C     1 
ATOM   1642 O  O     . ILE A 1 229 ? 144.203 127.918 173.662 1.00 86.66  ? 203 ILE A O     1 
ATOM   1643 C  CB    . ILE A 1 229 ? 141.854 126.790 175.350 1.00 91.05  ? 203 ILE A CB    1 
ATOM   1644 C  CG1   . ILE A 1 229 ? 140.621 126.993 176.233 1.00 89.88  ? 203 ILE A CG1   1 
ATOM   1645 C  CG2   . ILE A 1 229 ? 142.360 125.358 175.487 1.00 87.74  ? 203 ILE A CG2   1 
ATOM   1646 C  CD1   . ILE A 1 229 ? 139.459 126.097 175.870 1.00 88.88  ? 203 ILE A CD1   1 
ATOM   1647 N  N     . SER A 1 230 ? 145.253 127.077 175.474 1.00 91.58  ? 204 SER A N     1 
ATOM   1648 C  CA    . SER A 1 230 ? 146.477 126.724 174.768 1.00 90.68  ? 204 SER A CA    1 
ATOM   1649 C  C     . SER A 1 230 ? 146.574 125.249 174.414 1.00 89.90  ? 204 SER A C     1 
ATOM   1650 O  O     . SER A 1 230 ? 147.331 124.895 173.508 1.00 90.99  ? 204 SER A O     1 
ATOM   1651 C  CB    . SER A 1 230 ? 147.703 127.106 175.606 1.00 90.78  ? 204 SER A CB    1 
ATOM   1652 O  OG    . SER A 1 230 ? 148.004 126.103 176.561 1.00 90.90  ? 204 SER A OG    1 
ATOM   1653 N  N     . GLY A 1 231 ? 145.830 124.382 175.103 1.00 89.56  ? 205 GLY A N     1 
ATOM   1654 C  CA    . GLY A 1 231 ? 145.934 122.955 174.859 1.00 91.28  ? 205 GLY A CA    1 
ATOM   1655 C  C     . GLY A 1 231 ? 145.258 122.486 173.588 1.00 91.81  ? 205 GLY A C     1 
ATOM   1656 O  O     . GLY A 1 231 ? 145.585 121.403 173.092 1.00 91.97  ? 205 GLY A O     1 
ATOM   1657 N  N     . LEU A 1 232 ? 144.320 123.266 173.056 1.00 85.81  ? 206 LEU A N     1 
ATOM   1658 C  CA    . LEU A 1 232 ? 143.610 122.896 171.839 1.00 85.87  ? 206 LEU A CA    1 
ATOM   1659 C  C     . LEU A 1 232 ? 143.805 123.896 170.712 1.00 84.94  ? 206 LEU A C     1 
ATOM   1660 O  O     . LEU A 1 232 ? 144.088 123.494 169.578 1.00 87.40  ? 206 LEU A O     1 
ATOM   1661 C  CB    . LEU A 1 232 ? 142.111 122.726 172.133 1.00 85.59  ? 206 LEU A CB    1 
ATOM   1662 C  CG    . LEU A 1 232 ? 141.378 121.712 171.254 1.00 86.29  ? 206 LEU A CG    1 
ATOM   1663 C  CD1   . LEU A 1 232 ? 142.026 120.339 171.364 1.00 85.44  ? 206 LEU A CD1   1 
ATOM   1664 C  CD2   . LEU A 1 232 ? 139.905 121.645 171.622 1.00 85.60  ? 206 LEU A CD2   1 
ATOM   1665 N  N     . ILE A 1 233 ? 143.644 125.192 170.987 1.00 76.51  ? 207 ILE A N     1 
ATOM   1666 C  CA    . ILE A 1 233 ? 143.753 126.197 169.934 1.00 76.76  ? 207 ILE A CA    1 
ATOM   1667 C  C     . ILE A 1 233 ? 145.209 126.397 169.530 1.00 77.49  ? 207 ILE A C     1 
ATOM   1668 O  O     . ILE A 1 233 ? 145.548 126.363 168.341 1.00 75.69  ? 207 ILE A O     1 
ATOM   1669 C  CB    . ILE A 1 233 ? 143.099 127.515 170.392 1.00 78.64  ? 207 ILE A CB    1 
ATOM   1670 C  CG1   . ILE A 1 233 ? 141.576 127.361 170.455 1.00 78.94  ? 207 ILE A CG1   1 
ATOM   1671 C  CG2   . ILE A 1 233 ? 143.484 128.669 169.473 1.00 76.20  ? 207 ILE A CG2   1 
ATOM   1672 C  CD1   . ILE A 1 233 ? 140.905 127.231 169.101 1.00 77.70  ? 207 ILE A CD1   1 
ATOM   1673 N  N     . HIS A 1 234 ? 146.096 126.583 170.510 1.00 76.33  ? 208 HIS A N     1 
ATOM   1674 C  CA    . HIS A 1 234 ? 147.495 126.865 170.212 1.00 71.87  ? 208 HIS A CA    1 
ATOM   1675 C  C     . HIS A 1 234 ? 148.248 125.628 169.739 1.00 72.44  ? 208 HIS A C     1 
ATOM   1676 O  O     . HIS A 1 234 ? 149.209 125.752 168.973 1.00 71.99  ? 208 HIS A O     1 
ATOM   1677 C  CB    . HIS A 1 234 ? 148.184 127.461 171.441 1.00 71.47  ? 208 HIS A CB    1 
ATOM   1678 C  CG    . HIS A 1 234 ? 149.530 128.049 171.154 1.00 76.16  ? 208 HIS A CG    1 
ATOM   1679 N  ND1   . HIS A 1 234 ? 150.679 127.290 171.104 1.00 75.68  ? 208 HIS A ND1   1 
ATOM   1680 C  CD2   . HIS A 1 234 ? 149.910 129.324 170.900 1.00 76.02  ? 208 HIS A CD2   1 
ATOM   1681 C  CE1   . HIS A 1 234 ? 151.709 128.072 170.833 1.00 73.41  ? 208 HIS A CE1   1 
ATOM   1682 N  NE2   . HIS A 1 234 ? 151.269 129.310 170.704 1.00 76.46  ? 208 HIS A NE2   1 
ATOM   1683 N  N     . GLU A 1 235 ? 147.836 124.438 170.183 1.00 75.71  ? 209 GLU A N     1 
ATOM   1684 C  CA    . GLU A 1 235 ? 148.505 123.213 169.755 1.00 71.30  ? 209 GLU A CA    1 
ATOM   1685 C  C     . GLU A 1 235 ? 148.156 122.868 168.313 1.00 70.25  ? 209 GLU A C     1 
ATOM   1686 O  O     . GLU A 1 235 ? 149.004 122.380 167.558 1.00 71.64  ? 209 GLU A O     1 
ATOM   1687 C  CB    . GLU A 1 235 ? 148.137 122.060 170.691 1.00 73.60  ? 209 GLU A CB    1 
ATOM   1688 C  CG    . GLU A 1 235 ? 148.930 122.030 171.988 1.00 76.74  ? 209 GLU A CG    1 
ATOM   1689 C  CD    . GLU A 1 235 ? 150.412 122.274 171.778 1.00 77.58  ? 209 GLU A CD    1 
ATOM   1690 O  OE1   . GLU A 1 235 ? 151.051 121.485 171.050 1.00 76.13  ? 209 GLU A OE1   1 
ATOM   1691 O  OE2   . GLU A 1 235 ? 150.940 123.255 172.343 1.00 76.16  ? 209 GLU A OE2   1 
ATOM   1692 N  N     . MET A 1 236 ? 146.906 123.113 167.913 1.00 65.24  ? 210 MET A N     1 
ATOM   1693 C  CA    . MET A 1 236 ? 146.494 122.840 166.541 1.00 63.38  ? 210 MET A CA    1 
ATOM   1694 C  C     . MET A 1 236 ? 146.964 123.912 165.569 1.00 65.35  ? 210 MET A C     1 
ATOM   1695 O  O     . MET A 1 236 ? 146.873 123.711 164.354 1.00 65.37  ? 210 MET A O     1 
ATOM   1696 C  CB    . MET A 1 236 ? 144.973 122.702 166.464 1.00 64.01  ? 210 MET A CB    1 
ATOM   1697 C  CG    . MET A 1 236 ? 144.479 121.265 166.456 1.00 68.29  ? 210 MET A CG    1 
ATOM   1698 S  SD    . MET A 1 236 ? 144.373 120.584 164.789 1.00 83.73  ? 210 MET A SD    1 
ATOM   1699 C  CE    . MET A 1 236 ? 144.843 118.880 165.083 1.00 67.26  ? 210 MET A CE    1 
ATOM   1700 N  N     . MET A 1 237 ? 147.461 125.043 166.073 1.00 57.41  ? 211 MET A N     1 
ATOM   1701 C  CA    . MET A 1 237 ? 147.955 126.093 165.190 1.00 50.92  ? 211 MET A CA    1 
ATOM   1702 C  C     . MET A 1 237 ? 149.320 125.746 164.614 1.00 51.23  ? 211 MET A C     1 
ATOM   1703 O  O     . MET A 1 237 ? 149.721 126.318 163.596 1.00 53.19  ? 211 MET A O     1 
ATOM   1704 C  CB    . MET A 1 237 ? 148.016 127.422 165.942 1.00 48.23  ? 211 MET A CB    1 
ATOM   1705 C  CG    . MET A 1 237 ? 146.921 128.401 165.563 1.00 50.12  ? 211 MET A CG    1 
ATOM   1706 S  SD    . MET A 1 237 ? 146.643 129.658 166.823 1.00 61.38  ? 211 MET A SD    1 
ATOM   1707 C  CE    . MET A 1 237 ? 148.231 130.478 166.827 1.00 49.12  ? 211 MET A CE    1 
ATOM   1708 N  N     . LYS A 1 238 ? 150.041 124.812 165.245 1.00 44.03  ? 212 LYS A N     1 
ATOM   1709 C  CA    . LYS A 1 238 ? 151.361 124.397 164.775 1.00 39.95  ? 212 LYS A CA    1 
ATOM   1710 C  C     . LYS A 1 238 ? 151.314 123.697 163.423 1.00 43.78  ? 212 LYS A C     1 
ATOM   1711 O  O     . LYS A 1 238 ? 152.299 123.748 162.680 1.00 48.23  ? 212 LYS A O     1 
ATOM   1712 C  CB    . LYS A 1 238 ? 152.026 123.465 165.791 1.00 47.19  ? 212 LYS A CB    1 
ATOM   1713 C  CG    . LYS A 1 238 ? 152.965 124.128 166.795 1.00 44.59  ? 212 LYS A CG    1 
ATOM   1714 C  CD    . LYS A 1 238 ? 152.253 125.073 167.741 1.00 46.69  ? 212 LYS A CD    1 
ATOM   1715 C  CE    . LYS A 1 238 ? 153.073 125.292 168.999 1.00 50.21  ? 212 LYS A CE    1 
ATOM   1716 N  NZ    . LYS A 1 238 ? 153.349 124.015 169.713 1.00 52.72  ? 212 LYS A NZ    1 
ATOM   1717 N  N     . TYR A 1 239 ? 150.197 123.049 163.086 1.00 42.82  ? 213 TYR A N     1 
ATOM   1718 C  CA    . TYR A 1 239 ? 150.058 122.376 161.801 1.00 39.75  ? 213 TYR A CA    1 
ATOM   1719 C  C     . TYR A 1 239 ? 149.872 123.346 160.643 1.00 40.74  ? 213 TYR A C     1 
ATOM   1720 O  O     . TYR A 1 239 ? 149.972 122.927 159.485 1.00 43.09  ? 213 TYR A O     1 
ATOM   1721 C  CB    . TYR A 1 239 ? 148.890 121.391 161.854 1.00 43.98  ? 213 TYR A CB    1 
ATOM   1722 C  CG    . TYR A 1 239 ? 149.131 120.236 162.796 1.00 41.89  ? 213 TYR A CG    1 
ATOM   1723 C  CD1   . TYR A 1 239 ? 148.676 120.276 164.109 1.00 42.78  ? 213 TYR A CD1   1 
ATOM   1724 C  CD2   . TYR A 1 239 ? 149.826 119.109 162.376 1.00 37.92  ? 213 TYR A CD2   1 
ATOM   1725 C  CE1   . TYR A 1 239 ? 148.900 119.222 164.975 1.00 44.47  ? 213 TYR A CE1   1 
ATOM   1726 C  CE2   . TYR A 1 239 ? 150.055 118.050 163.233 1.00 47.47  ? 213 TYR A CE2   1 
ATOM   1727 C  CZ    . TYR A 1 239 ? 149.590 118.112 164.531 1.00 49.80  ? 213 TYR A CZ    1 
ATOM   1728 O  OH    . TYR A 1 239 ? 149.817 117.059 165.387 1.00 47.83  ? 213 TYR A OH    1 
ATOM   1729 N  N     . ASN A 1 240 ? 149.597 124.610 160.924 1.00 34.47  ? 214 ASN A N     1 
ATOM   1730 C  CA    . ASN A 1 240 ? 149.569 125.638 159.897 1.00 32.14  ? 214 ASN A CA    1 
ATOM   1731 C  C     . ASN A 1 240 ? 150.998 126.012 159.515 1.00 30.13  ? 214 ASN A C     1 
ATOM   1732 O  O     . ASN A 1 240 ? 151.813 126.272 160.406 1.00 34.98  ? 214 ASN A O     1 
ATOM   1733 C  CB    . ASN A 1 240 ? 148.816 126.860 160.410 1.00 31.66  ? 214 ASN A CB    1 
ATOM   1734 C  CG    . ASN A 1 240 ? 148.282 127.732 159.298 1.00 30.18  ? 214 ASN A CG    1 
ATOM   1735 O  OD1   . ASN A 1 240 ? 148.528 127.483 158.123 1.00 38.83  ? 214 ASN A OD1   1 
ATOM   1736 N  ND2   . ASN A 1 240 ? 147.542 128.766 159.667 1.00 27.94  ? 214 ASN A ND2   1 
ATOM   1737 N  N     . PRO A 1 241 ? 151.395 126.001 158.211 1.00 35.49  ? 215 PRO A N     1 
ATOM   1738 C  CA    . PRO A 1 241 ? 152.742 126.490 157.773 1.00 35.18  ? 215 PRO A CA    1 
ATOM   1739 C  C     . PRO A 1 241 ? 152.890 127.978 158.061 1.00 32.34  ? 215 PRO A C     1 
ATOM   1740 O  O     . PRO A 1 241 ? 154.031 128.439 158.257 1.00 37.32  ? 215 PRO A O     1 
ATOM   1741 C  CB    . PRO A 1 241 ? 152.779 126.165 156.286 1.00 33.84  ? 215 PRO A CB    1 
ATOM   1742 C  CG    . PRO A 1 241 ? 151.817 125.010 156.137 1.00 31.33  ? 215 PRO A CG    1 
ATOM   1743 C  CD    . PRO A 1 241 ? 150.690 125.405 157.019 1.00 32.27  ? 215 PRO A CD    1 
ATOM   1744 N  N     . VAL A 1 242 ? 151.773 128.693 158.135 1.00 31.98  ? 216 VAL A N     1 
ATOM   1745 C  CA    . VAL A 1 242 ? 151.771 130.157 158.424 1.00 27.09  ? 216 VAL A CA    1 
ATOM   1746 C  C     . VAL A 1 242 ? 152.367 130.349 159.827 1.00 28.78  ? 216 VAL A C     1 
ATOM   1747 O  O     . VAL A 1 242 ? 153.077 131.343 160.031 1.00 39.02  ? 216 VAL A O     1 
ATOM   1748 C  CB    . VAL A 1 242 ? 150.381 130.802 158.274 1.00 27.74  ? 216 VAL A CB    1 
ATOM   1749 C  CG1   . VAL A 1 242 ? 150.417 132.307 158.492 1.00 31.63  ? 216 VAL A CG1   1 
ATOM   1750 C  CG2   . VAL A 1 242 ? 149.749 130.475 156.928 1.00 23.28  ? 216 VAL A CG2   1 
ATOM   1751 N  N     . TYR A 1 243 ? 152.067 129.444 160.759 1.00 28.29  ? 217 TYR A N     1 
ATOM   1752 C  CA    . TYR A 1 243 ? 152.586 129.657 162.123 1.00 31.87  ? 217 TYR A CA    1 
ATOM   1753 C  C     . TYR A 1 243 ? 154.102 129.670 162.087 1.00 31.74  ? 217 TYR A C     1 
ATOM   1754 O  O     . TYR A 1 243 ? 154.696 130.590 162.657 1.00 36.79  ? 217 TYR A O     1 
ATOM   1755 C  CB    . TYR A 1 243 ? 152.120 128.478 162.984 1.00 31.04  ? 217 TYR A CB    1 
ATOM   1756 C  CG    . TYR A 1 243 ? 152.592 128.511 164.430 1.00 32.67  ? 217 TYR A CG    1 
ATOM   1757 C  CD1   . TYR A 1 243 ? 153.863 128.078 164.783 1.00 31.14  ? 217 TYR A CD1   1 
ATOM   1758 C  CD2   . TYR A 1 243 ? 151.765 128.982 165.441 1.00 29.91  ? 217 TYR A CD2   1 
ATOM   1759 C  CE1   . TYR A 1 243 ? 154.304 128.126 166.092 1.00 38.46  ? 217 TYR A CE1   1 
ATOM   1760 C  CE2   . TYR A 1 243 ? 152.191 129.027 166.756 1.00 33.83  ? 217 TYR A CE2   1 
ATOM   1761 C  CZ    . TYR A 1 243 ? 153.463 128.595 167.082 1.00 39.96  ? 217 TYR A CZ    1 
ATOM   1762 O  OH    . TYR A 1 243 ? 153.897 128.632 168.373 1.00 44.74  ? 217 TYR A OH    1 
ATOM   1763 N  N     . PHE A 1 244 ? 154.713 128.733 161.362 1.00 34.56  ? 218 PHE A N     1 
ATOM   1764 C  CA    . PHE A 1 244 ? 156.191 128.697 161.252 1.00 22.00  ? 218 PHE A CA    1 
ATOM   1765 C  C     . PHE A 1 244 ? 156.713 129.933 160.545 1.00 26.54  ? 218 PHE A C     1 
ATOM   1766 O  O     . PHE A 1 244 ? 157.692 130.506 161.024 1.00 33.28  ? 218 PHE A O     1 
ATOM   1767 C  CB    . PHE A 1 244 ? 156.588 127.425 160.498 1.00 29.70  ? 218 PHE A CB    1 
ATOM   1768 C  CG    . PHE A 1 244 ? 158.059 127.333 160.123 1.00 31.55  ? 218 PHE A CG    1 
ATOM   1769 C  CD1   . PHE A 1 244 ? 159.031 127.124 161.094 1.00 30.30  ? 218 PHE A CD1   1 
ATOM   1770 C  CD2   . PHE A 1 244 ? 158.466 127.461 158.802 1.00 27.04  ? 218 PHE A CD2   1 
ATOM   1771 C  CE1   . PHE A 1 244 ? 160.369 127.052 160.750 1.00 31.51  ? 218 PHE A CE1   1 
ATOM   1772 C  CE2   . PHE A 1 244 ? 159.806 127.385 158.464 1.00 32.58  ? 218 PHE A CE2   1 
ATOM   1773 C  CZ    . PHE A 1 244 ? 160.753 127.182 159.438 1.00 33.26  ? 218 PHE A CZ    1 
ATOM   1774 N  N     . ILE A 1 245 ? 156.075 130.339 159.447 1.00 25.37  ? 219 ILE A N     1 
ATOM   1775 C  CA    . ILE A 1 245 ? 156.634 131.490 158.686 1.00 25.24  ? 219 ILE A CA    1 
ATOM   1776 C  C     . ILE A 1 245 ? 156.579 132.783 159.515 1.00 26.13  ? 219 ILE A C     1 
ATOM   1777 O  O     . ILE A 1 245 ? 157.602 133.478 159.567 1.00 37.06  ? 219 ILE A O     1 
ATOM   1778 C  CB    . ILE A 1 245 ? 155.931 131.641 157.323 1.00 28.98  ? 219 ILE A CB    1 
ATOM   1779 C  CG1   . ILE A 1 245 ? 155.990 130.348 156.518 1.00 36.02  ? 219 ILE A CG1   1 
ATOM   1780 C  CG2   . ILE A 1 245 ? 156.508 132.810 156.528 1.00 23.52  ? 219 ILE A CG2   1 
ATOM   1781 C  CD1   . ILE A 1 245 ? 155.040 130.313 155.336 1.00 29.74  ? 219 ILE A CD1   1 
ATOM   1782 N  N     . ALA A 1 246 ? 155.453 133.058 160.182 1.00 28.27  ? 220 ALA A N     1 
ATOM   1783 C  CA    . ALA A 1 246 ? 155.357 134.275 161.016 1.00 30.31  ? 220 ALA A CA    1 
ATOM   1784 C  C     . ALA A 1 246 ? 156.323 134.206 162.196 1.00 32.00  ? 220 ALA A C     1 
ATOM   1785 O  O     . ALA A 1 246 ? 157.029 135.189 162.460 1.00 40.15  ? 220 ALA A O     1 
ATOM   1786 C  CB    . ALA A 1 246 ? 153.932 134.484 161.469 1.00 50.00  ? 220 ALA A CB    1 
ATOM   1787 N  N     . GLU A 1 247 ? 156.377 133.053 162.853 1.00 31.20  ? 221 GLU A N     1 
ATOM   1788 C  CA    . GLU A 1 247 ? 157.262 132.887 164.032 1.00 28.03  ? 221 GLU A CA    1 
ATOM   1789 C  C     . GLU A 1 247 ? 158.737 132.996 163.630 1.00 26.02  ? 221 GLU A C     1 
ATOM   1790 O  O     . GLU A 1 247 ? 159.497 133.630 164.376 1.00 29.84  ? 221 GLU A O     1 
ATOM   1791 C  CB    . GLU A 1 247 ? 156.850 131.591 164.729 1.00 35.30  ? 221 GLU A CB    1 
ATOM   1792 C  CG    . GLU A 1 247 ? 155.580 131.740 165.561 1.00 31.17  ? 221 GLU A CG    1 
ATOM   1793 C  CD    . GLU A 1 247 ? 155.502 133.028 166.360 1.00 40.98  ? 221 GLU A CD    1 
ATOM   1794 O  OE1   . GLU A 1 247 ? 154.745 133.940 165.970 1.00 35.15  ? 221 GLU A OE1   1 
ATOM   1795 O  OE2   . GLU A 1 247 ? 156.206 133.117 167.384 1.00 44.50  ? 221 GLU A OE2   1 
ATOM   1796 N  N     . SER A 1 248 ? 159.107 132.386 162.508 1.00 33.44  ? 222 SER A N     1 
ATOM   1797 C  CA    . SER A 1 248 ? 160.506 132.402 162.021 1.00 23.65  ? 222 SER A CA    1 
ATOM   1798 C  C     . SER A 1 248 ? 160.967 133.816 161.660 1.00 29.22  ? 222 SER A C     1 
ATOM   1799 O  O     . SER A 1 248 ? 162.102 134.152 162.021 1.00 38.58  ? 222 SER A O     1 
ATOM   1800 C  CB    . SER A 1 248 ? 160.632 131.470 160.858 1.00 22.57  ? 222 SER A CB    1 
ATOM   1801 O  OG    . SER A 1 248 ? 159.999 131.996 159.702 1.00 33.90  ? 222 SER A OG    1 
ATOM   1802 N  N     . TYR A 1 249 ? 160.125 134.601 160.983 1.00 28.63  ? 223 TYR A N     1 
ATOM   1803 C  CA    . TYR A 1 249 ? 160.453 136.009 160.635 1.00 21.74  ? 223 TYR A CA    1 
ATOM   1804 C  C     . TYR A 1 249 ? 160.597 136.831 161.904 1.00 29.37  ? 223 TYR A C     1 
ATOM   1805 O  O     . TYR A 1 249 ? 161.540 137.614 161.991 1.00 37.02  ? 223 TYR A O     1 
ATOM   1806 C  CB    . TYR A 1 249 ? 159.337 136.587 159.765 1.00 29.46  ? 223 TYR A CB    1 
ATOM   1807 C  CG    . TYR A 1 249 ? 159.345 136.308 158.268 1.00 29.55  ? 223 TYR A CG    1 
ATOM   1808 C  CD1   . TYR A 1 249 ? 159.585 135.038 157.762 1.00 28.13  ? 223 TYR A CD1   1 
ATOM   1809 C  CD2   . TYR A 1 249 ? 159.074 137.323 157.361 1.00 32.01  ? 223 TYR A CD2   1 
ATOM   1810 C  CE1   . TYR A 1 249 ? 159.564 134.787 156.401 1.00 28.49  ? 223 TYR A CE1   1 
ATOM   1811 C  CE2   . TYR A 1 249 ? 159.051 137.086 155.998 1.00 30.35  ? 223 TYR A CE2   1 
ATOM   1812 C  CZ    . TYR A 1 249 ? 159.297 135.815 155.518 1.00 32.33  ? 223 TYR A CZ    1 
ATOM   1813 O  OH    . TYR A 1 249 ? 159.272 135.583 154.177 1.00 36.17  ? 223 TYR A OH    1 
ATOM   1814 N  N     . ARG A 1 250 ? 159.711 136.630 162.878 1.00 30.45  ? 224 ARG A N     1 
ATOM   1815 C  CA    . ARG A 1 250 ? 159.745 137.353 164.173 1.00 21.33  ? 224 ARG A CA    1 
ATOM   1816 C  C     . ARG A 1 250 ? 161.029 137.009 164.937 1.00 19.67  ? 224 ARG A C     1 
ATOM   1817 O  O     . ARG A 1 250 ? 161.582 137.896 165.593 1.00 28.51  ? 224 ARG A O     1 
ATOM   1818 C  CB    . ARG A 1 250 ? 158.450 137.041 164.929 1.00 27.96  ? 224 ARG A CB    1 
ATOM   1819 C  CG    . ARG A 1 250 ? 157.278 137.921 164.522 1.00 27.73  ? 224 ARG A CG    1 
ATOM   1820 C  CD    . ARG A 1 250 ? 156.071 137.705 165.411 1.00 26.32  ? 224 ARG A CD    1 
ATOM   1821 N  NE    . ARG A 1 250 ? 154.865 138.303 164.830 1.00 29.37  ? 224 ARG A NE    1 
ATOM   1822 C  CZ    . ARG A 1 250 ? 153.719 137.667 164.659 1.00 31.40  ? 224 ARG A CZ    1 
ATOM   1823 N  NH1   . ARG A 1 250 ? 153.648 136.366 164.854 1.00 30.04  ? 224 ARG A NH1   1 
ATOM   1824 N  NH2   . ARG A 1 250 ? 152.646 138.336 164.291 1.00 20.72  ? 224 ARG A NH2   1 
ATOM   1825 N  N     . ALA A 1 251 ? 161.443 135.750 164.897 1.00 38.60  ? 225 ALA A N     1 
ATOM   1826 C  CA    . ALA A 1 251 ? 162.670 135.331 165.601 1.00 28.45  ? 225 ALA A CA    1 
ATOM   1827 C  C     . ALA A 1 251 ? 163.880 135.837 164.822 1.00 35.23  ? 225 ALA A C     1 
ATOM   1828 O  O     . ALA A 1 251 ? 164.883 136.192 165.461 1.00 44.79  ? 225 ALA A O     1 
ATOM   1829 C  CB    . ALA A 1 251 ? 162.691 133.838 165.736 1.00 31.35  ? 225 ALA A CB    1 
ATOM   1830 N  N     . ALA A 1 252 ? 163.777 135.904 163.491 1.00 35.90  ? 226 ALA A N     1 
ATOM   1831 C  CA    . ALA A 1 252 ? 164.907 136.443 162.744 1.00 26.89  ? 226 ALA A CA    1 
ATOM   1832 C  C     . ALA A 1 252 ? 165.015 137.956 162.900 1.00 28.76  ? 226 ALA A C     1 
ATOM   1833 O  O     . ALA A 1 252 ? 166.121 138.494 163.018 1.00 41.17  ? 226 ALA A O     1 
ATOM   1834 C  CB    . ALA A 1 252 ? 164.789 136.065 161.268 1.00 27.50  ? 226 ALA A CB    1 
ATOM   1835 N  N     . ILE A 1 253 ? 163.886 138.657 162.912 1.00 30.69  ? 227 ILE A N     1 
ATOM   1836 C  CA    . ILE A 1 253 ? 163.881 140.113 162.861 1.00 23.21  ? 227 ILE A CA    1 
ATOM   1837 C  C     . ILE A 1 253 ? 163.746 140.736 164.246 1.00 26.79  ? 227 ILE A C     1 
ATOM   1838 O  O     . ILE A 1 253 ? 164.529 141.614 164.609 1.00 40.30  ? 227 ILE A O     1 
ATOM   1839 C  CB    . ILE A 1 253 ? 162.767 140.602 161.910 1.00 30.04  ? 227 ILE A CB    1 
ATOM   1840 C  CG1   . ILE A 1 253 ? 163.032 140.098 160.490 1.00 26.74  ? 227 ILE A CG1   1 
ATOM   1841 C  CG2   . ILE A 1 253 ? 162.666 142.119 161.919 1.00 30.17  ? 227 ILE A CG2   1 
ATOM   1842 C  CD1   . ILE A 1 253 ? 161.850 140.217 159.560 1.00 27.02  ? 227 ILE A CD1   1 
ATOM   1843 N  N     . LEU A 1 254 ? 162.776 140.291 165.045 1.00 34.72  ? 228 LEU A N     1 
ATOM   1844 C  CA    . LEU A 1 254 ? 162.460 140.973 166.299 1.00 29.22  ? 228 LEU A CA    1 
ATOM   1845 C  C     . LEU A 1 254 ? 163.209 140.387 167.494 1.00 33.12  ? 228 LEU A C     1 
ATOM   1846 O  O     . LEU A 1 254 ? 163.907 141.111 168.210 1.00 40.93  ? 228 LEU A O     1 
ATOM   1847 C  CB    . LEU A 1 254 ? 160.951 140.923 166.558 1.00 31.48  ? 228 LEU A CB    1 
ATOM   1848 C  CG    . LEU A 1 254 ? 160.041 141.623 165.554 1.00 31.41  ? 228 LEU A CG    1 
ATOM   1849 C  CD1   . LEU A 1 254 ? 158.596 141.233 165.796 1.00 27.36  ? 228 LEU A CD1   1 
ATOM   1850 C  CD2   . LEU A 1 254 ? 160.211 143.126 165.625 1.00 29.24  ? 228 LEU A CD2   1 
ATOM   1851 N  N     . TYR A 1 255 ? 163.066 139.082 167.723 1.00 41.33  ? 229 TYR A N     1 
ATOM   1852 C  CA    . TYR A 1 255 ? 163.511 138.483 168.976 1.00 32.97  ? 229 TYR A CA    1 
ATOM   1853 C  C     . TYR A 1 255 ? 165.007 138.207 169.020 1.00 39.09  ? 229 TYR A C     1 
ATOM   1854 O  O     . TYR A 1 255 ? 165.537 137.998 170.119 1.00 46.56  ? 229 TYR A O     1 
ATOM   1855 C  CB    . TYR A 1 255 ? 162.745 137.185 169.236 1.00 36.03  ? 229 TYR A CB    1 
ATOM   1856 C  CG    . TYR A 1 255 ? 161.245 137.357 169.282 1.00 36.51  ? 229 TYR A CG    1 
ATOM   1857 C  CD1   . TYR A 1 255 ? 160.671 138.457 169.910 1.00 42.36  ? 229 TYR A CD1   1 
ATOM   1858 C  CD2   . TYR A 1 255 ? 160.403 136.419 168.700 1.00 35.30  ? 229 TYR A CD2   1 
ATOM   1859 C  CE1   . TYR A 1 255 ? 159.299 138.619 169.952 1.00 44.66  ? 229 TYR A CE1   1 
ATOM   1860 C  CE2   . TYR A 1 255 ? 159.031 136.571 168.738 1.00 36.43  ? 229 TYR A CE2   1 
ATOM   1861 C  CZ    . TYR A 1 255 ? 158.486 137.672 169.365 1.00 42.85  ? 229 TYR A CZ    1 
ATOM   1862 O  OH    . TYR A 1 255 ? 157.121 137.824 169.405 1.00 52.69  ? 229 TYR A OH    1 
ATOM   1863 N  N     . HIS A 1 256 ? 165.678 138.206 167.864 1.00 41.92  ? 230 HIS A N     1 
ATOM   1864 C  CA    . HIS A 1 256 ? 167.121 137.971 167.716 1.00 35.54  ? 230 HIS A CA    1 
ATOM   1865 C  C     . HIS A 1 256 ? 167.538 136.624 168.309 1.00 42.70  ? 230 HIS A C     1 
ATOM   1866 O  O     . HIS A 1 256 ? 168.400 136.532 169.184 1.00 44.51  ? 230 HIS A O     1 
ATOM   1867 C  CB    . HIS A 1 256 ? 167.941 139.117 168.322 1.00 36.93  ? 230 HIS A CB    1 
ATOM   1868 C  CG    . HIS A 1 256 ? 167.509 140.476 167.869 1.00 40.85  ? 230 HIS A CG    1 
ATOM   1869 N  ND1   . HIS A 1 256 ? 167.122 141.463 168.749 1.00 43.60  ? 230 HIS A ND1   1 
ATOM   1870 C  CD2   . HIS A 1 256 ? 167.406 141.013 166.631 1.00 41.49  ? 230 HIS A CD2   1 
ATOM   1871 C  CE1   . HIS A 1 256 ? 166.797 142.550 168.072 1.00 46.77  ? 230 HIS A CE1   1 
ATOM   1872 N  NE2   . HIS A 1 256 ? 166.960 142.303 166.785 1.00 45.70  ? 230 HIS A NE2   1 
ATOM   1873 N  N     . GLU A 1 257 ? 166.900 135.568 167.813 1.00 41.32  ? 231 GLU A N     1 
ATOM   1874 C  CA    . GLU A 1 257 ? 167.207 134.213 168.241 1.00 33.75  ? 231 GLU A CA    1 
ATOM   1875 C  C     . GLU A 1 257 ? 167.260 133.304 167.024 1.00 38.20  ? 231 GLU A C     1 
ATOM   1876 O  O     . GLU A 1 257 ? 166.646 133.578 165.991 1.00 40.12  ? 231 GLU A O     1 
ATOM   1877 C  CB    . GLU A 1 257 ? 166.175 133.688 169.246 1.00 38.53  ? 231 GLU A CB    1 
ATOM   1878 C  CG    . GLU A 1 257 ? 164.747 134.069 168.915 1.00 40.94  ? 231 GLU A CG    1 
ATOM   1879 C  CD    . GLU A 1 257 ? 163.734 133.101 169.491 1.00 51.45  ? 231 GLU A CD    1 
ATOM   1880 O  OE1   . GLU A 1 257 ? 163.053 133.468 170.472 1.00 49.67  ? 231 GLU A OE1   1 
ATOM   1881 O  OE2   . GLU A 1 257 ? 163.618 131.974 168.965 1.00 51.16  ? 231 GLU A OE2   1 
ATOM   1882 N  N     . TRP A 1 258 ? 168.015 132.217 167.156 1.00 41.29  ? 232 TRP A N     1 
ATOM   1883 C  CA    . TRP A 1 258 ? 168.048 131.177 166.134 1.00 35.08  ? 232 TRP A CA    1 
ATOM   1884 C  C     . TRP A 1 258 ? 166.814 130.306 166.315 1.00 35.27  ? 232 TRP A C     1 
ATOM   1885 O  O     . TRP A 1 258 ? 166.685 129.598 167.319 1.00 45.41  ? 232 TRP A O     1 
ATOM   1886 C  CB    . TRP A 1 258 ? 169.330 130.356 166.232 1.00 31.87  ? 232 TRP A CB    1 
ATOM   1887 C  CG    . TRP A 1 258 ? 170.581 131.177 166.239 1.00 41.03  ? 232 TRP A CG    1 
ATOM   1888 C  CD1   . TRP A 1 258 ? 171.401 131.411 167.301 1.00 39.26  ? 232 TRP A CD1   1 
ATOM   1889 C  CD2   . TRP A 1 258 ? 171.158 131.870 165.126 1.00 40.77  ? 232 TRP A CD2   1 
ATOM   1890 N  NE1   . TRP A 1 258 ? 172.453 132.209 166.921 1.00 37.13  ? 232 TRP A NE1   1 
ATOM   1891 C  CE2   . TRP A 1 258 ? 172.328 132.503 165.590 1.00 37.51  ? 232 TRP A CE2   1 
ATOM   1892 C  CE3   . TRP A 1 258 ? 170.800 132.016 163.783 1.00 33.73  ? 232 TRP A CE3   1 
ATOM   1893 C  CZ2   . TRP A 1 258 ? 173.139 133.272 164.759 1.00 34.51  ? 232 TRP A CZ2   1 
ATOM   1894 C  CZ3   . TRP A 1 258 ? 171.604 132.777 162.962 1.00 33.96  ? 232 TRP A CZ3   1 
ATOM   1895 C  CH2   . TRP A 1 258 ? 172.761 133.396 163.451 1.00 36.29  ? 232 TRP A CH2   1 
ATOM   1896 N  N     . TYR A 1 259 ? 165.903 130.361 165.343 1.00 33.76  ? 233 TYR A N     1 
ATOM   1897 C  CA    . TYR A 1 259 ? 164.599 129.729 165.506 1.00 37.51  ? 233 TYR A CA    1 
ATOM   1898 C  C     . TYR A 1 259 ? 164.683 128.212 165.366 1.00 37.87  ? 233 TYR A C     1 
ATOM   1899 O  O     . TYR A 1 259 ? 163.802 127.491 165.846 1.00 39.88  ? 233 TYR A O     1 
ATOM   1900 C  CB    . TYR A 1 259 ? 163.615 130.319 164.494 1.00 33.95  ? 233 TYR A CB    1 
ATOM   1901 C  CG    . TYR A 1 259 ? 162.182 129.897 164.708 1.00 34.35  ? 233 TYR A CG    1 
ATOM   1902 C  CD1   . TYR A 1 259 ? 161.481 130.295 165.840 1.00 38.23  ? 233 TYR A CD1   1 
ATOM   1903 C  CD2   . TYR A 1 259 ? 161.532 129.097 163.780 1.00 34.56  ? 233 TYR A CD2   1 
ATOM   1904 C  CE1   . TYR A 1 259 ? 160.171 129.905 166.039 1.00 30.73  ? 233 TYR A CE1   1 
ATOM   1905 C  CE2   . TYR A 1 259 ? 160.225 128.703 163.972 1.00 34.28  ? 233 TYR A CE2   1 
ATOM   1906 C  CZ    . TYR A 1 259 ? 159.550 129.109 165.100 1.00 34.07  ? 233 TYR A CZ    1 
ATOM   1907 O  OH    . TYR A 1 259 ? 158.249 128.712 165.288 1.00 45.37  ? 233 TYR A OH    1 
ATOM   1908 N  N     . PHE A 1 260 ? 165.742 127.705 164.731 1.00 46.85  ? 234 PHE A N     1 
ATOM   1909 C  CA    . PHE A 1 260 ? 165.808 126.278 164.441 1.00 42.45  ? 234 PHE A CA    1 
ATOM   1910 C  C     . PHE A 1 260 ? 166.402 125.459 165.583 1.00 41.51  ? 234 PHE A C     1 
ATOM   1911 O  O     . PHE A 1 260 ? 166.459 124.231 165.474 1.00 52.89  ? 234 PHE A O     1 
ATOM   1912 C  CB    . PHE A 1 260 ? 166.599 126.035 163.152 1.00 40.04  ? 234 PHE A CB    1 
ATOM   1913 C  CG    . PHE A 1 260 ? 167.816 126.903 162.999 1.00 42.35  ? 234 PHE A CG    1 
ATOM   1914 C  CD1   . PHE A 1 260 ? 168.992 126.594 163.661 1.00 40.66  ? 234 PHE A CD1   1 
ATOM   1915 C  CD2   . PHE A 1 260 ? 167.792 128.012 162.169 1.00 43.97  ? 234 PHE A CD2   1 
ATOM   1916 C  CE1   . PHE A 1 260 ? 170.115 127.386 163.520 1.00 41.95  ? 234 PHE A CE1   1 
ATOM   1917 C  CE2   . PHE A 1 260 ? 168.913 128.807 162.020 1.00 43.09  ? 234 PHE A CE2   1 
ATOM   1918 C  CZ    . PHE A 1 260 ? 170.074 128.492 162.696 1.00 43.00  ? 234 PHE A CZ    1 
ATOM   1919 N  N     . MET A 1 261 ? 166.856 126.098 166.664 1.00 47.85  ? 235 MET A N     1 
ATOM   1920 C  CA    . MET A 1 261 ? 167.335 125.332 167.812 1.00 49.19  ? 235 MET A CA    1 
ATOM   1921 C  C     . MET A 1 261 ? 166.184 124.680 168.567 1.00 54.23  ? 235 MET A C     1 
ATOM   1922 O  O     . MET A 1 261 ? 166.294 123.528 169.002 1.00 58.40  ? 235 MET A O     1 
ATOM   1923 C  CB    . MET A 1 261 ? 168.149 126.222 168.751 1.00 50.36  ? 235 MET A CB    1 
ATOM   1924 C  CG    . MET A 1 261 ? 169.125 127.146 168.058 1.00 54.30  ? 235 MET A CG    1 
ATOM   1925 S  SD    . MET A 1 261 ? 170.232 126.250 166.955 1.00 68.81  ? 235 MET A SD    1 
ATOM   1926 C  CE    . MET A 1 261 ? 171.724 126.191 167.941 1.00 52.10  ? 235 MET A CE    1 
ATOM   1927 N  N     . ASP A 1 262 ? 165.075 125.395 168.733 1.00 51.75  ? 236 ASP A N     1 
ATOM   1928 C  CA    . ASP A 1 262 ? 163.950 124.889 169.504 1.00 49.57  ? 236 ASP A CA    1 
ATOM   1929 C  C     . ASP A 1 262 ? 162.796 124.399 168.642 1.00 53.40  ? 236 ASP A C     1 
ATOM   1930 O  O     . ASP A 1 262 ? 161.883 123.756 169.169 1.00 60.30  ? 236 ASP A O     1 
ATOM   1931 C  CB    . ASP A 1 262 ? 163.441 125.974 170.458 1.00 52.19  ? 236 ASP A CB    1 
ATOM   1932 C  CG    . ASP A 1 262 ? 164.565 126.694 171.173 1.00 60.02  ? 236 ASP A CG    1 
ATOM   1933 O  OD1   . ASP A 1 262 ? 165.003 127.753 170.675 1.00 63.55  ? 236 ASP A OD1   1 
ATOM   1934 O  OD2   . ASP A 1 262 ? 165.013 126.202 172.229 1.00 57.93  ? 236 ASP A OD2   1 
ATOM   1935 N  N     . HIS A 1 263 ? 162.810 124.679 167.341 1.00 43.95  ? 237 HIS A N     1 
ATOM   1936 C  CA    . HIS A 1 263 ? 161.692 124.367 166.457 1.00 46.52  ? 237 HIS A CA    1 
ATOM   1937 C  C     . HIS A 1 263 ? 162.179 123.665 165.198 1.00 47.86  ? 237 HIS A C     1 
ATOM   1938 O  O     . HIS A 1 263 ? 161.725 123.941 164.086 1.00 56.41  ? 237 HIS A O     1 
ATOM   1939 C  CB    . HIS A 1 263 ? 160.918 125.633 166.104 1.00 39.61  ? 237 HIS A CB    1 
ATOM   1940 C  CG    . HIS A 1 263 ? 160.396 126.373 167.295 1.00 46.75  ? 237 HIS A CG    1 
ATOM   1941 N  ND1   . HIS A 1 263 ? 161.123 127.348 167.942 1.00 49.28  ? 237 HIS A ND1   1 
ATOM   1942 C  CD2   . HIS A 1 263 ? 159.220 126.279 167.958 1.00 45.69  ? 237 HIS A CD2   1 
ATOM   1943 C  CE1   . HIS A 1 263 ? 160.417 127.825 168.951 1.00 47.19  ? 237 HIS A CE1   1 
ATOM   1944 N  NE2   . HIS A 1 263 ? 159.258 127.193 168.983 1.00 48.57  ? 237 HIS A NE2   1 
ATOM   1945 N  N     . TRP A 1 264 ? 163.123 122.735 165.359 1.00 42.87  ? 238 TRP A N     1 
ATOM   1946 C  CA    . TRP A 1 264 ? 163.630 121.999 164.205 1.00 46.73  ? 238 TRP A CA    1 
ATOM   1947 C  C     . TRP A 1 264 ? 162.637 120.948 163.722 1.00 50.05  ? 238 TRP A C     1 
ATOM   1948 O  O     . TRP A 1 264 ? 162.583 120.658 162.520 1.00 52.68  ? 238 TRP A O     1 
ATOM   1949 C  CB    . TRP A 1 264 ? 164.977 121.357 164.540 1.00 46.41  ? 238 TRP A CB    1 
ATOM   1950 C  CG    . TRP A 1 264 ? 164.926 120.365 165.660 1.00 49.57  ? 238 TRP A CG    1 
ATOM   1951 C  CD1   . TRP A 1 264 ? 164.993 120.632 166.996 1.00 49.51  ? 238 TRP A CD1   1 
ATOM   1952 C  CD2   . TRP A 1 264 ? 164.801 118.944 165.540 1.00 51.94  ? 238 TRP A CD2   1 
ATOM   1953 N  NE1   . TRP A 1 264 ? 164.915 119.465 167.716 1.00 54.66  ? 238 TRP A NE1   1 
ATOM   1954 C  CE2   . TRP A 1 264 ? 164.797 118.414 166.846 1.00 53.51  ? 238 TRP A CE2   1 
ATOM   1955 C  CE3   . TRP A 1 264 ? 164.692 118.067 164.457 1.00 49.06  ? 238 TRP A CE3   1 
ATOM   1956 C  CZ2   . TRP A 1 264 ? 164.688 117.048 167.096 1.00 49.56  ? 238 TRP A CZ2   1 
ATOM   1957 C  CZ3   . TRP A 1 264 ? 164.583 116.712 164.707 1.00 54.04  ? 238 TRP A CZ3   1 
ATOM   1958 C  CH2   . TRP A 1 264 ? 164.582 116.216 166.017 1.00 51.75  ? 238 TRP A CH2   1 
ATOM   1959 N  N     . LYS A 1 265 ? 161.847 120.373 164.635 1.00 46.42  ? 239 LYS A N     1 
ATOM   1960 C  CA    . LYS A 1 265 ? 160.832 119.398 164.244 1.00 41.63  ? 239 LYS A CA    1 
ATOM   1961 C  C     . LYS A 1 265 ? 159.715 120.054 163.443 1.00 42.70  ? 239 LYS A C     1 
ATOM   1962 O  O     . LYS A 1 265 ? 159.206 119.471 162.478 1.00 52.65  ? 239 LYS A O     1 
ATOM   1963 C  CB    . LYS A 1 265 ? 160.267 118.708 165.484 1.00 45.32  ? 239 LYS A CB    1 
ATOM   1964 C  CG    . LYS A 1 265 ? 160.883 117.353 165.778 1.00 48.34  ? 239 LYS A CG    1 
ATOM   1965 C  CD    . LYS A 1 265 ? 160.224 116.700 166.981 1.00 50.54  ? 239 LYS A CD    1 
ATOM   1966 C  CE    . LYS A 1 265 ? 161.201 116.550 168.135 1.00 49.43  ? 239 LYS A CE    1 
ATOM   1967 N  NZ    . LYS A 1 265 ? 160.511 116.571 169.454 1.00 48.55  ? 239 LYS A NZ    1 
ATOM   1968 N  N     . LEU A 1 266 ? 159.329 121.273 163.829 1.00 39.53  ? 240 LEU A N     1 
ATOM   1969 C  CA    . LEU A 1 266 ? 158.338 122.031 163.071 1.00 37.26  ? 240 LEU A CA    1 
ATOM   1970 C  C     . LEU A 1 266 ? 158.860 122.397 161.686 1.00 36.29  ? 240 LEU A C     1 
ATOM   1971 O  O     . LEU A 1 266 ? 158.112 122.354 160.703 1.00 42.14  ? 240 LEU A O     1 
ATOM   1972 C  CB    . LEU A 1 266 ? 157.944 123.286 163.847 1.00 40.69  ? 240 LEU A CB    1 
ATOM   1973 C  CG    . LEU A 1 266 ? 156.618 123.953 163.487 1.00 41.47  ? 240 LEU A CG    1 
ATOM   1974 C  CD1   . LEU A 1 266 ? 155.464 122.979 163.629 1.00 38.24  ? 240 LEU A CD1   1 
ATOM   1975 C  CD2   . LEU A 1 266 ? 156.403 125.177 164.355 1.00 39.59  ? 240 LEU A CD2   1 
ATOM   1976 N  N     . MET A 1 267 ? 160.147 122.747 161.593 1.00 38.33  ? 241 MET A N     1 
ATOM   1977 C  CA    . MET A 1 267 ? 160.753 123.048 160.299 1.00 39.97  ? 241 MET A CA    1 
ATOM   1978 C  C     . MET A 1 267 ? 160.804 121.810 159.408 1.00 42.51  ? 241 MET A C     1 
ATOM   1979 O  O     . MET A 1 267 ? 160.565 121.898 158.198 1.00 49.19  ? 241 MET A O     1 
ATOM   1980 C  CB    . MET A 1 267 ? 162.160 123.611 160.495 1.00 40.48  ? 241 MET A CB    1 
ATOM   1981 C  CG    . MET A 1 267 ? 162.811 124.051 159.199 1.00 47.62  ? 241 MET A CG    1 
ATOM   1982 S  SD    . MET A 1 267 ? 164.239 125.120 159.395 1.00 56.89  ? 241 MET A SD    1 
ATOM   1983 C  CE    . MET A 1 267 ? 165.279 124.043 160.369 1.00 47.29  ? 241 MET A CE    1 
ATOM   1984 N  N     . LEU A 1 268 ? 161.112 120.647 159.996 1.00 38.48  ? 242 LEU A N     1 
ATOM   1985 C  CA    . LEU A 1 268 ? 161.112 119.394 159.242 1.00 36.41  ? 242 LEU A CA    1 
ATOM   1986 C  C     . LEU A 1 268 ? 159.712 119.034 158.755 1.00 35.51  ? 242 LEU A C     1 
ATOM   1987 O  O     . LEU A 1 268 ? 159.543 118.570 157.619 1.00 42.63  ? 242 LEU A O     1 
ATOM   1988 C  CB    . LEU A 1 268 ? 161.681 118.267 160.101 1.00 39.14  ? 242 LEU A CB    1 
ATOM   1989 C  CG    . LEU A 1 268 ? 163.202 118.195 160.229 1.00 42.29  ? 242 LEU A CG    1 
ATOM   1990 C  CD1   . LEU A 1 268 ? 163.605 117.016 161.096 1.00 42.14  ? 242 LEU A CD1   1 
ATOM   1991 C  CD2   . LEU A 1 268 ? 163.849 118.099 158.860 1.00 44.88  ? 242 LEU A CD2   1 
ATOM   1992 N  N     . TYR A 1 269 ? 158.700 119.249 159.602 1.00 31.73  ? 243 TYR A N     1 
ATOM   1993 C  CA    . TYR A 1 269 ? 157.312 119.017 159.207 1.00 32.88  ? 243 TYR A CA    1 
ATOM   1994 C  C     . TYR A 1 269 ? 156.894 119.948 158.074 1.00 31.78  ? 243 TYR A C     1 
ATOM   1995 O  O     . TYR A 1 269 ? 156.195 119.533 157.142 1.00 41.39  ? 243 TYR A O     1 
ATOM   1996 C  CB    . TYR A 1 269 ? 156.400 119.191 160.424 1.00 31.48  ? 243 TYR A CB    1 
ATOM   1997 C  CG    . TYR A 1 269 ? 154.957 119.510 160.104 1.00 36.87  ? 243 TYR A CG    1 
ATOM   1998 C  CD1   . TYR A 1 269 ? 154.101 118.529 159.618 1.00 36.58  ? 243 TYR A CD1   1 
ATOM   1999 C  CD2   . TYR A 1 269 ? 154.445 120.787 160.305 1.00 35.03  ? 243 TYR A CD2   1 
ATOM   2000 C  CE1   . TYR A 1 269 ? 152.780 118.812 159.329 1.00 31.23  ? 243 TYR A CE1   1 
ATOM   2001 C  CE2   . TYR A 1 269 ? 153.126 121.080 160.015 1.00 30.61  ? 243 TYR A CE2   1 
ATOM   2002 C  CZ    . TYR A 1 269 ? 152.300 120.088 159.529 1.00 35.62  ? 243 TYR A CZ    1 
ATOM   2003 O  OH    . TYR A 1 269 ? 150.986 120.374 159.243 1.00 42.52  ? 243 TYR A OH    1 
ATOM   2004 N  N     . ASN A 1 270 ? 157.337 121.204 158.128 1.00 37.11  ? 244 ASN A N     1 
ATOM   2005 C  CA    . ASN A 1 270 ? 157.014 122.165 157.079 1.00 29.25  ? 244 ASN A CA    1 
ATOM   2006 C  C     . ASN A 1 270 ? 157.713 121.830 155.762 1.00 38.39  ? 244 ASN A C     1 
ATOM   2007 O  O     . ASN A 1 270 ? 157.119 121.975 154.682 1.00 42.95  ? 244 ASN A O     1 
ATOM   2008 C  CB    . ASN A 1 270 ? 157.383 123.565 157.556 1.00 32.58  ? 244 ASN A CB    1 
ATOM   2009 C  CG    . ASN A 1 270 ? 156.359 124.141 158.503 1.00 34.48  ? 244 ASN A CG    1 
ATOM   2010 O  OD1   . ASN A 1 270 ? 155.421 124.802 158.080 1.00 37.93  ? 244 ASN A OD1   1 
ATOM   2011 N  ND2   . ASN A 1 270 ? 156.533 123.891 159.792 1.00 36.32  ? 244 ASN A ND2   1 
ATOM   2012 N  N     . PHE A 1 271 ? 158.971 121.377 155.832 1.00 38.34  ? 245 PHE A N     1 
ATOM   2013 C  CA    . PHE A 1 271 ? 159.675 120.917 154.635 1.00 31.24  ? 245 PHE A CA    1 
ATOM   2014 C  C     . PHE A 1 271 ? 159.001 119.691 154.031 1.00 39.77  ? 245 PHE A C     1 
ATOM   2015 O  O     . PHE A 1 271 ? 158.917 119.563 152.802 1.00 45.01  ? 245 PHE A O     1 
ATOM   2016 C  CB    . PHE A 1 271 ? 161.138 120.602 154.954 1.00 34.03  ? 245 PHE A CB    1 
ATOM   2017 C  CG    . PHE A 1 271 ? 161.991 121.812 155.215 1.00 40.05  ? 245 PHE A CG    1 
ATOM   2018 C  CD1   . PHE A 1 271 ? 161.593 123.075 154.803 1.00 46.41  ? 245 PHE A CD1   1 
ATOM   2019 C  CD2   . PHE A 1 271 ? 163.220 121.675 155.842 1.00 43.17  ? 245 PHE A CD2   1 
ATOM   2020 C  CE1   . PHE A 1 271 ? 162.392 124.182 155.039 1.00 38.68  ? 245 PHE A CE1   1 
ATOM   2021 C  CE2   . PHE A 1 271 ? 164.025 122.774 156.073 1.00 43.57  ? 245 PHE A CE2   1 
ATOM   2022 C  CZ    . PHE A 1 271 ? 163.609 124.029 155.672 1.00 40.06  ? 245 PHE A CZ    1 
ATOM   2023 N  N     . GLY A 1 272 ? 158.515 118.780 154.880 1.00 33.79  ? 246 GLY A N     1 
ATOM   2024 C  CA    . GLY A 1 272 ? 157.768 117.636 154.383 1.00 31.48  ? 246 GLY A CA    1 
ATOM   2025 C  C     . GLY A 1 272 ? 156.455 118.025 153.729 1.00 32.87  ? 246 GLY A C     1 
ATOM   2026 O  O     . GLY A 1 272 ? 156.052 117.425 152.730 1.00 41.41  ? 246 GLY A O     1 
ATOM   2027 N  N     . ILE A 1 273 ? 155.780 119.041 154.279 1.00 30.51  ? 247 ILE A N     1 
ATOM   2028 C  CA    . ILE A 1 273 ? 154.541 119.551 153.685 1.00 34.26  ? 247 ILE A CA    1 
ATOM   2029 C  C     . ILE A 1 273 ? 154.811 120.141 152.302 1.00 32.11  ? 247 ILE A C     1 
ATOM   2030 O  O     . ILE A 1 273 ? 154.073 119.880 151.339 1.00 35.47  ? 247 ILE A O     1 
ATOM   2031 C  CB    . ILE A 1 273 ? 153.883 120.576 154.633 1.00 36.38  ? 247 ILE A CB    1 
ATOM   2032 C  CG1   . ILE A 1 273 ? 153.197 119.857 155.805 1.00 33.00  ? 247 ILE A CG1   1 
ATOM   2033 C  CG2   . ILE A 1 273 ? 152.939 121.538 153.891 1.00 34.57  ? 247 ILE A CG2   1 
ATOM   2034 C  CD1   . ILE A 1 273 ? 151.731 119.517 155.591 1.00 38.07  ? 247 ILE A CD1   1 
ATOM   2035 N  N     . VAL A 1 274 ? 155.899 120.914 152.182 1.00 34.14  ? 248 VAL A N     1 
ATOM   2036 C  CA    . VAL A 1 274 ? 156.290 121.505 150.900 1.00 35.68  ? 248 VAL A CA    1 
ATOM   2037 C  C     . VAL A 1 274 ? 156.637 120.420 149.883 1.00 35.63  ? 248 VAL A C     1 
ATOM   2038 O  O     . VAL A 1 274 ? 156.211 120.480 148.720 1.00 38.95  ? 248 VAL A O     1 
ATOM   2039 C  CB    . VAL A 1 274 ? 157.457 122.493 151.110 1.00 40.88  ? 248 VAL A CB    1 
ATOM   2040 C  CG1   . VAL A 1 274 ? 158.257 122.724 149.828 1.00 33.43  ? 248 VAL A CG1   1 
ATOM   2041 C  CG2   . VAL A 1 274 ? 156.935 123.806 151.625 1.00 34.51  ? 248 VAL A CG2   1 
ATOM   2042 N  N     . ALA A 1 275 ? 157.380 119.395 150.317 1.00 39.54  ? 249 ALA A N     1 
ATOM   2043 C  CA    . ALA A 1 275 ? 157.764 118.302 149.425 1.00 34.08  ? 249 ALA A CA    1 
ATOM   2044 C  C     . ALA A 1 275 ? 156.556 117.494 148.963 1.00 32.01  ? 249 ALA A C     1 
ATOM   2045 O  O     . ALA A 1 275 ? 156.481 117.100 147.793 1.00 42.82  ? 249 ALA A O     1 
ATOM   2046 C  CB    . ALA A 1 275 ? 158.780 117.395 150.119 1.00 33.08  ? 249 ALA A CB    1 
ATOM   2047 N  N     . ILE A 1 276 ? 155.595 117.253 149.861 1.00 36.16  ? 250 ILE A N     1 
ATOM   2048 C  CA    . ILE A 1 276 ? 154.389 116.506 149.509 1.00 35.39  ? 250 ILE A CA    1 
ATOM   2049 C  C     . ILE A 1 276 ? 153.533 117.292 148.518 1.00 32.80  ? 250 ILE A C     1 
ATOM   2050 O  O     . ILE A 1 276 ? 153.033 116.732 147.528 1.00 41.10  ? 250 ILE A O     1 
ATOM   2051 C  CB    . ILE A 1 276 ? 153.615 116.141 150.794 1.00 37.29  ? 250 ILE A CB    1 
ATOM   2052 C  CG1   . ILE A 1 276 ? 154.250 114.924 151.468 1.00 37.19  ? 250 ILE A CG1   1 
ATOM   2053 C  CG2   . ILE A 1 276 ? 152.141 115.867 150.522 1.00 37.79  ? 250 ILE A CG2   1 
ATOM   2054 C  CD1   . ILE A 1 276 ? 153.952 114.819 152.945 1.00 39.13  ? 250 ILE A CD1   1 
ATOM   2055 N  N     . PHE A 1 277 ? 153.376 118.601 148.755 1.00 36.52  ? 251 PHE A N     1 
ATOM   2056 C  CA    . PHE A 1 277 ? 152.615 119.456 147.845 1.00 33.36  ? 251 PHE A CA    1 
ATOM   2057 C  C     . PHE A 1 277 ? 153.264 119.519 146.467 1.00 32.65  ? 251 PHE A C     1 
ATOM   2058 O  O     . PHE A 1 277 ? 152.578 119.412 145.443 1.00 43.23  ? 251 PHE A O     1 
ATOM   2059 C  CB    . PHE A 1 277 ? 152.482 120.859 148.437 1.00 34.74  ? 251 PHE A CB    1 
ATOM   2060 C  CG    . PHE A 1 277 ? 151.163 121.114 149.104 1.00 35.37  ? 251 PHE A CG    1 
ATOM   2061 C  CD1   . PHE A 1 277 ? 150.014 121.290 148.351 1.00 35.77  ? 251 PHE A CD1   1 
ATOM   2062 C  CD2   . PHE A 1 277 ? 151.071 121.173 150.486 1.00 34.39  ? 251 PHE A CD2   1 
ATOM   2063 C  CE1   . PHE A 1 277 ? 148.795 121.526 148.964 1.00 35.90  ? 251 PHE A CE1   1 
ATOM   2064 C  CE2   . PHE A 1 277 ? 149.858 121.406 151.104 1.00 37.79  ? 251 PHE A CE2   1 
ATOM   2065 C  CZ    . PHE A 1 277 ? 148.718 121.582 150.342 1.00 36.04  ? 251 PHE A CZ    1 
ATOM   2066 N  N     . PHE A 1 278 ? 154.596 119.649 146.431 1.00 31.80  ? 252 PHE A N     1 
ATOM   2067 C  CA    . PHE A 1 278 ? 155.321 119.674 145.164 1.00 30.29  ? 252 PHE A CA    1 
ATOM   2068 C  C     . PHE A 1 278 ? 155.211 118.347 144.424 1.00 34.81  ? 252 PHE A C     1 
ATOM   2069 O  O     . PHE A 1 278 ? 155.051 118.331 143.199 1.00 38.14  ? 252 PHE A O     1 
ATOM   2070 C  CB    . PHE A 1 278 ? 156.790 120.026 145.403 1.00 33.95  ? 252 PHE A CB    1 
ATOM   2071 C  CG    . PHE A 1 278 ? 157.607 120.097 144.145 1.00 37.34  ? 252 PHE A CG    1 
ATOM   2072 C  CD1   . PHE A 1 278 ? 157.460 121.157 143.265 1.00 36.96  ? 252 PHE A CD1   1 
ATOM   2073 C  CD2   . PHE A 1 278 ? 158.521 119.099 143.839 1.00 35.31  ? 252 PHE A CD2   1 
ATOM   2074 C  CE1   . PHE A 1 278 ? 158.210 121.222 142.103 1.00 33.38  ? 252 PHE A CE1   1 
ATOM   2075 C  CE2   . PHE A 1 278 ? 159.273 119.159 142.679 1.00 33.25  ? 252 PHE A CE2   1 
ATOM   2076 C  CZ    . PHE A 1 278 ? 159.116 120.222 141.812 1.00 27.43  ? 252 PHE A CZ    1 
ATOM   2077 N  N     . ALA A 1 279 ? 155.271 117.227 145.153 1.00 36.71  ? 253 ALA A N     1 
ATOM   2078 C  CA    . ALA A 1 279 ? 155.213 115.912 144.521 1.00 29.85  ? 253 ALA A CA    1 
ATOM   2079 C  C     . ALA A 1 279 ? 153.848 115.647 143.899 1.00 32.88  ? 253 ALA A C     1 
ATOM   2080 O  O     . ALA A 1 279 ? 153.754 115.241 142.732 1.00 36.91  ? 253 ALA A O     1 
ATOM   2081 C  CB    . ALA A 1 279 ? 155.564 114.826 145.538 1.00 31.82  ? 253 ALA A CB    1 
ATOM   2082 N  N     . ILE A 1 280 ? 152.776 115.912 144.655 1.00 31.77  ? 254 ILE A N     1 
ATOM   2083 C  CA    . ILE A 1 280 ? 151.427 115.672 144.145 1.00 28.92  ? 254 ILE A CA    1 
ATOM   2084 C  C     . ILE A 1 280 ? 151.097 116.644 143.013 1.00 31.74  ? 254 ILE A C     1 
ATOM   2085 O  O     . ILE A 1 280 ? 150.504 116.253 141.996 1.00 40.39  ? 254 ILE A O     1 
ATOM   2086 C  CB    . ILE A 1 280 ? 150.404 115.743 145.297 1.00 33.50  ? 254 ILE A CB    1 
ATOM   2087 C  CG1   . ILE A 1 280 ? 150.735 114.682 146.350 1.00 29.71  ? 254 ILE A CG1   1 
ATOM   2088 C  CG2   . ILE A 1 280 ? 148.986 115.530 144.788 1.00 29.57  ? 254 ILE A CG2   1 
ATOM   2089 C  CD1   . ILE A 1 280 ? 149.756 114.620 147.504 1.00 35.74  ? 254 ILE A CD1   1 
ATOM   2090 N  N     . GLY A 1 281 ? 151.526 117.908 143.141 1.00 35.57  ? 255 GLY A N     1 
ATOM   2091 C  CA    . GLY A 1 281 ? 151.273 118.880 142.090 1.00 24.59  ? 255 GLY A CA    1 
ATOM   2092 C  C     . GLY A 1 281 ? 152.019 118.584 140.803 1.00 25.65  ? 255 GLY A C     1 
ATOM   2093 O  O     . GLY A 1 281 ? 151.456 118.709 139.713 1.00 32.54  ? 255 GLY A O     1 
ATOM   2094 N  N     . ALA A 1 282 ? 153.287 118.167 140.910 1.00 31.42  ? 256 ALA A N     1 
ATOM   2095 C  CA    . ALA A 1 282 ? 154.064 117.819 139.725 1.00 29.62  ? 256 ALA A CA    1 
ATOM   2096 C  C     . ALA A 1 282 ? 153.519 116.568 139.049 1.00 32.18  ? 256 ALA A C     1 
ATOM   2097 O  O     . ALA A 1 282 ? 153.474 116.503 137.813 1.00 36.00  ? 256 ALA A O     1 
ATOM   2098 C  CB    . ALA A 1 282 ? 155.535 117.633 140.096 1.00 32.05  ? 256 ALA A CB    1 
ATOM   2099 N  N     . TYR A 1 283 ? 153.046 115.564 139.759 1.00 36.16  ? 257 TYR A N     1 
ATOM   2100 C  CA    . TYR A 1 283 ? 152.445 114.382 139.099 1.00 30.38  ? 257 TYR A CA    1 
ATOM   2101 C  C     . TYR A 1 283 ? 151.159 114.739 138.365 1.00 28.01  ? 257 TYR A C     1 
ATOM   2102 O  O     . TYR A 1 283 ? 150.981 114.271 137.260 1.00 37.40  ? 257 TYR A O     1 
ATOM   2103 C  CB    . TYR A 1 283 ? 152.282 113.329 140.193 1.00 35.80  ? 257 TYR A CB    1 
ATOM   2104 C  CG    . TYR A 1 283 ? 151.425 112.146 139.777 1.00 42.32  ? 257 TYR A CG    1 
ATOM   2105 C  CD1   . TYR A 1 283 ? 151.991 111.058 139.128 1.00 36.09  ? 257 TYR A CD1   1 
ATOM   2106 C  CD2   . TYR A 1 283 ? 150.055 112.135 139.998 1.00 39.38  ? 257 TYR A CD2   1 
ATOM   2107 C  CE1   . TYR A 1 283 ? 151.220 109.986 138.721 1.00 34.74  ? 257 TYR A CE1   1 
ATOM   2108 C  CE2   . TYR A 1 283 ? 149.273 111.074 139.585 1.00 38.28  ? 257 TYR A CE2   1 
ATOM   2109 C  CZ    . TYR A 1 283 ? 149.859 109.997 138.950 1.00 38.61  ? 257 TYR A CZ    1 
ATOM   2110 O  OH    . TYR A 1 283 ? 149.098 108.939 138.555 1.00 44.71  ? 257 TYR A OH    1 
ATOM   2111 N  N     . LEU A 1 284 ? 150.266 115.485 138.996 1.00 26.18  ? 258 LEU A N     1 
ATOM   2112 C  CA    . LEU A 1 284 ? 148.968 115.824 138.377 1.00 27.24  ? 258 LEU A CA    1 
ATOM   2113 C  C     . LEU A 1 284 ? 149.140 116.673 137.122 1.00 31.07  ? 258 LEU A C     1 
ATOM   2114 O  O     . LEU A 1 284 ? 148.445 116.412 136.166 1.00 33.33  ? 258 LEU A O     1 
ATOM   2115 C  CB    . LEU A 1 284 ? 148.079 116.496 139.413 1.00 33.44  ? 258 LEU A CB    1 
ATOM   2116 C  CG    . LEU A 1 284 ? 147.231 115.547 140.259 1.00 35.69  ? 258 LEU A CG    1 
ATOM   2117 C  CD1   . LEU A 1 284 ? 146.172 116.366 140.948 1.00 40.99  ? 258 LEU A CD1   1 
ATOM   2118 C  CD2   . LEU A 1 284 ? 146.598 114.477 139.390 1.00 35.45  ? 258 LEU A CD2   1 
ATOM   2119 N  N     . HIS A 1 285 ? 150.042 117.643 137.137 1.00 33.28  ? 259 HIS A N     1 
ATOM   2120 C  CA    . HIS A 1 285 ? 150.319 118.524 135.986 1.00 31.29  ? 259 HIS A CA    1 
ATOM   2121 C  C     . HIS A 1 285 ? 150.859 117.728 134.795 1.00 32.28  ? 259 HIS A C     1 
ATOM   2122 O  O     . HIS A 1 285 ? 150.372 117.922 133.710 1.00 36.29  ? 259 HIS A O     1 
ATOM   2123 C  CB    . HIS A 1 285 ? 151.290 119.605 136.472 1.00 26.49  ? 259 HIS A CB    1 
ATOM   2124 C  CG    . HIS A 1 285 ? 151.763 120.552 135.423 1.00 28.30  ? 259 HIS A CG    1 
ATOM   2125 N  ND1   . HIS A 1 285 ? 151.102 121.712 135.095 1.00 25.35  ? 259 HIS A ND1   1 
ATOM   2126 C  CD2   . HIS A 1 285 ? 152.821 120.494 134.617 1.00 32.80  ? 259 HIS A CD2   1 
ATOM   2127 C  CE1   . HIS A 1 285 ? 151.745 122.314 134.117 1.00 29.31  ? 259 HIS A CE1   1 
ATOM   2128 N  NE2   . HIS A 1 285 ? 152.785 121.588 133.809 1.00 34.46  ? 259 HIS A NE2   1 
ATOM   2129 N  N     . MET A 1 286 ? 151.785 116.813 135.002 1.00 27.89  ? 260 MET A N     1 
ATOM   2130 C  CA    . MET A 1 286 ? 152.346 115.966 133.934 1.00 28.38  ? 260 MET A CA    1 
ATOM   2131 C  C     . MET A 1 286 ? 151.285 115.038 133.329 1.00 31.77  ? 260 MET A C     1 
ATOM   2132 O  O     . MET A 1 286 ? 151.319 114.899 132.110 1.00 39.11  ? 260 MET A O     1 
ATOM   2133 C  CB    . MET A 1 286 ? 153.603 115.277 134.470 1.00 36.85  ? 260 MET A CB    1 
ATOM   2134 C  CG    . MET A 1 286 ? 154.731 116.227 134.824 1.00 34.98  ? 260 MET A CG    1 
ATOM   2135 S  SD    . MET A 1 286 ? 155.142 117.475 133.592 1.00 49.54  ? 260 MET A SD    1 
ATOM   2136 C  CE    . MET A 1 286 ? 155.516 116.442 132.173 1.00 38.69  ? 260 MET A CE    1 
ATOM   2137 N  N     . LYS A 1 287 ? 150.396 114.453 134.121 1.00 38.48  ? 261 LYS A N     1 
ATOM   2138 C  CA    . LYS A 1 287 ? 149.269 113.617 133.637 1.00 32.88  ? 261 LYS A CA    1 
ATOM   2139 C  C     . LYS A 1 287 ? 148.235 114.378 132.777 1.00 38.19  ? 261 LYS A C     1 
ATOM   2140 O  O     . LYS A 1 287 ? 147.731 113.758 131.832 1.00 47.15  ? 261 LYS A O     1 
ATOM   2141 C  CB    . LYS A 1 287 ? 148.680 112.989 134.894 1.00 34.91  ? 261 LYS A CB    1 
ATOM   2142 C  CG    . LYS A 1 287 ? 147.494 112.080 134.714 1.00 37.11  ? 261 LYS A CG    1 
ATOM   2143 C  CD    . LYS A 1 287 ? 147.148 111.361 136.007 1.00 41.39  ? 261 LYS A CD    1 
ATOM   2144 C  CE    . LYS A 1 287 ? 146.525 110.040 135.726 1.00 44.46  ? 261 LYS A CE    1 
ATOM   2145 N  NZ    . LYS A 1 287 ? 145.101 110.073 136.055 1.00 46.03  ? 261 LYS A NZ    1 
ATOM   2146 N  N     . TYR A 1 288 ? 147.855 115.598 133.128 1.00 36.48  ? 262 TYR A N     1 
ATOM   2147 C  CA    . TYR A 1 288 ? 146.791 116.334 132.407 1.00 35.71  ? 262 TYR A CA    1 
ATOM   2148 C  C     . TYR A 1 288 ? 147.249 117.443 131.509 1.00 32.80  ? 262 TYR A C     1 
ATOM   2149 O  O     . TYR A 1 288 ? 146.383 117.889 130.806 1.00 34.80  ? 262 TYR A O     1 
ATOM   2150 C  CB    . TYR A 1 288 ? 145.851 116.794 133.524 1.00 36.36  ? 262 TYR A CB    1 
ATOM   2151 C  CG    . TYR A 1 288 ? 145.169 115.654 134.255 1.00 36.38  ? 262 TYR A CG    1 
ATOM   2152 C  CD1   . TYR A 1 288 ? 144.191 114.893 133.634 1.00 33.44  ? 262 TYR A CD1   1 
ATOM   2153 C  CD2   . TYR A 1 288 ? 145.499 115.352 135.564 1.00 32.61  ? 262 TYR A CD2   1 
ATOM   2154 C  CE1   . TYR A 1 288 ? 143.558 113.862 134.299 1.00 36.94  ? 262 TYR A CE1   1 
ATOM   2155 C  CE2   . TYR A 1 288 ? 144.882 114.316 136.234 1.00 39.63  ? 262 TYR A CE2   1 
ATOM   2156 C  CZ    . TYR A 1 288 ? 143.910 113.571 135.601 1.00 41.96  ? 262 TYR A CZ    1 
ATOM   2157 O  OH    . TYR A 1 288 ? 143.306 112.558 136.272 1.00 44.25  ? 262 TYR A OH    1 
ATOM   2158 N  N     . ARG A 1 289 ? 148.525 117.756 131.403 1.00 38.54  ? 263 ARG A N     1 
ATOM   2159 C  CA    . ARG A 1 289 ? 148.988 118.953 130.644 1.00 37.62  ? 263 ARG A CA    1 
ATOM   2160 C  C     . ARG A 1 289 ? 148.638 118.879 129.143 1.00 41.72  ? 263 ARG A C     1 
ATOM   2161 O  O     . ARG A 1 289 ? 148.370 119.941 128.574 1.00 40.29  ? 263 ARG A O     1 
ATOM   2162 C  CB    . ARG A 1 289 ? 150.452 119.296 130.951 1.00 36.71  ? 263 ARG A CB    1 
ATOM   2163 C  CG    . ARG A 1 289 ? 151.545 118.298 130.608 1.00 34.60  ? 263 ARG A CG    1 
ATOM   2164 C  CD    . ARG A 1 289 ? 152.827 118.968 130.166 1.00 42.03  ? 263 ARG A CD    1 
ATOM   2165 N  NE    . ARG A 1 289 ? 153.409 119.908 131.128 1.00 47.84  ? 263 ARG A NE    1 
ATOM   2166 C  CZ    . ARG A 1 289 ? 154.673 120.312 131.108 1.00 44.44  ? 263 ARG A CZ    1 
ATOM   2167 N  NH1   . ARG A 1 289 ? 155.038 121.386 131.774 1.00 41.45  ? 263 ARG A NH1   1 
ATOM   2168 N  NH2   . ARG A 1 289 ? 155.576 119.640 130.424 1.00 41.44  ? 263 ARG A NH2   1 
ATOM   2169 N  N     . ASP A 1 290 ? 148.740 117.721 128.504 1.00 44.73  ? 264 ASP A N     1 
ATOM   2170 C  CA    . ASP A 1 290 ? 148.354 117.507 127.081 1.00 40.47  ? 264 ASP A CA    1 
ATOM   2171 C  C     . ASP A 1 290 ? 146.852 117.703 126.880 1.00 41.67  ? 264 ASP A C     1 
ATOM   2172 O  O     . ASP A 1 290 ? 146.485 117.942 125.747 1.00 48.95  ? 264 ASP A O     1 
ATOM   2173 C  CB    . ASP A 1 290 ? 148.898 116.191 126.562 1.00 42.72  ? 264 ASP A CB    1 
ATOM   2174 C  CG    . ASP A 1 290 ? 150.411 116.040 126.592 1.00 52.61  ? 264 ASP A CG    1 
ATOM   2175 O  OD1   . ASP A 1 290 ? 151.090 116.973 127.057 1.00 52.67  ? 264 ASP A OD1   1 
ATOM   2176 O  OD2   . ASP A 1 290 ? 150.901 114.978 126.153 1.00 54.51  ? 264 ASP A OD2   1 
ATOM   2177 N  N     . GLN A 1 291 ? 146.021 117.414 127.871 1.00 40.36  ? 265 GLN A N     1 
ATOM   2178 C  CA    . GLN A 1 291 ? 144.545 117.470 127.808 1.00 34.76  ? 265 GLN A CA    1 
ATOM   2179 C  C     . GLN A 1 291 ? 143.959 118.775 128.346 1.00 37.90  ? 265 GLN A C     1 
ATOM   2180 O  O     . GLN A 1 291 ? 142.773 118.801 128.457 1.00 39.02  ? 265 GLN A O     1 
ATOM   2181 C  CB    . GLN A 1 291 ? 144.122 116.208 128.541 1.00 35.47  ? 265 GLN A CB    1 
ATOM   2182 C  CG    . GLN A 1 291 ? 144.688 114.926 127.946 1.00 43.18  ? 265 GLN A CG    1 
ATOM   2183 C  CD    . GLN A 1 291 ? 145.733 114.275 128.824 1.00 49.56  ? 265 GLN A CD    1 
ATOM   2184 O  OE1   . GLN A 1 291 ? 146.929 114.293 128.514 1.00 49.21  ? 265 GLN A OE1   1 
ATOM   2185 N  NE2   . GLN A 1 291 ? 145.290 113.694 129.931 1.00 44.04  ? 265 GLN A NE2   1 
ATOM   2186 N  N     . PHE A 1 292 ? 144.730 119.804 128.652 1.00 40.90  ? 266 PHE A N     1 
ATOM   2187 C  CA    . PHE A 1 292 ? 144.288 121.070 129.307 1.00 33.34  ? 266 PHE A CA    1 
ATOM   2188 C  C     . PHE A 1 292 ? 143.275 121.800 128.441 1.00 39.01  ? 266 PHE A C     1 
ATOM   2189 O  O     . PHE A 1 292 ? 142.356 122.346 129.036 1.00 45.53  ? 266 PHE A O     1 
ATOM   2190 C  CB    . PHE A 1 292 ? 145.474 121.968 129.661 1.00 34.97  ? 266 PHE A CB    1 
ATOM   2191 C  CG    . PHE A 1 292 ? 146.164 121.700 130.992 1.00 37.06  ? 266 PHE A CG    1 
ATOM   2192 C  CD1   . PHE A 1 292 ? 147.395 122.274 131.285 1.00 38.27  ? 266 PHE A CD1   1 
ATOM   2193 C  CD2   . PHE A 1 292 ? 145.587 120.875 131.948 1.00 35.35  ? 266 PHE A CD2   1 
ATOM   2194 C  CE1   . PHE A 1 292 ? 148.023 122.028 132.494 1.00 34.07  ? 266 PHE A CE1   1 
ATOM   2195 C  CE2   . PHE A 1 292 ? 146.221 120.639 133.153 1.00 29.55  ? 266 PHE A CE2   1 
ATOM   2196 C  CZ    . PHE A 1 292 ? 147.438 121.206 133.423 1.00 33.18  ? 266 PHE A CZ    1 
ATOM   2197 N  N     . ALA A 1 293 ? 143.414 121.787 127.127 1.00 43.30  ? 267 ALA A N     1 
ATOM   2198 C  CA    . ALA A 1 293 ? 142.484 122.394 126.159 1.00 39.54  ? 267 ALA A CA    1 
ATOM   2199 C  C     . ALA A 1 293 ? 141.118 121.748 126.325 1.00 42.29  ? 267 ALA A C     1 
ATOM   2200 O  O     . ALA A 1 293 ? 140.127 122.478 126.211 1.00 49.92  ? 267 ALA A O     1 
ATOM   2201 C  CB    . ALA A 1 293 ? 143.034 122.150 124.799 1.00 39.36  ? 267 ALA A CB    1 
ATOM   2202 N  N     . ASP A 1 294 ? 141.064 120.453 126.607 1.00 40.22  ? 268 ASP A N     1 
ATOM   2203 C  CA    . ASP A 1 294 ? 139.802 119.723 126.890 1.00 40.55  ? 268 ASP A CA    1 
ATOM   2204 C  C     . ASP A 1 294 ? 139.064 120.253 128.123 1.00 46.61  ? 268 ASP A C     1 
ATOM   2205 O  O     . ASP A 1 294 ? 137.835 120.189 128.119 1.00 54.88  ? 268 ASP A O     1 
ATOM   2206 C  CB    . ASP A 1 294 ? 140.069 118.248 127.103 1.00 45.61  ? 268 ASP A CB    1 
ATOM   2207 C  CG    . ASP A 1 294 ? 140.861 117.549 126.011 1.00 52.91  ? 268 ASP A CG    1 
ATOM   2208 O  OD1   . ASP A 1 294 ? 141.149 118.203 124.989 1.00 50.32  ? 268 ASP A OD1   1 
ATOM   2209 O  OD2   . ASP A 1 294 ? 141.185 116.357 126.197 1.00 54.26  ? 268 ASP A OD2   1 
ATOM   2210 N  N     . PHE A 1 295 ? 139.758 120.644 129.185 1.00 45.33  ? 269 PHE A N     1 
ATOM   2211 C  CA    . PHE A 1 295 ? 139.120 121.058 130.455 1.00 41.04  ? 269 PHE A CA    1 
ATOM   2212 C  C     . PHE A 1 295 ? 138.887 122.521 130.496 1.00 41.83  ? 269 PHE A C     1 
ATOM   2213 O  O     . PHE A 1 295 ? 138.331 123.004 131.478 1.00 45.06  ? 269 PHE A O     1 
ATOM   2214 C  CB    . PHE A 1 295 ? 140.132 120.614 131.503 1.00 42.27  ? 269 PHE A CB    1 
ATOM   2215 C  CG    . PHE A 1 295 ? 140.281 119.117 131.676 1.00 41.06  ? 269 PHE A CG    1 
ATOM   2216 C  CD1   . PHE A 1 295 ? 139.354 118.397 132.409 1.00 35.86  ? 269 PHE A CD1   1 
ATOM   2217 C  CD2   . PHE A 1 295 ? 141.363 118.445 131.127 1.00 42.41  ? 269 PHE A CD2   1 
ATOM   2218 C  CE1   . PHE A 1 295 ? 139.505 117.038 132.569 1.00 45.61  ? 269 PHE A CE1   1 
ATOM   2219 C  CE2   . PHE A 1 295 ? 141.503 117.083 131.284 1.00 43.93  ? 269 PHE A CE2   1 
ATOM   2220 C  CZ    . PHE A 1 295 ? 140.577 116.385 132.008 1.00 43.85  ? 269 PHE A CZ    1 
ATOM   2221 N  N     . LEU A 1 296 ? 139.271 123.231 129.457 1.00 44.83  ? 270 LEU A N     1 
ATOM   2222 C  CA    . LEU A 1 296 ? 139.225 124.706 129.520 1.00 44.44  ? 270 LEU A CA    1 
ATOM   2223 C  C     . LEU A 1 296 ? 138.008 125.171 128.745 1.00 49.27  ? 270 LEU A C     1 
ATOM   2224 O  O     . LEU A 1 296 ? 137.627 126.333 128.828 1.00 57.01  ? 270 LEU A O     1 
ATOM   2225 C  CB    . LEU A 1 296 ? 140.521 125.302 128.983 1.00 46.19  ? 270 LEU A CB    1 
ATOM   2226 C  CG    . LEU A 1 296 ? 141.652 125.414 130.007 1.00 45.24  ? 270 LEU A CG    1 
ATOM   2227 C  CD1   . LEU A 1 296 ? 142.637 126.478 129.609 1.00 44.46  ? 270 LEU A CD1   1 
ATOM   2228 C  CD2   . LEU A 1 296 ? 141.116 125.667 131.404 1.00 43.49  ? 270 LEU A CD2   1 
ATOM   2229 O  OXT   . LEU A 1 296 ? 137.453 124.310 128.072 1.00 50.00  ? 270 LEU A OXT   1 
ATOM   2230 N  N     . MET B 2 1   ? 160.740 113.496 99.777  1.00 83.17  ? 1   MET B N     1 
ATOM   2231 C  CA    . MET B 2 1   ? 160.779 112.042 99.877  1.00 85.77  ? 1   MET B CA    1 
ATOM   2232 C  C     . MET B 2 1   ? 160.772 111.599 101.336 1.00 85.64  ? 1   MET B C     1 
ATOM   2233 O  O     . MET B 2 1   ? 160.483 110.443 101.643 1.00 84.60  ? 1   MET B O     1 
ATOM   2234 C  CB    . MET B 2 1   ? 162.013 111.486 99.163  1.00 86.07  ? 1   MET B CB    1 
ATOM   2235 C  CG    . MET B 2 1   ? 162.029 111.741 97.665  1.00 86.41  ? 1   MET B CG    1 
ATOM   2236 S  SD    . MET B 2 1   ? 161.107 110.503 96.734  1.00 94.13  ? 1   MET B SD    1 
ATOM   2237 C  CE    . MET B 2 1   ? 162.356 109.954 95.574  1.00 85.82  ? 1   MET B CE    1 
ATOM   2238 N  N     . ASN B 2 2   ? 161.091 112.529 102.231 1.00 71.68  ? 2   ASN B N     1 
ATOM   2239 C  CA    . ASN B 2 2   ? 161.107 112.269 103.664 1.00 70.89  ? 2   ASN B CA    1 
ATOM   2240 C  C     . ASN B 2 2   ? 159.837 112.824 104.294 1.00 67.51  ? 2   ASN B C     1 
ATOM   2241 O  O     . ASN B 2 2   ? 159.445 113.961 104.016 1.00 66.47  ? 2   ASN B O     1 
ATOM   2242 C  CB    . ASN B 2 2   ? 162.341 112.890 104.319 1.00 72.08  ? 2   ASN B CB    1 
ATOM   2243 C  CG    . ASN B 2 2   ? 163.206 111.865 105.021 1.00 75.44  ? 2   ASN B CG    1 
ATOM   2244 O  OD1   . ASN B 2 2   ? 162.719 110.831 105.477 1.00 74.34  ? 2   ASN B OD1   1 
ATOM   2245 N  ND2   . ASN B 2 2   ? 164.501 112.149 105.113 1.00 72.92  ? 2   ASN B ND2   1 
ATOM   2246 N  N     . VAL B 2 3   ? 159.201 112.017 105.143 1.00 60.48  ? 3   VAL B N     1 
ATOM   2247 C  CA    . VAL B 2 3   ? 157.942 112.411 105.759 1.00 56.76  ? 3   VAL B CA    1 
ATOM   2248 C  C     . VAL B 2 3   ? 158.219 113.357 106.920 1.00 55.53  ? 3   VAL B C     1 
ATOM   2249 O  O     . VAL B 2 3   ? 158.986 113.035 107.836 1.00 64.00  ? 3   VAL B O     1 
ATOM   2250 C  CB    . VAL B 2 3   ? 157.164 111.169 106.220 1.00 56.03  ? 3   VAL B CB    1 
ATOM   2251 C  CG1   . VAL B 2 3   ? 155.989 111.558 107.104 1.00 54.54  ? 3   VAL B CG1   1 
ATOM   2252 C  CG2   . VAL B 2 3   ? 156.694 110.364 105.021 1.00 57.16  ? 3   VAL B CG2   1 
ATOM   2253 N  N     . SER B 2 4   ? 157.597 114.534 106.884 1.00 44.32  ? 4   SER B N     1 
ATOM   2254 C  CA    . SER B 2 4   ? 157.727 115.520 107.950 1.00 45.32  ? 4   SER B CA    1 
ATOM   2255 C  C     . SER B 2 4   ? 156.603 115.438 108.972 1.00 47.50  ? 4   SER B C     1 
ATOM   2256 O  O     . SER B 2 4   ? 156.864 115.492 110.177 1.00 50.54  ? 4   SER B O     1 
ATOM   2257 C  CB    . SER B 2 4   ? 157.777 116.931 107.360 1.00 48.85  ? 4   SER B CB    1 
ATOM   2258 O  OG    . SER B 2 4   ? 156.493 117.348 106.940 1.00 51.54  ? 4   SER B OG    1 
ATOM   2259 N  N     . VAL B 2 5   ? 155.357 115.321 108.520 1.00 50.91  ? 5   VAL B N     1 
ATOM   2260 C  CA    . VAL B 2 5   ? 154.200 115.149 109.392 1.00 46.67  ? 5   VAL B CA    1 
ATOM   2261 C  C     . VAL B 2 5   ? 153.502 113.858 108.991 1.00 42.34  ? 5   VAL B C     1 
ATOM   2262 O  O     . VAL B 2 5   ? 153.202 113.654 107.811 1.00 49.17  ? 5   VAL B O     1 
ATOM   2263 C  CB    . VAL B 2 5   ? 153.223 116.340 109.302 1.00 44.31  ? 5   VAL B CB    1 
ATOM   2264 C  CG1   . VAL B 2 5   ? 152.069 116.160 110.273 1.00 40.49  ? 5   VAL B CG1   1 
ATOM   2265 C  CG2   . VAL B 2 5   ? 153.940 117.654 109.569 1.00 43.28  ? 5   VAL B CG2   1 
ATOM   2266 N  N     . ASN B 2 6   ? 153.250 112.986 109.966 1.00 43.71  ? 6   ASN B N     1 
ATOM   2267 C  CA    . ASN B 2 6   ? 152.553 111.726 109.725 1.00 46.31  ? 6   ASN B CA    1 
ATOM   2268 C  C     . ASN B 2 6   ? 151.362 111.654 110.670 1.00 47.33  ? 6   ASN B C     1 
ATOM   2269 O  O     . ASN B 2 6   ? 151.536 111.517 111.885 1.00 48.39  ? 6   ASN B O     1 
ATOM   2270 C  CB    . ASN B 2 6   ? 153.485 110.528 109.921 1.00 47.33  ? 6   ASN B CB    1 
ATOM   2271 C  CG    . ASN B 2 6   ? 152.999 109.280 109.202 1.00 46.97  ? 6   ASN B CG    1 
ATOM   2272 O  OD1   . ASN B 2 6   ? 151.802 109.082 109.004 1.00 49.83  ? 6   ASN B OD1   1 
ATOM   2273 N  ND2   . ASN B 2 6   ? 153.937 108.430 108.806 1.00 53.41  ? 6   ASN B ND2   1 
ATOM   2274 N  N     . ILE B 2 7   ? 150.160 111.740 110.111 1.00 49.73  ? 7   ILE B N     1 
ATOM   2275 C  CA    . ILE B 2 7   ? 148.915 111.658 110.866 1.00 47.39  ? 7   ILE B CA    1 
ATOM   2276 C  C     . ILE B 2 7   ? 148.307 110.290 110.592 1.00 43.53  ? 7   ILE B C     1 
ATOM   2277 O  O     . ILE B 2 7   ? 148.037 109.946 109.436 1.00 47.71  ? 7   ILE B O     1 
ATOM   2278 C  CB    . ILE B 2 7   ? 147.947 112.786 110.478 1.00 45.63  ? 7   ILE B CB    1 
ATOM   2279 C  CG1   . ILE B 2 7   ? 148.538 114.147 110.848 1.00 48.65  ? 7   ILE B CG1   1 
ATOM   2280 C  CG2   . ILE B 2 7   ? 146.600 112.589 111.136 1.00 44.11  ? 7   ILE B CG2   1 
ATOM   2281 C  CD1   . ILE B 2 7   ? 148.411 115.178 109.753 1.00 46.24  ? 7   ILE B CD1   1 
ATOM   2282 N  N     . LYS B 2 8   ? 148.104 109.505 111.648 1.00 41.52  ? 8   LYS B N     1 
ATOM   2283 C  CA    . LYS B 2 8   ? 147.606 108.137 111.529 1.00 44.92  ? 8   LYS B CA    1 
ATOM   2284 C  C     . LYS B 2 8   ? 146.364 107.979 112.394 1.00 50.75  ? 8   LYS B C     1 
ATOM   2285 O  O     . LYS B 2 8   ? 146.470 107.940 113.625 1.00 55.64  ? 8   LYS B O     1 
ATOM   2286 C  CB    . LYS B 2 8   ? 148.676 107.123 111.935 1.00 46.59  ? 8   LYS B CB    1 
ATOM   2287 C  CG    . LYS B 2 8   ? 149.966 107.211 111.136 1.00 52.39  ? 8   LYS B CG    1 
ATOM   2288 C  CD    . LYS B 2 8   ? 151.188 106.932 111.998 1.00 49.95  ? 8   LYS B CD    1 
ATOM   2289 C  CE    . LYS B 2 8   ? 151.201 107.792 113.253 1.00 52.73  ? 8   LYS B CE    1 
ATOM   2290 N  NZ    . LYS B 2 8   ? 151.985 109.042 113.072 1.00 52.75  ? 8   LYS B NZ    1 
ATOM   2291 N  N     . ASN B 2 9   ? 145.200 107.889 111.735 1.00 45.80  ? 9   ASN B N     1 
ATOM   2292 C  CA    . ASN B 2 9   ? 143.918 107.500 112.341 1.00 40.37  ? 9   ASN B CA    1 
ATOM   2293 C  C     . ASN B 2 9   ? 143.502 108.432 113.477 1.00 40.04  ? 9   ASN B C     1 
ATOM   2294 O  O     . ASN B 2 9   ? 143.004 107.995 114.516 1.00 47.49  ? 9   ASN B O     1 
ATOM   2295 C  CB    . ASN B 2 9   ? 143.960 106.048 112.824 1.00 42.07  ? 9   ASN B CB    1 
ATOM   2296 C  CG    . ASN B 2 9   ? 144.220 105.067 111.701 1.00 45.74  ? 9   ASN B CG    1 
ATOM   2297 O  OD1   . ASN B 2 9   ? 145.210 104.337 111.716 1.00 44.33  ? 9   ASN B OD1   1 
ATOM   2298 N  ND2   . ASN B 2 9   ? 143.326 105.040 110.720 1.00 50.56  ? 9   ASN B ND2   1 
ATOM   2299 N  N     . VAL B 2 10  ? 143.709 109.730 113.281 1.00 35.83  ? 10  VAL B N     1 
ATOM   2300 C  CA    . VAL B 2 10  ? 143.446 110.704 114.333 1.00 37.94  ? 10  VAL B CA    1 
ATOM   2301 C  C     . VAL B 2 10  ? 141.944 110.945 114.431 1.00 40.31  ? 10  VAL B C     1 
ATOM   2302 O  O     . VAL B 2 10  ? 141.272 111.219 113.429 1.00 44.04  ? 10  VAL B O     1 
ATOM   2303 C  CB    . VAL B 2 10  ? 144.232 112.004 114.081 1.00 39.11  ? 10  VAL B CB    1 
ATOM   2304 C  CG1   . VAL B 2 10  ? 143.547 113.219 114.703 1.00 38.74  ? 10  VAL B CG1   1 
ATOM   2305 C  CG2   . VAL B 2 10  ? 145.636 111.863 114.640 1.00 38.85  ? 10  VAL B CG2   1 
ATOM   2306 N  N     . THR B 2 11  ? 141.404 110.802 115.646 1.00 36.91  ? 11  THR B N     1 
ATOM   2307 C  CA    . THR B 2 11  ? 139.980 111.009 115.935 1.00 33.84  ? 11  THR B CA    1 
ATOM   2308 C  C     . THR B 2 11  ? 139.904 111.949 117.098 1.00 32.89  ? 11  THR B C     1 
ATOM   2309 O  O     . THR B 2 11  ? 140.721 111.823 117.961 1.00 48.92  ? 11  THR B O     1 
ATOM   2310 C  CB    . THR B 2 11  ? 139.276 109.680 116.231 1.00 39.15  ? 11  THR B CB    1 
ATOM   2311 O  OG1   . THR B 2 11  ? 138.990 109.030 115.002 1.00 47.60  ? 11  THR B OG1   1 
ATOM   2312 C  CG2   . THR B 2 11  ? 137.955 109.859 116.951 1.00 37.54  ? 11  THR B CG2   1 
ATOM   2313 N  N     . LYS B 2 12  ? 139.045 112.943 117.046 1.00 32.11  ? 12  LYS B N     1 
ATOM   2314 C  CA    . LYS B 2 12  ? 138.800 113.844 118.176 1.00 31.66  ? 12  LYS B CA    1 
ATOM   2315 C  C     . LYS B 2 12  ? 137.318 113.712 118.505 1.00 33.22  ? 12  LYS B C     1 
ATOM   2316 O  O     . LYS B 2 12  ? 136.530 113.991 117.630 1.00 41.82  ? 12  LYS B O     1 
ATOM   2317 C  CB    . LYS B 2 12  ? 139.151 115.306 117.887 1.00 32.80  ? 12  LYS B CB    1 
ATOM   2318 C  CG    . LYS B 2 12  ? 138.970 116.289 119.018 1.00 27.45  ? 12  LYS B CG    1 
ATOM   2319 C  CD    . LYS B 2 12  ? 140.157 116.279 119.964 1.00 28.39  ? 12  LYS B CD    1 
ATOM   2320 C  CE    . LYS B 2 12  ? 139.754 116.506 121.369 1.00 26.97  ? 12  LYS B CE    1 
ATOM   2321 N  NZ    . LYS B 2 12  ? 140.925 116.598 122.229 1.00 30.41  ? 12  LYS B NZ    1 
ATOM   2322 N  N     . GLU B 2 13  ? 136.991 113.417 119.749 1.00 42.31  ? 13  GLU B N     1 
ATOM   2323 C  CA    . GLU B 2 13  ? 135.602 113.211 120.202 1.00 37.29  ? 13  GLU B CA    1 
ATOM   2324 C  C     . GLU B 2 13  ? 135.331 114.199 121.325 1.00 36.93  ? 13  GLU B C     1 
ATOM   2325 O  O     . GLU B 2 13  ? 136.249 114.491 122.051 1.00 37.11  ? 13  GLU B O     1 
ATOM   2326 C  CB    . GLU B 2 13  ? 135.352 111.787 120.678 1.00 35.34  ? 13  GLU B CB    1 
ATOM   2327 C  CG    . GLU B 2 13  ? 135.964 110.730 119.773 1.00 45.35  ? 13  GLU B CG    1 
ATOM   2328 C  CD    . GLU B 2 13  ? 135.631 109.317 120.209 1.00 52.34  ? 13  GLU B CD    1 
ATOM   2329 O  OE1   . GLU B 2 13  ? 134.623 109.161 120.920 1.00 52.19  ? 13  GLU B OE1   1 
ATOM   2330 O  OE2   . GLU B 2 13  ? 136.367 108.377 119.839 1.00 54.41  ? 13  GLU B OE2   1 
ATOM   2331 N  N     . TYR B 2 14  ? 134.141 114.768 121.362 1.00 33.28  ? 14  TYR B N     1 
ATOM   2332 C  CA    . TYR B 2 14  ? 133.747 115.683 122.454 1.00 27.51  ? 14  TYR B CA    1 
ATOM   2333 C  C     . TYR B 2 14  ? 132.462 115.208 123.055 1.00 30.44  ? 14  TYR B C     1 
ATOM   2334 O  O     . TYR B 2 14  ? 131.547 114.876 122.322 1.00 31.94  ? 14  TYR B O     1 
ATOM   2335 C  CB    . TYR B 2 14  ? 133.610 117.111 121.940 1.00 28.95  ? 14  TYR B CB    1 
ATOM   2336 C  CG    . TYR B 2 14  ? 134.882 117.812 121.520 1.00 26.16  ? 14  TYR B CG    1 
ATOM   2337 C  CD1   . TYR B 2 14  ? 135.797 118.243 122.465 1.00 22.72  ? 14  TYR B CD1   1 
ATOM   2338 C  CD2   . TYR B 2 14  ? 135.124 118.092 120.184 1.00 26.53  ? 14  TYR B CD2   1 
ATOM   2339 C  CE1   . TYR B 2 14  ? 136.946 118.906 122.088 1.00 24.35  ? 14  TYR B CE1   1 
ATOM   2340 C  CE2   . TYR B 2 14  ? 136.263 118.763 119.796 1.00 20.77  ? 14  TYR B CE2   1 
ATOM   2341 C  CZ    . TYR B 2 14  ? 137.169 119.173 120.753 1.00 22.72  ? 14  TYR B CZ    1 
ATOM   2342 O  OH    . TYR B 2 14  ? 138.287 119.837 120.379 1.00 32.00  ? 14  TYR B OH    1 
ATOM   2343 N  N     . ARG B 2 15  ? 132.406 115.106 124.372 1.00 48.65  ? 15  ARG B N     1 
ATOM   2344 C  CA    . ARG B 2 15  ? 131.127 114.746 125.054 1.00 42.94  ? 15  ARG B CA    1 
ATOM   2345 C  C     . ARG B 2 15  ? 130.195 115.959 125.038 1.00 37.79  ? 15  ARG B C     1 
ATOM   2346 O  O     . ARG B 2 15  ? 130.648 117.054 125.282 1.00 42.56  ? 15  ARG B O     1 
ATOM   2347 C  CB    . ARG B 2 15  ? 131.352 114.021 126.389 1.00 43.81  ? 15  ARG B CB    1 
ATOM   2348 C  CG    . ARG B 2 15  ? 132.108 112.707 126.302 1.00 47.19  ? 15  ARG B CG    1 
ATOM   2349 C  CD    . ARG B 2 15  ? 131.220 111.543 125.956 1.00 43.34  ? 15  ARG B CD    1 
ATOM   2350 N  NE    . ARG B 2 15  ? 131.177 110.545 127.028 1.00 54.79  ? 15  ARG B NE    1 
ATOM   2351 C  CZ    . ARG B 2 15  ? 130.619 109.353 126.896 1.00 55.91  ? 15  ARG B CZ    1 
ATOM   2352 N  NH1   . ARG B 2 15  ? 130.851 108.638 125.809 1.00 51.56  ? 15  ARG B NH1   1 
ATOM   2353 N  NH2   . ARG B 2 15  ? 129.830 108.880 127.841 1.00 49.38  ? 15  ARG B NH2   1 
ATOM   2354 N  N     . ILE B 2 16  ? 128.932 115.728 124.766 1.00 41.13  ? 16  ILE B N     1 
ATOM   2355 C  CA    . ILE B 2 16  ? 127.963 116.836 124.564 1.00 39.57  ? 16  ILE B CA    1 
ATOM   2356 C  C     . ILE B 2 16  ? 126.905 116.793 125.668 1.00 38.12  ? 16  ILE B C     1 
ATOM   2357 O  O     . ILE B 2 16  ? 126.224 115.769 125.782 1.00 43.13  ? 16  ILE B O     1 
ATOM   2358 C  CB    . ILE B 2 16  ? 127.357 116.760 123.140 1.00 41.17  ? 16  ILE B CB    1 
ATOM   2359 C  CG1   . ILE B 2 16  ? 128.387 117.034 122.045 1.00 38.66  ? 16  ILE B CG1   1 
ATOM   2360 C  CG2   . ILE B 2 16  ? 126.138 117.668 122.992 1.00 38.80  ? 16  ILE B CG2   1 
ATOM   2361 C  CD1   . ILE B 2 16  ? 128.984 118.427 122.069 1.00 38.99  ? 16  ILE B CD1   1 
ATOM   2362 N  N     . TYR B 2 17  ? 126.745 117.874 126.409 1.00 41.46  ? 17  TYR B N     1 
ATOM   2363 C  CA    . TYR B 2 17  ? 125.842 117.967 127.546 1.00 43.98  ? 17  TYR B CA    1 
ATOM   2364 C  C     . TYR B 2 17  ? 124.900 119.147 127.367 1.00 46.14  ? 17  TYR B C     1 
ATOM   2365 O  O     . TYR B 2 17  ? 125.251 120.158 126.755 1.00 50.57  ? 17  TYR B O     1 
ATOM   2366 C  CB    . TYR B 2 17  ? 126.593 118.130 128.877 1.00 41.83  ? 17  TYR B CB    1 
ATOM   2367 C  CG    . TYR B 2 17  ? 127.707 117.140 129.100 1.00 43.34  ? 17  TYR B CG    1 
ATOM   2368 C  CD1   . TYR B 2 17  ? 127.438 115.783 129.228 1.00 44.22  ? 17  TYR B CD1   1 
ATOM   2369 C  CD2   . TYR B 2 17  ? 129.027 117.561 129.193 1.00 39.91  ? 17  TYR B CD2   1 
ATOM   2370 C  CE1   . TYR B 2 17  ? 128.454 114.873 129.434 1.00 40.60  ? 17  TYR B CE1   1 
ATOM   2371 C  CE2   . TYR B 2 17  ? 130.050 116.658 129.399 1.00 36.86  ? 17  TYR B CE2   1 
ATOM   2372 C  CZ    . TYR B 2 17  ? 129.756 115.317 129.521 1.00 40.94  ? 17  TYR B CZ    1 
ATOM   2373 O  OH    . TYR B 2 17  ? 130.771 114.413 129.728 1.00 53.41  ? 17  TYR B OH    1 
ATOM   2374 N  N     . ARG B 2 18  ? 123.695 119.006 127.915 1.00 48.86  ? 18  ARG B N     1 
ATOM   2375 C  CA    . ARG B 2 18  ? 122.733 120.096 127.970 1.00 52.71  ? 18  ARG B CA    1 
ATOM   2376 C  C     . ARG B 2 18  ? 122.549 120.666 129.367 1.00 54.62  ? 18  ARG B C     1 
ATOM   2377 O  O     . ARG B 2 18  ? 122.406 121.882 129.509 1.00 54.01  ? 18  ARG B O     1 
ATOM   2378 C  CB    . ARG B 2 18  ? 121.372 119.635 127.436 1.00 52.80  ? 18  ARG B CB    1 
ATOM   2379 C  CG    . ARG B 2 18  ? 121.443 118.953 126.081 1.00 51.51  ? 18  ARG B CG    1 
ATOM   2380 C  CD    . ARG B 2 18  ? 121.361 119.959 124.945 1.00 49.84  ? 18  ARG B CD    1 
ATOM   2381 N  NE    . ARG B 2 18  ? 119.986 120.208 124.530 1.00 55.09  ? 18  ARG B NE    1 
ATOM   2382 C  CZ    . ARG B 2 18  ? 119.455 119.773 123.396 1.00 54.47  ? 18  ARG B CZ    1 
ATOM   2383 N  NH1   . ARG B 2 18  ? 120.157 119.055 122.535 1.00 50.96  ? 18  ARG B NH1   1 
ATOM   2384 N  NH2   . ARG B 2 18  ? 118.189 120.066 123.118 1.00 51.26  ? 18  ARG B NH2   1 
ATOM   2385 N  N     . THR B 2 19  ? 122.548 119.822 130.396 1.00 57.63  ? 19  THR B N     1 
ATOM   2386 C  CA    . THR B 2 19  ? 122.413 120.259 131.777 1.00 56.09  ? 19  THR B CA    1 
ATOM   2387 C  C     . THR B 2 19  ? 123.676 119.904 132.550 1.00 55.94  ? 19  THR B C     1 
ATOM   2388 O  O     . THR B 2 19  ? 124.541 119.170 132.067 1.00 60.94  ? 19  THR B O     1 
ATOM   2389 C  CB    . THR B 2 19  ? 121.195 119.619 132.470 1.00 59.75  ? 19  THR B CB    1 
ATOM   2390 O  OG1   . THR B 2 19  ? 121.538 118.306 132.925 1.00 60.89  ? 19  THR B OG1   1 
ATOM   2391 C  CG2   . THR B 2 19  ? 120.010 119.524 131.520 1.00 55.65  ? 19  THR B CG2   1 
ATOM   2392 N  N     . ASN B 2 20  ? 123.773 120.444 133.769 1.00 53.36  ? 20  ASN B N     1 
ATOM   2393 C  CA    . ASN B 2 20  ? 124.875 120.081 134.655 1.00 52.83  ? 20  ASN B CA    1 
ATOM   2394 C  C     . ASN B 2 20  ? 124.685 118.688 135.239 1.00 55.94  ? 20  ASN B C     1 
ATOM   2395 O  O     . ASN B 2 20  ? 125.661 118.054 135.661 1.00 58.44  ? 20  ASN B O     1 
ATOM   2396 C  CB    . ASN B 2 20  ? 125.008 121.109 135.778 1.00 54.51  ? 20  ASN B CB    1 
ATOM   2397 C  CG    . ASN B 2 20  ? 126.263 121.947 135.657 1.00 57.16  ? 20  ASN B CG    1 
ATOM   2398 O  OD1   . ASN B 2 20  ? 127.344 121.431 135.379 1.00 57.92  ? 20  ASN B OD1   1 
ATOM   2399 N  ND2   . ASN B 2 20  ? 126.126 123.250 135.868 1.00 56.91  ? 20  ASN B ND2   1 
ATOM   2400 N  N     . LYS B 2 21  ? 123.439 118.207 135.279 1.00 56.44  ? 21  LYS B N     1 
ATOM   2401 C  CA    . LYS B 2 21  ? 123.156 116.870 135.793 1.00 57.13  ? 21  LYS B CA    1 
ATOM   2402 C  C     . LYS B 2 21  ? 123.735 115.792 134.883 1.00 59.25  ? 21  LYS B C     1 
ATOM   2403 O  O     . LYS B 2 21  ? 124.269 114.787 135.366 1.00 59.34  ? 21  LYS B O     1 
ATOM   2404 C  CB    . LYS B 2 21  ? 121.644 116.699 135.961 1.00 60.29  ? 21  LYS B CB    1 
ATOM   2405 C  CG    . LYS B 2 21  ? 121.178 115.297 136.316 1.00 59.92  ? 21  LYS B CG    1 
ATOM   2406 C  CD    . LYS B 2 21  ? 119.728 115.089 135.909 1.00 61.17  ? 21  LYS B CD    1 
ATOM   2407 C  CE    . LYS B 2 21  ? 119.562 113.839 135.062 1.00 65.38  ? 21  LYS B CE    1 
ATOM   2408 N  NZ    . LYS B 2 21  ? 120.068 114.032 133.675 1.00 62.78  ? 21  LYS B NZ    1 
ATOM   2409 N  N     . GLU B 2 22  ? 123.658 115.997 133.563 1.00 58.28  ? 22  GLU B N     1 
ATOM   2410 C  CA    . GLU B 2 22  ? 124.247 115.049 132.619 1.00 54.87  ? 22  GLU B CA    1 
ATOM   2411 C  C     . GLU B 2 22  ? 125.767 115.033 132.720 1.00 54.38  ? 22  GLU B C     1 
ATOM   2412 O  O     . GLU B 2 22  ? 126.390 113.969 132.625 1.00 57.41  ? 22  GLU B O     1 
ATOM   2413 C  CB    . GLU B 2 22  ? 123.816 115.387 131.192 1.00 58.05  ? 22  GLU B CB    1 
ATOM   2414 C  CG    . GLU B 2 22  ? 122.338 115.692 131.035 1.00 58.51  ? 22  GLU B CG    1 
ATOM   2415 C  CD    . GLU B 2 22  ? 122.003 116.247 129.664 1.00 60.91  ? 22  GLU B CD    1 
ATOM   2416 O  OE1   . GLU B 2 22  ? 122.942 116.581 128.913 1.00 59.75  ? 22  GLU B OE1   1 
ATOM   2417 O  OE2   . GLU B 2 22  ? 120.802 116.351 129.339 1.00 60.20  ? 22  GLU B OE2   1 
ATOM   2418 N  N     . ARG B 2 23  ? 126.357 116.227 132.798 1.00 46.05  ? 23  ARG B N     1 
ATOM   2419 C  CA    . ARG B 2 23  ? 127.824 116.359 132.960 1.00 46.22  ? 23  ARG B CA    1 
ATOM   2420 C  C     . ARG B 2 23  ? 128.293 115.615 134.216 1.00 52.93  ? 23  ARG B C     1 
ATOM   2421 O  O     . ARG B 2 23  ? 129.302 114.907 134.103 1.00 58.16  ? 23  ARG B O     1 
ATOM   2422 C  CB    . ARG B 2 23  ? 128.183 117.843 132.938 1.00 48.12  ? 23  ARG B CB    1 
ATOM   2423 C  CG    . ARG B 2 23  ? 129.669 118.130 132.842 1.00 50.21  ? 23  ARG B CG    1 
ATOM   2424 C  CD    . ARG B 2 23  ? 129.870 119.603 132.630 1.00 52.33  ? 23  ARG B CD    1 
ATOM   2425 N  NE    . ARG B 2 23  ? 130.037 120.223 133.946 1.00 54.93  ? 23  ARG B NE    1 
ATOM   2426 C  CZ    . ARG B 2 23  ? 130.978 121.091 134.258 1.00 53.66  ? 23  ARG B CZ    1 
ATOM   2427 N  NH1   . ARG B 2 23  ? 132.248 120.808 134.042 1.00 48.18  ? 23  ARG B NH1   1 
ATOM   2428 N  NH2   . ARG B 2 23  ? 130.630 122.251 134.771 1.00 54.74  ? 23  ARG B NH2   1 
ATOM   2429 N  N     . MET B 2 24  ? 127.635 115.810 135.359 1.00 59.95  ? 24  MET B N     1 
ATOM   2430 C  CA    . MET B 2 24  ? 127.939 115.125 136.645 1.00 59.22  ? 24  MET B CA    1 
ATOM   2431 C  C     . MET B 2 24  ? 127.717 113.607 136.583 1.00 59.39  ? 24  MET B C     1 
ATOM   2432 O  O     . MET B 2 24  ? 128.597 112.889 137.052 1.00 60.14  ? 24  MET B O     1 
ATOM   2433 C  CB    . MET B 2 24  ? 127.077 115.683 137.770 1.00 60.81  ? 24  MET B CB    1 
ATOM   2434 C  CG    . MET B 2 24  ? 127.571 115.304 139.142 1.00 63.90  ? 24  MET B CG    1 
ATOM   2435 S  SD    . MET B 2 24  ? 128.557 116.622 139.873 1.00 74.27  ? 24  MET B SD    1 
ATOM   2436 C  CE    . MET B 2 24  ? 127.230 117.804 140.139 1.00 60.48  ? 24  MET B CE    1 
ATOM   2437 N  N     . LYS B 2 25  ? 126.651 113.134 135.939 1.00 58.16  ? 25  LYS B N     1 
ATOM   2438 C  CA    . LYS B 2 25  ? 126.525 111.662 135.798 1.00 61.22  ? 25  LYS B CA    1 
ATOM   2439 C  C     . LYS B 2 25  ? 127.685 111.075 134.969 1.00 63.12  ? 25  LYS B C     1 
ATOM   2440 O  O     . LYS B 2 25  ? 128.195 110.028 135.349 1.00 63.81  ? 25  LYS B O     1 
ATOM   2441 C  CB    . LYS B 2 25  ? 125.190 111.273 135.162 1.00 60.77  ? 25  LYS B CB    1 
ATOM   2442 C  CG    . LYS B 2 25  ? 124.092 110.979 136.162 1.00 63.09  ? 25  LYS B CG    1 
ATOM   2443 C  CD    . LYS B 2 25  ? 122.881 111.876 135.951 1.00 63.53  ? 25  LYS B CD    1 
ATOM   2444 C  CE    . LYS B 2 25  ? 122.443 111.845 134.530 1.00 66.09  ? 25  LYS B CE    1 
ATOM   2445 N  NZ    . LYS B 2 25  ? 121.252 111.003 134.397 1.00 64.80  ? 25  LYS B NZ    1 
ATOM   2446 N  N     . ASP B 2 26  ? 128.089 111.726 133.888 1.00 59.22  ? 26  ASP B N     1 
ATOM   2447 C  CA    . ASP B 2 26  ? 129.173 111.190 133.035 1.00 61.37  ? 26  ASP B CA    1 
ATOM   2448 C  C     . ASP B 2 26  ? 130.470 111.136 133.831 1.00 60.01  ? 26  ASP B C     1 
ATOM   2449 O  O     . ASP B 2 26  ? 131.203 110.148 133.692 1.00 58.66  ? 26  ASP B O     1 
ATOM   2450 C  CB    . ASP B 2 26  ? 129.277 111.989 131.744 1.00 59.93  ? 26  ASP B CB    1 
ATOM   2451 C  CG    . ASP B 2 26  ? 129.929 111.285 130.570 1.00 60.12  ? 26  ASP B CG    1 
ATOM   2452 O  OD1   . ASP B 2 26  ? 129.202 110.657 129.797 1.00 61.08  ? 26  ASP B OD1   1 
ATOM   2453 O  OD2   . ASP B 2 26  ? 131.156 111.382 130.441 1.00 63.20  ? 26  ASP B OD2   1 
ATOM   2454 N  N     . ALA B 2 27  ? 130.743 112.169 134.619 1.00 65.28  ? 27  ALA B N     1 
ATOM   2455 C  CA    . ALA B 2 27  ? 131.944 112.219 135.482 1.00 65.59  ? 27  ALA B CA    1 
ATOM   2456 C  C     . ALA B 2 27  ? 131.928 111.143 136.560 1.00 67.32  ? 27  ALA B C     1 
ATOM   2457 O  O     . ALA B 2 27  ? 132.978 110.538 136.810 1.00 66.36  ? 27  ALA B O     1 
ATOM   2458 C  CB    . ALA B 2 27  ? 132.016 113.581 136.090 1.00 62.65  ? 27  ALA B CB    1 
ATOM   2459 N  N     . LEU B 2 28  ? 130.772 110.883 137.154 1.00 73.59  ? 28  LEU B N     1 
ATOM   2460 C  CA    . LEU B 2 28  ? 130.723 110.001 138.345 1.00 71.38  ? 28  LEU B CA    1 
ATOM   2461 C  C     . LEU B 2 28  ? 130.377 108.543 138.051 1.00 73.66  ? 28  LEU B C     1 
ATOM   2462 O  O     . LEU B 2 28  ? 130.520 107.738 138.980 1.00 77.16  ? 28  LEU B O     1 
ATOM   2463 C  CB    . LEU B 2 28  ? 129.671 110.659 139.237 1.00 71.84  ? 28  LEU B CB    1 
ATOM   2464 C  CG    . LEU B 2 28  ? 130.105 111.964 139.909 1.00 72.85  ? 28  LEU B CG    1 
ATOM   2465 C  CD1   . LEU B 2 28  ? 129.172 112.356 141.035 1.00 72.28  ? 28  LEU B CD1   1 
ATOM   2466 C  CD2   . LEU B 2 28  ? 131.538 111.887 140.399 1.00 70.04  ? 28  LEU B CD2   1 
ATOM   2467 N  N     . ILE B 2 29  ? 129.942 108.197 136.849 1.00 76.98  ? 29  ILE B N     1 
ATOM   2468 C  CA    . ILE B 2 29  ? 129.474 106.800 136.579 1.00 77.72  ? 29  ILE B CA    1 
ATOM   2469 C  C     . ILE B 2 29  ? 130.422 106.197 135.541 1.00 80.22  ? 29  ILE B C     1 
ATOM   2470 O  O     . ILE B 2 29  ? 130.573 106.802 134.463 1.00 78.55  ? 29  ILE B O     1 
ATOM   2471 C  CB    . ILE B 2 29  ? 127.997 106.765 136.166 1.00 75.30  ? 29  ILE B CB    1 
ATOM   2472 C  CG1   . ILE B 2 29  ? 127.103 107.410 137.217 1.00 74.22  ? 29  ILE B CG1   1 
ATOM   2473 C  CG2   . ILE B 2 29  ? 127.546 105.345 135.828 1.00 76.09  ? 29  ILE B CG2   1 
ATOM   2474 C  CD1   . ILE B 2 29  ? 125.644 107.486 136.812 1.00 77.95  ? 29  ILE B CD1   1 
ATOM   2475 N  N     . PRO B 2 30  ? 131.064 105.045 135.819 1.00 86.60  ? 30  PRO B N     1 
ATOM   2476 C  CA    . PRO B 2 30  ? 132.131 104.497 134.962 1.00 85.76  ? 30  PRO B CA    1 
ATOM   2477 C  C     . PRO B 2 30  ? 131.659 104.025 133.595 1.00 85.48  ? 30  PRO B C     1 
ATOM   2478 O  O     . PRO B 2 30  ? 132.465 103.982 132.658 1.00 85.73  ? 30  PRO B O     1 
ATOM   2479 C  CB    . PRO B 2 30  ? 132.679 103.327 135.796 1.00 84.80  ? 30  PRO B CB    1 
ATOM   2480 C  CG    . PRO B 2 30  ? 132.218 103.593 137.198 1.00 85.44  ? 30  PRO B CG    1 
ATOM   2481 C  CD    . PRO B 2 30  ? 130.891 104.260 137.051 1.00 83.93  ? 30  PRO B CD    1 
ATOM   2482 N  N     . LYS B 2 31  ? 130.386 103.669 133.447 1.00 80.59  ? 31  LYS B N     1 
ATOM   2483 C  CA    . LYS B 2 31  ? 129.856 103.157 132.185 1.00 81.70  ? 31  LYS B CA    1 
ATOM   2484 C  C     . LYS B 2 31  ? 128.628 103.951 131.760 1.00 82.66  ? 31  LYS B C     1 
ATOM   2485 O  O     . LYS B 2 31  ? 127.611 103.399 131.336 1.00 82.34  ? 31  LYS B O     1 
ATOM   2486 C  CB    . LYS B 2 31  ? 129.529 101.670 132.292 1.00 82.86  ? 31  LYS B CB    1 
ATOM   2487 C  CG    . LYS B 2 31  ? 130.750 100.763 132.309 1.00 83.75  ? 31  LYS B CG    1 
ATOM   2488 C  CD    . LYS B 2 31  ? 130.592 99.642  133.324 1.00 81.81  ? 31  LYS B CD    1 
ATOM   2489 C  CE    . LYS B 2 31  ? 131.861 98.811  133.433 1.00 82.72  ? 31  LYS B CE    1 
ATOM   2490 N  NZ    . LYS B 2 31  ? 132.308 98.295  132.109 1.00 81.72  ? 31  LYS B NZ    1 
ATOM   2491 N  N     . HIS B 2 32  ? 128.716 105.273 131.868 1.00 70.77  ? 32  HIS B N     1 
ATOM   2492 C  CA    . HIS B 2 32  ? 127.617 106.141 131.470 1.00 66.44  ? 32  HIS B CA    1 
ATOM   2493 C  C     . HIS B 2 32  ? 127.646 106.366 129.964 1.00 66.79  ? 32  HIS B C     1 
ATOM   2494 O  O     . HIS B 2 32  ? 128.701 106.652 129.390 1.00 67.84  ? 32  HIS B O     1 
ATOM   2495 C  CB    . HIS B 2 32  ? 127.698 107.477 132.209 1.00 66.37  ? 32  HIS B CB    1 
ATOM   2496 C  CG    . HIS B 2 32  ? 126.594 108.427 131.866 1.00 66.25  ? 32  HIS B CG    1 
ATOM   2497 N  ND1   . HIS B 2 32  ? 125.315 108.290 132.359 1.00 70.07  ? 32  HIS B ND1   1 
ATOM   2498 C  CD2   . HIS B 2 32  ? 126.580 109.532 131.084 1.00 63.79  ? 32  HIS B CD2   1 
ATOM   2499 C  CE1   . HIS B 2 32  ? 124.558 109.267 131.892 1.00 67.75  ? 32  HIS B CE1   1 
ATOM   2500 N  NE2   . HIS B 2 32  ? 125.302 110.035 131.117 1.00 64.48  ? 32  HIS B NE2   1 
ATOM   2501 N  N     . LYS B 2 33  ? 126.486 106.232 129.327 1.00 64.30  ? 33  LYS B N     1 
ATOM   2502 C  CA    . LYS B 2 33  ? 126.359 106.447 127.893 1.00 61.47  ? 33  LYS B CA    1 
ATOM   2503 C  C     . LYS B 2 33  ? 125.853 107.861 127.640 1.00 60.31  ? 33  LYS B C     1 
ATOM   2504 O  O     . LYS B 2 33  ? 124.890 108.305 128.273 1.00 61.70  ? 33  LYS B O     1 
ATOM   2505 C  CB    . LYS B 2 33  ? 125.414 105.416 127.275 1.00 60.85  ? 33  LYS B CB    1 
ATOM   2506 C  CG    . LYS B 2 33  ? 126.054 104.055 127.056 1.00 60.81  ? 33  LYS B CG    1 
ATOM   2507 C  CD    . LYS B 2 33  ? 126.175 103.728 125.580 1.00 63.74  ? 33  LYS B CD    1 
ATOM   2508 C  CE    . LYS B 2 33  ? 126.364 102.237 125.359 1.00 65.03  ? 33  LYS B CE    1 
ATOM   2509 N  NZ    . LYS B 2 33  ? 127.219 101.621 126.411 1.00 64.64  ? 33  LYS B NZ    1 
ATOM   2510 N  N     . ASN B 2 34  ? 126.503 108.562 126.715 1.00 58.85  ? 34  ASN B N     1 
ATOM   2511 C  CA    . ASN B 2 34  ? 126.242 109.976 126.494 1.00 54.29  ? 34  ASN B CA    1 
ATOM   2512 C  C     . ASN B 2 34  ? 126.423 110.300 125.019 1.00 53.06  ? 34  ASN B C     1 
ATOM   2513 O  O     . ASN B 2 34  ? 127.031 109.537 124.263 1.00 51.63  ? 34  ASN B O     1 
ATOM   2514 C  CB    . ASN B 2 34  ? 127.170 110.845 127.354 1.00 51.41  ? 34  ASN B CB    1 
ATOM   2515 C  CG    . ASN B 2 34  ? 126.603 112.220 127.626 1.00 51.64  ? 34  ASN B CG    1 
ATOM   2516 O  OD1   . ASN B 2 34  ? 126.864 113.168 126.889 1.00 51.46  ? 34  ASN B OD1   1 
ATOM   2517 N  ND2   . ASN B 2 34  ? 125.815 112.336 128.687 1.00 56.51  ? 34  ASN B ND2   1 
ATOM   2518 N  N     . LYS B 2 35  ? 125.876 111.445 124.617 1.00 49.41  ? 35  LYS B N     1 
ATOM   2519 C  CA    . LYS B 2 35  ? 126.038 111.918 123.250 1.00 47.00  ? 35  LYS B CA    1 
ATOM   2520 C  C     . LYS B 2 35  ? 127.473 112.368 123.011 1.00 47.83  ? 35  LYS B C     1 
ATOM   2521 O  O     . LYS B 2 35  ? 128.038 113.132 123.797 1.00 48.13  ? 35  LYS B O     1 
ATOM   2522 C  CB    . LYS B 2 35  ? 125.071 113.067 122.974 1.00 42.41  ? 35  LYS B CB    1 
ATOM   2523 C  CG    . LYS B 2 35  ? 125.082 113.550 121.539 1.00 45.60  ? 35  LYS B CG    1 
ATOM   2524 C  CD    . LYS B 2 35  ? 123.741 113.318 120.877 1.00 48.17  ? 35  LYS B CD    1 
ATOM   2525 C  CE    . LYS B 2 35  ? 122.815 114.491 121.117 1.00 49.92  ? 35  LYS B CE    1 
ATOM   2526 N  NZ    . LYS B 2 35  ? 121.410 114.185 120.736 1.00 49.99  ? 35  LYS B NZ    1 
ATOM   2527 N  N     . THR B 2 36  ? 128.059 111.891 121.918 1.00 43.13  ? 36  THR B N     1 
ATOM   2528 C  CA    . THR B 2 36  ? 129.438 112.196 121.572 1.00 37.81  ? 36  THR B CA    1 
ATOM   2529 C  C     . THR B 2 36  ? 129.491 112.783 120.170 1.00 40.52  ? 36  THR B C     1 
ATOM   2530 O  O     . THR B 2 36  ? 128.838 112.280 119.252 1.00 42.11  ? 36  THR B O     1 
ATOM   2531 C  CB    . THR B 2 36  ? 130.321 110.943 121.664 1.00 44.09  ? 36  THR B CB    1 
ATOM   2532 O  OG1   . THR B 2 36  ? 130.013 110.233 122.869 1.00 49.27  ? 36  THR B OG1   1 
ATOM   2533 C  CG2   . THR B 2 36  ? 131.792 111.317 121.677 1.00 37.10  ? 36  THR B CG2   1 
ATOM   2534 N  N     . PHE B 2 37  ? 130.269 113.850 120.014 1.00 37.07  ? 37  PHE B N     1 
ATOM   2535 C  CA    . PHE B 2 37  ? 130.417 114.551 118.747 1.00 27.63  ? 37  PHE B CA    1 
ATOM   2536 C  C     . PHE B 2 37  ? 131.808 114.289 118.191 1.00 28.52  ? 37  PHE B C     1 
ATOM   2537 O  O     . PHE B 2 37  ? 132.804 114.454 118.901 1.00 27.54  ? 37  PHE B O     1 
ATOM   2538 C  CB    . PHE B 2 37  ? 130.186 116.053 118.927 1.00 28.94  ? 37  PHE B CB    1 
ATOM   2539 C  CG    . PHE B 2 37  ? 130.445 116.860 117.692 1.00 31.98  ? 37  PHE B CG    1 
ATOM   2540 C  CD1   . PHE B 2 37  ? 129.591 116.777 116.604 1.00 27.81  ? 37  PHE B CD1   1 
ATOM   2541 C  CD2   . PHE B 2 37  ? 131.536 117.713 117.622 1.00 30.43  ? 37  PHE B CD2   1 
ATOM   2542 C  CE1   . PHE B 2 37  ? 129.823 117.524 115.467 1.00 25.12  ? 37  PHE B CE1   1 
ATOM   2543 C  CE2   . PHE B 2 37  ? 131.773 118.461 116.487 1.00 32.19  ? 37  PHE B CE2   1 
ATOM   2544 C  CZ    . PHE B 2 37  ? 130.916 118.367 115.410 1.00 28.57  ? 37  PHE B CZ    1 
ATOM   2545 N  N     . PHE B 2 38  ? 131.874 113.881 116.926 1.00 36.10  ? 38  PHE B N     1 
ATOM   2546 C  CA    . PHE B 2 38  ? 133.144 113.629 116.247 1.00 31.37  ? 38  PHE B CA    1 
ATOM   2547 C  C     . PHE B 2 38  ? 133.563 114.911 115.536 1.00 31.05  ? 38  PHE B C     1 
ATOM   2548 O  O     . PHE B 2 38  ? 133.062 115.238 114.461 1.00 35.79  ? 38  PHE B O     1 
ATOM   2549 C  CB    . PHE B 2 38  ? 133.024 112.472 115.263 1.00 32.63  ? 38  PHE B CB    1 
ATOM   2550 C  CG    . PHE B 2 38  ? 133.103 111.119 115.901 1.00 32.27  ? 38  PHE B CG    1 
ATOM   2551 C  CD1   . PHE B 2 38  ? 134.299 110.649 116.417 1.00 39.22  ? 38  PHE B CD1   1 
ATOM   2552 C  CD2   . PHE B 2 38  ? 131.986 110.305 115.964 1.00 39.52  ? 38  PHE B CD2   1 
ATOM   2553 C  CE1   . PHE B 2 38  ? 134.372 109.397 117.001 1.00 42.74  ? 38  PHE B CE1   1 
ATOM   2554 C  CE2   . PHE B 2 38  ? 132.059 109.052 116.543 1.00 43.17  ? 38  PHE B CE2   1 
ATOM   2555 C  CZ    . PHE B 2 38  ? 133.251 108.600 117.063 1.00 40.97  ? 38  PHE B CZ    1 
ATOM   2556 N  N     . ALA B 2 39  ? 134.484 115.651 116.156 1.00 32.87  ? 39  ALA B N     1 
ATOM   2557 C  CA    . ALA B 2 39  ? 135.102 116.776 115.465 1.00 29.82  ? 39  ALA B CA    1 
ATOM   2558 C  C     . ALA B 2 39  ? 135.995 116.289 114.333 1.00 32.49  ? 39  ALA B C     1 
ATOM   2559 O  O     . ALA B 2 39  ? 136.024 116.888 113.252 1.00 36.58  ? 39  ALA B O     1 
ATOM   2560 C  CB    . ALA B 2 39  ? 135.892 117.634 116.451 1.00 24.38  ? 39  ALA B CB    1 
ATOM   2561 N  N     . LEU B 2 40  ? 136.726 115.201 114.564 1.00 32.70  ? 40  LEU B N     1 
ATOM   2562 C  CA    . LEU B 2 40  ? 137.503 114.513 113.546 1.00 26.80  ? 40  LEU B CA    1 
ATOM   2563 C  C     . LEU B 2 40  ? 137.221 113.023 113.661 1.00 26.54  ? 40  LEU B C     1 
ATOM   2564 O  O     . LEU B 2 40  ? 136.944 112.523 114.754 1.00 39.25  ? 40  LEU B O     1 
ATOM   2565 C  CB    . LEU B 2 40  ? 139.002 114.786 113.704 1.00 32.13  ? 40  LEU B CB    1 
ATOM   2566 C  CG    . LEU B 2 40  ? 139.489 116.191 113.344 1.00 30.13  ? 40  LEU B CG    1 
ATOM   2567 C  CD1   . LEU B 2 40  ? 140.985 116.292 113.549 1.00 30.67  ? 40  LEU B CD1   1 
ATOM   2568 C  CD2   . LEU B 2 40  ? 139.118 116.550 111.915 1.00 24.53  ? 40  LEU B CD2   1 
ATOM   2569 N  N     . ASP B 2 41  ? 137.283 112.315 112.536 1.00 31.32  ? 41  ASP B N     1 
ATOM   2570 C  CA    . ASP B 2 41  ? 136.939 110.894 112.490 1.00 37.79  ? 41  ASP B CA    1 
ATOM   2571 C  C     . ASP B 2 41  ? 137.900 110.167 111.554 1.00 44.30  ? 41  ASP B C     1 
ATOM   2572 O  O     . ASP B 2 41  ? 137.681 110.148 110.339 1.00 45.32  ? 41  ASP B O     1 
ATOM   2573 C  CB    . ASP B 2 41  ? 135.491 110.702 112.051 1.00 41.49  ? 41  ASP B CB    1 
ATOM   2574 C  CG    . ASP B 2 41  ? 134.989 109.293 112.294 1.00 50.31  ? 41  ASP B CG    1 
ATOM   2575 O  OD1   . ASP B 2 41  ? 134.850 108.531 111.315 1.00 52.05  ? 41  ASP B OD1   1 
ATOM   2576 O  OD2   . ASP B 2 41  ? 134.733 108.945 113.465 1.00 47.70  ? 41  ASP B OD2   1 
ATOM   2577 N  N     . ASP B 2 42  ? 138.952 109.580 112.141 1.00 43.69  ? 42  ASP B N     1 
ATOM   2578 C  CA    . ASP B 2 42  ? 139.910 108.690 111.472 1.00 41.38  ? 42  ASP B CA    1 
ATOM   2579 C  C     . ASP B 2 42  ? 140.618 109.382 110.302 1.00 45.30  ? 42  ASP B C     1 
ATOM   2580 O  O     . ASP B 2 42  ? 140.493 108.990 109.140 1.00 53.31  ? 42  ASP B O     1 
ATOM   2581 C  CB    . ASP B 2 42  ? 139.229 107.392 111.022 1.00 41.16  ? 42  ASP B CB    1 
ATOM   2582 C  CG    . ASP B 2 42  ? 140.191 106.225 110.943 1.00 51.69  ? 42  ASP B CG    1 
ATOM   2583 O  OD1   . ASP B 2 42  ? 141.045 106.215 110.032 1.00 53.68  ? 42  ASP B OD1   1 
ATOM   2584 O  OD2   . ASP B 2 42  ? 140.091 105.314 111.790 1.00 54.32  ? 42  ASP B OD2   1 
ATOM   2585 N  N     . ILE B 2 43  ? 141.370 110.424 110.633 1.00 41.15  ? 43  ILE B N     1 
ATOM   2586 C  CA    . ILE B 2 43  ? 142.124 111.188 109.646 1.00 41.13  ? 43  ILE B CA    1 
ATOM   2587 C  C     . ILE B 2 43  ? 143.485 110.534 109.450 1.00 41.77  ? 43  ILE B C     1 
ATOM   2588 O  O     . ILE B 2 43  ? 144.212 110.288 110.418 1.00 42.94  ? 43  ILE B O     1 
ATOM   2589 C  CB    . ILE B 2 43  ? 142.274 112.654 110.084 1.00 44.34  ? 43  ILE B CB    1 
ATOM   2590 C  CG1   . ILE B 2 43  ? 140.905 113.257 110.418 1.00 37.12  ? 43  ILE B CG1   1 
ATOM   2591 C  CG2   . ILE B 2 43  ? 143.010 113.464 109.018 1.00 42.84  ? 43  ILE B CG2   1 
ATOM   2592 C  CD1   . ILE B 2 43  ? 140.078 113.640 109.210 1.00 44.38  ? 43  ILE B CD1   1 
ATOM   2593 N  N     . SER B 2 44  ? 143.832 110.251 108.196 1.00 43.51  ? 44  SER B N     1 
ATOM   2594 C  CA    . SER B 2 44  ? 145.120 109.650 107.863 1.00 41.70  ? 44  SER B CA    1 
ATOM   2595 C  C     . SER B 2 44  ? 145.686 110.353 106.637 1.00 42.62  ? 44  SER B C     1 
ATOM   2596 O  O     . SER B 2 44  ? 145.213 110.131 105.519 1.00 51.53  ? 44  SER B O     1 
ATOM   2597 C  CB    . SER B 2 44  ? 144.984 108.148 107.613 1.00 44.12  ? 44  SER B CB    1 
ATOM   2598 O  OG    . SER B 2 44  ? 144.876 107.437 108.832 1.00 44.75  ? 44  SER B OG    1 
ATOM   2599 N  N     . LEU B 2 45  ? 146.689 111.203 106.848 1.00 41.24  ? 45  LEU B N     1 
ATOM   2600 C  CA    . LEU B 2 45  ? 147.434 111.808 105.755 1.00 47.37  ? 45  LEU B CA    1 
ATOM   2601 C  C     . LEU B 2 45  ? 148.863 112.044 106.219 1.00 44.60  ? 45  LEU B C     1 
ATOM   2602 O  O     . LEU B 2 45  ? 149.112 112.288 107.401 1.00 46.64  ? 45  LEU B O     1 
ATOM   2603 C  CB    . LEU B 2 45  ? 146.790 113.119 105.273 1.00 48.43  ? 45  LEU B CB    1 
ATOM   2604 C  CG    . LEU B 2 45  ? 146.793 114.358 106.174 1.00 45.57  ? 45  LEU B CG    1 
ATOM   2605 C  CD1   . LEU B 2 45  ? 147.810 115.386 105.696 1.00 45.80  ? 45  LEU B CD1   1 
ATOM   2606 C  CD2   . LEU B 2 45  ? 145.407 114.973 106.235 1.00 48.12  ? 45  LEU B CD2   1 
ATOM   2607 N  N     . LYS B 2 46  ? 149.802 111.956 105.283 1.00 49.45  ? 46  LYS B N     1 
ATOM   2608 C  CA    . LYS B 2 46  ? 151.206 112.170 105.595 1.00 50.02  ? 46  LYS B CA    1 
ATOM   2609 C  C     . LYS B 2 46  ? 151.762 113.291 104.731 1.00 45.61  ? 46  LYS B C     1 
ATOM   2610 O  O     . LYS B 2 46  ? 151.468 113.377 103.536 1.00 42.57  ? 46  LYS B O     1 
ATOM   2611 C  CB    . LYS B 2 46  ? 152.033 110.884 105.416 1.00 45.79  ? 46  LYS B CB    1 
ATOM   2612 C  CG    . LYS B 2 46  ? 151.844 110.162 104.098 1.00 51.26  ? 46  LYS B CG    1 
ATOM   2613 C  CD    . LYS B 2 46  ? 152.812 108.995 103.975 1.00 53.85  ? 46  LYS B CD    1 
ATOM   2614 C  CE    . LYS B 2 46  ? 152.639 108.009 105.119 1.00 52.02  ? 46  LYS B CE    1 
ATOM   2615 N  NZ    . LYS B 2 46  ? 153.859 107.189 105.339 1.00 52.89  ? 46  LYS B NZ    1 
ATOM   2616 N  N     . ALA B 2 47  ? 152.556 114.155 105.353 1.00 50.60  ? 47  ALA B N     1 
ATOM   2617 C  CA    . ALA B 2 47  ? 153.141 115.314 104.699 1.00 45.88  ? 47  ALA B CA    1 
ATOM   2618 C  C     . ALA B 2 47  ? 154.636 115.106 104.517 1.00 46.45  ? 47  ALA B C     1 
ATOM   2619 O  O     . ALA B 2 47  ? 155.313 114.582 105.406 1.00 52.28  ? 47  ALA B O     1 
ATOM   2620 C  CB    . ALA B 2 47  ? 152.889 116.586 105.510 1.00 42.37  ? 47  ALA B CB    1 
ATOM   2621 N  N     . TYR B 2 48  ? 155.142 115.509 103.359 1.00 49.80  ? 48  TYR B N     1 
ATOM   2622 C  CA    . TYR B 2 48  ? 156.563 115.462 103.059 1.00 52.38  ? 48  TYR B CA    1 
ATOM   2623 C  C     . TYR B 2 48  ? 157.170 116.852 103.207 1.00 52.51  ? 48  TYR B C     1 
ATOM   2624 O  O     . TYR B 2 48  ? 156.462 117.844 103.395 1.00 56.85  ? 48  TYR B O     1 
ATOM   2625 C  CB    . TYR B 2 48  ? 156.808 114.917 101.648 1.00 52.91  ? 48  TYR B CB    1 
ATOM   2626 C  CG    . TYR B 2 48  ? 156.334 113.491 101.441 1.00 54.11  ? 48  TYR B CG    1 
ATOM   2627 C  CD1   . TYR B 2 48  ? 155.016 113.214 101.091 1.00 55.55  ? 48  TYR B CD1   1 
ATOM   2628 C  CD2   . TYR B 2 48  ? 157.206 112.422 101.603 1.00 55.76  ? 48  TYR B CD2   1 
ATOM   2629 C  CE1   . TYR B 2 48  ? 154.583 111.914 100.905 1.00 55.48  ? 48  TYR B CE1   1 
ATOM   2630 C  CE2   . TYR B 2 48  ? 156.783 111.118 101.419 1.00 56.09  ? 48  TYR B CE2   1 
ATOM   2631 C  CZ    . TYR B 2 48  ? 155.471 110.871 101.071 1.00 57.34  ? 48  TYR B CZ    1 
ATOM   2632 O  OH    . TYR B 2 48  ? 155.047 109.575 100.887 1.00 59.82  ? 48  TYR B OH    1 
ATOM   2633 N  N     . GLU B 2 49  ? 158.498 116.913 103.137 1.00 59.55  ? 49  GLU B N     1 
ATOM   2634 C  CA    . GLU B 2 49  ? 159.181 118.194 103.251 1.00 60.45  ? 49  GLU B CA    1 
ATOM   2635 C  C     . GLU B 2 49  ? 158.987 119.021 101.987 1.00 63.02  ? 49  GLU B C     1 
ATOM   2636 O  O     . GLU B 2 49  ? 159.116 118.519 100.867 1.00 62.51  ? 49  GLU B O     1 
ATOM   2637 C  CB    . GLU B 2 49  ? 160.672 117.993 103.524 1.00 58.01  ? 49  GLU B CB    1 
ATOM   2638 C  CG    . GLU B 2 49  ? 161.013 117.897 104.999 1.00 62.61  ? 49  GLU B CG    1 
ATOM   2639 C  CD    . GLU B 2 49  ? 161.767 116.633 105.340 1.00 67.36  ? 49  GLU B CD    1 
ATOM   2640 O  OE1   . GLU B 2 49  ? 161.598 116.122 106.467 1.00 68.69  ? 49  GLU B OE1   1 
ATOM   2641 O  OE2   . GLU B 2 49  ? 162.545 116.163 104.485 1.00 67.74  ? 49  GLU B OE2   1 
ATOM   2642 N  N     . GLY B 2 50  ? 158.678 120.303 102.175 1.00 51.86  ? 50  GLY B N     1 
ATOM   2643 C  CA    . GLY B 2 50  ? 158.379 121.192 101.078 1.00 49.44  ? 50  GLY B CA    1 
ATOM   2644 C  C     . GLY B 2 50  ? 156.934 121.192 100.632 1.00 53.59  ? 50  GLY B C     1 
ATOM   2645 O  O     . GLY B 2 50  ? 156.596 121.912 99.685  1.00 57.52  ? 50  GLY B O     1 
ATOM   2646 N  N     . ASP B 2 51  ? 156.074 120.410 101.278 1.00 47.58  ? 51  ASP B N     1 
ATOM   2647 C  CA    . ASP B 2 51  ? 154.664 120.384 100.917 1.00 42.70  ? 51  ASP B CA    1 
ATOM   2648 C  C     . ASP B 2 51  ? 153.949 121.595 101.498 1.00 38.67  ? 51  ASP B C     1 
ATOM   2649 O  O     . ASP B 2 51  ? 154.075 121.892 102.689 1.00 39.41  ? 51  ASP B O     1 
ATOM   2650 C  CB    . ASP B 2 51  ? 154.010 119.098 101.423 1.00 43.76  ? 51  ASP B CB    1 
ATOM   2651 C  CG    . ASP B 2 51  ? 154.046 117.981 100.402 1.00 48.87  ? 51  ASP B CG    1 
ATOM   2652 O  OD1   . ASP B 2 51  ? 154.483 118.228 99.259  1.00 51.96  ? 51  ASP B OD1   1 
ATOM   2653 O  OD2   . ASP B 2 51  ? 153.631 116.855 100.740 1.00 50.69  ? 51  ASP B OD2   1 
ATOM   2654 N  N     . VAL B 2 52  ? 153.196 122.295 100.660 1.00 39.62  ? 52  VAL B N     1 
ATOM   2655 C  CA    . VAL B 2 52  ? 152.336 123.385 101.099 1.00 39.02  ? 52  VAL B CA    1 
ATOM   2656 C  C     . VAL B 2 52  ? 150.906 122.890 100.932 1.00 34.49  ? 52  VAL B C     1 
ATOM   2657 O  O     . VAL B 2 52  ? 150.409 122.758 99.809  1.00 37.60  ? 52  VAL B O     1 
ATOM   2658 C  CB    . VAL B 2 52  ? 152.591 124.677 100.315 1.00 38.42  ? 52  VAL B CB    1 
ATOM   2659 C  CG1   . VAL B 2 52  ? 151.847 125.832 100.953 1.00 35.77  ? 52  VAL B CG1   1 
ATOM   2660 C  CG2   . VAL B 2 52  ? 154.078 124.971 100.252 1.00 30.29  ? 52  VAL B CG2   1 
ATOM   2661 N  N     . ILE B 2 53  ? 150.241 122.611 102.048 1.00 30.72  ? 53  ILE B N     1 
ATOM   2662 C  CA    . ILE B 2 53  ? 148.963 121.909 102.056 1.00 29.65  ? 53  ILE B CA    1 
ATOM   2663 C  C     . ILE B 2 53  ? 147.869 122.871 102.493 1.00 32.42  ? 53  ILE B C     1 
ATOM   2664 O  O     . ILE B 2 53  ? 147.960 123.483 103.564 1.00 32.94  ? 53  ILE B O     1 
ATOM   2665 C  CB    . ILE B 2 53  ? 149.010 120.671 102.968 1.00 35.70  ? 53  ILE B CB    1 
ATOM   2666 C  CG1   . ILE B 2 53  ? 150.145 119.745 102.531 1.00 35.80  ? 53  ILE B CG1   1 
ATOM   2667 C  CG2   . ILE B 2 53  ? 147.684 119.931 102.940 1.00 33.49  ? 53  ILE B CG2   1 
ATOM   2668 C  CD1   . ILE B 2 53  ? 150.521 118.719 103.555 1.00 34.37  ? 53  ILE B CD1   1 
ATOM   2669 N  N     . GLY B 2 54  ? 146.836 122.998 101.664 1.00 38.07  ? 54  GLY B N     1 
ATOM   2670 C  CA    . GLY B 2 54  ? 145.692 123.834 101.975 1.00 27.26  ? 54  GLY B CA    1 
ATOM   2671 C  C     . GLY B 2 54  ? 144.556 123.004 102.543 1.00 28.17  ? 54  GLY B C     1 
ATOM   2672 O  O     . GLY B 2 54  ? 144.157 121.994 101.961 1.00 35.30  ? 54  GLY B O     1 
ATOM   2673 N  N     . LEU B 2 55  ? 144.045 123.444 103.688 1.00 33.69  ? 55  LEU B N     1 
ATOM   2674 C  CA    . LEU B 2 55  ? 142.924 122.794 104.354 1.00 31.42  ? 55  LEU B CA    1 
ATOM   2675 C  C     . LEU B 2 55  ? 141.650 123.559 104.024 1.00 30.20  ? 55  LEU B C     1 
ATOM   2676 O  O     . LEU B 2 55  ? 141.451 124.678 104.510 1.00 31.37  ? 55  LEU B O     1 
ATOM   2677 C  CB    . LEU B 2 55  ? 143.142 122.735 105.867 1.00 28.61  ? 55  LEU B CB    1 
ATOM   2678 C  CG    . LEU B 2 55  ? 143.674 121.433 106.475 1.00 35.58  ? 55  LEU B CG    1 
ATOM   2679 C  CD1   . LEU B 2 55  ? 144.998 121.013 105.854 1.00 34.84  ? 55  LEU B CD1   1 
ATOM   2680 C  CD2   . LEU B 2 55  ? 143.808 121.556 107.983 1.00 33.43  ? 55  LEU B CD2   1 
ATOM   2681 N  N     . VAL B 2 56  ? 140.790 122.957 103.203 1.00 27.94  ? 56  VAL B N     1 
ATOM   2682 C  CA    . VAL B 2 56  ? 139.570 123.601 102.740 1.00 28.09  ? 56  VAL B CA    1 
ATOM   2683 C  C     . VAL B 2 56  ? 138.366 122.852 103.295 1.00 28.70  ? 56  VAL B C     1 
ATOM   2684 O  O     . VAL B 2 56  ? 138.461 121.703 103.732 1.00 36.19  ? 56  VAL B O     1 
ATOM   2685 C  CB    . VAL B 2 56  ? 139.493 123.678 101.199 1.00 29.05  ? 56  VAL B CB    1 
ATOM   2686 C  CG1   . VAL B 2 56  ? 140.673 124.458 100.645 1.00 26.32  ? 56  VAL B CG1   1 
ATOM   2687 C  CG2   . VAL B 2 56  ? 139.429 122.286 100.591 1.00 28.04  ? 56  VAL B CG2   1 
ATOM   2688 N  N     . GLY B 2 57  ? 137.228 123.528 103.283 1.00 29.14  ? 57  GLY B N     1 
ATOM   2689 C  CA    . GLY B 2 57  ? 135.992 122.943 103.759 1.00 19.28  ? 57  GLY B CA    1 
ATOM   2690 C  C     . GLY B 2 57  ? 135.071 124.004 104.310 1.00 22.61  ? 57  GLY B C     1 
ATOM   2691 O  O     . GLY B 2 57  ? 135.456 125.151 104.524 1.00 40.40  ? 57  GLY B O     1 
ATOM   2692 N  N     . ILE B 2 58  ? 133.830 123.589 104.550 1.00 30.28  ? 58  ILE B N     1 
ATOM   2693 C  CA    . ILE B 2 58  ? 132.785 124.475 105.053 1.00 28.18  ? 58  ILE B CA    1 
ATOM   2694 C  C     . ILE B 2 58  ? 132.985 124.712 106.544 1.00 27.19  ? 58  ILE B C     1 
ATOM   2695 O  O     . ILE B 2 58  ? 133.863 124.103 107.165 1.00 38.04  ? 58  ILE B O     1 
ATOM   2696 C  CB    . ILE B 2 58  ? 131.384 123.909 104.757 1.00 31.16  ? 58  ILE B CB    1 
ATOM   2697 C  CG1   . ILE B 2 58  ? 131.169 122.583 105.488 1.00 32.89  ? 58  ILE B CG1   1 
ATOM   2698 C  CG2   . ILE B 2 58  ? 131.191 123.735 103.261 1.00 23.49  ? 58  ILE B CG2   1 
ATOM   2699 C  CD1   . ILE B 2 58  ? 129.716 122.200 105.647 1.00 27.56  ? 58  ILE B CD1   1 
ATOM   2700 N  N     . ASN B 2 59  ? 132.208 125.638 107.108 1.00 24.13  ? 59  ASN B N     1 
ATOM   2701 C  CA    . ASN B 2 59  ? 132.311 125.980 108.523 1.00 28.47  ? 59  ASN B CA    1 
ATOM   2702 C  C     . ASN B 2 59  ? 131.968 124.787 109.409 1.00 33.36  ? 59  ASN B C     1 
ATOM   2703 O  O     . ASN B 2 59  ? 130.995 124.070 109.161 1.00 41.66  ? 59  ASN B O     1 
ATOM   2704 C  CB    . ASN B 2 59  ? 131.379 127.149 108.845 1.00 26.96  ? 59  ASN B CB    1 
ATOM   2705 C  CG    . ASN B 2 59  ? 131.863 128.459 108.264 1.00 27.03  ? 59  ASN B CG    1 
ATOM   2706 O  OD1   . ASN B 2 59  ? 131.077 129.364 107.998 1.00 34.74  ? 59  ASN B OD1   1 
ATOM   2707 N  ND2   . ASN B 2 59  ? 133.169 128.568 108.069 1.00 33.95  ? 59  ASN B ND2   1 
ATOM   2708 N  N     . GLY B 2 60  ? 132.782 124.575 110.440 1.00 25.60  ? 60  GLY B N     1 
ATOM   2709 C  CA    . GLY B 2 60  ? 132.606 123.457 111.340 1.00 18.00  ? 60  GLY B CA    1 
ATOM   2710 C  C     . GLY B 2 60  ? 133.054 122.116 110.806 1.00 31.15  ? 60  GLY B C     1 
ATOM   2711 O  O     . GLY B 2 60  ? 132.611 121.087 111.325 1.00 40.87  ? 60  GLY B O     1 
ATOM   2712 N  N     . SER B 2 61  ? 133.910 122.092 109.782 1.00 25.81  ? 61  SER B N     1 
ATOM   2713 C  CA    . SER B 2 61  ? 134.342 120.821 109.207 1.00 21.48  ? 61  SER B CA    1 
ATOM   2714 C  C     . SER B 2 61  ? 135.349 120.112 110.101 1.00 30.50  ? 61  SER B C     1 
ATOM   2715 O  O     . SER B 2 61  ? 135.345 118.880 110.189 1.00 40.51  ? 61  SER B O     1 
ATOM   2716 C  CB    . SER B 2 61  ? 134.938 121.044 107.819 1.00 27.05  ? 61  SER B CB    1 
ATOM   2717 O  OG    . SER B 2 61  ? 133.944 121.445 106.899 1.00 34.42  ? 61  SER B OG    1 
ATOM   2718 N  N     . GLY B 2 62  ? 136.226 120.862 110.758 1.00 19.60  ? 62  GLY B N     1 
ATOM   2719 C  CA    . GLY B 2 62  ? 137.221 120.260 111.621 1.00 17.84  ? 62  GLY B CA    1 
ATOM   2720 C  C     . GLY B 2 62  ? 138.644 120.574 111.217 1.00 20.36  ? 62  GLY B C     1 
ATOM   2721 O  O     . GLY B 2 62  ? 139.577 119.889 111.642 1.00 39.27  ? 62  GLY B O     1 
ATOM   2722 N  N     . LYS B 2 63  ? 138.827 121.603 110.389 1.00 24.80  ? 63  LYS B N     1 
ATOM   2723 C  CA    . LYS B 2 63  ? 140.165 121.940 109.919 1.00 30.13  ? 63  LYS B CA    1 
ATOM   2724 C  C     . LYS B 2 63  ? 140.984 122.679 110.974 1.00 22.53  ? 63  LYS B C     1 
ATOM   2725 O  O     . LYS B 2 63  ? 142.209 122.524 111.012 1.00 31.19  ? 63  LYS B O     1 
ATOM   2726 C  CB    . LYS B 2 63  ? 140.076 122.744 108.619 1.00 29.17  ? 63  LYS B CB    1 
ATOM   2727 C  CG    . LYS B 2 63  ? 139.353 124.065 108.724 1.00 37.81  ? 63  LYS B CG    1 
ATOM   2728 C  CD    . LYS B 2 63  ? 139.041 124.631 107.353 1.00 30.69  ? 63  LYS B CD    1 
ATOM   2729 C  CE    . LYS B 2 63  ? 137.709 124.132 106.856 1.00 31.44  ? 63  LYS B CE    1 
ATOM   2730 N  NZ    . LYS B 2 63  ? 136.640 125.125 107.121 1.00 28.85  ? 63  LYS B NZ    1 
ATOM   2731 N  N     . SER B 2 64  ? 140.341 123.461 111.846 1.00 18.65  ? 64  SER B N     1 
ATOM   2732 C  CA    . SER B 2 64  ? 141.073 124.070 112.952 1.00 18.25  ? 64  SER B CA    1 
ATOM   2733 C  C     . SER B 2 64  ? 141.430 123.033 114.007 1.00 28.20  ? 64  SER B C     1 
ATOM   2734 O  O     . SER B 2 64  ? 142.478 123.137 114.649 1.00 38.31  ? 64  SER B O     1 
ATOM   2735 C  CB    . SER B 2 64  ? 140.263 125.206 113.572 1.00 23.08  ? 64  SER B CB    1 
ATOM   2736 O  OG    . SER B 2 64  ? 140.093 126.268 112.652 1.00 38.54  ? 64  SER B OG    1 
ATOM   2737 N  N     . THR B 2 65  ? 140.573 122.023 114.188 1.00 23.81  ? 65  THR B N     1 
ATOM   2738 C  CA    . THR B 2 65  ? 140.892 120.912 115.082 1.00 28.66  ? 65  THR B CA    1 
ATOM   2739 C  C     . THR B 2 65  ? 142.095 120.125 114.574 1.00 27.88  ? 65  THR B C     1 
ATOM   2740 O  O     . THR B 2 65  ? 143.005 119.797 115.347 1.00 38.80  ? 65  THR B O     1 
ATOM   2741 C  CB    . THR B 2 65  ? 139.669 120.001 115.226 1.00 31.83  ? 65  THR B CB    1 
ATOM   2742 O  OG1   . THR B 2 65  ? 138.565 120.760 115.730 1.00 35.04  ? 65  THR B OG1   1 
ATOM   2743 C  CG2   . THR B 2 65  ? 139.952 118.847 116.173 1.00 27.90  ? 65  THR B CG2   1 
ATOM   2744 N  N     . LEU B 2 66  ? 142.136 119.856 113.265 1.00 27.33  ? 66  LEU B N     1 
ATOM   2745 C  CA    . LEU B 2 66  ? 143.276 119.166 112.671 1.00 24.30  ? 66  LEU B CA    1 
ATOM   2746 C  C     . LEU B 2 66  ? 144.535 120.024 112.722 1.00 31.98  ? 66  LEU B C     1 
ATOM   2747 O  O     . LEU B 2 66  ? 145.631 119.510 112.967 1.00 39.33  ? 66  LEU B O     1 
ATOM   2748 C  CB    . LEU B 2 66  ? 142.948 118.766 111.233 1.00 28.26  ? 66  LEU B CB    1 
ATOM   2749 C  CG    . LEU B 2 66  ? 143.962 117.888 110.498 1.00 30.93  ? 66  LEU B CG    1 
ATOM   2750 C  CD1   . LEU B 2 66  ? 144.154 116.566 111.221 1.00 29.66  ? 66  LEU B CD1   1 
ATOM   2751 C  CD2   . LEU B 2 66  ? 143.516 117.654 109.067 1.00 24.37  ? 66  LEU B CD2   1 
ATOM   2752 N  N     . SER B 2 67  ? 144.393 121.338 112.523 1.00 34.40  ? 67  SER B N     1 
ATOM   2753 C  CA    . SER B 2 67  ? 145.548 122.229 112.579 1.00 23.90  ? 67  SER B CA    1 
ATOM   2754 C  C     . SER B 2 67  ? 146.094 122.362 113.999 1.00 27.71  ? 67  SER B C     1 
ATOM   2755 O  O     . SER B 2 67  ? 147.309 122.466 114.191 1.00 37.65  ? 67  SER B O     1 
ATOM   2756 C  CB    . SER B 2 67  ? 145.181 123.598 112.009 1.00 28.60  ? 67  SER B CB    1 
ATOM   2757 O  OG    . SER B 2 67  ? 144.745 124.482 113.025 1.00 38.18  ? 67  SER B OG    1 
ATOM   2758 N  N     . ASN B 2 68  ? 145.217 122.354 115.007 1.00 28.88  ? 68  ASN B N     1 
ATOM   2759 C  CA    . ASN B 2 68  ? 145.680 122.402 116.391 1.00 23.96  ? 68  ASN B CA    1 
ATOM   2760 C  C     . ASN B 2 68  ? 146.280 121.070 116.821 1.00 29.39  ? 68  ASN B C     1 
ATOM   2761 O  O     . ASN B 2 68  ? 147.176 121.032 117.671 1.00 41.62  ? 68  ASN B O     1 
ATOM   2762 C  CB    . ASN B 2 68  ? 144.532 122.792 117.322 1.00 32.08  ? 68  ASN B CB    1 
ATOM   2763 C  CG    . ASN B 2 68  ? 144.080 124.223 117.124 1.00 34.89  ? 68  ASN B CG    1 
ATOM   2764 O  OD1   . ASN B 2 68  ? 144.840 125.069 116.660 1.00 39.13  ? 68  ASN B OD1   1 
ATOM   2765 N  ND2   . ASN B 2 68  ? 142.832 124.499 117.479 1.00 39.21  ? 68  ASN B ND2   1 
ATOM   2766 N  N     . ILE B 2 69  ? 145.783 119.966 116.259 1.00 34.75  ? 69  ILE B N     1 
ATOM   2767 C  CA    . ILE B 2 69  ? 146.364 118.656 116.538 1.00 34.76  ? 69  ILE B CA    1 
ATOM   2768 C  C     . ILE B 2 69  ? 147.756 118.547 115.919 1.00 32.97  ? 69  ILE B C     1 
ATOM   2769 O  O     . ILE B 2 69  ? 148.689 118.022 116.542 1.00 43.91  ? 69  ILE B O     1 
ATOM   2770 C  CB    . ILE B 2 69  ? 145.399 117.554 116.051 1.00 35.05  ? 69  ILE B CB    1 
ATOM   2771 C  CG1   . ILE B 2 69  ? 144.372 117.243 117.141 1.00 29.79  ? 69  ILE B CG1   1 
ATOM   2772 C  CG2   . ILE B 2 69  ? 146.120 116.282 115.635 1.00 36.24  ? 69  ILE B CG2   1 
ATOM   2773 C  CD1   . ILE B 2 69  ? 143.170 116.489 116.648 1.00 32.28  ? 69  ILE B CD1   1 
ATOM   2774 N  N     . ILE B 2 70  ? 147.922 119.068 114.698 1.00 33.68  ? 70  ILE B N     1 
ATOM   2775 C  CA    . ILE B 2 70  ? 149.235 119.112 114.053 1.00 33.75  ? 70  ILE B CA    1 
ATOM   2776 C  C     . ILE B 2 70  ? 150.180 120.037 114.817 1.00 40.82  ? 70  ILE B C     1 
ATOM   2777 O  O     . ILE B 2 70  ? 151.341 119.692 115.071 1.00 43.85  ? 70  ILE B O     1 
ATOM   2778 C  CB    . ILE B 2 70  ? 149.081 119.536 112.577 1.00 38.46  ? 70  ILE B CB    1 
ATOM   2779 C  CG1   . ILE B 2 70  ? 148.501 118.390 111.748 1.00 38.83  ? 70  ILE B CG1   1 
ATOM   2780 C  CG2   . ILE B 2 70  ? 150.406 119.988 111.976 1.00 32.91  ? 70  ILE B CG2   1 
ATOM   2781 C  CD1   . ILE B 2 70  ? 147.806 118.846 110.484 1.00 31.31  ? 70  ILE B CD1   1 
ATOM   2782 N  N     . GLY B 2 71  ? 149.685 121.201 115.239 1.00 40.95  ? 71  GLY B N     1 
ATOM   2783 C  CA    . GLY B 2 71  ? 150.502 122.163 115.957 1.00 36.58  ? 71  GLY B CA    1 
ATOM   2784 C  C     . GLY B 2 71  ? 150.832 121.781 117.385 1.00 44.28  ? 71  GLY B C     1 
ATOM   2785 O  O     . GLY B 2 71  ? 151.689 122.430 117.994 1.00 53.53  ? 71  GLY B O     1 
ATOM   2786 N  N     . GLY B 2 72  ? 150.208 120.751 117.957 1.00 41.23  ? 72  GLY B N     1 
ATOM   2787 C  CA    . GLY B 2 72  ? 150.505 120.257 119.318 1.00 40.12  ? 72  GLY B CA    1 
ATOM   2788 C  C     . GLY B 2 72  ? 149.654 120.835 120.438 1.00 39.93  ? 72  GLY B C     1 
ATOM   2789 O  O     . GLY B 2 72  ? 149.797 120.358 121.544 1.00 47.77  ? 72  GLY B O     1 
ATOM   2790 N  N     . SER B 2 73  ? 148.848 121.854 120.199 1.00 31.52  ? 73  SER B N     1 
ATOM   2791 C  CA    . SER B 2 73  ? 147.935 122.479 121.188 1.00 32.30  ? 73  SER B CA    1 
ATOM   2792 C  C     . SER B 2 73  ? 146.854 121.499 121.659 1.00 39.41  ? 73  SER B C     1 
ATOM   2793 O  O     . SER B 2 73  ? 146.409 121.667 122.790 1.00 40.99  ? 73  SER B O     1 
ATOM   2794 C  CB    . SER B 2 73  ? 147.365 123.756 120.666 1.00 40.30  ? 73  SER B CB    1 
ATOM   2795 O  OG    . SER B 2 73  ? 147.810 124.023 119.346 1.00 45.58  ? 73  SER B OG    1 
ATOM   2796 N  N     . LEU B 2 74  ? 146.363 120.642 120.768 1.00 36.07  ? 74  LEU B N     1 
ATOM   2797 C  CA    . LEU B 2 74  ? 145.245 119.725 121.049 1.00 26.26  ? 74  LEU B CA    1 
ATOM   2798 C  C     . LEU B 2 74  ? 145.690 118.276 120.903 1.00 33.22  ? 74  LEU B C     1 
ATOM   2799 O  O     . LEU B 2 74  ? 146.506 117.981 120.026 1.00 41.25  ? 74  LEU B O     1 
ATOM   2800 C  CB    . LEU B 2 74  ? 144.071 120.096 120.147 1.00 36.08  ? 74  LEU B CB    1 
ATOM   2801 C  CG    . LEU B 2 74  ? 142.739 119.385 120.368 1.00 36.21  ? 74  LEU B CG    1 
ATOM   2802 C  CD1   . LEU B 2 74  ? 142.066 119.994 121.579 1.00 37.39  ? 74  LEU B CD1   1 
ATOM   2803 C  CD2   . LEU B 2 74  ? 141.929 119.647 119.116 1.00 30.77  ? 74  LEU B CD2   1 
ATOM   2804 N  N     . SER B 2 75  ? 145.299 117.453 121.858 1.00 37.66  ? 75  SER B N     1 
ATOM   2805 C  CA    . SER B 2 75  ? 145.611 116.015 121.832 1.00 36.50  ? 75  SER B CA    1 
ATOM   2806 C  C     . SER B 2 75  ? 144.545 115.216 121.077 1.00 38.94  ? 75  SER B C     1 
ATOM   2807 O  O     . SER B 2 75  ? 143.361 115.491 121.246 1.00 40.37  ? 75  SER B O     1 
ATOM   2808 C  CB    . SER B 2 75  ? 145.801 115.507 123.239 1.00 37.05  ? 75  SER B CB    1 
ATOM   2809 O  OG    . SER B 2 75  ? 146.680 114.393 123.262 1.00 46.97  ? 75  SER B OG    1 
ATOM   2810 N  N     . PRO B 2 76  ? 144.922 114.261 120.213 1.00 36.43  ? 76  PRO B N     1 
ATOM   2811 C  CA    . PRO B 2 76  ? 143.927 113.360 119.592 1.00 32.74  ? 76  PRO B CA    1 
ATOM   2812 C  C     . PRO B 2 76  ? 143.246 112.469 120.623 1.00 35.96  ? 76  PRO B C     1 
ATOM   2813 O  O     . PRO B 2 76  ? 143.888 112.096 121.617 1.00 46.76  ? 76  PRO B O     1 
ATOM   2814 C  CB    . PRO B 2 76  ? 144.786 112.510 118.677 1.00 37.69  ? 76  PRO B CB    1 
ATOM   2815 C  CG    . PRO B 2 76  ? 146.101 113.219 118.492 1.00 35.56  ? 76  PRO B CG    1 
ATOM   2816 C  CD    . PRO B 2 76  ? 146.309 113.979 119.743 1.00 29.66  ? 76  PRO B CD    1 
ATOM   2817 N  N     . THR B 2 77  ? 141.949 112.219 120.513 1.00 34.83  ? 77  THR B N     1 
ATOM   2818 C  CA    . THR B 2 77  ? 141.303 111.197 121.356 1.00 40.29  ? 77  THR B CA    1 
ATOM   2819 C  C     . THR B 2 77  ? 141.888 109.843 120.994 1.00 41.77  ? 77  THR B C     1 
ATOM   2820 O  O     . THR B 2 77  ? 142.193 109.077 121.909 1.00 46.80  ? 77  THR B O     1 
ATOM   2821 C  CB    . THR B 2 77  ? 139.779 111.256 121.223 1.00 40.16  ? 77  THR B CB    1 
ATOM   2822 O  OG1   . THR B 2 77  ? 139.364 112.471 121.826 1.00 35.96  ? 77  THR B OG1   1 
ATOM   2823 C  CG2   . THR B 2 77  ? 139.070 110.121 121.934 1.00 42.90  ? 77  THR B CG2   1 
ATOM   2824 N  N     . VAL B 2 78  ? 142.073 109.562 119.713 1.00 41.81  ? 78  VAL B N     1 
ATOM   2825 C  CA    . VAL B 2 78  ? 142.622 108.273 119.211 1.00 41.22  ? 78  VAL B CA    1 
ATOM   2826 C  C     . VAL B 2 78  ? 143.581 108.631 118.070 1.00 42.36  ? 78  VAL B C     1 
ATOM   2827 O  O     . VAL B 2 78  ? 143.407 109.689 117.504 1.00 41.74  ? 78  VAL B O     1 
ATOM   2828 C  CB    . VAL B 2 78  ? 141.614 107.193 118.753 1.00 43.85  ? 78  VAL B CB    1 
ATOM   2829 C  CG1   . VAL B 2 78  ? 142.203 105.791 118.767 1.00 42.72  ? 78  VAL B CG1   1 
ATOM   2830 C  CG2   . VAL B 2 78  ? 140.305 107.233 119.525 1.00 46.82  ? 78  VAL B CG2   1 
ATOM   2831 N  N     . GLY B 2 79  ? 144.550 107.772 117.785 1.00 49.96  ? 79  GLY B N     1 
ATOM   2832 C  CA    . GLY B 2 79  ? 145.547 107.948 116.726 1.00 45.50  ? 79  GLY B CA    1 
ATOM   2833 C  C     . GLY B 2 79  ? 146.758 108.701 117.178 1.00 46.90  ? 79  GLY B C     1 
ATOM   2834 O  O     . GLY B 2 79  ? 146.755 109.193 118.302 1.00 52.85  ? 79  GLY B O     1 
ATOM   2835 N  N     . LYS B 2 80  ? 147.744 108.819 116.299 1.00 46.62  ? 80  LYS B N     1 
ATOM   2836 C  CA    . LYS B 2 80  ? 149.011 109.510 116.620 1.00 45.51  ? 80  LYS B CA    1 
ATOM   2837 C  C     . LYS B 2 80  ? 149.426 110.475 115.526 1.00 49.21  ? 80  LYS B C     1 
ATOM   2838 O  O     . LYS B 2 80  ? 149.074 110.237 114.365 1.00 55.32  ? 80  LYS B O     1 
ATOM   2839 C  CB    . LYS B 2 80  ? 150.136 108.478 116.675 1.00 50.62  ? 80  LYS B CB    1 
ATOM   2840 C  CG    . LYS B 2 80  ? 150.976 108.499 117.937 1.00 54.12  ? 80  LYS B CG    1 
ATOM   2841 C  CD    . LYS B 2 80  ? 152.440 108.836 117.683 1.00 52.79  ? 80  LYS B CD    1 
ATOM   2842 C  CE    . LYS B 2 80  ? 152.932 109.958 118.536 1.00 53.82  ? 80  LYS B CE    1 
ATOM   2843 N  NZ    . LYS B 2 80  ? 154.141 110.560 117.970 1.00 51.43  ? 80  LYS B NZ    1 
ATOM   2844 N  N     . VAL B 2 81  ? 150.058 111.562 115.911 1.00 49.03  ? 81  VAL B N     1 
ATOM   2845 C  CA    . VAL B 2 81  ? 150.680 112.498 114.948 1.00 47.59  ? 81  VAL B CA    1 
ATOM   2846 C  C     . VAL B 2 81  ? 152.188 112.379 115.188 1.00 48.16  ? 81  VAL B C     1 
ATOM   2847 O  O     . VAL B 2 81  ? 152.609 112.566 116.318 1.00 54.88  ? 81  VAL B O     1 
ATOM   2848 C  CB    . VAL B 2 81  ? 150.192 113.951 115.117 1.00 50.84  ? 81  VAL B CB    1 
ATOM   2849 C  CG1   . VAL B 2 81  ? 150.907 114.919 114.185 1.00 45.57  ? 81  VAL B CG1   1 
ATOM   2850 C  CG2   . VAL B 2 81  ? 148.690 114.055 114.924 1.00 47.72  ? 81  VAL B CG2   1 
ATOM   2851 N  N     . ASP B 2 82  ? 152.966 112.099 114.150 1.00 51.02  ? 82  ASP B N     1 
ATOM   2852 C  CA    . ASP B 2 82  ? 154.443 112.075 114.241 1.00 49.26  ? 82  ASP B CA    1 
ATOM   2853 C  C     . ASP B 2 82  ? 154.974 113.250 113.441 1.00 47.17  ? 82  ASP B C     1 
ATOM   2854 O  O     . ASP B 2 82  ? 154.719 113.310 112.245 1.00 51.02  ? 82  ASP B O     1 
ATOM   2855 C  CB    . ASP B 2 82  ? 155.032 110.872 113.547 1.00 50.26  ? 82  ASP B CB    1 
ATOM   2856 C  CG    . ASP B 2 82  ? 154.850 109.525 114.222 1.00 55.61  ? 82  ASP B CG    1 
ATOM   2857 O  OD1   . ASP B 2 82  ? 154.825 108.519 113.490 1.00 56.96  ? 82  ASP B OD1   1 
ATOM   2858 O  OD2   . ASP B 2 82  ? 154.740 109.494 115.460 1.00 57.33  ? 82  ASP B OD2   1 
ATOM   2859 N  N     . ARG B 2 83  ? 155.737 114.115 114.080 1.00 49.48  ? 83  ARG B N     1 
ATOM   2860 C  CA    . ARG B 2 83  ? 156.264 115.326 113.416 1.00 47.92  ? 83  ARG B CA    1 
ATOM   2861 C  C     . ARG B 2 83  ? 157.782 115.223 113.418 1.00 48.43  ? 83  ARG B C     1 
ATOM   2862 O  O     . ARG B 2 83  ? 158.327 114.883 114.465 1.00 53.50  ? 83  ARG B O     1 
ATOM   2863 C  CB    . ARG B 2 83  ? 155.770 116.551 114.192 1.00 45.77  ? 83  ARG B CB    1 
ATOM   2864 C  CG    . ARG B 2 83  ? 154.304 116.673 114.562 1.00 49.32  ? 83  ARG B CG    1 
ATOM   2865 C  CD    . ARG B 2 83  ? 154.176 117.733 115.635 1.00 45.32  ? 83  ARG B CD    1 
ATOM   2866 N  NE    . ARG B 2 83  ? 152.828 117.817 116.203 1.00 49.20  ? 83  ARG B NE    1 
ATOM   2867 C  CZ    . ARG B 2 83  ? 152.393 117.059 117.192 1.00 50.83  ? 83  ARG B CZ    1 
ATOM   2868 N  NH1   . ARG B 2 83  ? 153.243 116.307 117.857 1.00 52.36  ? 83  ARG B NH1   1 
ATOM   2869 N  NH2   . ARG B 2 83  ? 151.117 117.054 117.516 1.00 53.34  ? 83  ARG B NH2   1 
ATOM   2870 N  N     . ASN B 2 84  ? 158.421 115.378 112.274 1.00 53.73  ? 84  ASN B N     1 
ATOM   2871 C  CA    . ASN B 2 84  ? 159.895 115.443 112.270 1.00 54.18  ? 84  ASN B CA    1 
ATOM   2872 C  C     . ASN B 2 84  ? 160.188 116.922 112.133 1.00 57.37  ? 84  ASN B C     1 
ATOM   2873 O  O     . ASN B 2 84  ? 160.095 117.448 111.011 1.00 60.01  ? 84  ASN B O     1 
ATOM   2874 C  CB    . ASN B 2 84  ? 160.478 114.642 111.118 1.00 57.39  ? 84  ASN B CB    1 
ATOM   2875 C  CG    . ASN B 2 84  ? 161.986 114.664 111.115 1.00 62.84  ? 84  ASN B CG    1 
ATOM   2876 O  OD1   . ASN B 2 84  ? 162.614 114.269 112.102 1.00 61.80  ? 84  ASN B OD1   1 
ATOM   2877 N  ND2   . ASN B 2 84  ? 162.582 115.128 110.026 1.00 61.82  ? 84  ASN B ND2   1 
ATOM   2878 N  N     . GLY B 2 85  ? 160.624 117.533 113.212 1.00 54.47  ? 85  GLY B N     1 
ATOM   2879 C  CA    . GLY B 2 85  ? 160.874 118.967 113.177 1.00 56.21  ? 85  GLY B CA    1 
ATOM   2880 C  C     . GLY B 2 85  ? 160.053 119.788 114.111 1.00 55.78  ? 85  GLY B C     1 
ATOM   2881 O  O     . GLY B 2 85  ? 159.109 119.238 114.689 1.00 55.22  ? 85  GLY B O     1 
ATOM   2882 N  N     . GLU B 2 86  ? 160.473 121.033 114.300 1.00 52.95  ? 86  GLU B N     1 
ATOM   2883 C  CA    . GLU B 2 86  ? 159.741 122.009 115.122 1.00 53.43  ? 86  GLU B CA    1 
ATOM   2884 C  C     . GLU B 2 86  ? 158.476 122.490 114.422 1.00 54.21  ? 86  GLU B C     1 
ATOM   2885 O  O     . GLU B 2 86  ? 158.483 122.538 113.204 1.00 53.99  ? 86  GLU B O     1 
ATOM   2886 C  CB    . GLU B 2 86  ? 160.709 123.162 115.368 1.00 54.09  ? 86  GLU B CB    1 
ATOM   2887 C  CG    . GLU B 2 86  ? 162.122 122.694 115.697 1.00 57.42  ? 86  GLU B CG    1 
ATOM   2888 C  CD    . GLU B 2 86  ? 162.396 122.475 117.176 1.00 61.81  ? 86  GLU B CD    1 
ATOM   2889 O  OE1   . GLU B 2 86  ? 161.540 121.890 117.871 1.00 58.72  ? 86  GLU B OE1   1 
ATOM   2890 O  OE2   . GLU B 2 86  ? 163.479 122.894 117.634 1.00 60.52  ? 86  GLU B OE2   1 
ATOM   2891 N  N     . VAL B 2 87  ? 157.465 122.859 115.194 1.00 46.68  ? 87  VAL B N     1 
ATOM   2892 C  CA    . VAL B 2 87  ? 156.187 123.360 114.637 1.00 42.78  ? 87  VAL B CA    1 
ATOM   2893 C  C     . VAL B 2 87  ? 155.980 124.786 115.161 1.00 41.33  ? 87  VAL B C     1 
ATOM   2894 O  O     . VAL B 2 87  ? 156.186 125.004 116.342 1.00 44.35  ? 87  VAL B O     1 
ATOM   2895 C  CB    . VAL B 2 87  ? 154.978 122.441 114.918 1.00 39.11  ? 87  VAL B CB    1 
ATOM   2896 C  CG1   . VAL B 2 87  ? 153.714 122.957 114.249 1.00 40.11  ? 87  VAL B CG1   1 
ATOM   2897 C  CG2   . VAL B 2 87  ? 155.245 121.012 114.477 1.00 40.34  ? 87  VAL B CG2   1 
ATOM   2898 N  N     . SER B 2 88  ? 155.648 125.714 114.283 1.00 36.70  ? 88  SER B N     1 
ATOM   2899 C  CA    . SER B 2 88  ? 155.299 127.087 114.697 1.00 35.14  ? 88  SER B CA    1 
ATOM   2900 C  C     . SER B 2 88  ? 153.940 127.410 114.093 1.00 38.23  ? 88  SER B C     1 
ATOM   2901 O  O     . SER B 2 88  ? 153.636 126.892 113.042 1.00 37.57  ? 88  SER B O     1 
ATOM   2902 C  CB    . SER B 2 88  ? 156.310 128.104 114.326 1.00 39.10  ? 88  SER B CB    1 
ATOM   2903 O  OG    . SER B 2 88  ? 157.286 128.256 115.346 1.00 49.57  ? 88  SER B OG    1 
ATOM   2904 N  N     . VAL B 2 89  ? 153.150 128.190 114.800 1.00 83.56  ? 89  VAL B N     1 
ATOM   2905 C  CA    . VAL B 2 89  ? 151.793 128.563 114.358 1.00 83.69  ? 89  VAL B CA    1 
ATOM   2906 C  C     . VAL B 2 89  ? 151.799 130.082 114.184 1.00 87.24  ? 89  VAL B C     1 
ATOM   2907 O  O     . VAL B 2 89  ? 152.202 130.775 115.092 1.00 88.73  ? 89  VAL B O     1 
ATOM   2908 C  CB    . VAL B 2 89  ? 150.754 128.088 115.393 1.00 81.13  ? 89  VAL B CB    1 
ATOM   2909 C  CG1   . VAL B 2 89  ? 149.341 128.470 114.984 1.00 81.75  ? 89  VAL B CG1   1 
ATOM   2910 C  CG2   . VAL B 2 89  ? 150.851 126.591 115.648 1.00 81.26  ? 89  VAL B CG2   1 
ATOM   2911 N  N     . ILE B 2 90  ? 151.341 130.557 113.045 1.00 90.21  ? 90  ILE B N     1 
ATOM   2912 C  CA    . ILE B 2 90  ? 151.224 132.026 112.940 1.00 90.06  ? 90  ILE B CA    1 
ATOM   2913 C  C     . ILE B 2 90  ? 149.815 132.421 113.392 1.00 92.56  ? 90  ILE B C     1 
ATOM   2914 O  O     . ILE B 2 90  ? 148.875 132.238 112.615 1.00 88.00  ? 90  ILE B O     1 
ATOM   2915 C  CB    . ILE B 2 90  ? 151.638 132.564 111.552 1.00 86.97  ? 90  ILE B CB    1 
ATOM   2916 C  CG1   . ILE B 2 90  ? 153.147 132.477 111.374 1.00 87.57  ? 90  ILE B CG1   1 
ATOM   2917 C  CG2   . ILE B 2 90  ? 151.139 133.988 111.320 1.00 91.32  ? 90  ILE B CG2   1 
ATOM   2918 C  CD1   . ILE B 2 90  ? 153.618 132.668 109.949 1.00 90.81  ? 90  ILE B CD1   1 
ATOM   2919 N  N     . ALA B 2 91  ? 149.699 132.851 114.652 1.00 107.82 ? 91  ALA B N     1 
ATOM   2920 C  CA    . ALA B 2 91  ? 148.457 133.442 115.180 1.00 106.39 ? 91  ALA B CA    1 
ATOM   2921 C  C     . ALA B 2 91  ? 148.931 134.786 115.722 1.00 109.92 ? 91  ALA B C     1 
ATOM   2922 O  O     . ALA B 2 91  ? 149.559 134.745 116.801 1.00 112.90 ? 91  ALA B O     1 
ATOM   2923 C  CB    . ALA B 2 91  ? 147.955 132.557 116.272 1.00 100.00 ? 91  ALA B CB    1 
ATOM   2924 N  N     . ILE B 2 92  ? 148.541 135.917 115.123 1.00 103.77 ? 92  ILE B N     1 
ATOM   2925 C  CA    . ILE B 2 92  ? 149.131 137.260 115.456 1.00 105.91 ? 92  ILE B CA    1 
ATOM   2926 C  C     . ILE B 2 92  ? 148.859 137.740 116.899 1.00 102.19 ? 92  ILE B C     1 
ATOM   2927 O  O     . ILE B 2 92  ? 149.785 138.288 117.516 1.00 103.81 ? 92  ILE B O     1 
ATOM   2928 C  CB    . ILE B 2 92  ? 148.776 138.294 114.355 1.00 103.74 ? 92  ILE B CB    1 
ATOM   2929 C  CG1   . ILE B 2 92  ? 147.355 138.824 114.448 1.00 98.05  ? 92  ILE B CG1   1 
ATOM   2930 C  CG2   . ILE B 2 92  ? 149.068 137.714 112.970 1.00 102.88 ? 92  ILE B CG2   1 
ATOM   2931 C  CD1   . ILE B 2 92  ? 146.901 139.540 113.191 1.00 95.59  ? 92  ILE B CD1   1 
ATOM   2932 N  N     . SER B 2 93  ? 147.670 137.518 117.434 1.00 99.53  ? 93  SER B N     1 
ATOM   2933 C  CA    . SER B 2 93  ? 147.292 138.098 118.746 1.00 104.19 ? 93  SER B CA    1 
ATOM   2934 C  C     . SER B 2 93  ? 147.566 137.294 120.024 1.00 105.59 ? 93  SER B C     1 
ATOM   2935 O  O     . SER B 2 93  ? 147.428 137.914 121.092 1.00 105.35 ? 93  SER B O     1 
ATOM   2936 C  CB    . SER B 2 93  ? 145.830 138.374 118.657 1.00 107.85 ? 93  SER B CB    1 
ATOM   2937 O  OG    . SER B 2 93  ? 145.275 137.842 117.461 1.00 111.19 ? 93  SER B OG    1 
ATOM   2938 N  N     . ALA B 2 94  ? 148.093 136.074 119.974 1.00 105.70 ? 94  ALA B N     1 
ATOM   2939 C  CA    . ALA B 2 94  ? 148.129 135.187 121.188 1.00 107.12 ? 94  ALA B CA    1 
ATOM   2940 C  C     . ALA B 2 94  ? 148.924 135.788 122.364 1.00 108.37 ? 94  ALA B C     1 
ATOM   2941 O  O     . ALA B 2 94  ? 148.394 135.753 123.474 1.00 108.76 ? 94  ALA B O     1 
ATOM   2942 C  CB    . ALA B 2 94  ? 148.619 133.797 120.826 1.00 104.27 ? 94  ALA B CB    1 
ATOM   2943 N  N     . GLY B 2 95  ? 150.067 136.417 122.133 1.00 103.24 ? 95  GLY B N     1 
ATOM   2944 C  CA    . GLY B 2 95  ? 150.774 137.115 123.230 1.00 99.77  ? 95  GLY B CA    1 
ATOM   2945 C  C     . GLY B 2 95  ? 150.472 138.611 123.359 1.00 100.49 ? 95  GLY B C     1 
ATOM   2946 O  O     . GLY B 2 95  ? 151.212 139.233 124.145 1.00 95.56  ? 95  GLY B O     1 
ATOM   2947 N  N     . LEU B 2 96  ? 149.533 139.220 122.590 1.00 94.46  ? 96  LEU B N     1 
ATOM   2948 C  CA    . LEU B 2 96  ? 149.390 140.721 122.624 1.00 89.27  ? 96  LEU B CA    1 
ATOM   2949 C  C     . LEU B 2 96  ? 148.509 141.223 123.773 1.00 87.82  ? 96  LEU B C     1 
ATOM   2950 O  O     . LEU B 2 96  ? 147.327 140.899 123.790 1.00 89.31  ? 96  LEU B O     1 
ATOM   2951 C  CB    . LEU B 2 96  ? 149.003 141.367 121.294 1.00 84.56  ? 96  LEU B CB    1 
ATOM   2952 C  CG    . LEU B 2 96  ? 150.132 142.065 120.532 1.00 89.18  ? 96  LEU B CG    1 
ATOM   2953 C  CD1   . LEU B 2 96  ? 151.191 141.071 120.113 1.00 86.30  ? 96  LEU B CD1   1 
ATOM   2954 C  CD2   . LEU B 2 96  ? 149.630 142.833 119.330 1.00 88.22  ? 96  LEU B CD2   1 
ATOM   2955 N  N     . SER B 2 97  ? 149.041 142.133 124.575 1.00 72.27  ? 97  SER B N     1 
ATOM   2956 C  CA    . SER B 2 97  ? 148.372 142.720 125.746 1.00 71.22  ? 97  SER B CA    1 
ATOM   2957 C  C     . SER B 2 97  ? 148.105 144.187 125.430 1.00 68.45  ? 97  SER B C     1 
ATOM   2958 O  O     . SER B 2 97  ? 149.037 144.845 125.014 1.00 73.11  ? 97  SER B O     1 
ATOM   2959 C  CB    . SER B 2 97  ? 149.246 142.569 126.953 1.00 69.07  ? 97  SER B CB    1 
ATOM   2960 O  OG    . SER B 2 97  ? 148.660 143.182 128.090 1.00 71.32  ? 97  SER B OG    1 
ATOM   2961 N  N     . GLY B 2 98  ? 146.881 144.656 125.621 1.00 66.64  ? 98  GLY B N     1 
ATOM   2962 C  CA    . GLY B 2 98  ? 146.534 146.064 125.440 1.00 66.99  ? 98  GLY B CA    1 
ATOM   2963 C  C     . GLY B 2 98  ? 147.289 146.928 126.410 1.00 73.22  ? 98  GLY B C     1 
ATOM   2964 O  O     . GLY B 2 98  ? 147.602 148.042 126.057 1.00 75.06  ? 98  GLY B O     1 
ATOM   2965 N  N     . GLN B 2 99  ? 147.467 146.474 127.636 1.00 34.58  ? 99  GLN B N     1 
ATOM   2966 C  CA    . GLN B 2 99  ? 148.168 147.216 128.711 1.00 30.62  ? 99  GLN B CA    1 
ATOM   2967 C  C     . GLN B 2 99  ? 149.639 147.453 128.364 1.00 33.35  ? 99  GLN B C     1 
ATOM   2968 O  O     . GLN B 2 99  ? 150.137 148.513 128.694 1.00 40.41  ? 99  GLN B O     1 
ATOM   2969 C  CB    . GLN B 2 99  ? 147.915 146.454 130.013 1.00 30.41  ? 99  GLN B CB    1 
ATOM   2970 C  CG    . GLN B 2 99  ? 146.442 146.257 130.337 1.00 32.19  ? 99  GLN B CG    1 
ATOM   2971 C  CD    . GLN B 2 99  ? 145.998 144.817 130.224 1.00 40.18  ? 99  GLN B CD    1 
ATOM   2972 O  OE1   . GLN B 2 99  ? 146.538 144.023 129.445 1.00 43.00  ? 99  GLN B OE1   1 
ATOM   2973 N  NE2   . GLN B 2 99  ? 144.995 144.461 131.010 1.00 43.24  ? 99  GLN B NE2   1 
ATOM   2974 N  N     . LEU B 2 100 ? 150.312 146.476 127.779 1.00 29.78  ? 100 LEU B N     1 
ATOM   2975 C  CA    . LEU B 2 100 ? 151.724 146.628 127.375 1.00 28.15  ? 100 LEU B CA    1 
ATOM   2976 C  C     . LEU B 2 100 ? 151.874 147.523 126.150 1.00 26.23  ? 100 LEU B C     1 
ATOM   2977 O  O     . LEU B 2 100 ? 150.960 147.559 125.336 1.00 33.73  ? 100 LEU B O     1 
ATOM   2978 C  CB    . LEU B 2 100 ? 152.446 145.282 127.262 1.00 28.22  ? 100 LEU B CB    1 
ATOM   2979 C  CG    . LEU B 2 100 ? 152.474 144.414 128.520 1.00 29.94  ? 100 LEU B CG    1 
ATOM   2980 C  CD1   . LEU B 2 100 ? 153.208 143.135 128.216 1.00 26.89  ? 100 LEU B CD1   1 
ATOM   2981 C  CD2   . LEU B 2 100 ? 153.073 145.131 129.714 1.00 25.54  ? 100 LEU B CD2   1 
ATOM   2982 N  N     . THR B 2 101 ? 152.968 148.252 126.075 1.00 23.07  ? 101 THR B N     1 
ATOM   2983 C  CA    . THR B 2 101 ? 153.324 149.046 124.897 1.00 24.06  ? 101 THR B CA    1 
ATOM   2984 C  C     . THR B 2 101 ? 153.813 148.126 123.801 1.00 30.77  ? 101 THR B C     1 
ATOM   2985 O  O     . THR B 2 101 ? 154.028 146.966 124.068 1.00 38.71  ? 101 THR B O     1 
ATOM   2986 C  CB    . THR B 2 101 ? 154.337 150.133 125.255 1.00 26.01  ? 101 THR B CB    1 
ATOM   2987 O  OG1   . THR B 2 101 ? 155.648 149.586 125.237 1.00 33.89  ? 101 THR B OG1   1 
ATOM   2988 C  CG2   . THR B 2 101 ? 154.040 150.781 126.592 1.00 22.04  ? 101 THR B CG2   1 
ATOM   2989 N  N     . GLY B 2 102 ? 153.877 148.604 122.571 1.00 28.92  ? 102 GLY B N     1 
ATOM   2990 C  CA    . GLY B 2 102 ? 154.274 147.742 121.462 1.00 25.38  ? 102 GLY B CA    1 
ATOM   2991 C  C     . GLY B 2 102 ? 155.657 147.202 121.642 1.00 26.27  ? 102 GLY B C     1 
ATOM   2992 O  O     . GLY B 2 102 ? 155.840 146.049 121.268 1.00 34.89  ? 102 GLY B O     1 
ATOM   2993 N  N     . ILE B 2 103 ? 156.604 147.973 122.137 1.00 28.84  ? 103 ILE B N     1 
ATOM   2994 C  CA    . ILE B 2 103 ? 157.989 147.528 122.444 1.00 29.61  ? 103 ILE B CA    1 
ATOM   2995 C  C     . ILE B 2 103 ? 157.970 146.441 123.523 1.00 31.68  ? 103 ILE B C     1 
ATOM   2996 O  O     . ILE B 2 103 ? 158.693 145.455 123.361 1.00 35.04  ? 103 ILE B O     1 
ATOM   2997 C  CB    . ILE B 2 103 ? 158.794 148.768 122.892 1.00 33.44  ? 103 ILE B CB    1 
ATOM   2998 C  CG1   . ILE B 2 103 ? 159.132 149.675 121.728 1.00 27.18  ? 103 ILE B CG1   1 
ATOM   2999 C  CG2   . ILE B 2 103 ? 160.051 148.391 123.671 1.00 40.36  ? 103 ILE B CG2   1 
ATOM   3000 C  CD1   . ILE B 2 103 ? 160.604 149.684 121.374 1.00 37.42  ? 103 ILE B CD1   1 
ATOM   3001 N  N     . GLU B 2 104 ? 157.176 146.595 124.567 1.00 29.17  ? 104 GLU B N     1 
ATOM   3002 C  CA    . GLU B 2 104 ? 156.985 145.584 125.629 1.00 25.08  ? 104 GLU B CA    1 
ATOM   3003 C  C     . GLU B 2 104 ? 156.308 144.311 125.122 1.00 29.00  ? 104 GLU B C     1 
ATOM   3004 O  O     . GLU B 2 104 ? 156.757 143.253 125.519 1.00 44.30  ? 104 GLU B O     1 
ATOM   3005 C  CB    . GLU B 2 104 ? 156.236 146.242 126.785 1.00 34.07  ? 104 GLU B CB    1 
ATOM   3006 C  CG    . GLU B 2 104 ? 156.998 147.378 127.450 1.00 30.55  ? 104 GLU B CG    1 
ATOM   3007 C  CD    . GLU B 2 104 ? 156.107 148.074 128.456 1.00 37.23  ? 104 GLU B CD    1 
ATOM   3008 O  OE1   . GLU B 2 104 ? 154.909 147.760 128.490 1.00 37.21  ? 104 GLU B OE1   1 
ATOM   3009 O  OE2   . GLU B 2 104 ? 156.597 148.932 129.207 1.00 42.28  ? 104 GLU B OE2   1 
ATOM   3010 N  N     . ASN B 2 105 ? 155.310 144.411 124.249 1.00 31.85  ? 105 ASN B N     1 
ATOM   3011 C  CA    . ASN B 2 105 ? 154.624 143.231 123.664 1.00 26.54  ? 105 ASN B CA    1 
ATOM   3012 C  C     . ASN B 2 105 ? 155.609 142.392 122.860 1.00 23.65  ? 105 ASN B C     1 
ATOM   3013 O  O     . ASN B 2 105 ? 155.415 141.193 122.841 1.00 32.80  ? 105 ASN B O     1 
ATOM   3014 C  CB    . ASN B 2 105 ? 153.342 143.582 122.909 1.00 27.08  ? 105 ASN B CB    1 
ATOM   3015 C  CG    . ASN B 2 105 ? 152.130 143.585 123.794 1.00 27.11  ? 105 ASN B CG    1 
ATOM   3016 O  OD1   . ASN B 2 105 ? 151.716 142.530 124.265 1.00 40.18  ? 105 ASN B OD1   1 
ATOM   3017 N  ND2   . ASN B 2 105 ? 151.562 144.750 124.032 1.00 30.01  ? 105 ASN B ND2   1 
ATOM   3018 N  N     . ILE B 2 106 ? 156.530 143.017 122.138 1.00 25.78  ? 106 ILE B N     1 
ATOM   3019 C  CA    . ILE B 2 106 ? 157.482 142.255 121.291 1.00 27.61  ? 106 ILE B CA    1 
ATOM   3020 C  C     . ILE B 2 106 ? 158.328 141.353 122.177 1.00 28.90  ? 106 ILE B C     1 
ATOM   3021 O  O     . ILE B 2 106 ? 158.360 140.179 121.895 1.00 36.67  ? 106 ILE B O     1 
ATOM   3022 C  CB    . ILE B 2 106 ? 158.378 143.206 120.453 1.00 29.44  ? 106 ILE B CB    1 
ATOM   3023 C  CG1   . ILE B 2 106 ? 157.586 144.069 119.480 1.00 32.44  ? 106 ILE B CG1   1 
ATOM   3024 C  CG2   . ILE B 2 106 ? 159.497 142.447 119.743 1.00 28.06  ? 106 ILE B CG2   1 
ATOM   3025 C  CD1   . ILE B 2 106 ? 158.329 145.302 119.002 1.00 29.28  ? 106 ILE B CD1   1 
ATOM   3026 N  N     . GLU B 2 107 ? 158.850 141.874 123.281 1.00 37.87  ? 107 GLU B N     1 
ATOM   3027 C  CA    . GLU B 2 107 ? 159.619 141.067 124.251 1.00 31.48  ? 107 GLU B CA    1 
ATOM   3028 C  C     . GLU B 2 107 ? 158.789 140.004 124.965 1.00 29.70  ? 107 GLU B C     1 
ATOM   3029 O  O     . GLU B 2 107 ? 159.264 138.900 125.039 1.00 32.35  ? 107 GLU B O     1 
ATOM   3030 C  CB    . GLU B 2 107 ? 160.295 141.980 125.267 1.00 32.04  ? 107 GLU B CB    1 
ATOM   3031 C  CG    . GLU B 2 107 ? 161.331 141.195 126.064 1.00 32.96  ? 107 GLU B CG    1 
ATOM   3032 C  CD    . GLU B 2 107 ? 161.876 141.817 127.324 1.00 44.08  ? 107 GLU B CD    1 
ATOM   3033 O  OE1   . GLU B 2 107 ? 161.405 142.898 127.693 1.00 48.16  ? 107 GLU B OE1   1 
ATOM   3034 O  OE2   . GLU B 2 107 ? 162.788 141.218 127.920 1.00 46.20  ? 107 GLU B OE2   1 
ATOM   3035 N  N     . PHE B 2 108 ? 157.598 140.334 125.411 1.00 30.16  ? 108 PHE B N     1 
ATOM   3036 C  CA    . PHE B 2 108 ? 156.709 139.388 126.085 1.00 22.97  ? 108 PHE B CA    1 
ATOM   3037 C  C     . PHE B 2 108 ? 156.252 138.276 125.174 1.00 32.61  ? 108 PHE B C     1 
ATOM   3038 O  O     . PHE B 2 108 ? 156.269 137.130 125.611 1.00 34.32  ? 108 PHE B O     1 
ATOM   3039 C  CB    . PHE B 2 108 ? 155.542 140.262 126.522 1.00 24.16  ? 108 PHE B CB    1 
ATOM   3040 C  CG    . PHE B 2 108 ? 154.407 139.563 127.250 1.00 32.56  ? 108 PHE B CG    1 
ATOM   3041 C  CD1   . PHE B 2 108 ? 154.596 139.017 128.509 1.00 33.42  ? 108 PHE B CD1   1 
ATOM   3042 C  CD2   . PHE B 2 108 ? 153.154 139.455 126.668 1.00 33.84  ? 108 PHE B CD2   1 
ATOM   3043 C  CE1   . PHE B 2 108 ? 153.560 138.380 129.166 1.00 34.82  ? 108 PHE B CE1   1 
ATOM   3044 C  CE2   . PHE B 2 108 ? 152.121 138.815 127.329 1.00 34.12  ? 108 PHE B CE2   1 
ATOM   3045 C  CZ    . PHE B 2 108 ? 152.329 138.276 128.573 1.00 34.09  ? 108 PHE B CZ    1 
ATOM   3046 N  N     . LYS B 2 109 ? 155.840 138.600 123.956 1.00 39.12  ? 109 LYS B N     1 
ATOM   3047 C  CA    . LYS B 2 109 ? 155.398 137.570 122.994 1.00 34.47  ? 109 LYS B CA    1 
ATOM   3048 C  C     . LYS B 2 109 ? 156.581 136.701 122.587 1.00 33.51  ? 109 LYS B C     1 
ATOM   3049 O  O     . LYS B 2 109 ? 156.394 135.513 122.572 1.00 36.53  ? 109 LYS B O     1 
ATOM   3050 C  CB    . LYS B 2 109 ? 154.627 138.173 121.816 1.00 34.85  ? 109 LYS B CB    1 
ATOM   3051 C  CG    . LYS B 2 109 ? 153.887 137.208 120.913 1.00 36.29  ? 109 LYS B CG    1 
ATOM   3052 C  CD    . LYS B 2 109 ? 153.355 137.863 119.646 1.00 47.37  ? 109 LYS B CD    1 
ATOM   3053 C  CE    . LYS B 2 109 ? 152.660 136.913 118.725 1.00 43.41  ? 109 LYS B CE    1 
ATOM   3054 N  NZ    . LYS B 2 109 ? 151.821 135.973 119.471 1.00 45.19  ? 109 LYS B NZ    1 
ATOM   3055 N  N     . MET B 2 110 ? 157.734 137.286 122.319 1.00 35.83  ? 110 MET B N     1 
ATOM   3056 C  CA    . MET B 2 110 ? 158.975 136.599 121.912 1.00 38.58  ? 110 MET B CA    1 
ATOM   3057 C  C     . MET B 2 110 ? 159.472 135.692 123.041 1.00 37.99  ? 110 MET B C     1 
ATOM   3058 O  O     . MET B 2 110 ? 160.040 134.667 122.711 1.00 44.26  ? 110 MET B O     1 
ATOM   3059 C  CB    . MET B 2 110 ? 160.003 137.612 121.410 1.00 36.92  ? 110 MET B CB    1 
ATOM   3060 C  CG    . MET B 2 110 ? 159.835 137.959 119.960 1.00 35.88  ? 110 MET B CG    1 
ATOM   3061 S  SD    . MET B 2 110 ? 161.229 138.978 119.464 1.00 56.53  ? 110 MET B SD    1 
ATOM   3062 C  CE    . MET B 2 110 ? 162.187 137.711 118.630 1.00 40.74  ? 110 MET B CE    1 
ATOM   3063 N  N     . LEU B 2 111 ? 159.380 136.104 124.293 1.00 41.50  ? 111 LEU B N     1 
ATOM   3064 C  CA    . LEU B 2 111 ? 159.727 135.277 125.473 1.00 31.26  ? 111 LEU B CA    1 
ATOM   3065 C  C     . LEU B 2 111 ? 158.785 134.087 125.533 1.00 34.65  ? 111 LEU B C     1 
ATOM   3066 O  O     . LEU B 2 111 ? 159.255 133.004 125.866 1.00 42.95  ? 111 LEU B O     1 
ATOM   3067 C  CB    . LEU B 2 111 ? 159.691 136.080 126.771 1.00 33.56  ? 111 LEU B CB    1 
ATOM   3068 C  CG    . LEU B 2 111 ? 160.847 137.044 127.045 1.00 32.85  ? 111 LEU B CG    1 
ATOM   3069 C  CD1   . LEU B 2 111 ? 160.497 137.946 128.209 1.00 37.97  ? 111 LEU B CD1   1 
ATOM   3070 C  CD2   . LEU B 2 111 ? 162.172 136.357 127.272 1.00 35.49  ? 111 LEU B CD2   1 
ATOM   3071 N  N     . CYS B 2 112 ? 157.514 134.300 125.235 1.00 41.00  ? 112 CYS B N     1 
ATOM   3072 C  CA    . CYS B 2 112 ? 156.489 133.241 125.267 1.00 34.90  ? 112 CYS B CA    1 
ATOM   3073 C  C     . CYS B 2 112 ? 156.640 132.343 124.034 1.00 43.26  ? 112 CYS B C     1 
ATOM   3074 O  O     . CYS B 2 112 ? 156.220 131.198 124.129 1.00 50.42  ? 112 CYS B O     1 
ATOM   3075 C  CB    . CYS B 2 112 ? 155.099 133.811 125.508 1.00 42.80  ? 112 CYS B CB    1 
ATOM   3076 S  SG    . CYS B 2 112 ? 154.883 134.719 127.058 1.00 49.19  ? 112 CYS B SG    1 
ATOM   3077 N  N     . MET B 2 113 ? 157.171 132.836 122.903 1.00 45.14  ? 113 MET B N     1 
ATOM   3078 C  CA    . MET B 2 113 ? 157.491 131.866 121.854 1.00 44.93  ? 113 MET B CA    1 
ATOM   3079 C  C     . MET B 2 113 ? 158.752 131.062 122.140 1.00 48.68  ? 113 MET B C     1 
ATOM   3080 O  O     . MET B 2 113 ? 158.968 130.039 121.484 1.00 59.73  ? 113 MET B O     1 
ATOM   3081 C  CB    . MET B 2 113 ? 157.648 132.533 120.483 1.00 46.26  ? 113 MET B CB    1 
ATOM   3082 C  CG    . MET B 2 113 ? 156.620 133.578 120.138 1.00 44.26  ? 113 MET B CG    1 
ATOM   3083 S  SD    . MET B 2 113 ? 157.149 134.648 118.792 1.00 55.89  ? 113 MET B SD    1 
ATOM   3084 C  CE    . MET B 2 113 ? 155.665 134.681 117.808 1.00 46.78  ? 113 MET B CE    1 
ATOM   3085 N  N     . GLY B 2 114 ? 159.588 131.489 123.079 1.00 38.18  ? 114 GLY B N     1 
ATOM   3086 C  CA    . GLY B 2 114 ? 160.775 130.740 123.425 1.00 38.52  ? 114 GLY B CA    1 
ATOM   3087 C  C     . GLY B 2 114 ? 162.087 131.320 122.952 1.00 44.78  ? 114 GLY B C     1 
ATOM   3088 O  O     . GLY B 2 114 ? 163.098 130.612 122.983 1.00 48.07  ? 114 GLY B O     1 
ATOM   3089 N  N     . PHE B 2 115 ? 162.105 132.572 122.506 1.00 47.91  ? 115 PHE B N     1 
ATOM   3090 C  CA    . PHE B 2 115 ? 163.354 133.208 122.119 1.00 47.44  ? 115 PHE B CA    1 
ATOM   3091 C  C     . PHE B 2 115 ? 164.170 133.571 123.355 1.00 47.06  ? 115 PHE B C     1 
ATOM   3092 O  O     . PHE B 2 115 ? 163.632 133.768 124.447 1.00 49.04  ? 115 PHE B O     1 
ATOM   3093 C  CB    . PHE B 2 115 ? 163.084 134.462 121.287 1.00 47.30  ? 115 PHE B CB    1 
ATOM   3094 C  CG    . PHE B 2 115 ? 162.551 134.178 119.913 1.00 48.24  ? 115 PHE B CG    1 
ATOM   3095 C  CD1   . PHE B 2 115 ? 161.187 134.058 119.694 1.00 47.67  ? 115 PHE B CD1   1 
ATOM   3096 C  CD2   . PHE B 2 115 ? 163.415 134.036 118.838 1.00 48.33  ? 115 PHE B CD2   1 
ATOM   3097 C  CE1   . PHE B 2 115 ? 160.694 133.798 118.429 1.00 46.77  ? 115 PHE B CE1   1 
ATOM   3098 C  CE2   . PHE B 2 115 ? 162.929 133.777 117.570 1.00 50.26  ? 115 PHE B CE2   1 
ATOM   3099 C  CZ    . PHE B 2 115 ? 161.567 133.659 117.366 1.00 47.01  ? 115 PHE B CZ    1 
ATOM   3100 N  N     . LYS B 2 116 ? 165.484 133.651 123.174 1.00 52.97  ? 116 LYS B N     1 
ATOM   3101 C  CA    . LYS B 2 116 ? 166.369 134.026 124.264 1.00 52.85  ? 116 LYS B CA    1 
ATOM   3102 C  C     . LYS B 2 116 ? 166.546 135.541 124.307 1.00 54.82  ? 116 LYS B C     1 
ATOM   3103 O  O     . LYS B 2 116 ? 166.095 136.269 123.421 1.00 63.94  ? 116 LYS B O     1 
ATOM   3104 C  CB    . LYS B 2 116 ? 167.717 133.322 124.127 1.00 55.20  ? 116 LYS B CB    1 
ATOM   3105 C  CG    . LYS B 2 116 ? 167.609 131.809 124.048 1.00 55.76  ? 116 LYS B CG    1 
ATOM   3106 C  CD    . LYS B 2 116 ? 166.883 131.250 125.261 1.00 56.20  ? 116 LYS B CD    1 
ATOM   3107 C  CE    . LYS B 2 116 ? 166.042 130.041 124.893 1.00 56.04  ? 116 LYS B CE    1 
ATOM   3108 N  NZ    . LYS B 2 116 ? 165.342 129.471 126.077 1.00 56.51  ? 116 LYS B NZ    1 
ATOM   3109 N  N     . ARG B 2 117 ? 167.210 136.007 125.369 1.00 50.48  ? 117 ARG B N     1 
ATOM   3110 C  CA    . ARG B 2 117 ? 167.358 137.441 125.619 1.00 51.56  ? 117 ARG B CA    1 
ATOM   3111 C  C     . ARG B 2 117 ? 168.199 138.119 124.542 1.00 54.04  ? 117 ARG B C     1 
ATOM   3112 O  O     . ARG B 2 117 ? 167.850 139.203 124.053 1.00 54.22  ? 117 ARG B O     1 
ATOM   3113 C  CB    . ARG B 2 117 ? 167.983 137.653 126.998 1.00 48.51  ? 117 ARG B CB    1 
ATOM   3114 C  CG    . ARG B 2 117 ? 167.872 139.063 127.537 1.00 52.94  ? 117 ARG B CG    1 
ATOM   3115 C  CD    . ARG B 2 117 ? 168.747 139.248 128.767 1.00 53.20  ? 117 ARG B CD    1 
ATOM   3116 N  NE    . ARG B 2 117 ? 168.955 137.998 129.488 1.00 54.96  ? 117 ARG B NE    1 
ATOM   3117 C  CZ    . ARG B 2 117 ? 169.552 137.904 130.669 1.00 57.84  ? 117 ARG B CZ    1 
ATOM   3118 N  NH1   . ARG B 2 117 ? 169.985 138.976 131.311 1.00 56.18  ? 117 ARG B NH1   1 
ATOM   3119 N  NH2   . ARG B 2 117 ? 169.716 136.704 131.219 1.00 51.30  ? 117 ARG B NH2   1 
ATOM   3120 N  N     . LYS B 2 118 ? 169.309 137.483 124.157 1.00 58.32  ? 118 LYS B N     1 
ATOM   3121 C  CA    . LYS B 2 118 ? 170.186 138.044 123.132 1.00 54.55  ? 118 LYS B CA    1 
ATOM   3122 C  C     . LYS B 2 118 ? 169.509 138.054 121.768 1.00 55.58  ? 118 LYS B C     1 
ATOM   3123 O  O     . LYS B 2 118 ? 169.693 138.994 120.990 1.00 55.37  ? 118 LYS B O     1 
ATOM   3124 C  CB    . LYS B 2 118 ? 171.503 137.264 123.069 1.00 54.87  ? 118 LYS B CB    1 
ATOM   3125 C  CG    . LYS B 2 118 ? 172.661 137.819 123.915 1.00 59.18  ? 118 LYS B CG    1 
ATOM   3126 C  CD    . LYS B 2 118 ? 172.327 138.009 125.389 1.00 58.98  ? 118 LYS B CD    1 
ATOM   3127 C  CE    . LYS B 2 118 ? 173.591 138.154 126.223 1.00 57.96  ? 118 LYS B CE    1 
ATOM   3128 N  NZ    . LYS B 2 118 ? 174.381 136.891 126.253 1.00 55.18  ? 118 LYS B NZ    1 
ATOM   3129 N  N     . GLU B 2 119 ? 168.703 137.029 121.477 1.00 55.92  ? 119 GLU B N     1 
ATOM   3130 C  CA    . GLU B 2 119 ? 167.964 136.986 120.217 1.00 55.83  ? 119 GLU B CA    1 
ATOM   3131 C  C     . GLU B 2 119 ? 166.914 138.091 120.145 1.00 58.08  ? 119 GLU B C     1 
ATOM   3132 O  O     . GLU B 2 119 ? 166.779 138.754 119.109 1.00 54.48  ? 119 GLU B O     1 
ATOM   3133 C  CB    . GLU B 2 119 ? 167.316 135.614 120.042 1.00 52.49  ? 119 GLU B CB    1 
ATOM   3134 C  CG    . GLU B 2 119 ? 168.292 134.515 119.660 1.00 57.84  ? 119 GLU B CG    1 
ATOM   3135 C  CD    . GLU B 2 119 ? 167.894 133.160 120.209 1.00 61.61  ? 119 GLU B CD    1 
ATOM   3136 O  OE1   . GLU B 2 119 ? 168.710 132.547 120.928 1.00 63.05  ? 119 GLU B OE1   1 
ATOM   3137 O  OE2   . GLU B 2 119 ? 166.766 132.708 119.923 1.00 61.33  ? 119 GLU B OE2   1 
ATOM   3138 N  N     . ILE B 2 120 ? 166.172 138.304 121.239 1.00 53.31  ? 120 ILE B N     1 
ATOM   3139 C  CA    . ILE B 2 120 ? 165.146 139.347 121.283 1.00 46.83  ? 120 ILE B CA    1 
ATOM   3140 C  C     . ILE B 2 120 ? 165.781 140.725 121.146 1.00 47.14  ? 120 ILE B C     1 
ATOM   3141 O  O     . ILE B 2 120 ? 165.309 141.573 120.375 1.00 53.44  ? 120 ILE B O     1 
ATOM   3142 C  CB    . ILE B 2 120 ? 164.320 139.226 122.579 1.00 48.10  ? 120 ILE B CB    1 
ATOM   3143 C  CG1   . ILE B 2 120 ? 163.464 137.963 122.549 1.00 47.24  ? 120 ILE B CG1   1 
ATOM   3144 C  CG2   . ILE B 2 120 ? 163.424 140.440 122.785 1.00 47.89  ? 120 ILE B CG2   1 
ATOM   3145 C  CD1   . ILE B 2 120 ? 162.766 137.672 123.851 1.00 44.06  ? 120 ILE B CD1   1 
ATOM   3146 N  N     . LYS B 2 121 ? 166.893 140.950 121.859 1.00 49.32  ? 121 LYS B N     1 
ATOM   3147 C  CA    . LYS B 2 121 ? 167.618 142.213 121.737 1.00 49.86  ? 121 LYS B CA    1 
ATOM   3148 C  C     . LYS B 2 121 ? 168.225 142.395 120.350 1.00 50.51  ? 121 LYS B C     1 
ATOM   3149 O  O     . LYS B 2 121 ? 168.383 143.531 119.889 1.00 52.02  ? 121 LYS B O     1 
ATOM   3150 C  CB    . LYS B 2 121 ? 168.714 142.295 122.799 1.00 50.81  ? 121 LYS B CB    1 
ATOM   3151 C  CG    . LYS B 2 121 ? 169.065 143.713 123.208 1.00 53.13  ? 121 LYS B CG    1 
ATOM   3152 C  CD    . LYS B 2 121 ? 170.546 143.992 123.013 1.00 53.43  ? 121 LYS B CD    1 
ATOM   3153 C  CE    . LYS B 2 121 ? 170.943 145.320 123.636 1.00 54.12  ? 121 LYS B CE    1 
ATOM   3154 N  NZ    . LYS B 2 121 ? 172.161 145.893 122.998 1.00 53.60  ? 121 LYS B NZ    1 
ATOM   3155 N  N     . ALA B 2 122 ? 168.572 141.297 119.673 1.00 53.19  ? 122 ALA B N     1 
ATOM   3156 C  CA    . ALA B 2 122 ? 169.116 141.404 118.326 1.00 52.32  ? 122 ALA B CA    1 
ATOM   3157 C  C     . ALA B 2 122 ? 168.044 141.782 117.311 1.00 51.99  ? 122 ALA B C     1 
ATOM   3158 O  O     . ALA B 2 122 ? 168.266 142.667 116.477 1.00 54.93  ? 122 ALA B O     1 
ATOM   3159 C  CB    . ALA B 2 122 ? 169.792 140.091 117.928 1.00 50.35  ? 122 ALA B CB    1 
ATOM   3160 N  N     . MET B 2 123 ? 166.878 141.137 117.356 1.00 55.21  ? 123 MET B N     1 
ATOM   3161 C  CA    . MET B 2 123 ? 165.929 141.345 116.263 1.00 54.86  ? 123 MET B CA    1 
ATOM   3162 C  C     . MET B 2 123 ? 164.705 142.177 116.633 1.00 52.41  ? 123 MET B C     1 
ATOM   3163 O  O     . MET B 2 123 ? 163.749 142.199 115.857 1.00 58.33  ? 123 MET B O     1 
ATOM   3164 C  CB    . MET B 2 123 ? 165.471 140.012 115.659 1.00 55.90  ? 123 MET B CB    1 
ATOM   3165 C  CG    . MET B 2 123 ? 164.813 139.069 116.611 1.00 52.70  ? 123 MET B CG    1 
ATOM   3166 S  SD    . MET B 2 123 ? 165.392 137.365 116.475 1.00 73.20  ? 123 MET B SD    1 
ATOM   3167 C  CE    . MET B 2 123 ? 164.648 136.862 114.926 1.00 57.83  ? 123 MET B CE    1 
ATOM   3168 N  N     . THR B 2 124 ? 164.700 142.856 117.782 1.00 43.99  ? 124 THR B N     1 
ATOM   3169 C  CA    . THR B 2 124 ? 163.705 143.906 118.015 1.00 44.92  ? 124 THR B CA    1 
ATOM   3170 C  C     . THR B 2 124 ? 163.696 145.045 116.978 1.00 46.62  ? 124 THR B C     1 
ATOM   3171 O  O     . THR B 2 124 ? 162.588 145.424 116.546 1.00 45.38  ? 124 THR B O     1 
ATOM   3172 C  CB    . THR B 2 124 ? 163.872 144.444 119.444 1.00 45.43  ? 124 THR B CB    1 
ATOM   3173 O  OG1   . THR B 2 124 ? 163.847 143.351 120.368 1.00 52.19  ? 124 THR B OG1   1 
ATOM   3174 C  CG2   . THR B 2 124 ? 162.755 145.407 119.807 1.00 41.68  ? 124 THR B CG2   1 
ATOM   3175 N  N     . PRO B 2 125 ? 164.837 145.648 116.547 1.00 55.25  ? 125 PRO B N     1 
ATOM   3176 C  CA    . PRO B 2 125 ? 164.715 146.820 115.647 1.00 49.28  ? 125 PRO B CA    1 
ATOM   3177 C  C     . PRO B 2 125 ? 164.149 146.538 114.261 1.00 46.86  ? 125 PRO B C     1 
ATOM   3178 O  O     . PRO B 2 125 ? 163.434 147.393 113.726 1.00 49.59  ? 125 PRO B O     1 
ATOM   3179 C  CB    . PRO B 2 125 ? 166.155 147.350 115.561 1.00 53.03  ? 125 PRO B CB    1 
ATOM   3180 C  CG    . PRO B 2 125 ? 166.822 146.825 116.749 1.00 46.30  ? 125 PRO B CG    1 
ATOM   3181 C  CD    . PRO B 2 125 ? 166.262 145.469 116.908 1.00 49.09  ? 125 PRO B CD    1 
ATOM   3182 N  N     . LYS B 2 126 ? 164.420 145.378 113.658 1.00 43.50  ? 126 LYS B N     1 
ATOM   3183 C  CA    . LYS B 2 126 ? 163.794 145.104 112.367 1.00 45.21  ? 126 LYS B CA    1 
ATOM   3184 C  C     . LYS B 2 126 ? 162.328 144.710 112.514 1.00 45.82  ? 126 LYS B C     1 
ATOM   3185 O  O     . LYS B 2 126 ? 161.550 144.884 111.573 1.00 49.10  ? 126 LYS B O     1 
ATOM   3186 C  CB    . LYS B 2 126 ? 164.576 144.062 111.564 1.00 49.07  ? 126 LYS B CB    1 
ATOM   3187 C  CG    . LYS B 2 126 ? 166.060 144.364 111.419 1.00 52.34  ? 126 LYS B CG    1 
ATOM   3188 C  CD    . LYS B 2 126 ? 166.951 143.171 111.664 1.00 53.42  ? 126 LYS B CD    1 
ATOM   3189 C  CE    . LYS B 2 126 ? 166.977 142.786 113.111 1.00 54.91  ? 126 LYS B CE    1 
ATOM   3190 N  NZ    . LYS B 2 126 ? 168.014 143.538 113.873 1.00 50.23  ? 126 LYS B NZ    1 
ATOM   3191 N  N     . ILE B 2 127 ? 161.915 144.230 113.692 1.00 42.42  ? 127 ILE B N     1 
ATOM   3192 C  CA    . ILE B 2 127 ? 160.482 144.070 113.951 1.00 37.40  ? 127 ILE B CA    1 
ATOM   3193 C  C     . ILE B 2 127 ? 159.799 145.432 114.019 1.00 37.11  ? 127 ILE B C     1 
ATOM   3194 O  O     . ILE B 2 127 ? 158.713 145.630 113.450 1.00 43.57  ? 127 ILE B O     1 
ATOM   3195 C  CB    . ILE B 2 127 ? 160.248 143.238 115.230 1.00 36.99  ? 127 ILE B CB    1 
ATOM   3196 C  CG1   . ILE B 2 127 ? 160.646 141.782 115.003 1.00 35.68  ? 127 ILE B CG1   1 
ATOM   3197 C  CG2   . ILE B 2 127 ? 158.794 143.288 115.678 1.00 32.19  ? 127 ILE B CG2   1 
ATOM   3198 C  CD1   . ILE B 2 127 ? 160.608 140.942 116.255 1.00 35.11  ? 127 ILE B CD1   1 
ATOM   3199 N  N     . ILE B 2 128 ? 160.444 146.399 114.685 1.00 37.73  ? 128 ILE B N     1 
ATOM   3200 C  CA    . ILE B 2 128 ? 159.926 147.769 114.738 1.00 36.79  ? 128 ILE B CA    1 
ATOM   3201 C  C     . ILE B 2 128 ? 159.878 148.389 113.343 1.00 40.08  ? 128 ILE B C     1 
ATOM   3202 O  O     . ILE B 2 128 ? 158.904 149.061 112.978 1.00 44.95  ? 128 ILE B O     1 
ATOM   3203 C  CB    . ILE B 2 128 ? 160.777 148.614 115.707 1.00 38.44  ? 128 ILE B CB    1 
ATOM   3204 C  CG1   . ILE B 2 128 ? 160.677 148.066 117.126 1.00 37.78  ? 128 ILE B CG1   1 
ATOM   3205 C  CG2   . ILE B 2 128 ? 160.354 150.077 115.699 1.00 36.85  ? 128 ILE B CG2   1 
ATOM   3206 C  CD1   . ILE B 2 128 ? 161.789 148.548 118.013 1.00 39.17  ? 128 ILE B CD1   1 
ATOM   3207 N  N     . GLU B 2 129 ? 160.915 148.148 112.535 1.00 42.03  ? 129 GLU B N     1 
ATOM   3208 C  CA    . GLU B 2 129 ? 160.966 148.692 111.179 1.00 43.01  ? 129 GLU B CA    1 
ATOM   3209 C  C     . GLU B 2 129 ? 159.922 148.037 110.278 1.00 47.47  ? 129 GLU B C     1 
ATOM   3210 O  O     . GLU B 2 129 ? 159.340 148.700 109.412 1.00 52.62  ? 129 GLU B O     1 
ATOM   3211 C  CB    . GLU B 2 129 ? 162.408 148.558 110.644 1.00 43.21  ? 129 GLU B CB    1 
ATOM   3212 C  CG    . GLU B 2 129 ? 162.739 148.610 109.115 1.00 49.83  ? 129 GLU B CG    1 
ATOM   3213 C  CD    . GLU B 2 129 ? 162.311 147.392 108.289 1.00 56.90  ? 129 GLU B CD    1 
ATOM   3214 O  OE1   . GLU B 2 129 ? 161.627 147.579 107.260 1.00 53.26  ? 129 GLU B OE1   1 
ATOM   3215 O  OE2   . GLU B 2 129 ? 162.659 146.256 108.674 1.00 54.13  ? 129 GLU B OE2   1 
ATOM   3216 N  N     . PHE B 2 130 ? 159.679 146.736 110.461 1.00 45.13  ? 130 PHE B N     1 
ATOM   3217 C  CA    . PHE B 2 130 ? 158.693 146.036 109.647 1.00 41.86  ? 130 PHE B CA    1 
ATOM   3218 C  C     . PHE B 2 130 ? 157.274 146.445 110.016 1.00 39.29  ? 130 PHE B C     1 
ATOM   3219 O  O     . PHE B 2 130 ? 156.400 146.508 109.145 1.00 45.73  ? 130 PHE B O     1 
ATOM   3220 C  CB    . PHE B 2 130 ? 158.873 144.525 109.801 1.00 38.97  ? 130 PHE B CB    1 
ATOM   3221 C  CG    . PHE B 2 130 ? 158.150 143.715 108.762 1.00 40.98  ? 130 PHE B CG    1 
ATOM   3222 C  CD1   . PHE B 2 130 ? 158.740 143.455 107.535 1.00 43.04  ? 130 PHE B CD1   1 
ATOM   3223 C  CD2   . PHE B 2 130 ? 156.886 143.203 109.016 1.00 37.47  ? 130 PHE B CD2   1 
ATOM   3224 C  CE1   . PHE B 2 130 ? 158.080 142.705 106.579 1.00 43.24  ? 130 PHE B CE1   1 
ATOM   3225 C  CE2   . PHE B 2 130 ? 156.220 142.455 108.064 1.00 42.28  ? 130 PHE B CE2   1 
ATOM   3226 C  CZ    . PHE B 2 130 ? 156.819 142.206 106.844 1.00 40.79  ? 130 PHE B CZ    1 
ATOM   3227 N  N     . SER B 2 131 ? 157.022 146.716 111.300 1.00 42.12  ? 131 SER B N     1 
ATOM   3228 C  CA    . SER B 2 131 ? 155.672 147.055 111.741 1.00 35.63  ? 131 SER B CA    1 
ATOM   3229 C  C     . SER B 2 131 ? 155.211 148.421 111.244 1.00 43.25  ? 131 SER B C     1 
ATOM   3230 O  O     . SER B 2 131 ? 154.001 148.621 111.092 1.00 47.86  ? 131 SER B O     1 
ATOM   3231 C  CB    . SER B 2 131 ? 155.594 146.999 113.266 1.00 33.39  ? 131 SER B CB    1 
ATOM   3232 O  OG    . SER B 2 131 ? 156.117 148.179 113.847 1.00 47.53  ? 131 SER B OG    1 
ATOM   3233 N  N     . GLU B 2 132 ? 156.151 149.344 110.993 1.00 48.41  ? 132 GLU B N     1 
ATOM   3234 C  CA    . GLU B 2 132 ? 155.897 150.703 110.489 1.00 47.13  ? 132 GLU B CA    1 
ATOM   3235 C  C     . GLU B 2 132 ? 154.941 151.489 111.383 1.00 41.64  ? 132 GLU B C     1 
ATOM   3236 O  O     . GLU B 2 132 ? 154.122 152.270 110.896 1.00 49.24  ? 132 GLU B O     1 
ATOM   3237 C  CB    . GLU B 2 132 ? 155.374 150.689 109.047 1.00 45.43  ? 132 GLU B CB    1 
ATOM   3238 C  CG    . GLU B 2 132 ? 156.193 149.850 108.089 1.00 48.60  ? 132 GLU B CG    1 
ATOM   3239 C  CD    . GLU B 2 132 ? 155.556 149.756 106.718 1.00 54.47  ? 132 GLU B CD    1 
ATOM   3240 O  OE1   . GLU B 2 132 ? 154.311 149.692 106.644 1.00 57.41  ? 132 GLU B OE1   1 
ATOM   3241 O  OE2   . GLU B 2 132 ? 156.298 149.744 105.715 1.00 55.33  ? 132 GLU B OE2   1 
ATOM   3242 N  N     . LEU B 2 133 ? 155.036 151.289 112.697 1.00 37.78  ? 133 LEU B N     1 
ATOM   3243 C  CA    . LEU B 2 133 ? 154.127 151.953 113.620 1.00 33.76  ? 133 LEU B CA    1 
ATOM   3244 C  C     . LEU B 2 133 ? 154.584 153.359 113.980 1.00 43.71  ? 133 LEU B C     1 
ATOM   3245 O  O     . LEU B 2 133 ? 153.755 154.176 114.394 1.00 45.34  ? 133 LEU B O     1 
ATOM   3246 C  CB    . LEU B 2 133 ? 153.961 151.112 114.886 1.00 37.60  ? 133 LEU B CB    1 
ATOM   3247 C  CG    . LEU B 2 133 ? 153.213 149.797 114.656 1.00 41.62  ? 133 LEU B CG    1 
ATOM   3248 C  CD1   . LEU B 2 133 ? 153.192 148.943 115.907 1.00 34.97  ? 133 LEU B CD1   1 
ATOM   3249 C  CD2   . LEU B 2 133 ? 151.803 150.068 114.168 1.00 39.59  ? 133 LEU B CD2   1 
ATOM   3250 N  N     . GLY B 2 134 ? 155.870 153.654 113.830 1.00 41.54  ? 134 GLY B N     1 
ATOM   3251 C  CA    . GLY B 2 134 ? 156.343 155.011 114.049 1.00 36.43  ? 134 GLY B CA    1 
ATOM   3252 C  C     . GLY B 2 134 ? 156.413 155.348 115.523 1.00 41.65  ? 134 GLY B C     1 
ATOM   3253 O  O     . GLY B 2 134 ? 157.084 154.673 116.311 1.00 43.80  ? 134 GLY B O     1 
ATOM   3254 N  N     . GLU B 2 135 ? 155.706 156.412 115.904 1.00 49.16  ? 135 GLU B N     1 
ATOM   3255 C  CA    . GLU B 2 135 ? 155.751 156.904 117.274 1.00 41.80  ? 135 GLU B CA    1 
ATOM   3256 C  C     . GLU B 2 135 ? 154.878 156.071 118.206 1.00 41.81  ? 135 GLU B C     1 
ATOM   3257 O  O     . GLU B 2 135 ? 155.064 156.117 119.427 1.00 45.85  ? 135 GLU B O     1 
ATOM   3258 C  CB    . GLU B 2 135 ? 155.327 158.376 117.285 1.00 45.61  ? 135 GLU B CB    1 
ATOM   3259 C  CG    . GLU B 2 135 ? 155.661 159.146 118.547 1.00 46.13  ? 135 GLU B CG    1 
ATOM   3260 C  CD    . GLU B 2 135 ? 156.191 160.529 118.245 1.00 54.30  ? 135 GLU B CD    1 
ATOM   3261 O  OE1   . GLU B 2 135 ? 156.321 160.874 117.052 1.00 52.64  ? 135 GLU B OE1   1 
ATOM   3262 O  OE2   . GLU B 2 135 ? 156.511 161.260 119.199 1.00 55.07  ? 135 GLU B OE2   1 
ATOM   3263 N  N     . PHE B 2 136 ? 153.962 155.273 117.658 1.00 30.64  ? 136 PHE B N     1 
ATOM   3264 C  CA    . PHE B 2 136 ? 153.032 154.500 118.469 1.00 28.31  ? 136 PHE B CA    1 
ATOM   3265 C  C     . PHE B 2 136 ? 153.635 153.220 119.033 1.00 29.00  ? 136 PHE B C     1 
ATOM   3266 O  O     . PHE B 2 136 ? 152.946 152.513 119.773 1.00 30.76  ? 136 PHE B O     1 
ATOM   3267 C  CB    . PHE B 2 136 ? 151.779 154.167 117.656 1.00 34.27  ? 136 PHE B CB    1 
ATOM   3268 C  CG    . PHE B 2 136 ? 150.680 155.181 117.799 1.00 37.00  ? 136 PHE B CG    1 
ATOM   3269 C  CD1   . PHE B 2 136 ? 149.748 155.071 118.819 1.00 30.71  ? 136 PHE B CD1   1 
ATOM   3270 C  CD2   . PHE B 2 136 ? 150.587 156.252 116.924 1.00 33.32  ? 136 PHE B CD2   1 
ATOM   3271 C  CE1   . PHE B 2 136 ? 148.737 156.006 118.960 1.00 26.46  ? 136 PHE B CE1   1 
ATOM   3272 C  CE2   . PHE B 2 136 ? 149.580 157.192 117.059 1.00 25.67  ? 136 PHE B CE2   1 
ATOM   3273 C  CZ    . PHE B 2 136 ? 148.654 157.067 118.079 1.00 28.67  ? 136 PHE B CZ    1 
ATOM   3274 N  N     . ILE B 2 137 ? 154.896 152.905 118.719 1.00 29.66  ? 137 ILE B N     1 
ATOM   3275 C  CA    . ILE B 2 137 ? 155.538 151.726 119.292 1.00 27.37  ? 137 ILE B CA    1 
ATOM   3276 C  C     . ILE B 2 137 ? 155.845 151.917 120.779 1.00 28.28  ? 137 ILE B C     1 
ATOM   3277 O  O     . ILE B 2 137 ? 156.023 150.933 121.505 1.00 33.18  ? 137 ILE B O     1 
ATOM   3278 C  CB    . ILE B 2 137 ? 156.802 151.361 118.469 1.00 32.03  ? 137 ILE B CB    1 
ATOM   3279 C  CG1   . ILE B 2 137 ? 157.198 149.892 118.663 1.00 32.50  ? 137 ILE B CG1   1 
ATOM   3280 C  CG2   . ILE B 2 137 ? 157.969 152.277 118.787 1.00 25.51  ? 137 ILE B CG2   1 
ATOM   3281 C  CD1   . ILE B 2 137 ? 156.137 148.905 118.247 1.00 30.62  ? 137 ILE B CD1   1 
ATOM   3282 N  N     . TYR B 2 138 ? 155.878 153.160 121.261 1.00 35.88  ? 138 TYR B N     1 
ATOM   3283 C  CA    . TYR B 2 138 ? 156.018 153.442 122.683 1.00 29.88  ? 138 TYR B CA    1 
ATOM   3284 C  C     . TYR B 2 138 ? 154.677 153.673 123.366 1.00 33.73  ? 138 TYR B C     1 
ATOM   3285 O  O     . TYR B 2 138 ? 154.647 153.994 124.557 1.00 43.20  ? 138 TYR B O     1 
ATOM   3286 C  CB    . TYR B 2 138 ? 156.927 154.654 122.914 1.00 35.82  ? 138 TYR B CB    1 
ATOM   3287 C  CG    . TYR B 2 138 ? 158.214 154.651 122.118 1.00 37.44  ? 138 TYR B CG    1 
ATOM   3288 C  CD1   . TYR B 2 138 ? 158.294 155.278 120.878 1.00 33.52  ? 138 TYR B CD1   1 
ATOM   3289 C  CD2   . TYR B 2 138 ? 159.341 153.994 122.596 1.00 36.71  ? 138 TYR B CD2   1 
ATOM   3290 C  CE1   . TYR B 2 138 ? 159.470 155.274 120.152 1.00 39.63  ? 138 TYR B CE1   1 
ATOM   3291 C  CE2   . TYR B 2 138 ? 160.518 153.979 121.875 1.00 35.13  ? 138 TYR B CE2   1 
ATOM   3292 C  CZ    . TYR B 2 138 ? 160.576 154.618 120.654 1.00 42.65  ? 138 TYR B CZ    1 
ATOM   3293 O  OH    . TYR B 2 138 ? 161.746 154.605 119.933 1.00 45.74  ? 138 TYR B OH    1 
ATOM   3294 N  N     . GLN B 2 139 ? 153.573 153.514 122.644 1.00 32.16  ? 139 GLN B N     1 
ATOM   3295 C  CA    . GLN B 2 139 ? 152.222 153.695 123.145 1.00 21.74  ? 139 GLN B CA    1 
ATOM   3296 C  C     . GLN B 2 139 ? 151.583 152.343 123.455 1.00 25.43  ? 139 GLN B C     1 
ATOM   3297 O  O     . GLN B 2 139 ? 151.966 151.331 122.861 1.00 34.84  ? 139 GLN B O     1 
ATOM   3298 C  CB    . GLN B 2 139 ? 151.365 154.452 122.122 1.00 25.77  ? 139 GLN B CB    1 
ATOM   3299 C  CG    . GLN B 2 139 ? 151.640 155.943 122.085 1.00 29.87  ? 139 GLN B CG    1 
ATOM   3300 C  CD    . GLN B 2 139 ? 151.528 156.585 123.454 1.00 32.69  ? 139 GLN B CD    1 
ATOM   3301 O  OE1   . GLN B 2 139 ? 150.454 156.612 124.051 1.00 36.23  ? 139 GLN B OE1   1 
ATOM   3302 N  NE2   . GLN B 2 139 ? 152.640 157.101 123.961 1.00 29.24  ? 139 GLN B NE2   1 
ATOM   3303 N  N     . PRO B 2 140 ? 150.635 152.287 124.398 1.00 29.85  ? 140 PRO B N     1 
ATOM   3304 C  CA    . PRO B 2 140 ? 149.965 151.014 124.703 1.00 27.40  ? 140 PRO B CA    1 
ATOM   3305 C  C     . PRO B 2 140 ? 149.144 150.486 123.532 1.00 31.86  ? 140 PRO B C     1 
ATOM   3306 O  O     . PRO B 2 140 ? 148.647 151.243 122.699 1.00 31.67  ? 140 PRO B O     1 
ATOM   3307 C  CB    . PRO B 2 140 ? 149.072 151.361 125.899 1.00 23.23  ? 140 PRO B CB    1 
ATOM   3308 C  CG    . PRO B 2 140 ? 149.722 152.526 126.528 1.00 26.74  ? 140 PRO B CG    1 
ATOM   3309 C  CD    . PRO B 2 140 ? 150.334 153.314 125.413 1.00 30.29  ? 140 PRO B CD    1 
ATOM   3310 N  N     . VAL B 2 141 ? 149.016 149.158 123.488 1.00 30.07  ? 141 VAL B N     1 
ATOM   3311 C  CA    . VAL B 2 141 ? 148.417 148.465 122.350 1.00 31.25  ? 141 VAL B CA    1 
ATOM   3312 C  C     . VAL B 2 141 ? 146.900 148.656 122.328 1.00 29.65  ? 141 VAL B C     1 
ATOM   3313 O  O     . VAL B 2 141 ? 146.278 148.647 121.257 1.00 32.39  ? 141 VAL B O     1 
ATOM   3314 C  CB    . VAL B 2 141 ? 148.881 146.986 122.402 1.00 30.44  ? 141 VAL B CB    1 
ATOM   3315 C  CG1   . VAL B 2 141 ? 147.933 146.003 121.726 1.00 32.29  ? 141 VAL B CG1   1 
ATOM   3316 C  CG2   . VAL B 2 141 ? 150.267 146.872 121.789 1.00 19.81  ? 141 VAL B CG2   1 
ATOM   3317 N  N     . LYS B 2 142 ? 146.294 148.941 123.486 1.00 34.12  ? 142 LYS B N     1 
ATOM   3318 C  CA    . LYS B 2 142 ? 144.861 149.229 123.531 1.00 27.47  ? 142 LYS B CA    1 
ATOM   3319 C  C     . LYS B 2 142 ? 144.515 150.559 122.865 1.00 36.49  ? 142 LYS B C     1 
ATOM   3320 O  O     . LYS B 2 142 ? 143.350 150.797 122.530 1.00 45.51  ? 142 LYS B O     1 
ATOM   3321 C  CB    . LYS B 2 142 ? 144.369 149.228 124.977 1.00 30.01  ? 142 LYS B CB    1 
ATOM   3322 C  CG    . LYS B 2 142 ? 145.070 150.238 125.862 1.00 33.18  ? 142 LYS B CG    1 
ATOM   3323 C  CD    . LYS B 2 142 ? 144.229 150.599 127.068 1.00 35.14  ? 142 LYS B CD    1 
ATOM   3324 C  CE    . LYS B 2 142 ? 145.103 151.058 128.218 1.00 40.18  ? 142 LYS B CE    1 
ATOM   3325 N  NZ    . LYS B 2 142 ? 145.173 152.539 128.324 1.00 41.41  ? 142 LYS B NZ    1 
ATOM   3326 N  N     . LYS B 2 143 ? 145.502 151.430 122.661 1.00 30.87  ? 143 LYS B N     1 
ATOM   3327 C  CA    . LYS B 2 143 ? 145.308 152.677 121.933 1.00 20.68  ? 143 LYS B CA    1 
ATOM   3328 C  C     . LYS B 2 143 ? 145.523 152.527 120.433 1.00 24.48  ? 143 LYS B C     1 
ATOM   3329 O  O     . LYS B 2 143 ? 145.452 153.526 119.713 1.00 30.68  ? 143 LYS B O     1 
ATOM   3330 C  CB    . LYS B 2 143 ? 146.249 153.753 122.479 1.00 31.80  ? 143 LYS B CB    1 
ATOM   3331 C  CG    . LYS B 2 143 ? 145.952 154.157 123.906 1.00 31.25  ? 143 LYS B CG    1 
ATOM   3332 C  CD    . LYS B 2 143 ? 147.042 155.050 124.472 1.00 30.08  ? 143 LYS B CD    1 
ATOM   3333 C  CE    . LYS B 2 143 ? 146.719 155.490 125.893 1.00 36.41  ? 143 LYS B CE    1 
ATOM   3334 N  NZ    . LYS B 2 143 ? 145.316 155.184 126.290 1.00 37.64  ? 143 LYS B NZ    1 
ATOM   3335 N  N     . TYR B 2 144 ? 145.790 151.318 119.950 1.00 34.77  ? 144 TYR B N     1 
ATOM   3336 C  CA    . TYR B 2 144 ? 146.056 151.113 118.534 1.00 24.36  ? 144 TYR B CA    1 
ATOM   3337 C  C     . TYR B 2 144 ? 144.749 151.003 117.758 1.00 31.22  ? 144 TYR B C     1 
ATOM   3338 O  O     . TYR B 2 144 ? 143.672 150.786 118.320 1.00 36.57  ? 144 TYR B O     1 
ATOM   3339 C  CB    . TYR B 2 144 ? 146.866 149.834 118.294 1.00 18.56  ? 144 TYR B CB    1 
ATOM   3340 C  CG    . TYR B 2 144 ? 148.347 149.867 118.627 1.00 26.67  ? 144 TYR B CG    1 
ATOM   3341 C  CD1   . TYR B 2 144 ? 148.894 150.861 119.433 1.00 24.24  ? 144 TYR B CD1   1 
ATOM   3342 C  CD2   . TYR B 2 144 ? 149.198 148.884 118.136 1.00 24.20  ? 144 TYR B CD2   1 
ATOM   3343 C  CE1   . TYR B 2 144 ? 150.236 150.873 119.737 1.00 17.77  ? 144 TYR B CE1   1 
ATOM   3344 C  CE2   . TYR B 2 144 ? 150.545 148.890 118.432 1.00 18.99  ? 144 TYR B CE2   1 
ATOM   3345 C  CZ    . TYR B 2 144 ? 151.059 149.888 119.231 1.00 28.86  ? 144 TYR B CZ    1 
ATOM   3346 O  OH    . TYR B 2 144 ? 152.400 149.898 119.528 1.00 33.37  ? 144 TYR B OH    1 
ATOM   3347 N  N     . SER B 2 145 ? 144.857 151.153 116.444 1.00 28.39  ? 145 SER B N     1 
ATOM   3348 C  CA    . SER B 2 145 ? 143.801 150.712 115.554 1.00 24.68  ? 145 SER B CA    1 
ATOM   3349 C  C     . SER B 2 145 ? 143.921 149.204 115.334 1.00 27.78  ? 145 SER B C     1 
ATOM   3350 O  O     . SER B 2 145 ? 144.904 148.573 115.730 1.00 35.68  ? 145 SER B O     1 
ATOM   3351 C  CB    . SER B 2 145 ? 143.864 151.477 114.234 1.00 24.97  ? 145 SER B CB    1 
ATOM   3352 O  OG    . SER B 2 145 ? 144.584 150.761 113.250 1.00 35.16  ? 145 SER B OG    1 
ATOM   3353 N  N     . SER B 2 146 ? 142.890 148.620 114.714 1.00 29.70  ? 146 SER B N     1 
ATOM   3354 C  CA    . SER B 2 146 ? 142.881 147.177 114.476 1.00 18.46  ? 146 SER B CA    1 
ATOM   3355 C  C     . SER B 2 146 ? 143.953 146.767 113.473 1.00 29.15  ? 146 SER B C     1 
ATOM   3356 O  O     . SER B 2 146 ? 144.603 145.726 113.640 1.00 38.36  ? 146 SER B O     1 
ATOM   3357 C  CB    . SER B 2 146 ? 141.501 146.732 113.996 1.00 27.54  ? 146 SER B CB    1 
ATOM   3358 O  OG    . SER B 2 146 ? 140.474 147.398 114.707 1.00 40.72  ? 146 SER B OG    1 
ATOM   3359 N  N     . GLY B 2 147 ? 144.152 147.579 112.433 1.00 23.70  ? 147 GLY B N     1 
ATOM   3360 C  CA    . GLY B 2 147 ? 145.205 147.299 111.472 1.00 15.16  ? 147 GLY B CA    1 
ATOM   3361 C  C     . GLY B 2 147 ? 146.594 147.431 112.063 1.00 22.28  ? 147 GLY B C     1 
ATOM   3362 O  O     . GLY B 2 147 ? 147.492 146.661 111.724 1.00 32.71  ? 147 GLY B O     1 
ATOM   3363 N  N     . MET B 2 148 ? 146.813 148.401 112.999 1.00 27.11  ? 148 MET B N     1 
ATOM   3364 C  CA    . MET B 2 148 ? 148.106 148.573 113.659 1.00 24.46  ? 148 MET B CA    1 
ATOM   3365 C  C     . MET B 2 148 ? 148.429 147.397 114.574 1.00 28.67  ? 148 MET B C     1 
ATOM   3366 O  O     . MET B 2 148 ? 149.570 146.912 114.602 1.00 33.14  ? 148 MET B O     1 
ATOM   3367 C  CB    . MET B 2 148 ? 148.110 149.883 114.447 1.00 21.77  ? 148 MET B CB    1 
ATOM   3368 C  CG    . MET B 2 148 ? 148.108 151.128 113.578 1.00 29.66  ? 148 MET B CG    1 
ATOM   3369 S  SD    . MET B 2 148 ? 147.606 152.612 114.466 1.00 35.90  ? 148 MET B SD    1 
ATOM   3370 C  CE    . MET B 2 148 ? 148.991 152.837 115.574 1.00 25.11  ? 148 MET B CE    1 
ATOM   3371 N  N     . ARG B 2 149 ? 147.426 146.921 115.320 1.00 26.60  ? 149 ARG B N     1 
ATOM   3372 C  CA    . ARG B 2 149 ? 147.586 145.742 116.166 1.00 22.90  ? 149 ARG B CA    1 
ATOM   3373 C  C     . ARG B 2 149 ? 147.882 144.501 115.333 1.00 27.38  ? 149 ARG B C     1 
ATOM   3374 O  O     . ARG B 2 149 ? 148.730 143.676 115.703 1.00 40.55  ? 149 ARG B O     1 
ATOM   3375 C  CB    . ARG B 2 149 ? 146.320 145.534 116.996 1.00 19.00  ? 149 ARG B CB    1 
ATOM   3376 C  CG    . ARG B 2 149 ? 146.566 145.165 118.436 1.00 33.34  ? 149 ARG B CG    1 
ATOM   3377 C  CD    . ARG B 2 149 ? 145.263 144.978 119.196 1.00 39.49  ? 149 ARG B CD    1 
ATOM   3378 N  NE    . ARG B 2 149 ? 144.170 145.764 118.634 1.00 40.79  ? 149 ARG B NE    1 
ATOM   3379 C  CZ    . ARG B 2 149 ? 143.793 146.956 119.079 1.00 38.66  ? 149 ARG B CZ    1 
ATOM   3380 N  NH1   . ARG B 2 149 ? 144.414 147.546 120.087 1.00 35.75  ? 149 ARG B NH1   1 
ATOM   3381 N  NH2   . ARG B 2 149 ? 142.769 147.572 118.497 1.00 38.44  ? 149 ARG B NH2   1 
ATOM   3382 N  N     . ALA B 2 150 ? 147.195 144.365 114.195 1.00 26.58  ? 150 ALA B N     1 
ATOM   3383 C  CA    . ALA B 2 150 ? 147.434 143.244 113.294 1.00 20.67  ? 150 ALA B CA    1 
ATOM   3384 C  C     . ALA B 2 150 ? 148.838 143.290 112.696 1.00 24.04  ? 150 ALA B C     1 
ATOM   3385 O  O     . ALA B 2 150 ? 149.502 142.254 112.577 1.00 31.14  ? 150 ALA B O     1 
ATOM   3386 C  CB    . ALA B 2 150 ? 146.376 143.240 112.194 1.00 23.20  ? 150 ALA B CB    1 
ATOM   3387 N  N     . LYS B 2 151 ? 149.305 144.489 112.328 1.00 29.33  ? 151 LYS B N     1 
ATOM   3388 C  CA    . LYS B 2 151 ? 150.652 144.654 111.786 1.00 25.04  ? 151 LYS B CA    1 
ATOM   3389 C  C     . LYS B 2 151 ? 151.719 144.310 112.816 1.00 28.27  ? 151 LYS B C     1 
ATOM   3390 O  O     . LYS B 2 151 ? 152.704 143.634 112.492 1.00 31.92  ? 151 LYS B O     1 
ATOM   3391 C  CB    . LYS B 2 151 ? 150.845 146.087 111.288 1.00 28.34  ? 151 LYS B CB    1 
ATOM   3392 C  CG    . LYS B 2 151 ? 150.206 146.389 109.945 1.00 32.21  ? 151 LYS B CG    1 
ATOM   3393 C  CD    . LYS B 2 151 ? 150.606 147.764 109.431 1.00 31.86  ? 151 LYS B CD    1 
ATOM   3394 C  CE    . LYS B 2 151 ? 150.317 148.852 110.448 1.00 31.34  ? 151 LYS B CE    1 
ATOM   3395 N  NZ    . LYS B 2 151 ? 150.915 150.156 110.053 1.00 39.20  ? 151 LYS B NZ    1 
ATOM   3396 N  N     . LEU B 2 152 ? 151.536 144.759 114.065 1.00 31.88  ? 152 LEU B N     1 
ATOM   3397 C  CA    . LEU B 2 152 ? 152.498 144.444 115.119 1.00 25.36  ? 152 LEU B CA    1 
ATOM   3398 C  C     . LEU B 2 152 ? 152.521 142.950 115.432 1.00 28.75  ? 152 LEU B C     1 
ATOM   3399 O  O     . LEU B 2 152 ? 153.600 142.355 115.574 1.00 36.34  ? 152 LEU B O     1 
ATOM   3400 C  CB    . LEU B 2 152 ? 152.187 145.251 116.380 1.00 25.26  ? 152 LEU B CB    1 
ATOM   3401 C  CG    . LEU B 2 152 ? 153.128 145.010 117.565 1.00 27.23  ? 152 LEU B CG    1 
ATOM   3402 C  CD1   . LEU B 2 152 ? 154.546 145.428 117.217 1.00 21.69  ? 152 LEU B CD1   1 
ATOM   3403 C  CD2   . LEU B 2 152 ? 152.644 145.733 118.807 1.00 30.63  ? 152 LEU B CD2   1 
ATOM   3404 N  N     . GLY B 2 153 ? 151.340 142.325 115.517 1.00 28.07  ? 153 GLY B N     1 
ATOM   3405 C  CA    . GLY B 2 153 ? 151.278 140.895 115.776 1.00 24.40  ? 153 GLY B CA    1 
ATOM   3406 C  C     . GLY B 2 153 ? 151.883 140.062 114.663 1.00 27.64  ? 153 GLY B C     1 
ATOM   3407 O  O     . GLY B 2 153 ? 152.585 139.081 114.923 1.00 37.07  ? 153 GLY B O     1 
ATOM   3408 N  N     . PHE B 2 154 ? 151.651 140.461 113.408 1.00 31.63  ? 154 PHE B N     1 
ATOM   3409 C  CA    . PHE B 2 154 ? 152.266 139.773 112.279 1.00 23.67  ? 154 PHE B CA    1 
ATOM   3410 C  C     . PHE B 2 154 ? 153.778 139.964 112.261 1.00 30.59  ? 154 PHE B C     1 
ATOM   3411 O  O     . PHE B 2 154 ? 154.516 139.031 111.924 1.00 38.75  ? 154 PHE B O     1 
ATOM   3412 C  CB    . PHE B 2 154 ? 151.650 140.260 110.967 1.00 31.63  ? 154 PHE B CB    1 
ATOM   3413 C  CG    . PHE B 2 154 ? 151.930 139.363 109.795 1.00 32.72  ? 154 PHE B CG    1 
ATOM   3414 C  CD1   . PHE B 2 154 ? 151.078 138.313 109.492 1.00 34.23  ? 154 PHE B CD1   1 
ATOM   3415 C  CD2   . PHE B 2 154 ? 153.044 139.569 108.994 1.00 30.72  ? 154 PHE B CD2   1 
ATOM   3416 C  CE1   . PHE B 2 154 ? 151.333 137.484 108.417 1.00 34.44  ? 154 PHE B CE1   1 
ATOM   3417 C  CE2   . PHE B 2 154 ? 153.308 138.741 107.923 1.00 30.90  ? 154 PHE B CE2   1 
ATOM   3418 C  CZ    . PHE B 2 154 ? 152.448 137.701 107.631 1.00 34.33  ? 154 PHE B CZ    1 
ATOM   3419 N  N     . SER B 2 155 ? 154.255 141.165 112.609 1.00 34.69  ? 155 SER B N     1 
ATOM   3420 C  CA    . SER B 2 155 ? 155.691 141.430 112.609 1.00 29.26  ? 155 SER B CA    1 
ATOM   3421 C  C     . SER B 2 155 ? 156.410 140.619 113.679 1.00 38.08  ? 155 SER B C     1 
ATOM   3422 O  O     . SER B 2 155 ? 157.538 140.162 113.462 1.00 37.72  ? 155 SER B O     1 
ATOM   3423 C  CB    . SER B 2 155 ? 155.950 142.923 112.805 1.00 31.20  ? 155 SER B CB    1 
ATOM   3424 O  OG    . SER B 2 155 ? 155.095 143.695 111.982 1.00 40.94  ? 155 SER B OG    1 
ATOM   3425 N  N     . ILE B 2 156 ? 155.780 140.431 114.842 1.00 29.89  ? 156 ILE B N     1 
ATOM   3426 C  CA    . ILE B 2 156 ? 156.374 139.543 115.840 1.00 30.07  ? 156 ILE B CA    1 
ATOM   3427 C  C     . ILE B 2 156 ? 156.287 138.085 115.391 1.00 31.78  ? 156 ILE B C     1 
ATOM   3428 O  O     . ILE B 2 156 ? 157.259 137.330 115.511 1.00 38.79  ? 156 ILE B O     1 
ATOM   3429 C  CB    . ILE B 2 156 ? 155.729 139.748 117.224 1.00 37.85  ? 156 ILE B CB    1 
ATOM   3430 C  CG1   . ILE B 2 156 ? 155.819 141.210 117.651 1.00 28.83  ? 156 ILE B CG1   1 
ATOM   3431 C  CG2   . ILE B 2 156 ? 156.428 138.897 118.268 1.00 31.33  ? 156 ILE B CG2   1 
ATOM   3432 C  CD1   . ILE B 2 156 ? 154.820 141.586 118.719 1.00 19.74  ? 156 ILE B CD1   1 
ATOM   3433 N  N     . ASN B 2 157 ? 155.140 137.674 114.837 1.00 38.11  ? 157 ASN B N     1 
ATOM   3434 C  CA    . ASN B 2 157 ? 154.912 136.266 114.528 1.00 35.68  ? 157 ASN B CA    1 
ATOM   3435 C  C     . ASN B 2 157 ? 155.724 135.771 113.335 1.00 38.76  ? 157 ASN B C     1 
ATOM   3436 O  O     . ASN B 2 157 ? 155.991 134.569 113.236 1.00 48.40  ? 157 ASN B O     1 
ATOM   3437 C  CB    . ASN B 2 157 ? 153.424 136.024 114.271 1.00 36.43  ? 157 ASN B CB    1 
ATOM   3438 C  CG    . ASN B 2 157 ? 152.852 134.935 115.148 1.00 45.43  ? 157 ASN B CG    1 
ATOM   3439 O  OD1   . ASN B 2 157 ? 151.755 135.069 115.691 1.00 45.95  ? 157 ASN B OD1   1 
ATOM   3440 N  ND2   . ASN B 2 157 ? 153.594 133.846 115.296 1.00 48.68  ? 157 ASN B ND2   1 
ATOM   3441 N  N     . ILE B 2 158 ? 156.130 136.667 112.431 1.00 38.18  ? 158 ILE B N     1 
ATOM   3442 C  CA    . ILE B 2 158 ? 156.807 136.243 111.206 1.00 40.22  ? 158 ILE B CA    1 
ATOM   3443 C  C     . ILE B 2 158 ? 158.277 135.912 111.417 1.00 40.83  ? 158 ILE B C     1 
ATOM   3444 O  O     . ILE B 2 158 ? 158.921 135.385 110.499 1.00 45.30  ? 158 ILE B O     1 
ATOM   3445 C  CB    . ILE B 2 158 ? 156.594 137.336 110.137 1.00 40.65  ? 158 ILE B CB    1 
ATOM   3446 C  CG1   . ILE B 2 158 ? 156.456 136.713 108.746 1.00 41.81  ? 158 ILE B CG1   1 
ATOM   3447 C  CG2   . ILE B 2 158 ? 157.691 138.402 110.184 1.00 39.55  ? 158 ILE B CG2   1 
ATOM   3448 C  CD1   . ILE B 2 158 ? 155.339 135.705 108.641 1.00 39.85  ? 158 ILE B CD1   1 
ATOM   3449 N  N     . THR B 2 159 ? 158.821 136.156 112.608 1.00 40.22  ? 159 THR B N     1 
ATOM   3450 C  CA    . THR B 2 159 ? 160.245 135.975 112.868 1.00 40.61  ? 159 THR B CA    1 
ATOM   3451 C  C     . THR B 2 159 ? 160.612 134.559 113.303 1.00 42.40  ? 159 THR B C     1 
ATOM   3452 O  O     . THR B 2 159 ? 161.786 134.311 113.597 1.00 43.74  ? 159 THR B O     1 
ATOM   3453 C  CB    . THR B 2 159 ? 160.714 136.971 113.932 1.00 42.61  ? 159 THR B CB    1 
ATOM   3454 O  OG1   . THR B 2 159 ? 159.875 136.872 115.090 1.00 44.41  ? 159 THR B OG1   1 
ATOM   3455 C  CG2   . THR B 2 159 ? 160.650 138.387 113.390 1.00 41.78  ? 159 THR B CG2   1 
ATOM   3456 N  N     . VAL B 2 160 ? 159.655 133.629 113.352 1.00 44.74  ? 160 VAL B N     1 
ATOM   3457 C  CA    . VAL B 2 160 ? 159.975 132.258 113.742 1.00 43.89  ? 160 VAL B CA    1 
ATOM   3458 C  C     . VAL B 2 160 ? 160.687 131.539 112.598 1.00 49.81  ? 160 VAL B C     1 
ATOM   3459 O  O     . VAL B 2 160 ? 160.603 131.922 111.427 1.00 53.10  ? 160 VAL B O     1 
ATOM   3460 C  CB    . VAL B 2 160 ? 158.708 131.501 114.168 1.00 46.87  ? 160 VAL B CB    1 
ATOM   3461 C  CG1   . VAL B 2 160 ? 158.142 132.093 115.447 1.00 48.91  ? 160 VAL B CG1   1 
ATOM   3462 C  CG2   . VAL B 2 160 ? 157.670 131.529 113.054 1.00 47.68  ? 160 VAL B CG2   1 
ATOM   3463 N  N     . ASN B 2 161 ? 161.420 130.483 112.953 1.00 53.98  ? 161 ASN B N     1 
ATOM   3464 C  CA    . ASN B 2 161 ? 162.129 129.649 111.978 1.00 48.22  ? 161 ASN B CA    1 
ATOM   3465 C  C     . ASN B 2 161 ? 161.883 128.177 112.289 1.00 49.88  ? 161 ASN B C     1 
ATOM   3466 O  O     . ASN B 2 161 ? 162.753 127.485 112.828 1.00 52.40  ? 161 ASN B O     1 
ATOM   3467 C  CB    . ASN B 2 161 ? 163.624 129.973 111.978 1.00 48.76  ? 161 ASN B CB    1 
ATOM   3468 C  CG    . ASN B 2 161 ? 164.343 129.404 110.774 1.00 51.97  ? 161 ASN B CG    1 
ATOM   3469 O  OD1   . ASN B 2 161 ? 163.807 129.391 109.666 1.00 57.45  ? 161 ASN B OD1   1 
ATOM   3470 N  ND2   . ASN B 2 161 ? 165.566 128.935 110.983 1.00 53.11  ? 161 ASN B ND2   1 
ATOM   3471 N  N     . PRO B 2 162 ? 160.702 127.662 111.956 1.00 52.44  ? 162 PRO B N     1 
ATOM   3472 C  CA    . PRO B 2 162 ? 160.377 126.272 112.274 1.00 47.94  ? 162 PRO B CA    1 
ATOM   3473 C  C     . PRO B 2 162 ? 160.776 125.313 111.156 1.00 46.52  ? 162 PRO B C     1 
ATOM   3474 O  O     . PRO B 2 162 ? 161.387 125.692 110.156 1.00 52.05  ? 162 PRO B O     1 
ATOM   3475 C  CB    . PRO B 2 162 ? 158.854 126.313 112.427 1.00 44.45  ? 162 PRO B CB    1 
ATOM   3476 C  CG    . PRO B 2 162 ? 158.427 127.372 111.441 1.00 45.09  ? 162 PRO B CG    1 
ATOM   3477 C  CD    . PRO B 2 162 ? 159.601 128.307 111.217 1.00 43.13  ? 162 PRO B CD    1 
ATOM   3478 N  N     . ASP B 2 163 ? 160.424 124.044 111.360 1.00 42.20  ? 163 ASP B N     1 
ATOM   3479 C  CA    . ASP B 2 163 ? 160.473 123.082 110.266 1.00 45.93  ? 163 ASP B CA    1 
ATOM   3480 C  C     . ASP B 2 163 ? 159.092 122.885 109.656 1.00 42.45  ? 163 ASP B C     1 
ATOM   3481 O  O     . ASP B 2 163 ? 158.965 122.688 108.443 1.00 42.72  ? 163 ASP B O     1 
ATOM   3482 C  CB    . ASP B 2 163 ? 161.035 121.747 110.754 1.00 47.59  ? 163 ASP B CB    1 
ATOM   3483 C  CG    . ASP B 2 163 ? 162.514 121.818 111.068 1.00 53.59  ? 163 ASP B CG    1 
ATOM   3484 O  OD1   . ASP B 2 163 ? 163.310 122.050 110.134 1.00 51.22  ? 163 ASP B OD1   1 
ATOM   3485 O  OD2   . ASP B 2 163 ? 162.882 121.640 112.247 1.00 51.24  ? 163 ASP B OD2   1 
ATOM   3486 N  N     . ILE B 2 164 ? 158.053 122.937 110.485 1.00 37.98  ? 164 ILE B N     1 
ATOM   3487 C  CA    . ILE B 2 164 ? 156.666 122.844 110.050 1.00 38.56  ? 164 ILE B CA    1 
ATOM   3488 C  C     . ILE B 2 164 ? 155.967 124.132 110.460 1.00 33.89  ? 164 ILE B C     1 
ATOM   3489 O  O     . ILE B 2 164 ? 156.059 124.549 111.618 1.00 35.04  ? 164 ILE B O     1 
ATOM   3490 C  CB    . ILE B 2 164 ? 155.961 121.613 110.654 1.00 42.73  ? 164 ILE B CB    1 
ATOM   3491 C  CG1   . ILE B 2 164 ? 156.702 120.330 110.271 1.00 39.48  ? 164 ILE B CG1   1 
ATOM   3492 C  CG2   . ILE B 2 164 ? 154.510 121.541 110.198 1.00 38.15  ? 164 ILE B CG2   1 
ATOM   3493 C  CD1   . ILE B 2 164 ? 156.816 119.334 111.398 1.00 38.19  ? 164 ILE B CD1   1 
ATOM   3494 N  N     . LEU B 2 165 ? 155.285 124.765 109.511 1.00 34.22  ? 165 LEU B N     1 
ATOM   3495 C  CA    . LEU B 2 165 ? 154.585 126.017 109.754 1.00 31.56  ? 165 LEU B CA    1 
ATOM   3496 C  C     . LEU B 2 165 ? 153.087 125.809 109.593 1.00 30.75  ? 165 LEU B C     1 
ATOM   3497 O  O     . LEU B 2 165 ? 152.641 125.126 108.668 1.00 33.11  ? 165 LEU B O     1 
ATOM   3498 C  CB    . LEU B 2 165 ? 155.070 127.111 108.800 1.00 37.04  ? 165 LEU B CB    1 
ATOM   3499 C  CG    . LEU B 2 165 ? 154.595 128.535 109.087 1.00 34.06  ? 165 LEU B CG    1 
ATOM   3500 C  CD1   . LEU B 2 165 ? 155.076 128.999 110.451 1.00 28.89  ? 165 LEU B CD1   1 
ATOM   3501 C  CD2   . LEU B 2 165 ? 155.069 129.480 108.000 1.00 33.48  ? 165 LEU B CD2   1 
ATOM   3502 N  N     . VAL B 2 166 ? 152.313 126.386 110.508 1.00 31.72  ? 166 VAL B N     1 
ATOM   3503 C  CA    . VAL B 2 166 ? 150.856 126.348 110.457 1.00 32.25  ? 166 VAL B CA    1 
ATOM   3504 C  C     . VAL B 2 166 ? 150.356 127.783 110.385 1.00 34.77  ? 166 VAL B C     1 
ATOM   3505 O  O     . VAL B 2 166 ? 150.668 128.595 111.263 1.00 37.06  ? 166 VAL B O     1 
ATOM   3506 C  CB    . VAL B 2 166 ? 150.250 125.621 111.671 1.00 36.38  ? 166 VAL B CB    1 
ATOM   3507 C  CG1   . VAL B 2 166 ? 148.734 125.639 111.598 1.00 36.24  ? 166 VAL B CG1   1 
ATOM   3508 C  CG2   . VAL B 2 166 ? 150.764 124.190 111.751 1.00 28.00  ? 166 VAL B CG2   1 
ATOM   3509 N  N     . ILE B 2 167 ? 149.588 128.095 109.343 1.00 40.58  ? 167 ILE B N     1 
ATOM   3510 C  CA    . ILE B 2 167 ? 149.032 129.425 109.125 1.00 38.61  ? 167 ILE B CA    1 
ATOM   3511 C  C     . ILE B 2 167 ? 147.515 129.312 109.096 1.00 41.63  ? 167 ILE B C     1 
ATOM   3512 O  O     . ILE B 2 167 ? 146.961 128.468 108.384 1.00 44.46  ? 167 ILE B O     1 
ATOM   3513 C  CB    . ILE B 2 167 ? 149.561 130.058 107.819 1.00 39.43  ? 167 ILE B CB    1 
ATOM   3514 C  CG1   . ILE B 2 167 ? 151.090 130.097 107.817 1.00 37.77  ? 167 ILE B CG1   1 
ATOM   3515 C  CG2   . ILE B 2 167 ? 149.000 131.455 107.625 1.00 40.69  ? 167 ILE B CG2   1 
ATOM   3516 C  CD1   . ILE B 2 167 ? 151.688 130.375 106.460 1.00 40.52  ? 167 ILE B CD1   1 
ATOM   3517 N  N     . ASP B 2 168 ? 146.842 130.160 109.875 1.00 58.27  ? 168 ASP B N     1 
ATOM   3518 C  CA    . ASP B 2 168 ? 145.388 130.129 110.007 1.00 53.56  ? 168 ASP B CA    1 
ATOM   3519 C  C     . ASP B 2 168 ? 144.797 131.444 109.512 1.00 56.56  ? 168 ASP B C     1 
ATOM   3520 O  O     . ASP B 2 168 ? 145.031 132.501 110.111 1.00 54.04  ? 168 ASP B O     1 
ATOM   3521 C  CB    . ASP B 2 168 ? 144.984 129.862 111.455 1.00 49.17  ? 168 ASP B CB    1 
ATOM   3522 C  CG    . ASP B 2 168 ? 143.808 128.910 111.566 1.00 60.19  ? 168 ASP B CG    1 
ATOM   3523 O  OD1   . ASP B 2 168 ? 143.892 127.946 112.356 1.00 62.27  ? 168 ASP B OD1   1 
ATOM   3524 O  OD2   . ASP B 2 168 ? 142.795 129.124 110.869 1.00 60.60  ? 168 ASP B OD2   1 
ATOM   3525 N  N     . GLU B 2 169 ? 144.053 131.374 108.405 1.00 60.27  ? 169 GLU B N     1 
ATOM   3526 C  CA    . GLU B 2 169 ? 143.104 132.366 107.895 1.00 60.26  ? 169 GLU B CA    1 
ATOM   3527 C  C     . GLU B 2 169 ? 143.726 133.674 107.418 1.00 63.30  ? 169 GLU B C     1 
ATOM   3528 O  O     . GLU B 2 169 ? 142.974 134.581 107.040 1.00 66.23  ? 169 GLU B O     1 
ATOM   3529 C  CB    . GLU B 2 169 ? 142.011 132.701 108.921 1.00 63.41  ? 169 GLU B CB    1 
ATOM   3530 C  CG    . GLU B 2 169 ? 141.119 131.524 109.288 1.00 60.45  ? 169 GLU B CG    1 
ATOM   3531 C  CD    . GLU B 2 169 ? 139.964 131.331 108.325 1.00 62.57  ? 169 GLU B CD    1 
ATOM   3532 O  OE1   . GLU B 2 169 ? 139.725 132.225 107.488 1.00 60.88  ? 169 GLU B OE1   1 
ATOM   3533 O  OE2   . GLU B 2 169 ? 139.293 130.280 108.409 1.00 64.12  ? 169 GLU B OE2   1 
ATOM   3534 N  N     . ALA B 2 170 ? 145.052 133.810 107.396 1.00 60.38  ? 170 ALA B N     1 
ATOM   3535 C  CA    . ALA B 2 170 ? 145.648 135.090 107.015 1.00 59.24  ? 170 ALA B CA    1 
ATOM   3536 C  C     . ALA B 2 170 ? 147.044 134.865 106.453 1.00 60.78  ? 170 ALA B C     1 
ATOM   3537 O  O     . ALA B 2 170 ? 147.983 134.623 107.215 1.00 62.40  ? 170 ALA B O     1 
ATOM   3538 C  CB    . ALA B 2 170 ? 145.693 136.036 108.209 1.00 56.58  ? 170 ALA B CB    1 
ATOM   3539 N  N     . LEU B 2 171 ? 147.182 134.959 105.128 1.00 46.25  ? 171 LEU B N     1 
ATOM   3540 C  CA    . LEU B 2 171 ? 148.512 135.112 104.549 1.00 43.27  ? 171 LEU B CA    1 
ATOM   3541 C  C     . LEU B 2 171 ? 149.035 136.525 104.754 1.00 49.96  ? 171 LEU B C     1 
ATOM   3542 O  O     . LEU B 2 171 ? 150.227 136.720 105.019 1.00 53.88  ? 171 LEU B O     1 
ATOM   3543 C  CB    . LEU B 2 171 ? 148.497 134.786 103.054 1.00 44.98  ? 171 LEU B CB    1 
ATOM   3544 C  CG    . LEU B 2 171 ? 148.597 133.329 102.601 1.00 45.46  ? 171 LEU B CG    1 
ATOM   3545 C  CD1   . LEU B 2 171 ? 149.051 133.236 101.152 1.00 45.03  ? 171 LEU B CD1   1 
ATOM   3546 C  CD2   . LEU B 2 171 ? 149.480 132.498 103.517 1.00 44.43  ? 171 LEU B CD2   1 
ATOM   3547 N  N     . SER B 2 172 ? 148.161 137.517 104.631 1.00 52.64  ? 172 SER B N     1 
ATOM   3548 C  CA    . SER B 2 172 ? 148.525 138.919 104.726 1.00 47.56  ? 172 SER B CA    1 
ATOM   3549 C  C     . SER B 2 172 ? 147.713 139.597 105.818 1.00 48.37  ? 172 SER B C     1 
ATOM   3550 O  O     . SER B 2 172 ? 146.782 139.022 106.388 1.00 53.00  ? 172 SER B O     1 
ATOM   3551 C  CB    . SER B 2 172 ? 148.312 139.636 103.389 1.00 46.67  ? 172 SER B CB    1 
ATOM   3552 O  OG    . SER B 2 172 ? 146.956 140.001 103.212 1.00 55.83  ? 172 SER B OG    1 
ATOM   3553 N  N     . VAL B 2 173 ? 148.078 140.849 106.095 1.00 45.49  ? 173 VAL B N     1 
ATOM   3554 C  CA    . VAL B 2 173 ? 147.473 141.623 107.170 1.00 43.71  ? 173 VAL B CA    1 
ATOM   3555 C  C     . VAL B 2 173 ? 147.676 143.100 106.850 1.00 45.70  ? 173 VAL B C     1 
ATOM   3556 O  O     . VAL B 2 173 ? 148.615 143.481 106.146 1.00 48.83  ? 173 VAL B O     1 
ATOM   3557 C  CB    . VAL B 2 173 ? 148.067 141.203 108.545 1.00 42.12  ? 173 VAL B CB    1 
ATOM   3558 C  CG1   . VAL B 2 173 ? 148.998 142.259 109.154 1.00 36.33  ? 173 VAL B CG1   1 
ATOM   3559 C  CG2   . VAL B 2 173 ? 146.964 140.792 109.500 1.00 42.11  ? 173 VAL B CG2   1 
ATOM   3560 N  N     . GLY B 2 174 ? 146.750 143.932 107.324 1.00 44.94  ? 174 GLY B N     1 
ATOM   3561 C  CA    . GLY B 2 174 ? 146.852 145.360 107.113 1.00 40.90  ? 174 GLY B CA    1 
ATOM   3562 C  C     . GLY B 2 174 ? 146.122 145.828 105.867 1.00 44.05  ? 174 GLY B C     1 
ATOM   3563 O  O     . GLY B 2 174 ? 145.234 145.161 105.331 1.00 46.49  ? 174 GLY B O     1 
ATOM   3564 N  N     . ASP B 2 175 ? 146.516 147.011 105.403 1.00 41.98  ? 175 ASP B N     1 
ATOM   3565 C  CA    . ASP B 2 175 ? 145.924 147.601 104.210 1.00 41.02  ? 175 ASP B CA    1 
ATOM   3566 C  C     . ASP B 2 175 ? 146.632 147.076 102.957 1.00 44.28  ? 175 ASP B C     1 
ATOM   3567 O  O     . ASP B 2 175 ? 147.407 146.118 103.007 1.00 48.64  ? 175 ASP B O     1 
ATOM   3568 C  CB    . ASP B 2 175 ? 145.890 149.131 104.345 1.00 40.33  ? 175 ASP B CB    1 
ATOM   3569 C  CG    . ASP B 2 175 ? 147.279 149.790 104.478 1.00 48.00  ? 175 ASP B CG    1 
ATOM   3570 O  OD1   . ASP B 2 175 ? 148.291 149.359 103.889 1.00 54.89  ? 175 ASP B OD1   1 
ATOM   3571 O  OD2   . ASP B 2 175 ? 147.350 150.800 105.207 1.00 46.69  ? 175 ASP B OD2   1 
ATOM   3572 N  N     . GLN B 2 176 ? 146.360 147.707 101.811 1.00 47.74  ? 176 GLN B N     1 
ATOM   3573 C  CA    . GLN B 2 176 ? 146.929 147.249 100.547 1.00 46.36  ? 176 GLN B CA    1 
ATOM   3574 C  C     . GLN B 2 176 ? 148.425 147.522 100.461 1.00 49.94  ? 176 GLN B C     1 
ATOM   3575 O  O     . GLN B 2 176 ? 149.151 146.777 99.794  1.00 51.94  ? 176 GLN B O     1 
ATOM   3576 C  CB    . GLN B 2 176 ? 146.202 147.910 99.377  1.00 48.14  ? 176 GLN B CB    1 
ATOM   3577 C  CG    . GLN B 2 176 ? 144.866 147.272 99.038  1.00 48.76  ? 176 GLN B CG    1 
ATOM   3578 C  CD    . GLN B 2 176 ? 143.699 147.941 99.737  1.00 51.00  ? 176 GLN B CD    1 
ATOM   3579 O  OE1   . GLN B 2 176 ? 143.874 148.654 100.724 1.00 54.54  ? 176 GLN B OE1   1 
ATOM   3580 N  NE2   . GLN B 2 176 ? 142.495 147.709 99.228  1.00 52.73  ? 176 GLN B NE2   1 
ATOM   3581 N  N     . THR B 2 177 ? 148.905 148.568 101.132 1.00 51.95  ? 177 THR B N     1 
ATOM   3582 C  CA    . THR B 2 177 ? 150.321 148.906 101.112 1.00 49.26  ? 177 THR B CA    1 
ATOM   3583 C  C     . THR B 2 177 ? 151.166 147.992 101.990 1.00 50.76  ? 177 THR B C     1 
ATOM   3584 O  O     . THR B 2 177 ? 152.392 147.983 101.844 1.00 57.96  ? 177 THR B O     1 
ATOM   3585 C  CB    . THR B 2 177 ? 150.518 150.358 101.552 1.00 53.29  ? 177 THR B CB    1 
ATOM   3586 O  OG1   . THR B 2 177 ? 150.418 150.446 102.978 1.00 50.30  ? 177 THR B OG1   1 
ATOM   3587 C  CG2   . THR B 2 177 ? 149.459 151.250 100.924 1.00 50.84  ? 177 THR B CG2   1 
ATOM   3588 N  N     . PHE B 2 178 ? 150.547 147.226 102.891 1.00 43.26  ? 178 PHE B N     1 
ATOM   3589 C  CA    . PHE B 2 178 ? 151.265 146.340 103.795 1.00 40.60  ? 178 PHE B CA    1 
ATOM   3590 C  C     . PHE B 2 178 ? 151.193 144.871 103.406 1.00 45.01  ? 178 PHE B C     1 
ATOM   3591 O  O     . PHE B 2 178 ? 152.041 144.092 103.850 1.00 48.36  ? 178 PHE B O     1 
ATOM   3592 C  CB    . PHE B 2 178 ? 150.727 146.497 105.225 1.00 41.11  ? 178 PHE B CB    1 
ATOM   3593 C  CG    . PHE B 2 178 ? 151.678 146.031 106.289 1.00 46.16  ? 178 PHE B CG    1 
ATOM   3594 C  CD1   . PHE B 2 178 ? 152.754 146.816 106.664 1.00 45.71  ? 178 PHE B CD1   1 
ATOM   3595 C  CD2   . PHE B 2 178 ? 151.493 144.808 106.918 1.00 41.56  ? 178 PHE B CD2   1 
ATOM   3596 C  CE1   . PHE B 2 178 ? 153.629 146.393 107.642 1.00 45.54  ? 178 PHE B CE1   1 
ATOM   3597 C  CE2   . PHE B 2 178 ? 152.369 144.374 107.895 1.00 44.40  ? 178 PHE B CE2   1 
ATOM   3598 C  CZ    . PHE B 2 178 ? 153.437 145.171 108.260 1.00 44.22  ? 178 PHE B CZ    1 
ATOM   3599 N  N     . ALA B 2 179 ? 150.218 144.480 102.580 1.00 51.42  ? 179 ALA B N     1 
ATOM   3600 C  CA    . ALA B 2 179 ? 149.962 143.066 102.318 1.00 49.35  ? 179 ALA B CA    1 
ATOM   3601 C  C     . ALA B 2 179 ? 151.049 142.426 101.462 1.00 47.16  ? 179 ALA B C     1 
ATOM   3602 O  O     . ALA B 2 179 ? 151.282 141.214 101.564 1.00 54.04  ? 179 ALA B O     1 
ATOM   3603 C  CB    . ALA B 2 179 ? 148.600 142.907 101.646 1.00 48.60  ? 179 ALA B CB    1 
ATOM   3604 N  N     . GLN B 2 180 ? 151.721 143.217 100.621 1.00 44.01  ? 180 GLN B N     1 
ATOM   3605 C  CA    . GLN B 2 180 ? 152.743 142.666 99.736  1.00 49.39  ? 180 GLN B CA    1 
ATOM   3606 C  C     . GLN B 2 180 ? 153.981 142.228 100.512 1.00 50.09  ? 180 GLN B C     1 
ATOM   3607 O  O     . GLN B 2 180 ? 154.615 141.232 100.154 1.00 53.35  ? 180 GLN B O     1 
ATOM   3608 C  CB    . GLN B 2 180 ? 153.111 143.685 98.658  1.00 51.25  ? 180 GLN B CB    1 
ATOM   3609 C  CG    . GLN B 2 180 ? 153.883 143.093 97.489  1.00 53.67  ? 180 GLN B CG    1 
ATOM   3610 C  CD    . GLN B 2 180 ? 153.171 141.909 96.859  1.00 55.41  ? 180 GLN B CD    1 
ATOM   3611 O  OE1   . GLN B 2 180 ? 152.011 142.008 96.460  1.00 54.76  ? 180 GLN B OE1   1 
ATOM   3612 N  NE2   . GLN B 2 180 ? 153.864 140.780 96.772  1.00 48.83  ? 180 GLN B NE2   1 
ATOM   3613 N  N     . LYS B 2 181 ? 154.332 142.951 101.582 1.00 49.19  ? 181 LYS B N     1 
ATOM   3614 C  CA    . LYS B 2 181 ? 155.448 142.538 102.430 1.00 45.31  ? 181 LYS B CA    1 
ATOM   3615 C  C     . LYS B 2 181 ? 155.146 141.227 103.146 1.00 46.39  ? 181 LYS B C     1 
ATOM   3616 O  O     . LYS B 2 181 ? 156.028 140.368 103.290 1.00 54.13  ? 181 LYS B O     1 
ATOM   3617 C  CB    . LYS B 2 181 ? 155.767 143.632 103.448 1.00 50.89  ? 181 LYS B CB    1 
ATOM   3618 C  CG    . LYS B 2 181 ? 155.811 145.038 102.875 1.00 49.63  ? 181 LYS B CG    1 
ATOM   3619 C  CD    . LYS B 2 181 ? 155.868 146.094 103.977 1.00 54.85  ? 181 LYS B CD    1 
ATOM   3620 C  CE    . LYS B 2 181 ? 156.933 145.779 105.020 1.00 51.11  ? 181 LYS B CE    1 
ATOM   3621 N  NZ    . LYS B 2 181 ? 157.121 146.893 105.987 1.00 46.41  ? 181 LYS B NZ    1 
ATOM   3622 N  N     . CYS B 2 182 ? 153.900 141.060 103.596 1.00 45.80  ? 182 CYS B N     1 
ATOM   3623 C  CA    . CYS B 2 182 ? 153.476 139.807 104.210 1.00 43.62  ? 182 CYS B CA    1 
ATOM   3624 C  C     . CYS B 2 182 ? 153.516 138.656 103.213 1.00 46.09  ? 182 CYS B C     1 
ATOM   3625 O  O     . CYS B 2 182 ? 153.954 137.548 103.554 1.00 50.88  ? 182 CYS B O     1 
ATOM   3626 C  CB    . CYS B 2 182 ? 152.071 139.964 104.785 1.00 44.57  ? 182 CYS B CB    1 
ATOM   3627 S  SG    . CYS B 2 182 ? 151.862 141.369 105.894 1.00 52.84  ? 182 CYS B SG    1 
ATOM   3628 N  N     . LEU B 2 183 ? 153.067 138.903 101.975 1.00 45.58  ? 183 LEU B N     1 
ATOM   3629 C  CA    . LEU B 2 183 ? 153.148 137.883 100.929 1.00 44.98  ? 183 LEU B CA    1 
ATOM   3630 C  C     . LEU B 2 183 ? 154.592 137.515 100.606 1.00 45.46  ? 183 LEU B C     1 
ATOM   3631 O  O     . LEU B 2 183 ? 154.900 136.338 100.398 1.00 54.86  ? 183 LEU B O     1 
ATOM   3632 C  CB    . LEU B 2 183 ? 152.426 138.347 99.663  1.00 51.14  ? 183 LEU B CB    1 
ATOM   3633 C  CG    . LEU B 2 183 ? 150.971 137.940 99.407  1.00 46.93  ? 183 LEU B CG    1 
ATOM   3634 C  CD1   . LEU B 2 183 ? 150.123 137.947 100.659 1.00 48.07  ? 183 LEU B CD1   1 
ATOM   3635 C  CD2   . LEU B 2 183 ? 150.357 138.840 98.345  1.00 51.07  ? 183 LEU B CD2   1 
ATOM   3636 N  N     . ASP B 2 184 ? 155.488 138.508 100.575 1.00 46.94  ? 184 ASP B N     1 
ATOM   3637 C  CA    . ASP B 2 184 ? 156.904 138.231 100.335 1.00 51.04  ? 184 ASP B CA    1 
ATOM   3638 C  C     . ASP B 2 184 ? 157.520 137.415 101.464 1.00 49.67  ? 184 ASP B C     1 
ATOM   3639 O  O     . ASP B 2 184 ? 158.320 136.510 101.211 1.00 50.66  ? 184 ASP B O     1 
ATOM   3640 C  CB    . ASP B 2 184 ? 157.677 139.534 100.135 1.00 53.36  ? 184 ASP B CB    1 
ATOM   3641 C  CG    . ASP B 2 184 ? 157.260 140.273 98.882  1.00 57.76  ? 184 ASP B CG    1 
ATOM   3642 O  OD1   . ASP B 2 184 ? 156.515 139.690 98.067  1.00 56.35  ? 184 ASP B OD1   1 
ATOM   3643 O  OD2   . ASP B 2 184 ? 157.674 141.438 98.711  1.00 60.51  ? 184 ASP B OD2   1 
ATOM   3644 N  N     . LYS B 2 185 ? 157.146 137.703 102.714 1.00 45.30  ? 185 LYS B N     1 
ATOM   3645 C  CA    . LYS B 2 185 ? 157.690 136.945 103.840 1.00 48.24  ? 185 LYS B CA    1 
ATOM   3646 C  C     . LYS B 2 185 ? 157.175 135.505 103.857 1.00 54.46  ? 185 LYS B C     1 
ATOM   3647 O  O     . LYS B 2 185 ? 157.942 134.566 104.118 1.00 54.90  ? 185 LYS B O     1 
ATOM   3648 C  CB    . LYS B 2 185 ? 157.364 137.657 105.150 1.00 49.33  ? 185 LYS B CB    1 
ATOM   3649 C  CG    . LYS B 2 185 ? 158.587 137.975 105.989 1.00 50.81  ? 185 LYS B CG    1 
ATOM   3650 C  CD    . LYS B 2 185 ? 159.167 139.330 105.627 1.00 50.15  ? 185 LYS B CD    1 
ATOM   3651 C  CE    . LYS B 2 185 ? 160.430 139.618 106.420 1.00 53.00  ? 185 LYS B CE    1 
ATOM   3652 N  NZ    . LYS B 2 185 ? 161.029 140.931 106.056 1.00 55.63  ? 185 LYS B NZ    1 
ATOM   3653 N  N     . ILE B 2 186 ? 155.887 135.309 103.560 1.00 51.86  ? 186 ILE B N     1 
ATOM   3654 C  CA    . ILE B 2 186 ? 155.326 133.959 103.515 1.00 46.60  ? 186 ILE B CA    1 
ATOM   3655 C  C     . ILE B 2 186 ? 155.898 133.173 102.333 1.00 46.49  ? 186 ILE B C     1 
ATOM   3656 O  O     . ILE B 2 186 ? 156.190 131.973 102.443 1.00 52.26  ? 186 ILE B O     1 
ATOM   3657 C  CB    . ILE B 2 186 ? 153.786 134.037 103.485 1.00 51.81  ? 186 ILE B CB    1 
ATOM   3658 C  CG1   . ILE B 2 186 ? 153.257 134.612 104.803 1.00 47.23  ? 186 ILE B CG1   1 
ATOM   3659 C  CG2   . ILE B 2 186 ? 153.161 132.681 103.246 1.00 48.89  ? 186 ILE B CG2   1 
ATOM   3660 C  CD1   . ILE B 2 186 ? 153.474 133.719 106.005 1.00 48.36  ? 186 ILE B CD1   1 
ATOM   3661 N  N     . TYR B 2 187 ? 156.115 133.840 101.197 1.00 47.66  ? 187 TYR B N     1 
ATOM   3662 C  CA    . TYR B 2 187 ? 156.748 133.181 100.061 1.00 50.52  ? 187 TYR B CA    1 
ATOM   3663 C  C     . TYR B 2 187 ? 158.216 132.869 100.324 1.00 53.01  ? 187 TYR B C     1 
ATOM   3664 O  O     . TYR B 2 187 ? 158.728 131.875 99.798  1.00 51.44  ? 187 TYR B O     1 
ATOM   3665 C  CB    . TYR B 2 187 ? 156.604 134.037 98.798  1.00 55.45  ? 187 TYR B CB    1 
ATOM   3666 C  CG    . TYR B 2 187 ? 155.264 133.936 98.080  1.00 55.06  ? 187 TYR B CG    1 
ATOM   3667 C  CD1   . TYR B 2 187 ? 155.189 134.109 96.704  1.00 57.00  ? 187 TYR B CD1   1 
ATOM   3668 C  CD2   . TYR B 2 187 ? 154.084 133.660 98.768  1.00 55.65  ? 187 TYR B CD2   1 
ATOM   3669 C  CE1   . TYR B 2 187 ? 153.981 134.020 96.034  1.00 58.05  ? 187 TYR B CE1   1 
ATOM   3670 C  CE2   . TYR B 2 187 ? 152.874 133.569 98.110  1.00 55.64  ? 187 TYR B CE2   1 
ATOM   3671 C  CZ    . TYR B 2 187 ? 152.829 133.747 96.743  1.00 61.95  ? 187 TYR B CZ    1 
ATOM   3672 O  OH    . TYR B 2 187 ? 151.627 133.657 96.084  1.00 63.07  ? 187 TYR B OH    1 
ATOM   3673 N  N     . GLU B 2 188 ? 158.896 133.691 101.130 1.00 56.59  ? 188 GLU B N     1 
ATOM   3674 C  CA    . GLU B 2 188 ? 160.244 133.356 101.577 1.00 53.12  ? 188 GLU B CA    1 
ATOM   3675 C  C     . GLU B 2 188 ? 160.237 132.130 102.479 1.00 54.00  ? 188 GLU B C     1 
ATOM   3676 O  O     . GLU B 2 188 ? 161.171 131.325 102.438 1.00 53.08  ? 188 GLU B O     1 
ATOM   3677 C  CB    . GLU B 2 188 ? 160.878 134.543 102.301 1.00 52.43  ? 188 GLU B CB    1 
ATOM   3678 C  CG    . GLU B 2 188 ? 161.481 135.590 101.384 1.00 55.97  ? 188 GLU B CG    1 
ATOM   3679 C  CD    . GLU B 2 188 ? 161.488 136.970 102.008 1.00 59.90  ? 188 GLU B CD    1 
ATOM   3680 O  OE1   . GLU B 2 188 ? 161.504 137.966 101.254 1.00 59.36  ? 188 GLU B OE1   1 
ATOM   3681 O  OE2   . GLU B 2 188 ? 161.482 137.060 103.253 1.00 56.88  ? 188 GLU B OE2   1 
ATOM   3682 N  N     . PHE B 2 189 ? 159.208 131.991 103.322 1.00 52.61  ? 189 PHE B N     1 
ATOM   3683 C  CA    . PHE B 2 189 ? 159.034 130.757 104.093 1.00 47.44  ? 189 PHE B CA    1 
ATOM   3684 C  C     . PHE B 2 189 ? 158.836 129.555 103.176 1.00 51.88  ? 189 PHE B C     1 
ATOM   3685 O  O     . PHE B 2 189 ? 159.343 128.461 103.451 1.00 49.43  ? 189 PHE B O     1 
ATOM   3686 C  CB    . PHE B 2 189 ? 157.841 130.876 105.041 1.00 46.02  ? 189 PHE B CB    1 
ATOM   3687 C  CG    . PHE B 2 189 ? 158.179 131.441 106.382 1.00 47.95  ? 189 PHE B CG    1 
ATOM   3688 C  CD1   . PHE B 2 189 ? 159.216 130.912 107.131 1.00 49.61  ? 189 PHE B CD1   1 
ATOM   3689 C  CD2   . PHE B 2 189 ? 157.441 132.489 106.906 1.00 49.82  ? 189 PHE B CD2   1 
ATOM   3690 C  CE1   . PHE B 2 189 ? 159.521 131.431 108.372 1.00 52.99  ? 189 PHE B CE1   1 
ATOM   3691 C  CE2   . PHE B 2 189 ? 157.740 133.010 108.144 1.00 51.11  ? 189 PHE B CE2   1 
ATOM   3692 C  CZ    . PHE B 2 189 ? 158.779 132.482 108.878 1.00 52.74  ? 189 PHE B CZ    1 
ATOM   3693 N  N     . LYS B 2 190 ? 158.083 129.742 102.091 1.00 56.30  ? 190 LYS B N     1 
ATOM   3694 C  CA    . LYS B 2 190 ? 157.879 128.669 101.122 1.00 48.10  ? 190 LYS B CA    1 
ATOM   3695 C  C     . LYS B 2 190 ? 159.162 128.328 100.367 1.00 51.94  ? 190 LYS B C     1 
ATOM   3696 O  O     . LYS B 2 190 ? 159.356 127.177 99.960  1.00 53.57  ? 190 LYS B O     1 
ATOM   3697 C  CB    . LYS B 2 190 ? 156.771 129.060 100.141 1.00 50.24  ? 190 LYS B CB    1 
ATOM   3698 C  CG    . LYS B 2 190 ? 156.231 127.910 99.308  1.00 48.40  ? 190 LYS B CG    1 
ATOM   3699 C  CD    . LYS B 2 190 ? 155.239 128.387 98.264  1.00 49.93  ? 190 LYS B CD    1 
ATOM   3700 C  CE    . LYS B 2 190 ? 154.862 127.261 97.316  1.00 50.20  ? 190 LYS B CE    1 
ATOM   3701 N  NZ    . LYS B 2 190 ? 154.024 127.740 96.185  1.00 49.04  ? 190 LYS B NZ    1 
ATOM   3702 N  N     . GLU B 2 191 ? 160.053 129.305 100.180 1.00 63.05  ? 191 GLU B N     1 
ATOM   3703 C  CA    . GLU B 2 191 ? 161.247 129.102 99.366  1.00 60.58  ? 191 GLU B CA    1 
ATOM   3704 C  C     . GLU B 2 191 ? 162.326 128.264 100.046 1.00 61.22  ? 191 GLU B C     1 
ATOM   3705 O  O     . GLU B 2 191 ? 163.146 127.663 99.345  1.00 62.76  ? 191 GLU B O     1 
ATOM   3706 C  CB    . GLU B 2 191 ? 161.837 130.451 98.951  1.00 61.21  ? 191 GLU B CB    1 
ATOM   3707 C  CG    . GLU B 2 191 ? 161.398 130.920 97.573  1.00 63.27  ? 191 GLU B CG    1 
ATOM   3708 C  CD    . GLU B 2 191 ? 160.899 132.352 97.567  1.00 68.24  ? 191 GLU B CD    1 
ATOM   3709 O  OE1   . GLU B 2 191 ? 159.974 132.657 96.785  1.00 64.46  ? 191 GLU B OE1   1 
ATOM   3710 O  OE2   . GLU B 2 191 ? 161.430 133.173 98.345  1.00 66.47  ? 191 GLU B OE2   1 
ATOM   3711 N  N     . GLN B 2 192 ? 162.358 128.203 101.378 1.00 56.22  ? 192 GLN B N     1 
ATOM   3712 C  CA    . GLN B 2 192 ? 163.363 127.394 102.063 1.00 57.77  ? 192 GLN B CA    1 
ATOM   3713 C  C     . GLN B 2 192 ? 162.904 125.968 102.346 1.00 60.11  ? 192 GLN B C     1 
ATOM   3714 O  O     . GLN B 2 192 ? 163.462 125.343 103.258 1.00 59.69  ? 192 GLN B O     1 
ATOM   3715 C  CB    . GLN B 2 192 ? 163.802 128.058 103.372 1.00 56.43  ? 192 GLN B CB    1 
ATOM   3716 C  CG    . GLN B 2 192 ? 163.696 129.562 103.378 1.00 57.41  ? 192 GLN B CG    1 
ATOM   3717 C  CD    . GLN B 2 192 ? 163.706 130.151 104.773 1.00 59.09  ? 192 GLN B CD    1 
ATOM   3718 O  OE1   . GLN B 2 192 ? 163.681 129.427 105.766 1.00 59.83  ? 192 GLN B OE1   1 
ATOM   3719 N  NE2   . GLN B 2 192 ? 163.734 131.476 104.854 1.00 58.54  ? 192 GLN B NE2   1 
ATOM   3720 N  N     . ASN B 2 193 ? 161.912 125.470 101.594 1.00 58.95  ? 193 ASN B N     1 
ATOM   3721 C  CA    . ASN B 2 193 ? 161.478 124.066 101.600 1.00 58.18  ? 193 ASN B CA    1 
ATOM   3722 C  C     . ASN B 2 193 ? 160.979 123.622 102.977 1.00 58.10  ? 193 ASN B C     1 
ATOM   3723 O  O     . ASN B 2 193 ? 161.508 122.690 103.586 1.00 59.30  ? 193 ASN B O     1 
ATOM   3724 C  CB    . ASN B 2 193 ? 162.593 123.145 101.091 1.00 61.07  ? 193 ASN B CB    1 
ATOM   3725 C  CG    . ASN B 2 193 ? 162.064 121.850 100.518 1.00 64.91  ? 193 ASN B CG    1 
ATOM   3726 O  OD1   . ASN B 2 193 ? 161.439 121.836 99.458  1.00 66.68  ? 193 ASN B OD1   1 
ATOM   3727 N  ND2   . ASN B 2 193 ? 162.320 120.748 101.213 1.00 63.32  ? 193 ASN B ND2   1 
ATOM   3728 N  N     . LYS B 2 194 ? 159.944 124.298 103.464 1.00 51.32  ? 194 LYS B N     1 
ATOM   3729 C  CA    . LYS B 2 194 ? 159.313 123.969 104.733 1.00 48.00  ? 194 LYS B CA    1 
ATOM   3730 C  C     . LYS B 2 194 ? 157.921 123.407 104.489 1.00 50.91  ? 194 LYS B C     1 
ATOM   3731 O  O     . LYS B 2 194 ? 157.248 123.784 103.525 1.00 53.34  ? 194 LYS B O     1 
ATOM   3732 C  CB    . LYS B 2 194 ? 159.220 125.198 105.643 1.00 47.71  ? 194 LYS B CB    1 
ATOM   3733 C  CG    . LYS B 2 194 ? 160.542 125.891 105.902 1.00 52.59  ? 194 LYS B CG    1 
ATOM   3734 C  CD    . LYS B 2 194 ? 160.327 127.244 106.560 1.00 54.66  ? 194 LYS B CD    1 
ATOM   3735 C  CE    . LYS B 2 194 ? 161.481 127.619 107.480 1.00 51.29  ? 194 LYS B CE    1 
ATOM   3736 N  NZ    . LYS B 2 194 ? 162.603 126.641 107.443 1.00 47.51  ? 194 LYS B NZ    1 
ATOM   3737 N  N     . THR B 2 195 ? 157.495 122.499 105.364 1.00 43.60  ? 195 THR B N     1 
ATOM   3738 C  CA    . THR B 2 195 ? 156.136 121.978 105.304 1.00 42.20  ? 195 THR B CA    1 
ATOM   3739 C  C     . THR B 2 195 ? 155.175 123.005 105.889 1.00 37.26  ? 195 THR B C     1 
ATOM   3740 O  O     . THR B 2 195 ? 155.256 123.334 107.075 1.00 36.90  ? 195 THR B O     1 
ATOM   3741 C  CB    . THR B 2 195 ? 156.035 120.657 106.061 1.00 45.27  ? 195 THR B CB    1 
ATOM   3742 O  OG1   . THR B 2 195 ? 157.169 119.839 105.754 1.00 48.86  ? 195 THR B OG1   1 
ATOM   3743 C  CG2   . THR B 2 195 ? 154.764 119.917 105.675 1.00 39.21  ? 195 THR B CG2   1 
ATOM   3744 N  N     . ILE B 2 196 ? 154.270 123.518 105.061 1.00 37.13  ? 196 ILE B N     1 
ATOM   3745 C  CA    . ILE B 2 196 ? 153.353 124.580 105.457 1.00 38.85  ? 196 ILE B CA    1 
ATOM   3746 C  C     . ILE B 2 196 ? 151.929 124.050 105.379 1.00 33.72  ? 196 ILE B C     1 
ATOM   3747 O  O     . ILE B 2 196 ? 151.525 123.487 104.357 1.00 34.57  ? 196 ILE B O     1 
ATOM   3748 C  CB    . ILE B 2 196 ? 153.521 125.834 104.580 1.00 33.55  ? 196 ILE B CB    1 
ATOM   3749 C  CG1   . ILE B 2 196 ? 154.979 126.291 104.572 1.00 33.77  ? 196 ILE B CG1   1 
ATOM   3750 C  CG2   . ILE B 2 196 ? 152.627 126.961 105.071 1.00 29.69  ? 196 ILE B CG2   1 
ATOM   3751 C  CD1   . ILE B 2 196 ? 155.278 127.337 103.532 1.00 33.49  ? 196 ILE B CD1   1 
ATOM   3752 N  N     . PHE B 2 197 ? 151.179 124.219 106.464 1.00 27.98  ? 197 PHE B N     1 
ATOM   3753 C  CA    . PHE B 2 197 ? 149.756 123.916 106.504 1.00 31.01  ? 197 PHE B CA    1 
ATOM   3754 C  C     . PHE B 2 197 ? 148.977 125.222 106.502 1.00 33.53  ? 197 PHE B C     1 
ATOM   3755 O  O     . PHE B 2 197 ? 149.170 126.066 107.383 1.00 30.31  ? 197 PHE B O     1 
ATOM   3756 C  CB    . PHE B 2 197 ? 149.405 123.085 107.740 1.00 27.94  ? 197 PHE B CB    1 
ATOM   3757 C  CG    . PHE B 2 197 ? 149.798 121.642 107.630 1.00 30.79  ? 197 PHE B CG    1 
ATOM   3758 C  CD1   . PHE B 2 197 ? 148.945 120.720 107.042 1.00 31.12  ? 197 PHE B CD1   1 
ATOM   3759 C  CD2   . PHE B 2 197 ? 151.024 121.206 108.110 1.00 28.69  ? 197 PHE B CD2   1 
ATOM   3760 C  CE1   . PHE B 2 197 ? 149.305 119.389 106.940 1.00 32.84  ? 197 PHE B CE1   1 
ATOM   3761 C  CE2   . PHE B 2 197 ? 151.392 119.877 108.009 1.00 29.92  ? 197 PHE B CE2   1 
ATOM   3762 C  CZ    . PHE B 2 197 ? 150.531 118.967 107.422 1.00 32.58  ? 197 PHE B CZ    1 
ATOM   3763 N  N     . PHE B 2 198 ? 148.103 125.388 105.514 1.00 36.13  ? 198 PHE B N     1 
ATOM   3764 C  CA    . PHE B 2 198 ? 147.344 126.618 105.329 1.00 28.65  ? 198 PHE B CA    1 
ATOM   3765 C  C     . PHE B 2 198 ? 145.862 126.316 105.499 1.00 30.15  ? 198 PHE B C     1 
ATOM   3766 O  O     . PHE B 2 198 ? 145.329 125.417 104.842 1.00 37.97  ? 198 PHE B O     1 
ATOM   3767 C  CB    . PHE B 2 198 ? 147.623 127.229 103.954 1.00 32.69  ? 198 PHE B CB    1 
ATOM   3768 C  CG    . PHE B 2 198 ? 147.036 128.596 103.767 1.00 37.62  ? 198 PHE B CG    1 
ATOM   3769 C  CD1   . PHE B 2 198 ? 146.977 129.491 104.825 1.00 34.15  ? 198 PHE B CD1   1 
ATOM   3770 C  CD2   . PHE B 2 198 ? 146.543 128.989 102.532 1.00 34.39  ? 198 PHE B CD2   1 
ATOM   3771 C  CE1   . PHE B 2 198 ? 146.435 130.748 104.657 1.00 32.87  ? 198 PHE B CE1   1 
ATOM   3772 C  CE2   . PHE B 2 198 ? 146.002 130.247 102.357 1.00 32.51  ? 198 PHE B CE2   1 
ATOM   3773 C  CZ    . PHE B 2 198 ? 145.948 131.125 103.423 1.00 34.92  ? 198 PHE B CZ    1 
ATOM   3774 N  N     . VAL B 2 199 ? 145.205 127.070 106.373 1.00 28.43  ? 199 VAL B N     1 
ATOM   3775 C  CA    . VAL B 2 199 ? 143.785 126.912 106.664 1.00 41.34  ? 199 VAL B CA    1 
ATOM   3776 C  C     . VAL B 2 199 ? 143.097 128.221 106.308 1.00 40.89  ? 199 VAL B C     1 
ATOM   3777 O  O     . VAL B 2 199 ? 143.303 129.232 106.987 1.00 47.25  ? 199 VAL B O     1 
ATOM   3778 C  CB    . VAL B 2 199 ? 143.551 126.560 108.142 1.00 41.07  ? 199 VAL B CB    1 
ATOM   3779 C  CG1   . VAL B 2 199 ? 142.072 126.539 108.460 1.00 36.16  ? 199 VAL B CG1   1 
ATOM   3780 C  CG2   . VAL B 2 199 ? 144.205 125.239 108.493 1.00 40.55  ? 199 VAL B CG2   1 
ATOM   3781 N  N     . SER B 2 200 ? 142.275 128.209 105.259 1.00 38.70  ? 200 SER B N     1 
ATOM   3782 C  CA    . SER B 2 200 ? 141.614 129.432 104.820 1.00 42.93  ? 200 SER B CA    1 
ATOM   3783 C  C     . SER B 2 200 ? 140.391 129.100 103.978 1.00 43.22  ? 200 SER B C     1 
ATOM   3784 O  O     . SER B 2 200 ? 140.205 127.969 103.523 1.00 41.25  ? 200 SER B O     1 
ATOM   3785 C  CB    . SER B 2 200 ? 142.562 130.331 104.023 1.00 43.21  ? 200 SER B CB    1 
ATOM   3786 O  OG    . SER B 2 200 ? 142.230 130.341 102.647 1.00 49.35  ? 200 SER B OG    1 
ATOM   3787 N  N     . HIS B 2 201 ? 139.556 130.122 103.781 1.00 42.40  ? 201 HIS B N     1 
ATOM   3788 C  CA    . HIS B 2 201 ? 138.462 130.085 102.826 1.00 39.31  ? 201 HIS B CA    1 
ATOM   3789 C  C     . HIS B 2 201 ? 138.762 130.860 101.553 1.00 42.13  ? 201 HIS B C     1 
ATOM   3790 O  O     . HIS B 2 201 ? 138.037 130.700 100.566 1.00 47.37  ? 201 HIS B O     1 
ATOM   3791 C  CB    . HIS B 2 201 ? 137.181 130.648 103.456 1.00 36.75  ? 201 HIS B CB    1 
ATOM   3792 C  CG    . HIS B 2 201 ? 136.605 129.786 104.532 1.00 40.85  ? 201 HIS B CG    1 
ATOM   3793 N  ND1   . HIS B 2 201 ? 135.808 128.695 104.264 1.00 44.62  ? 201 HIS B ND1   1 
ATOM   3794 C  CD2   . HIS B 2 201 ? 136.705 129.857 105.879 1.00 39.37  ? 201 HIS B CD2   1 
ATOM   3795 C  CE1   . HIS B 2 201 ? 135.443 128.131 105.401 1.00 33.00  ? 201 HIS B CE1   1 
ATOM   3796 N  NE2   . HIS B 2 201 ? 135.973 128.817 106.395 1.00 36.12  ? 201 HIS B NE2   1 
ATOM   3797 N  N     . ASN B 2 202 ? 139.795 131.699 101.555 1.00 47.65  ? 202 ASN B N     1 
ATOM   3798 C  CA    . ASN B 2 202 ? 140.183 132.481 100.384 1.00 40.94  ? 202 ASN B CA    1 
ATOM   3799 C  C     . ASN B 2 202 ? 140.827 131.546 99.372  1.00 40.40  ? 202 ASN B C     1 
ATOM   3800 O  O     . ASN B 2 202 ? 142.002 131.195 99.491  1.00 48.73  ? 202 ASN B O     1 
ATOM   3801 C  CB    . ASN B 2 202 ? 141.135 133.601 100.787 1.00 44.02  ? 202 ASN B CB    1 
ATOM   3802 C  CG    . ASN B 2 202 ? 141.176 134.729 99.774  1.00 51.01  ? 202 ASN B CG    1 
ATOM   3803 O  OD1   . ASN B 2 202 ? 140.610 134.627 98.686  1.00 48.95  ? 202 ASN B OD1   1 
ATOM   3804 N  ND2   . ASN B 2 202 ? 141.853 135.813 100.129 1.00 49.30  ? 202 ASN B ND2   1 
ATOM   3805 N  N     . LEU B 2 203 ? 140.056 131.145 98.362  1.00 37.06  ? 203 LEU B N     1 
ATOM   3806 C  CA    . LEU B 2 203 ? 140.528 130.140 97.418  1.00 41.63  ? 203 LEU B CA    1 
ATOM   3807 C  C     . LEU B 2 203 ? 141.546 130.698 96.432  1.00 46.61  ? 203 LEU B C     1 
ATOM   3808 O  O     . LEU B 2 203 ? 142.307 129.926 95.841  1.00 45.83  ? 203 LEU B O     1 
ATOM   3809 C  CB    . LEU B 2 203 ? 139.341 129.530 96.670  1.00 45.21  ? 203 LEU B CB    1 
ATOM   3810 C  CG    . LEU B 2 203 ? 138.353 128.685 97.486  1.00 47.31  ? 203 LEU B CG    1 
ATOM   3811 C  CD1   . LEU B 2 203 ? 137.537 127.791 96.572  1.00 47.56  ? 203 LEU B CD1   1 
ATOM   3812 C  CD2   . LEU B 2 203 ? 139.049 127.854 98.561  1.00 37.55  ? 203 LEU B CD2   1 
ATOM   3813 N  N     . GLY B 2 204 ? 141.573 132.019 96.236  1.00 49.82  ? 204 GLY B N     1 
ATOM   3814 C  CA    . GLY B 2 204 ? 142.602 132.614 95.395  1.00 43.57  ? 204 GLY B CA    1 
ATOM   3815 C  C     . GLY B 2 204 ? 143.991 132.507 95.996  1.00 45.99  ? 204 GLY B C     1 
ATOM   3816 O  O     . GLY B 2 204 ? 144.949 132.145 95.304  1.00 48.92  ? 204 GLY B O     1 
ATOM   3817 N  N     . GLN B 2 205 ? 144.116 132.801 97.295  1.00 45.49  ? 205 GLN B N     1 
ATOM   3818 C  CA    . GLN B 2 205 ? 145.396 132.655 97.982  1.00 45.86  ? 205 GLN B CA    1 
ATOM   3819 C  C     . GLN B 2 205 ? 145.795 131.191 98.095  1.00 47.79  ? 205 GLN B C     1 
ATOM   3820 O  O     . GLN B 2 205 ? 146.984 130.856 98.032  1.00 53.65  ? 205 GLN B O     1 
ATOM   3821 C  CB    . GLN B 2 205 ? 145.326 133.295 99.369  1.00 42.59  ? 205 GLN B CB    1 
ATOM   3822 C  CG    . GLN B 2 205 ? 145.328 134.811 99.362  1.00 49.90  ? 205 GLN B CG    1 
ATOM   3823 C  CD    . GLN B 2 205 ? 145.428 135.402 100.755 1.00 51.88  ? 205 GLN B CD    1 
ATOM   3824 O  OE1   . GLN B 2 205 ? 145.205 134.715 101.751 1.00 49.61  ? 205 GLN B OE1   1 
ATOM   3825 N  NE2   . GLN B 2 205 ? 145.764 136.683 100.830 1.00 52.61  ? 205 GLN B NE2   1 
ATOM   3826 N  N     . VAL B 2 206 ? 144.808 130.309 98.264  1.00 43.95  ? 206 VAL B N     1 
ATOM   3827 C  CA    . VAL B 2 206 ? 145.057 128.871 98.318  1.00 37.67  ? 206 VAL B CA    1 
ATOM   3828 C  C     . VAL B 2 206 ? 145.582 128.367 96.976  1.00 41.78  ? 206 VAL B C     1 
ATOM   3829 O  O     . VAL B 2 206 ? 146.552 127.599 96.921  1.00 42.94  ? 206 VAL B O     1 
ATOM   3830 C  CB    . VAL B 2 206 ? 143.769 128.143 98.754  1.00 41.06  ? 206 VAL B CB    1 
ATOM   3831 C  CG1   . VAL B 2 206 ? 143.812 126.674 98.405  1.00 40.84  ? 206 VAL B CG1   1 
ATOM   3832 C  CG2   . VAL B 2 206 ? 143.538 128.326 100.244 1.00 42.06  ? 206 VAL B CG2   1 
ATOM   3833 N  N     . ARG B 2 207 ? 144.975 128.820 95.875  1.00 47.97  ? 207 ARG B N     1 
ATOM   3834 C  CA    . ARG B 2 207 ? 145.410 128.397 94.546  1.00 48.21  ? 207 ARG B CA    1 
ATOM   3835 C  C     . ARG B 2 207 ? 146.785 128.960 94.202  1.00 47.80  ? 207 ARG B C     1 
ATOM   3836 O  O     . ARG B 2 207 ? 147.629 128.253 93.639  1.00 50.25  ? 207 ARG B O     1 
ATOM   3837 C  CB    . ARG B 2 207 ? 144.377 128.822 93.501  1.00 48.07  ? 207 ARG B CB    1 
ATOM   3838 C  CG    . ARG B 2 207 ? 144.771 128.523 92.064  1.00 48.10  ? 207 ARG B CG    1 
ATOM   3839 C  CD    . ARG B 2 207 ? 143.600 128.701 91.117  1.00 50.88  ? 207 ARG B CD    1 
ATOM   3840 N  NE    . ARG B 2 207 ? 142.907 127.446 90.858  1.00 51.71  ? 207 ARG B NE    1 
ATOM   3841 C  CZ    . ARG B 2 207 ? 141.668 127.181 91.249  1.00 54.56  ? 207 ARG B CZ    1 
ATOM   3842 N  NH1   . ARG B 2 207 ? 140.955 128.063 91.931  1.00 49.38  ? 207 ARG B NH1   1 
ATOM   3843 N  NH2   . ARG B 2 207 ? 141.131 126.002 90.948  1.00 51.87  ? 207 ARG B NH2   1 
ATOM   3844 N  N     . GLN B 2 208 ? 147.040 130.220 94.550  1.00 50.40  ? 208 GLN B N     1 
ATOM   3845 C  CA    . GLN B 2 208 ? 148.318 130.839 94.232  1.00 50.69  ? 208 GLN B CA    1 
ATOM   3846 C  C     . GLN B 2 208 ? 149.434 130.467 95.203  1.00 49.70  ? 208 GLN B C     1 
ATOM   3847 O  O     . GLN B 2 208 ? 150.604 130.727 94.902  1.00 49.54  ? 208 GLN B O     1 
ATOM   3848 C  CB    . GLN B 2 208 ? 148.154 132.365 94.163  1.00 48.71  ? 208 GLN B CB    1 
ATOM   3849 C  CG    . GLN B 2 208 ? 148.433 133.114 95.455  1.00 54.10  ? 208 GLN B CG    1 
ATOM   3850 C  CD    . GLN B 2 208 ? 147.570 134.352 95.608  1.00 59.16  ? 208 GLN B CD    1 
ATOM   3851 O  OE1   . GLN B 2 208 ? 146.858 134.745 94.683  1.00 55.45  ? 208 GLN B OE1   1 
ATOM   3852 N  NE2   . GLN B 2 208 ? 147.636 134.980 96.776  1.00 57.05  ? 208 GLN B NE2   1 
ATOM   3853 N  N     . PHE B 2 209 ? 149.118 129.838 96.333  1.00 49.81  ? 209 PHE B N     1 
ATOM   3854 C  CA    . PHE B 2 209 ? 150.119 129.520 97.345  1.00 45.56  ? 209 PHE B CA    1 
ATOM   3855 C  C     . PHE B 2 209 ? 150.352 128.029 97.536  1.00 49.53  ? 209 PHE B C     1 
ATOM   3856 O  O     . PHE B 2 209 ? 151.505 127.594 97.572  1.00 48.52  ? 209 PHE B O     1 
ATOM   3857 C  CB    . PHE B 2 209 ? 149.713 130.154 98.687  1.00 45.62  ? 209 PHE B CB    1 
ATOM   3858 C  CG    . PHE B 2 209 ? 150.678 129.890 99.810  1.00 49.46  ? 209 PHE B CG    1 
ATOM   3859 C  CD1   . PHE B 2 209 ? 152.039 130.112 99.649  1.00 50.10  ? 209 PHE B CD1   1 
ATOM   3860 C  CD2   . PHE B 2 209 ? 150.219 129.434 101.036 1.00 48.43  ? 209 PHE B CD2   1 
ATOM   3861 C  CE1   . PHE B 2 209 ? 152.923 129.871 100.687 1.00 48.49  ? 209 PHE B CE1   1 
ATOM   3862 C  CE2   . PHE B 2 209 ? 151.096 129.197 102.078 1.00 47.16  ? 209 PHE B CE2   1 
ATOM   3863 C  CZ    . PHE B 2 209 ? 152.449 129.409 101.901 1.00 46.93  ? 209 PHE B CZ    1 
ATOM   3864 N  N     . CYS B 2 210 ? 149.297 127.230 97.656  1.00 47.64  ? 210 CYS B N     1 
ATOM   3865 C  CA    . CYS B 2 210 ? 149.435 125.839 98.064  1.00 44.55  ? 210 CYS B CA    1 
ATOM   3866 C  C     . CYS B 2 210 ? 149.758 124.935 96.881  1.00 42.05  ? 210 CYS B C     1 
ATOM   3867 O  O     . CYS B 2 210 ? 149.520 125.281 95.721  1.00 46.97  ? 210 CYS B O     1 
ATOM   3868 C  CB    . CYS B 2 210 ? 148.158 125.354 98.752  1.00 39.06  ? 210 CYS B CB    1 
ATOM   3869 S  SG    . CYS B 2 210 ? 147.685 126.337 100.192 1.00 53.00  ? 210 CYS B SG    1 
ATOM   3870 N  N     . THR B 2 211 ? 150.322 123.766 97.195  1.00 38.29  ? 211 THR B N     1 
ATOM   3871 C  CA    . THR B 2 211 ? 150.604 122.738 96.204  1.00 37.75  ? 211 THR B CA    1 
ATOM   3872 C  C     . THR B 2 211 ? 149.776 121.476 96.390  1.00 39.63  ? 211 THR B C     1 
ATOM   3873 O  O     . THR B 2 211 ? 149.664 120.687 95.448  1.00 38.95  ? 211 THR B O     1 
ATOM   3874 C  CB    . THR B 2 211 ? 152.092 122.356 96.228  1.00 40.79  ? 211 THR B CB    1 
ATOM   3875 O  OG1   . THR B 2 211 ? 152.456 121.911 97.541  1.00 43.59  ? 211 THR B OG1   1 
ATOM   3876 C  CG2   . THR B 2 211 ? 152.954 123.547 95.847  1.00 42.10  ? 211 THR B CG2   1 
ATOM   3877 N  N     . LYS B 2 212 ? 149.207 121.265 97.575  1.00 43.41  ? 212 LYS B N     1 
ATOM   3878 C  CA    . LYS B 2 212 ? 148.341 120.129 97.845  1.00 35.71  ? 212 LYS B CA    1 
ATOM   3879 C  C     . LYS B 2 212 ? 147.116 120.615 98.603  1.00 36.72  ? 212 LYS B C     1 
ATOM   3880 O  O     . LYS B 2 212 ? 147.155 121.633 99.296  1.00 41.26  ? 212 LYS B O     1 
ATOM   3881 C  CB    . LYS B 2 212 ? 149.066 119.039 98.643  1.00 36.13  ? 212 LYS B CB    1 
ATOM   3882 C  CG    . LYS B 2 212 ? 149.908 118.109 97.791  1.00 37.51  ? 212 LYS B CG    1 
ATOM   3883 C  CD    . LYS B 2 212 ? 150.789 117.229 98.651  1.00 42.47  ? 212 LYS B CD    1 
ATOM   3884 C  CE    . LYS B 2 212 ? 150.990 115.864 98.019  1.00 44.40  ? 212 LYS B CE    1 
ATOM   3885 N  NZ    . LYS B 2 212 ? 151.514 114.873 98.999  1.00 46.88  ? 212 LYS B NZ    1 
ATOM   3886 N  N     . ILE B 2 213 ? 146.015 119.881 98.456  1.00 37.15  ? 213 ILE B N     1 
ATOM   3887 C  CA    . ILE B 2 213 ? 144.739 120.244 99.064  1.00 38.40  ? 213 ILE B CA    1 
ATOM   3888 C  C     . ILE B 2 213 ? 144.254 119.083 99.918  1.00 36.70  ? 213 ILE B C     1 
ATOM   3889 O  O     . ILE B 2 213 ? 144.203 117.941 99.449  1.00 39.94  ? 213 ILE B O     1 
ATOM   3890 C  CB    . ILE B 2 213 ? 143.683 120.615 98.002  1.00 40.41  ? 213 ILE B CB    1 
ATOM   3891 C  CG1   . ILE B 2 213 ? 144.132 121.837 97.207  1.00 35.25  ? 213 ILE B CG1   1 
ATOM   3892 C  CG2   . ILE B 2 213 ? 142.336 120.905 98.643  1.00 34.98  ? 213 ILE B CG2   1 
ATOM   3893 C  CD1   . ILE B 2 213 ? 144.369 123.043 98.059  1.00 37.60  ? 213 ILE B CD1   1 
ATOM   3894 N  N     . ALA B 2 214 ? 143.908 119.373 101.169 1.00 36.34  ? 214 ALA B N     1 
ATOM   3895 C  CA    . ALA B 2 214 ? 143.223 118.433 102.046 1.00 32.22  ? 214 ALA B CA    1 
ATOM   3896 C  C     . ALA B 2 214 ? 141.807 118.942 102.285 1.00 32.43  ? 214 ALA B C     1 
ATOM   3897 O  O     . ALA B 2 214 ? 141.610 119.913 103.023 1.00 33.51  ? 214 ALA B O     1 
ATOM   3898 C  CB    . ALA B 2 214 ? 143.969 118.266 103.369 1.00 29.52  ? 214 ALA B CB    1 
ATOM   3899 N  N     . TRP B 2 215 ? 140.830 118.291 101.661 1.00 32.68  ? 215 TRP B N     1 
ATOM   3900 C  CA    . TRP B 2 215 ? 139.423 118.663 101.772 1.00 29.22  ? 215 TRP B CA    1 
ATOM   3901 C  C     . TRP B 2 215 ? 138.834 117.927 102.971 1.00 31.29  ? 215 TRP B C     1 
ATOM   3902 O  O     . TRP B 2 215 ? 138.868 116.694 103.030 1.00 32.67  ? 215 TRP B O     1 
ATOM   3903 C  CB    . TRP B 2 215 ? 138.682 118.332 100.474 1.00 32.23  ? 215 TRP B CB    1 
ATOM   3904 C  CG    . TRP B 2 215 ? 137.212 118.706 100.412 1.00 33.55  ? 215 TRP B CG    1 
ATOM   3905 C  CD1   . TRP B 2 215 ? 136.500 119.458 101.308 1.00 30.28  ? 215 TRP B CD1   1 
ATOM   3906 C  CD2   . TRP B 2 215 ? 136.291 118.350 99.376  1.00 30.10  ? 215 TRP B CD2   1 
ATOM   3907 N  NE1   . TRP B 2 215 ? 135.197 119.572 100.902 1.00 32.01  ? 215 TRP B NE1   1 
ATOM   3908 C  CE2   . TRP B 2 215 ? 135.041 118.904 99.716  1.00 36.51  ? 215 TRP B CE2   1 
ATOM   3909 C  CE3   . TRP B 2 215 ? 136.400 117.611 98.194  1.00 33.29  ? 215 TRP B CE3   1 
ATOM   3910 C  CZ2   . TRP B 2 215 ? 133.911 118.745 98.917  1.00 33.62  ? 215 TRP B CZ2   1 
ATOM   3911 C  CZ3   . TRP B 2 215 ? 135.277 117.453 97.403  1.00 32.60  ? 215 TRP B CZ3   1 
ATOM   3912 C  CH2   . TRP B 2 215 ? 134.050 118.017 97.768  1.00 32.31  ? 215 TRP B CH2   1 
ATOM   3913 N  N     . ILE B 2 216 ? 138.288 118.689 103.915 1.00 27.21  ? 216 ILE B N     1 
ATOM   3914 C  CA    . ILE B 2 216 ? 137.658 118.148 105.114 1.00 31.62  ? 216 ILE B CA    1 
ATOM   3915 C  C     . ILE B 2 216 ? 136.158 118.377 105.014 1.00 31.65  ? 216 ILE B C     1 
ATOM   3916 O  O     . ILE B 2 216 ? 135.708 119.509 104.801 1.00 38.11  ? 216 ILE B O     1 
ATOM   3917 C  CB    . ILE B 2 216 ? 138.230 118.794 106.388 1.00 34.77  ? 216 ILE B CB    1 
ATOM   3918 C  CG1   . ILE B 2 216 ? 139.757 118.887 106.308 1.00 39.91  ? 216 ILE B CG1   1 
ATOM   3919 C  CG2   . ILE B 2 216 ? 137.794 118.021 107.624 1.00 27.09  ? 216 ILE B CG2   1 
ATOM   3920 C  CD1   . ILE B 2 216 ? 140.464 117.547 106.339 1.00 34.26  ? 216 ILE B CD1   1 
ATOM   3921 N  N     . GLU B 2 217 ? 135.382 117.307 105.170 1.00 35.58  ? 217 GLU B N     1 
ATOM   3922 C  CA    . GLU B 2 217 ? 133.926 117.382 105.078 1.00 37.99  ? 217 GLU B CA    1 
ATOM   3923 C  C     . GLU B 2 217 ? 133.328 116.557 106.208 1.00 38.92  ? 217 GLU B C     1 
ATOM   3924 O  O     . GLU B 2 217 ? 133.426 115.326 106.197 1.00 45.38  ? 217 GLU B O     1 
ATOM   3925 C  CB    . GLU B 2 217 ? 133.432 116.885 103.718 1.00 36.65  ? 217 GLU B CB    1 
ATOM   3926 C  CG    . GLU B 2 217 ? 131.921 116.739 103.615 1.00 37.67  ? 217 GLU B CG    1 
ATOM   3927 C  CD    . GLU B 2 217 ? 131.390 117.117 102.247 1.00 49.45  ? 217 GLU B CD    1 
ATOM   3928 O  OE1   . GLU B 2 217 ? 131.536 118.292 101.851 1.00 49.29  ? 217 GLU B OE1   1 
ATOM   3929 O  OE2   . GLU B 2 217 ? 130.827 116.237 101.564 1.00 49.97  ? 217 GLU B OE2   1 
ATOM   3930 N  N     . GLY B 2 218 ? 132.709 117.234 107.171 1.00 35.91  ? 218 GLY B N     1 
ATOM   3931 C  CA    . GLY B 2 218 ? 132.015 116.565 108.261 1.00 31.47  ? 218 GLY B CA    1 
ATOM   3932 C  C     . GLY B 2 218 ? 132.913 115.788 109.198 1.00 38.23  ? 218 GLY B C     1 
ATOM   3933 O  O     . GLY B 2 218 ? 132.524 114.717 109.680 1.00 44.42  ? 218 GLY B O     1 
ATOM   3934 N  N     . GLY B 2 219 ? 134.108 116.303 109.471 1.00 39.72  ? 219 GLY B N     1 
ATOM   3935 C  CA    . GLY B 2 219 ? 135.048 115.610 110.326 1.00 29.03  ? 219 GLY B CA    1 
ATOM   3936 C  C     . GLY B 2 219 ? 135.879 114.551 109.645 1.00 33.08  ? 219 GLY B C     1 
ATOM   3937 O  O     . GLY B 2 219 ? 136.700 113.911 110.309 1.00 38.01  ? 219 GLY B O     1 
ATOM   3938 N  N     . LYS B 2 220 ? 135.707 114.354 108.343 1.00 35.05  ? 220 LYS B N     1 
ATOM   3939 C  CA    . LYS B 2 220 ? 136.413 113.323 107.602 1.00 34.58  ? 220 LYS B CA    1 
ATOM   3940 C  C     . LYS B 2 220 ? 137.219 113.951 106.476 1.00 34.04  ? 220 LYS B C     1 
ATOM   3941 O  O     . LYS B 2 220 ? 136.877 115.014 105.954 1.00 40.66  ? 220 LYS B O     1 
ATOM   3942 C  CB    . LYS B 2 220 ? 135.440 112.287 107.024 1.00 34.56  ? 220 LYS B CB    1 
ATOM   3943 C  CG    . LYS B 2 220 ? 134.936 111.275 108.033 1.00 39.36  ? 220 LYS B CG    1 
ATOM   3944 C  CD    . LYS B 2 220 ? 133.423 111.202 108.021 1.00 40.54  ? 220 LYS B CD    1 
ATOM   3945 C  CE    . LYS B 2 220 ? 132.944 109.762 108.009 1.00 43.67  ? 220 LYS B CE    1 
ATOM   3946 N  NZ    . LYS B 2 220 ? 131.466 109.668 108.162 1.00 46.32  ? 220 LYS B NZ    1 
ATOM   3947 N  N     . LEU B 2 221 ? 138.301 113.277 106.104 1.00 34.35  ? 221 LEU B N     1 
ATOM   3948 C  CA    . LEU B 2 221 ? 139.104 113.690 104.958 1.00 36.93  ? 221 LEU B CA    1 
ATOM   3949 C  C     . LEU B 2 221 ? 138.380 113.235 103.699 1.00 33.79  ? 221 LEU B C     1 
ATOM   3950 O  O     . LEU B 2 221 ? 138.379 112.050 103.362 1.00 39.41  ? 221 LEU B O     1 
ATOM   3951 C  CB    . LEU B 2 221 ? 140.508 113.107 105.043 1.00 38.60  ? 221 LEU B CB    1 
ATOM   3952 C  CG    . LEU B 2 221 ? 141.451 113.434 103.886 1.00 35.58  ? 221 LEU B CG    1 
ATOM   3953 C  CD1   . LEU B 2 221 ? 141.830 114.904 103.899 1.00 32.46  ? 221 LEU B CD1   1 
ATOM   3954 C  CD2   . LEU B 2 221 ? 142.687 112.555 103.950 1.00 36.23  ? 221 LEU B CD2   1 
ATOM   3955 N  N     . LYS B 2 222 ? 137.740 114.182 103.011 1.00 39.04  ? 222 LYS B N     1 
ATOM   3956 C  CA    . LYS B 2 222 ? 137.000 113.845 101.799 1.00 38.81  ? 222 LYS B CA    1 
ATOM   3957 C  C     . LYS B 2 222 ? 137.943 113.525 100.647 1.00 40.34  ? 222 LYS B C     1 
ATOM   3958 O  O     . LYS B 2 222 ? 137.740 112.541 99.927  1.00 47.05  ? 222 LYS B O     1 
ATOM   3959 C  CB    . LYS B 2 222 ? 136.060 114.990 101.425 1.00 36.50  ? 222 LYS B CB    1 
ATOM   3960 C  CG    . LYS B 2 222 ? 135.155 114.687 100.247 1.00 40.44  ? 222 LYS B CG    1 
ATOM   3961 C  CD    . LYS B 2 222 ? 133.698 114.693 100.656 1.00 41.61  ? 222 LYS B CD    1 
ATOM   3962 C  CE    . LYS B 2 222 ? 132.829 114.038 99.599  1.00 44.80  ? 222 LYS B CE    1 
ATOM   3963 N  NZ    . LYS B 2 222 ? 133.188 114.493 98.231  1.00 48.76  ? 222 LYS B NZ    1 
ATOM   3964 N  N     . ASP B 2 223 ? 138.981 114.337 100.462 1.00 39.07  ? 223 ASP B N     1 
ATOM   3965 C  CA    . ASP B 2 223 ? 139.954 114.099 99.408  1.00 38.51  ? 223 ASP B CA    1 
ATOM   3966 C  C     . ASP B 2 223 ? 141.277 114.732 99.807  1.00 38.91  ? 223 ASP B C     1 
ATOM   3967 O  O     . ASP B 2 223 ? 141.317 115.742 100.513 1.00 43.09  ? 223 ASP B O     1 
ATOM   3968 C  CB    . ASP B 2 223 ? 139.477 114.652 98.062  1.00 37.15  ? 223 ASP B CB    1 
ATOM   3969 C  CG    . ASP B 2 223 ? 140.159 113.984 96.888  1.00 45.89  ? 223 ASP B CG    1 
ATOM   3970 O  OD1   . ASP B 2 223 ? 140.918 113.017 97.108  1.00 50.23  ? 223 ASP B OD1   1 
ATOM   3971 O  OD2   . ASP B 2 223 ? 139.940 114.426 95.743  1.00 48.46  ? 223 ASP B OD2   1 
ATOM   3972 N  N     . TYR B 2 224 ? 142.361 114.117 99.343  1.00 39.03  ? 224 TYR B N     1 
ATOM   3973 C  CA    . TYR B 2 224 ? 143.703 114.625 99.589  1.00 37.78  ? 224 TYR B CA    1 
ATOM   3974 C  C     . TYR B 2 224 ? 144.553 114.325 98.365  1.00 42.77  ? 224 TYR B C     1 
ATOM   3975 O  O     . TYR B 2 224 ? 144.576 113.185 97.893  1.00 47.22  ? 224 TYR B O     1 
ATOM   3976 C  CB    . TYR B 2 224 ? 144.311 113.996 100.847 1.00 38.90  ? 224 TYR B CB    1 
ATOM   3977 C  CG    . TYR B 2 224 ? 145.741 114.399 101.119 1.00 44.18  ? 224 TYR B CG    1 
ATOM   3978 C  CD1   . TYR B 2 224 ? 146.082 115.731 101.326 1.00 46.04  ? 224 TYR B CD1   1 
ATOM   3979 C  CD2   . TYR B 2 224 ? 146.751 113.446 101.180 1.00 44.83  ? 224 TYR B CD2   1 
ATOM   3980 C  CE1   . TYR B 2 224 ? 147.390 116.103 101.578 1.00 38.20  ? 224 TYR B CE1   1 
ATOM   3981 C  CE2   . TYR B 2 224 ? 148.061 113.808 101.432 1.00 43.83  ? 224 TYR B CE2   1 
ATOM   3982 C  CZ    . TYR B 2 224 ? 148.373 115.137 101.629 1.00 43.84  ? 224 TYR B CZ    1 
ATOM   3983 O  OH    . TYR B 2 224 ? 149.675 115.500 101.880 1.00 48.80  ? 224 TYR B OH    1 
ATOM   3984 N  N     . GLY B 2 225 ? 145.238 115.342 97.854  1.00 41.54  ? 225 GLY B N     1 
ATOM   3985 C  CA    . GLY B 2 225 ? 146.040 115.173 96.657  1.00 42.94  ? 225 GLY B CA    1 
ATOM   3986 C  C     . GLY B 2 225 ? 146.531 116.515 96.155  1.00 45.21  ? 225 GLY B C     1 
ATOM   3987 O  O     . GLY B 2 225 ? 146.582 117.488 96.906  1.00 45.66  ? 225 GLY B O     1 
ATOM   3988 N  N     . GLU B 2 226 ? 146.884 116.548 94.870  1.00 48.29  ? 226 GLU B N     1 
ATOM   3989 C  CA    . GLU B 2 226 ? 147.422 117.758 94.260  1.00 49.68  ? 226 GLU B CA    1 
ATOM   3990 C  C     . GLU B 2 226 ? 146.346 118.832 94.142  1.00 51.30  ? 226 GLU B C     1 
ATOM   3991 O  O     . GLU B 2 226 ? 145.146 118.546 94.186  1.00 54.80  ? 226 GLU B O     1 
ATOM   3992 C  CB    . GLU B 2 226 ? 148.004 117.448 92.881  1.00 50.28  ? 226 GLU B CB    1 
ATOM   3993 C  CG    . GLU B 2 226 ? 148.971 116.278 92.861  1.00 51.99  ? 226 GLU B CG    1 
ATOM   3994 C  CD    . GLU B 2 226 ? 150.252 116.564 93.617  1.00 55.96  ? 226 GLU B CD    1 
ATOM   3995 O  OE1   . GLU B 2 226 ? 150.732 117.715 93.563  1.00 58.28  ? 226 GLU B OE1   1 
ATOM   3996 O  OE2   . GLU B 2 226 ? 150.781 115.637 94.266  1.00 57.47  ? 226 GLU B OE2   1 
ATOM   3997 N  N     . LEU B 2 227 ? 146.796 120.083 94.002  1.00 49.60  ? 227 LEU B N     1 
ATOM   3998 C  CA    . LEU B 2 227 ? 145.883 121.225 93.998  1.00 46.54  ? 227 LEU B CA    1 
ATOM   3999 C  C     . LEU B 2 227 ? 144.983 121.218 92.767  1.00 45.97  ? 227 LEU B C     1 
ATOM   4000 O  O     . LEU B 2 227 ? 143.766 121.416 92.874  1.00 50.96  ? 227 LEU B O     1 
ATOM   4001 C  CB    . LEU B 2 227 ? 146.681 122.527 94.079  1.00 46.22  ? 227 LEU B CB    1 
ATOM   4002 C  CG    . LEU B 2 227 ? 145.901 123.842 94.022  1.00 48.15  ? 227 LEU B CG    1 
ATOM   4003 C  CD1   . LEU B 2 227 ? 146.234 124.706 95.221  1.00 44.99  ? 227 LEU B CD1   1 
ATOM   4004 C  CD2   . LEU B 2 227 ? 146.201 124.586 92.733  1.00 49.50  ? 227 LEU B CD2   1 
ATOM   4005 N  N     . ASP B 2 228 ? 145.559 120.943 91.595  1.00 50.50  ? 228 ASP B N     1 
ATOM   4006 C  CA    . ASP B 2 228 ? 144.801 120.894 90.349  1.00 54.36  ? 228 ASP B CA    1 
ATOM   4007 C  C     . ASP B 2 228 ? 143.878 119.686 90.260  1.00 57.43  ? 228 ASP B C     1 
ATOM   4008 O  O     . ASP B 2 228 ? 143.012 119.654 89.380  1.00 57.96  ? 228 ASP B O     1 
ATOM   4009 C  CB    . ASP B 2 228 ? 145.758 120.894 89.157  1.00 54.35  ? 228 ASP B CB    1 
ATOM   4010 C  CG    . ASP B 2 228 ? 146.326 122.268 88.865  1.00 59.42  ? 228 ASP B CG    1 
ATOM   4011 O  OD1   . ASP B 2 228 ? 147.559 122.380 88.705  1.00 57.09  ? 228 ASP B OD1   1 
ATOM   4012 O  OD2   . ASP B 2 228 ? 145.539 123.234 88.795  1.00 60.18  ? 228 ASP B OD2   1 
ATOM   4013 N  N     . ASP B 2 229 ? 144.044 118.699 91.139  1.00 59.30  ? 229 ASP B N     1 
ATOM   4014 C  CA    . ASP B 2 229 ? 143.205 117.510 91.167  1.00 56.24  ? 229 ASP B CA    1 
ATOM   4015 C  C     . ASP B 2 229 ? 142.048 117.693 92.149  1.00 56.81  ? 229 ASP B C     1 
ATOM   4016 O  O     . ASP B 2 229 ? 140.913 117.318 91.847  1.00 60.95  ? 229 ASP B O     1 
ATOM   4017 C  CB    . ASP B 2 229 ? 144.083 116.296 91.525  1.00 56.56  ? 229 ASP B CB    1 
ATOM   4018 C  CG    . ASP B 2 229 ? 143.299 115.094 92.061  1.00 62.82  ? 229 ASP B CG    1 
ATOM   4019 O  OD1   . ASP B 2 229 ? 143.857 114.390 92.928  1.00 67.09  ? 229 ASP B OD1   1 
ATOM   4020 O  OD2   . ASP B 2 229 ? 142.209 114.759 91.544  1.00 61.39  ? 229 ASP B OD2   1 
ATOM   4021 N  N     . VAL B 2 230 ? 142.311 118.290 93.310  1.00 48.15  ? 230 VAL B N     1 
ATOM   4022 C  CA    . VAL B 2 230 ? 141.326 118.315 94.390  1.00 51.35  ? 230 VAL B CA    1 
ATOM   4023 C  C     . VAL B 2 230 ? 140.571 119.641 94.449  1.00 50.35  ? 230 VAL B C     1 
ATOM   4024 O  O     . VAL B 2 230 ? 139.358 119.648 94.678  1.00 56.89  ? 230 VAL B O     1 
ATOM   4025 C  CB    . VAL B 2 230 ? 142.024 117.989 95.729  1.00 44.60  ? 230 VAL B CB    1 
ATOM   4026 C  CG1   . VAL B 2 230 ? 141.015 117.879 96.861  1.00 45.62  ? 230 VAL B CG1   1 
ATOM   4027 C  CG2   . VAL B 2 230 ? 142.790 116.689 95.608  1.00 41.38  ? 230 VAL B CG2   1 
ATOM   4028 N  N     . LEU B 2 231 ? 141.262 120.770 94.260  1.00 45.09  ? 231 LEU B N     1 
ATOM   4029 C  CA    . LEU B 2 231 ? 140.610 122.078 94.349  1.00 44.36  ? 231 LEU B CA    1 
ATOM   4030 C  C     . LEU B 2 231 ? 139.500 122.333 93.318  1.00 47.31  ? 231 LEU B C     1 
ATOM   4031 O  O     . LEU B 2 231 ? 138.505 122.981 93.696  1.00 44.73  ? 231 LEU B O     1 
ATOM   4032 C  CB    . LEU B 2 231 ? 141.671 123.190 94.302  1.00 47.86  ? 231 LEU B CB    1 
ATOM   4033 C  CG    . LEU B 2 231 ? 141.226 124.585 94.751  1.00 48.13  ? 231 LEU B CG    1 
ATOM   4034 C  CD1   . LEU B 2 231 ? 140.737 124.561 96.192  1.00 46.87  ? 231 LEU B CD1   1 
ATOM   4035 C  CD2   . LEU B 2 231 ? 142.339 125.605 94.569  1.00 40.87  ? 231 LEU B CD2   1 
ATOM   4036 N  N     . PRO B 2 232 ? 139.593 121.912 92.035  1.00 49.85  ? 232 PRO B N     1 
ATOM   4037 C  CA    . PRO B 2 232 ? 138.397 122.009 91.174  1.00 50.82  ? 232 PRO B CA    1 
ATOM   4038 C  C     . PRO B 2 232 ? 137.193 121.215 91.659  1.00 47.84  ? 232 PRO B C     1 
ATOM   4039 O  O     . PRO B 2 232 ? 136.060 121.647 91.430  1.00 51.15  ? 232 PRO B O     1 
ATOM   4040 C  CB    . PRO B 2 232 ? 138.905 121.493 89.823  1.00 52.44  ? 232 PRO B CB    1 
ATOM   4041 C  CG    . PRO B 2 232 ? 140.303 121.885 89.806  1.00 53.21  ? 232 PRO B CG    1 
ATOM   4042 C  CD    . PRO B 2 232 ? 140.785 121.640 91.199  1.00 49.03  ? 232 PRO B CD    1 
ATOM   4043 N  N     . LYS B 2 233 ? 137.392 120.083 92.339  1.00 44.05  ? 233 LYS B N     1 
ATOM   4044 C  CA    . LYS B 2 233 ? 136.245 119.329 92.843  1.00 47.50  ? 233 LYS B CA    1 
ATOM   4045 C  C     . LYS B 2 233 ? 135.597 120.019 94.040  1.00 46.43  ? 233 LYS B C     1 
ATOM   4046 O  O     . LYS B 2 233 ? 134.367 119.997 94.179  1.00 46.73  ? 233 LYS B O     1 
ATOM   4047 C  CB    . LYS B 2 233 ? 136.662 117.900 93.186  1.00 46.60  ? 233 LYS B CB    1 
ATOM   4048 C  CG    . LYS B 2 233 ? 137.655 117.318 92.199  1.00 47.40  ? 233 LYS B CG    1 
ATOM   4049 C  CD    . LYS B 2 233 ? 137.436 115.830 91.984  1.00 47.89  ? 233 LYS B CD    1 
ATOM   4050 C  CE    . LYS B 2 233 ? 137.860 115.024 93.195  1.00 50.26  ? 233 LYS B CE    1 
ATOM   4051 N  NZ    . LYS B 2 233 ? 139.083 115.586 93.826  1.00 51.61  ? 233 LYS B NZ    1 
ATOM   4052 N  N     . TYR B 2 234 ? 136.398 120.655 94.901  1.00 38.47  ? 234 TYR B N     1 
ATOM   4053 C  CA    . TYR B 2 234 ? 135.830 121.455 95.984  1.00 37.66  ? 234 TYR B CA    1 
ATOM   4054 C  C     . TYR B 2 234 ? 135.109 122.685 95.444  1.00 41.24  ? 234 TYR B C     1 
ATOM   4055 O  O     . TYR B 2 234 ? 134.057 123.074 95.968  1.00 38.94  ? 234 TYR B O     1 
ATOM   4056 C  CB    . TYR B 2 234 ? 136.918 121.868 96.974  1.00 34.15  ? 234 TYR B CB    1 
ATOM   4057 C  CG    . TYR B 2 234 ? 136.402 122.711 98.119  1.00 40.96  ? 234 TYR B CG    1 
ATOM   4058 C  CD1   . TYR B 2 234 ? 135.385 122.248 98.943  1.00 36.99  ? 234 TYR B CD1   1 
ATOM   4059 C  CD2   . TYR B 2 234 ? 136.925 123.974 98.371  1.00 37.98  ? 234 TYR B CD2   1 
ATOM   4060 C  CE1   . TYR B 2 234 ? 134.905 123.014 99.990  1.00 30.52  ? 234 TYR B CE1   1 
ATOM   4061 C  CE2   . TYR B 2 234 ? 136.452 124.749 99.415  1.00 34.97  ? 234 TYR B CE2   1 
ATOM   4062 C  CZ    . TYR B 2 234 ? 135.443 124.262 100.221 1.00 34.30  ? 234 TYR B CZ    1 
ATOM   4063 O  OH    . TYR B 2 234 ? 134.969 125.028 101.259 1.00 40.86  ? 234 TYR B OH    1 
ATOM   4064 N  N     . GLU B 2 235 ? 135.656 123.301 94.390  1.00 50.98  ? 235 GLU B N     1 
ATOM   4065 C  CA    . GLU B 2 235 ? 134.973 124.419 93.744  1.00 48.12  ? 235 GLU B CA    1 
ATOM   4066 C  C     . GLU B 2 235 ? 133.669 123.973 93.090  1.00 49.80  ? 235 GLU B C     1 
ATOM   4067 O  O     . GLU B 2 235 ? 132.668 124.697 93.133  1.00 53.87  ? 235 GLU B O     1 
ATOM   4068 C  CB    . GLU B 2 235 ? 135.896 125.071 92.715  1.00 51.59  ? 235 GLU B CB    1 
ATOM   4069 C  CG    . GLU B 2 235 ? 136.695 126.240 93.259  1.00 49.46  ? 235 GLU B CG    1 
ATOM   4070 C  CD    . GLU B 2 235 ? 138.027 126.419 92.558  1.00 55.86  ? 235 GLU B CD    1 
ATOM   4071 O  OE1   . GLU B 2 235 ? 138.257 125.751 91.529  1.00 55.94  ? 235 GLU B OE1   1 
ATOM   4072 O  OE2   . GLU B 2 235 ? 138.845 127.230 93.038  1.00 56.48  ? 235 GLU B OE2   1 
ATOM   4073 N  N     . ALA B 2 236 ? 133.664 122.780 92.486  1.00 49.77  ? 236 ALA B N     1 
ATOM   4074 C  CA    . ALA B 2 236 ? 132.448 122.234 91.890  1.00 49.11  ? 236 ALA B CA    1 
ATOM   4075 C  C     . ALA B 2 236 ? 131.394 121.937 92.948  1.00 49.00  ? 236 ALA B C     1 
ATOM   4076 O  O     . ALA B 2 236 ? 130.202 122.174 92.723  1.00 53.46  ? 236 ALA B O     1 
ATOM   4077 C  CB    . ALA B 2 236 ? 132.775 120.973 91.092  1.00 47.30  ? 236 ALA B CB    1 
ATOM   4078 N  N     . PHE B 2 237 ? 131.817 121.429 94.112  1.00 51.31  ? 237 PHE B N     1 
ATOM   4079 C  CA    . PHE B 2 237 ? 130.895 121.245 95.231  1.00 45.88  ? 237 PHE B CA    1 
ATOM   4080 C  C     . PHE B 2 237 ? 130.336 122.579 95.712  1.00 42.51  ? 237 PHE B C     1 
ATOM   4081 O  O     . PHE B 2 237 ? 129.146 122.678 96.043  1.00 50.00  ? 237 PHE B O     1 
ATOM   4082 C  CB    . PHE B 2 237 ? 131.597 120.512 96.379  1.00 44.98  ? 237 PHE B CB    1 
ATOM   4083 C  CG    . PHE B 2 237 ? 130.958 120.733 97.727  1.00 45.94  ? 237 PHE B CG    1 
ATOM   4084 C  CD1   . PHE B 2 237 ? 129.756 120.118 98.046  1.00 46.89  ? 237 PHE B CD1   1 
ATOM   4085 C  CD2   . PHE B 2 237 ? 131.560 121.550 98.675  1.00 51.19  ? 237 PHE B CD2   1 
ATOM   4086 C  CE1   . PHE B 2 237 ? 129.162 120.320 99.280  1.00 45.73  ? 237 PHE B CE1   1 
ATOM   4087 C  CE2   . PHE B 2 237 ? 130.969 121.757 99.908  1.00 48.63  ? 237 PHE B CE2   1 
ATOM   4088 C  CZ    . PHE B 2 237 ? 129.770 121.139 100.210 1.00 47.09  ? 237 PHE B CZ    1 
ATOM   4089 N  N     . LEU B 2 238 ? 131.186 123.611 95.763  1.00 48.33  ? 238 LEU B N     1 
ATOM   4090 C  CA    . LEU B 2 238 ? 130.745 124.927 96.216  1.00 48.95  ? 238 LEU B CA    1 
ATOM   4091 C  C     . LEU B 2 238 ? 129.719 125.539 95.269  1.00 50.21  ? 238 LEU B C     1 
ATOM   4092 O  O     . LEU B 2 238 ? 128.719 126.104 95.721  1.00 50.40  ? 238 LEU B O     1 
ATOM   4093 C  CB    . LEU B 2 238 ? 131.944 125.859 96.379  1.00 52.84  ? 238 LEU B CB    1 
ATOM   4094 C  CG    . LEU B 2 238 ? 132.720 125.745 97.693  1.00 48.97  ? 238 LEU B CG    1 
ATOM   4095 C  CD1   . LEU B 2 238 ? 133.767 126.842 97.787  1.00 48.90  ? 238 LEU B CD1   1 
ATOM   4096 C  CD2   . LEU B 2 238 ? 131.785 125.792 98.893  1.00 45.59  ? 238 LEU B CD2   1 
ATOM   4097 N  N     . ASN B 2 239 ? 129.938 125.430 93.954  1.00 55.89  ? 239 ASN B N     1 
ATOM   4098 C  CA    . ASN B 2 239 ? 128.944 125.956 93.016  1.00 56.85  ? 239 ASN B CA    1 
ATOM   4099 C  C     . ASN B 2 239 ? 127.708 125.065 92.947  1.00 57.91  ? 239 ASN B C     1 
ATOM   4100 O  O     . ASN B 2 239 ? 126.616 125.540 92.615  1.00 64.80  ? 239 ASN B O     1 
ATOM   4101 C  CB    . ASN B 2 239 ? 129.527 126.153 91.610  1.00 58.81  ? 239 ASN B CB    1 
ATOM   4102 C  CG    . ASN B 2 239 ? 130.952 126.687 91.611  1.00 64.09  ? 239 ASN B CG    1 
ATOM   4103 O  OD1   . ASN B 2 239 ? 131.772 126.272 90.791  1.00 65.44  ? 239 ASN B OD1   1 
ATOM   4104 N  ND2   . ASN B 2 239 ? 131.231 127.661 92.473  1.00 59.21  ? 239 ASN B ND2   1 
ATOM   4105 N  N     . ASP B 2 240 ? 127.855 123.772 93.245  1.00 60.28  ? 240 ASP B N     1 
ATOM   4106 C  CA    . ASP B 2 240 ? 126.697 122.887 93.264  1.00 57.38  ? 240 ASP B CA    1 
ATOM   4107 C  C     . ASP B 2 240 ? 125.819 123.150 94.480  1.00 61.24  ? 240 ASP B C     1 
ATOM   4108 O  O     . ASP B 2 240 ? 124.611 122.890 94.445  1.00 65.95  ? 240 ASP B O     1 
ATOM   4109 C  CB    . ASP B 2 240 ? 127.153 121.429 93.238  1.00 58.81  ? 240 ASP B CB    1 
ATOM   4110 C  CG    . ASP B 2 240 ? 127.222 120.863 91.834  1.00 67.37  ? 240 ASP B CG    1 
ATOM   4111 O  OD1   . ASP B 2 240 ? 127.189 119.623 91.691  1.00 67.17  ? 240 ASP B OD1   1 
ATOM   4112 O  OD2   . ASP B 2 240 ? 127.311 121.656 90.873  1.00 69.71  ? 240 ASP B OD2   1 
ATOM   4113 N  N     . PHE B 2 241 ? 126.408 123.655 95.568  1.00 58.11  ? 241 PHE B N     1 
ATOM   4114 C  CA    . PHE B 2 241 ? 125.636 123.878 96.786  1.00 54.05  ? 241 PHE B CA    1 
ATOM   4115 C  C     . PHE B 2 241 ? 124.694 125.072 96.655  1.00 56.96  ? 241 PHE B C     1 
ATOM   4116 O  O     . PHE B 2 241 ? 123.590 125.060 97.212  1.00 62.37  ? 241 PHE B O     1 
ATOM   4117 C  CB    . PHE B 2 241 ? 126.572 124.067 97.978  1.00 56.72  ? 241 PHE B CB    1 
ATOM   4118 C  CG    . PHE B 2 241 ? 125.895 123.905 99.305  1.00 56.11  ? 241 PHE B CG    1 
ATOM   4119 C  CD1   . PHE B 2 241 ? 125.629 122.643 99.810  1.00 56.97  ? 241 PHE B CD1   1 
ATOM   4120 C  CD2   . PHE B 2 241 ? 125.504 125.013 100.040 1.00 58.74  ? 241 PHE B CD2   1 
ATOM   4121 C  CE1   . PHE B 2 241 ? 124.999 122.490 101.030 1.00 57.18  ? 241 PHE B CE1   1 
ATOM   4122 C  CE2   . PHE B 2 241 ? 124.876 124.866 101.262 1.00 57.72  ? 241 PHE B CE2   1 
ATOM   4123 C  CZ    . PHE B 2 241 ? 124.624 123.601 101.757 1.00 59.72  ? 241 PHE B CZ    1 
ATOM   4124 N  N     . LYS B 2 242 ? 125.109 126.118 95.934  1.00 57.05  ? 242 LYS B N     1 
ATOM   4125 C  CA    . LYS B 2 242 ? 124.258 127.300 95.806  1.00 59.23  ? 242 LYS B CA    1 
ATOM   4126 C  C     . LYS B 2 242 ? 123.083 127.085 94.865  1.00 61.32  ? 242 LYS B C     1 
ATOM   4127 O  O     . LYS B 2 242 ? 122.118 127.853 94.926  1.00 65.07  ? 242 LYS B O     1 
ATOM   4128 C  CB    . LYS B 2 242 ? 125.059 128.511 95.318  1.00 61.29  ? 242 LYS B CB    1 
ATOM   4129 C  CG    . LYS B 2 242 ? 126.534 128.477 95.642  1.00 64.39  ? 242 LYS B CG    1 
ATOM   4130 C  CD    . LYS B 2 242 ? 126.815 128.805 97.098  1.00 61.04  ? 242 LYS B CD    1 
ATOM   4131 C  CE    . LYS B 2 242 ? 128.249 129.272 97.278  1.00 61.24  ? 242 LYS B CE    1 
ATOM   4132 N  NZ    . LYS B 2 242 ? 128.668 130.202 96.194  1.00 61.59  ? 242 LYS B NZ    1 
ATOM   4133 N  N     . LYS B 2 243 ? 123.137 126.073 94.003  1.00 65.16  ? 243 LYS B N     1 
ATOM   4134 C  CA    . LYS B 2 243 ? 122.068 125.795 93.058  1.00 66.57  ? 243 LYS B CA    1 
ATOM   4135 C  C     . LYS B 2 243 ? 120.996 124.878 93.629  1.00 67.39  ? 243 LYS B C     1 
ATOM   4136 O  O     . LYS B 2 243 ? 120.044 124.545 92.919  1.00 71.15  ? 243 LYS B O     1 
ATOM   4137 C  CB    . LYS B 2 243 ? 122.645 125.191 91.774  1.00 66.62  ? 243 LYS B CB    1 
ATOM   4138 C  CG    . LYS B 2 243 ? 123.071 126.234 90.754  1.00 68.13  ? 243 LYS B CG    1 
ATOM   4139 C  CD    . LYS B 2 243 ? 124.342 125.832 90.026  1.00 69.35  ? 243 LYS B CD    1 
ATOM   4140 C  CE    . LYS B 2 243 ? 124.042 124.917 88.852  1.00 70.31  ? 243 LYS B CE    1 
ATOM   4141 N  NZ    . LYS B 2 243 ? 125.135 123.933 88.618  1.00 70.37  ? 243 LYS B NZ    1 
ATOM   4142 N  N     . LYS B 2 244 ? 121.128 124.462 94.883  1.00 63.51  ? 244 LYS B N     1 
ATOM   4143 C  CA    . LYS B 2 244 ? 120.101 123.677 95.549  1.00 64.58  ? 244 LYS B CA    1 
ATOM   4144 C  C     . LYS B 2 244 ? 119.086 124.593 96.224  1.00 65.52  ? 244 LYS B C     1 
ATOM   4145 O  O     . LYS B 2 244 ? 119.332 125.780 96.447  1.00 65.93  ? 244 LYS B O     1 
ATOM   4146 C  CB    . LYS B 2 244 ? 120.716 122.740 96.589  1.00 63.79  ? 244 LYS B CB    1 
ATOM   4147 C  CG    . LYS B 2 244 ? 121.880 121.911 96.094  1.00 64.55  ? 244 LYS B CG    1 
ATOM   4148 C  CD    . LYS B 2 244 ? 122.688 121.371 97.261  1.00 64.93  ? 244 LYS B CD    1 
ATOM   4149 C  CE    . LYS B 2 244 ? 122.656 119.855 97.304  1.00 66.64  ? 244 LYS B CE    1 
ATOM   4150 N  NZ    . LYS B 2 244 ? 123.793 119.304 98.088  1.00 67.64  ? 244 LYS B NZ    1 
ATOM   4151 N  N     . SER B 2 245 ? 117.932 124.019 96.550  1.00 66.98  ? 245 SER B N     1 
ATOM   4152 C  CA    . SER B 2 245 ? 116.933 124.733 97.327  1.00 66.64  ? 245 SER B CA    1 
ATOM   4153 C  C     . SER B 2 245 ? 117.329 124.748 98.803  1.00 67.49  ? 245 SER B C     1 
ATOM   4154 O  O     . SER B 2 245 ? 118.298 124.110 99.221  1.00 71.05  ? 245 SER B O     1 
ATOM   4155 C  CB    . SER B 2 245 ? 115.556 124.096 97.144  1.00 66.87  ? 245 SER B CB    1 
ATOM   4156 O  OG    . SER B 2 245 ? 115.581 122.719 97.473  1.00 68.29  ? 245 SER B OG    1 
ATOM   4157 N  N     . LYS B 2 246 ? 116.562 125.501 99.597  1.00 68.42  ? 246 LYS B N     1 
ATOM   4158 C  CA    . LYS B 2 246 ? 116.839 125.597 101.029 1.00 67.24  ? 246 LYS B CA    1 
ATOM   4159 C  C     . LYS B 2 246 ? 116.565 124.276 101.737 1.00 65.81  ? 246 LYS B C     1 
ATOM   4160 O  O     . LYS B 2 246 ? 117.267 123.915 102.691 1.00 67.78  ? 246 LYS B O     1 
ATOM   4161 C  CB    . LYS B 2 246 ? 116.009 126.720 101.649 1.00 69.32  ? 246 LYS B CB    1 
ATOM   4162 C  CG    . LYS B 2 246 ? 116.570 128.113 101.416 1.00 68.97  ? 246 LYS B CG    1 
ATOM   4163 C  CD    . LYS B 2 246 ? 116.541 128.939 102.693 1.00 70.27  ? 246 LYS B CD    1 
ATOM   4164 C  CE    . LYS B 2 246 ? 117.047 130.353 102.453 1.00 71.71  ? 246 LYS B CE    1 
ATOM   4165 N  NZ    . LYS B 2 246 ? 118.518 130.464 102.657 1.00 69.99  ? 246 LYS B NZ    1 
ATOM   4166 N  N     . ALA B 2 247 ? 115.547 123.540 101.279 1.00 65.58  ? 247 ALA B N     1 
ATOM   4167 C  CA    . ALA B 2 247 ? 115.255 122.226 101.842 1.00 67.00  ? 247 ALA B CA    1 
ATOM   4168 C  C     . ALA B 2 247 ? 116.365 121.231 101.531 1.00 67.98  ? 247 ALA B C     1 
ATOM   4169 O  O     . ALA B 2 247 ? 116.721 120.407 102.379 1.00 69.40  ? 247 ALA B O     1 
ATOM   4170 C  CB    . ALA B 2 247 ? 113.914 121.716 101.316 1.00 68.02  ? 247 ALA B CB    1 
ATOM   4171 N  N     . GLU B 2 248 ? 116.932 121.302 100.323 1.00 65.63  ? 248 GLU B N     1 
ATOM   4172 C  CA    . GLU B 2 248 ? 118.029 120.411 99.952  1.00 66.90  ? 248 GLU B CA    1 
ATOM   4173 C  C     . GLU B 2 248 ? 119.297 120.723 100.741 1.00 67.78  ? 248 GLU B C     1 
ATOM   4174 O  O     . GLU B 2 248 ? 120.019 119.806 101.151 1.00 67.15  ? 248 GLU B O     1 
ATOM   4175 C  CB    . GLU B 2 248 ? 118.295 120.509 98.451  1.00 65.91  ? 248 GLU B CB    1 
ATOM   4176 C  CG    . GLU B 2 248 ? 117.542 119.488 97.621  1.00 68.61  ? 248 GLU B CG    1 
ATOM   4177 C  CD    . GLU B 2 248 ? 117.594 119.794 96.138  1.00 70.95  ? 248 GLU B CD    1 
ATOM   4178 O  OE1   . GLU B 2 248 ? 117.593 118.841 95.331  1.00 69.29  ? 248 GLU B OE1   1 
ATOM   4179 O  OE2   . GLU B 2 248 ? 117.635 120.990 95.780  1.00 71.24  ? 248 GLU B OE2   1 
ATOM   4180 N  N     . GLN B 2 249 ? 119.577 122.010 100.968 1.00 60.14  ? 249 GLN B N     1 
ATOM   4181 C  CA    . GLN B 2 249 ? 120.732 122.396 101.775 1.00 60.24  ? 249 GLN B CA    1 
ATOM   4182 C  C     . GLN B 2 249 ? 120.554 121.985 103.232 1.00 59.15  ? 249 GLN B C     1 
ATOM   4183 O  O     . GLN B 2 249 ? 121.512 121.542 103.881 1.00 60.51  ? 249 GLN B O     1 
ATOM   4184 C  CB    . GLN B 2 249 ? 120.963 123.902 101.667 1.00 61.73  ? 249 GLN B CB    1 
ATOM   4185 C  CG    . GLN B 2 249 ? 121.391 124.362 100.286 1.00 59.34  ? 249 GLN B CG    1 
ATOM   4186 C  CD    . GLN B 2 249 ? 121.558 125.863 100.203 1.00 59.34  ? 249 GLN B CD    1 
ATOM   4187 O  OE1   . GLN B 2 249 ? 121.471 126.564 101.209 1.00 61.26  ? 249 GLN B OE1   1 
ATOM   4188 N  NE2   . GLN B 2 249 ? 121.798 126.365 98.999  1.00 61.93  ? 249 GLN B NE2   1 
ATOM   4189 N  N     . LYS B 2 250 ? 119.332 122.117 103.758 1.00 62.73  ? 250 LYS B N     1 
ATOM   4190 C  CA    . LYS B 2 250 ? 119.052 121.659 105.117 1.00 62.90  ? 250 LYS B CA    1 
ATOM   4191 C  C     . LYS B 2 250 ? 119.163 120.143 105.227 1.00 62.23  ? 250 LYS B C     1 
ATOM   4192 O  O     . LYS B 2 250 ? 119.645 119.625 106.239 1.00 63.17  ? 250 LYS B O     1 
ATOM   4193 C  CB    . LYS B 2 250 ? 117.665 122.127 105.554 1.00 64.54  ? 250 LYS B CB    1 
ATOM   4194 C  CG    . LYS B 2 250 ? 117.550 122.395 107.042 1.00 63.78  ? 250 LYS B CG    1 
ATOM   4195 C  CD    . LYS B 2 250 ? 116.185 121.991 107.569 1.00 67.97  ? 250 LYS B CD    1 
ATOM   4196 C  CE    . LYS B 2 250 ? 116.194 121.871 109.083 1.00 66.13  ? 250 LYS B CE    1 
ATOM   4197 N  NZ    . LYS B 2 250 ? 116.740 123.092 109.734 1.00 63.96  ? 250 LYS B NZ    1 
ATOM   4198 N  N     . GLU B 2 251 ? 118.730 119.420 104.188 1.00 63.71  ? 251 GLU B N     1 
ATOM   4199 C  CA    . GLU B 2 251 ? 118.860 117.966 104.169 1.00 62.61  ? 251 GLU B CA    1 
ATOM   4200 C  C     . GLU B 2 251 ? 120.324 117.543 104.120 1.00 62.51  ? 251 GLU B C     1 
ATOM   4201 O  O     . GLU B 2 251 ? 120.719 116.581 104.789 1.00 66.60  ? 251 GLU B O     1 
ATOM   4202 C  CB    . GLU B 2 251 ? 118.094 117.397 102.973 1.00 63.77  ? 251 GLU B CB    1 
ATOM   4203 C  CG    . GLU B 2 251 ? 117.859 115.889 102.986 1.00 66.20  ? 251 GLU B CG    1 
ATOM   4204 C  CD    . GLU B 2 251 ? 117.631 115.323 104.378 1.00 71.58  ? 251 GLU B CD    1 
ATOM   4205 O  OE1   . GLU B 2 251 ? 118.559 114.703 104.939 1.00 71.12  ? 251 GLU B OE1   1 
ATOM   4206 O  OE2   . GLU B 2 251 ? 116.515 115.495 104.912 1.00 67.75  ? 251 GLU B OE2   1 
ATOM   4207 N  N     . PHE B 2 252 ? 121.145 118.261 103.345 1.00 61.30  ? 252 PHE B N     1 
ATOM   4208 C  CA    . PHE B 2 252 ? 122.579 117.974 103.300 1.00 57.86  ? 252 PHE B CA    1 
ATOM   4209 C  C     . PHE B 2 252 ? 123.245 118.243 104.644 1.00 56.33  ? 252 PHE B C     1 
ATOM   4210 O  O     . PHE B 2 252 ? 124.080 117.450 105.097 1.00 61.15  ? 252 PHE B O     1 
ATOM   4211 C  CB    . PHE B 2 252 ? 123.252 118.797 102.199 1.00 58.37  ? 252 PHE B CB    1 
ATOM   4212 C  CG    . PHE B 2 252 ? 124.738 118.564 102.086 1.00 60.44  ? 252 PHE B CG    1 
ATOM   4213 C  CD1   . PHE B 2 252 ? 125.226 117.448 101.425 1.00 62.65  ? 252 PHE B CD1   1 
ATOM   4214 C  CD2   . PHE B 2 252 ? 125.647 119.462 102.636 1.00 60.25  ? 252 PHE B CD2   1 
ATOM   4215 C  CE1   . PHE B 2 252 ? 126.589 117.226 101.319 1.00 62.15  ? 252 PHE B CE1   1 
ATOM   4216 C  CE2   . PHE B 2 252 ? 127.008 119.245 102.535 1.00 58.81  ? 252 PHE B CE2   1 
ATOM   4217 C  CZ    . PHE B 2 252 ? 127.480 118.127 101.874 1.00 58.74  ? 252 PHE B CZ    1 
ATOM   4218 N  N     . ARG B 2 253 ? 122.889 119.357 105.294 1.00 58.77  ? 253 ARG B N     1 
ATOM   4219 C  CA    . ARG B 2 253 ? 123.455 119.673 106.603 1.00 56.83  ? 253 ARG B CA    1 
ATOM   4220 C  C     . ARG B 2 253 ? 123.023 118.662 107.661 1.00 59.41  ? 253 ARG B C     1 
ATOM   4221 O  O     . ARG B 2 253 ? 123.828 118.260 108.510 1.00 61.06  ? 253 ARG B O     1 
ATOM   4222 C  CB    . ARG B 2 253 ? 123.056 121.088 107.018 1.00 57.80  ? 253 ARG B CB    1 
ATOM   4223 C  CG    . ARG B 2 253 ? 124.170 122.108 106.877 1.00 59.53  ? 253 ARG B CG    1 
ATOM   4224 C  CD    . ARG B 2 253 ? 123.696 123.506 107.234 1.00 61.25  ? 253 ARG B CD    1 
ATOM   4225 N  NE    . ARG B 2 253 ? 123.136 124.211 106.088 1.00 61.15  ? 253 ARG B NE    1 
ATOM   4226 C  CZ    . ARG B 2 253 ? 121.852 124.508 105.945 1.00 63.98  ? 253 ARG B CZ    1 
ATOM   4227 N  NH1   . ARG B 2 253 ? 120.957 124.166 106.857 1.00 61.26  ? 253 ARG B NH1   1 
ATOM   4228 N  NH2   . ARG B 2 253 ? 121.455 125.168 104.861 1.00 63.72  ? 253 ARG B NH2   1 
ATOM   4229 N  N     . ASN B 2 254 ? 121.761 118.223 107.610 1.00 64.54  ? 254 ASN B N     1 
ATOM   4230 C  CA    . ASN B 2 254 ? 121.269 117.234 108.564 1.00 62.52  ? 254 ASN B CA    1 
ATOM   4231 C  C     . ASN B 2 254 ? 121.911 115.871 108.339 1.00 58.44  ? 254 ASN B C     1 
ATOM   4232 O  O     . ASN B 2 254 ? 122.224 115.165 109.303 1.00 63.43  ? 254 ASN B O     1 
ATOM   4233 C  CB    . ASN B 2 254 ? 119.747 117.133 108.471 1.00 61.86  ? 254 ASN B CB    1 
ATOM   4234 C  CG    . ASN B 2 254 ? 119.049 118.245 109.219 1.00 63.58  ? 254 ASN B CG    1 
ATOM   4235 O  OD1   . ASN B 2 254 ? 119.641 118.890 110.082 1.00 61.81  ? 254 ASN B OD1   1 
ATOM   4236 N  ND2   . ASN B 2 254 ? 117.785 118.482 108.888 1.00 65.34  ? 254 ASN B ND2   1 
ATOM   4237 N  N     . LYS B 2 255 ? 122.127 115.488 107.077 1.00 56.98  ? 255 LYS B N     1 
ATOM   4238 C  CA    . LYS B 2 255 ? 122.780 114.215 106.787 1.00 58.45  ? 255 LYS B CA    1 
ATOM   4239 C  C     . LYS B 2 255 ? 124.254 114.266 107.175 1.00 59.92  ? 255 LYS B C     1 
ATOM   4240 O  O     . LYS B 2 255 ? 124.830 113.249 107.576 1.00 63.90  ? 255 LYS B O     1 
ATOM   4241 C  CB    . LYS B 2 255 ? 122.565 113.867 105.303 1.00 59.64  ? 255 LYS B CB    1 
ATOM   4242 C  CG    . LYS B 2 255 ? 123.084 112.513 104.739 1.00 59.56  ? 255 LYS B CG    1 
ATOM   4243 C  CD    . LYS B 2 255 ? 124.564 112.451 104.346 1.00 63.67  ? 255 LYS B CD    1 
ATOM   4244 C  CE    . LYS B 2 255 ? 124.983 113.694 103.578 1.00 63.39  ? 255 LYS B CE    1 
ATOM   4245 N  NZ    . LYS B 2 255 ? 126.463 113.847 103.547 1.00 63.28  ? 255 LYS B NZ    1 
ATOM   4246 N  N     . LEU B 2 256 ? 124.883 115.439 107.049 1.00 56.66  ? 256 LEU B N     1 
ATOM   4247 C  CA    . LEU B 2 256 ? 126.257 115.595 107.514 1.00 55.29  ? 256 LEU B CA    1 
ATOM   4248 C  C     . LEU B 2 256 ? 126.345 115.504 109.033 1.00 52.46  ? 256 LEU B C     1 
ATOM   4249 O  O     . LEU B 2 256 ? 127.261 114.874 109.572 1.00 58.06  ? 256 LEU B O     1 
ATOM   4250 C  CB    . LEU B 2 256 ? 126.825 116.928 107.023 1.00 54.93  ? 256 LEU B CB    1 
ATOM   4251 C  CG    . LEU B 2 256 ? 128.277 116.928 106.546 1.00 54.27  ? 256 LEU B CG    1 
ATOM   4252 C  CD1   . LEU B 2 256 ? 128.465 115.916 105.434 1.00 53.76  ? 256 LEU B CD1   1 
ATOM   4253 C  CD2   . LEU B 2 256 ? 128.684 118.313 106.081 1.00 55.33  ? 256 LEU B CD2   1 
ATOM   4254 N  N     . ASP B 2 257 ? 125.397 116.123 109.740 1.00 56.80  ? 257 ASP B N     1 
ATOM   4255 C  CA    . ASP B 2 257 ? 125.442 116.147 111.196 1.00 54.85  ? 257 ASP B CA    1 
ATOM   4256 C  C     . ASP B 2 257 ? 124.909 114.871 111.837 1.00 55.54  ? 257 ASP B C     1 
ATOM   4257 O  O     . ASP B 2 257 ? 125.129 114.663 113.034 1.00 58.71  ? 257 ASP B O     1 
ATOM   4258 C  CB    . ASP B 2 257 ? 124.655 117.350 111.720 1.00 53.61  ? 257 ASP B CB    1 
ATOM   4259 C  CG    . ASP B 2 257 ? 125.552 118.435 112.278 1.00 61.83  ? 257 ASP B CG    1 
ATOM   4260 O  OD1   . ASP B 2 257 ? 126.786 118.238 112.296 1.00 59.83  ? 257 ASP B OD1   1 
ATOM   4261 O  OD2   . ASP B 2 257 ? 125.025 119.486 112.699 1.00 62.78  ? 257 ASP B OD2   1 
ATOM   4262 N  N     . GLU B 2 258 ? 124.203 114.029 111.077 1.00 61.80  ? 258 GLU B N     1 
ATOM   4263 C  CA    . GLU B 2 258 ? 123.667 112.788 111.632 1.00 62.14  ? 258 GLU B CA    1 
ATOM   4264 C  C     . GLU B 2 258 ? 124.776 111.800 111.976 1.00 63.12  ? 258 GLU B C     1 
ATOM   4265 O  O     . GLU B 2 258 ? 124.760 111.191 113.053 1.00 65.49  ? 258 GLU B O     1 
ATOM   4266 C  CB    . GLU B 2 258 ? 122.677 112.173 110.642 1.00 61.98  ? 258 GLU B CB    1 
ATOM   4267 C  CG    . GLU B 2 258 ? 122.294 110.734 110.922 1.00 63.96  ? 258 GLU B CG    1 
ATOM   4268 C  CD    . GLU B 2 258 ? 121.071 110.301 110.140 1.00 68.86  ? 258 GLU B CD    1 
ATOM   4269 O  OE1   . GLU B 2 258 ? 120.950 110.694 108.961 1.00 68.29  ? 258 GLU B OE1   1 
ATOM   4270 O  OE2   . GLU B 2 258 ? 120.232 109.568 110.704 1.00 68.94  ? 258 GLU B OE2   1 
ATOM   4271 N  N     . SER B 2 259 ? 125.754 111.638 111.085 1.00 54.53  ? 259 SER B N     1 
ATOM   4272 C  CA    . SER B 2 259 ? 126.863 110.725 111.324 1.00 51.96  ? 259 SER B CA    1 
ATOM   4273 C  C     . SER B 2 259 ? 127.849 111.236 112.366 1.00 49.23  ? 259 SER B C     1 
ATOM   4274 O  O     . SER B 2 259 ? 128.562 110.426 112.967 1.00 54.60  ? 259 SER B O     1 
ATOM   4275 C  CB    . SER B 2 259 ? 127.605 110.447 110.015 1.00 50.88  ? 259 SER B CB    1 
ATOM   4276 O  OG    . SER B 2 259 ? 128.217 111.624 109.516 1.00 53.76  ? 259 SER B OG    1 
ATOM   4277 N  N     . ARG B 2 260 ? 127.904 112.546 112.601 1.00 39.01  ? 260 ARG B N     1 
ATOM   4278 C  CA    . ARG B 2 260 ? 128.856 113.113 113.547 1.00 32.04  ? 260 ARG B CA    1 
ATOM   4279 C  C     . ARG B 2 260 ? 128.406 112.993 114.995 1.00 34.36  ? 260 ARG B C     1 
ATOM   4280 O  O     . ARG B 2 260 ? 129.216 113.203 115.903 1.00 36.60  ? 260 ARG B O     1 
ATOM   4281 C  CB    . ARG B 2 260 ? 129.109 114.586 113.220 1.00 32.47  ? 260 ARG B CB    1 
ATOM   4282 C  CG    . ARG B 2 260 ? 130.328 114.837 112.357 1.00 29.13  ? 260 ARG B CG    1 
ATOM   4283 C  CD    . ARG B 2 260 ? 130.457 116.311 112.036 1.00 33.93  ? 260 ARG B CD    1 
ATOM   4284 N  NE    . ARG B 2 260 ? 131.739 116.855 112.461 1.00 33.57  ? 260 ARG B NE    1 
ATOM   4285 C  CZ    . ARG B 2 260 ? 132.215 118.030 112.076 1.00 27.18  ? 260 ARG B CZ    1 
ATOM   4286 N  NH1   . ARG B 2 260 ? 131.536 118.816 111.259 1.00 29.43  ? 260 ARG B NH1   1 
ATOM   4287 N  NH2   . ARG B 2 260 ? 133.401 118.428 112.526 1.00 33.29  ? 260 ARG B NH2   1 
ATOM   4288 N  N     . PHE B 2 261 ? 127.140 112.664 115.235 1.00 44.74  ? 261 PHE B N     1 
ATOM   4289 C  CA    . PHE B 2 261 ? 126.602 112.524 116.582 1.00 37.76  ? 261 PHE B CA    1 
ATOM   4290 C  C     . PHE B 2 261 ? 126.255 111.064 116.839 1.00 42.02  ? 261 PHE B C     1 
ATOM   4291 O  O     . PHE B 2 261 ? 125.674 110.398 115.976 1.00 46.68  ? 261 PHE B O     1 
ATOM   4292 C  CB    . PHE B 2 261 ? 125.367 113.404 116.774 1.00 37.49  ? 261 PHE B CB    1 
ATOM   4293 C  CG    . PHE B 2 261 ? 125.681 114.851 117.031 1.00 36.38  ? 261 PHE B CG    1 
ATOM   4294 C  CD1   . PHE B 2 261 ? 125.733 115.761 115.986 1.00 40.10  ? 261 PHE B CD1   1 
ATOM   4295 C  CD2   . PHE B 2 261 ? 125.917 115.303 118.320 1.00 39.14  ? 261 PHE B CD2   1 
ATOM   4296 C  CE1   . PHE B 2 261 ? 126.018 117.095 116.221 1.00 39.95  ? 261 PHE B CE1   1 
ATOM   4297 C  CE2   . PHE B 2 261 ? 126.201 116.634 118.563 1.00 35.54  ? 261 PHE B CE2   1 
ATOM   4298 C  CZ    . PHE B 2 261 ? 126.251 117.531 117.512 1.00 35.65  ? 261 PHE B CZ    1 
ATOM   4299 N  N     . VAL B 2 262 ? 126.613 110.570 118.026 1.00 45.09  ? 262 VAL B N     1 
ATOM   4300 C  CA    . VAL B 2 262 ? 126.429 109.171 118.384 1.00 48.23  ? 262 VAL B CA    1 
ATOM   4301 C  C     . VAL B 2 262 ? 126.353 109.073 119.906 1.00 47.18  ? 262 VAL B C     1 
ATOM   4302 O  O     . VAL B 2 262 ? 127.006 109.822 120.637 1.00 46.74  ? 262 VAL B O     1 
ATOM   4303 C  CB    . VAL B 2 262 ? 127.568 108.286 117.797 1.00 47.64  ? 262 VAL B CB    1 
ATOM   4304 C  CG1   . VAL B 2 262 ? 128.934 108.775 118.245 1.00 45.53  ? 262 VAL B CG1   1 
ATOM   4305 C  CG2   . VAL B 2 262 ? 127.377 106.791 118.083 1.00 47.32  ? 262 VAL B CG2   1 
ATOM   4306 N  N     . ILE B 2 263 ? 125.497 108.172 120.384 1.00 55.13  ? 263 ILE B N     1 
ATOM   4307 C  CA    . ILE B 2 263 ? 125.382 107.862 121.804 1.00 54.78  ? 263 ILE B CA    1 
ATOM   4308 C  C     . ILE B 2 263 ? 126.330 106.710 122.110 1.00 54.75  ? 263 ILE B C     1 
ATOM   4309 O  O     . ILE B 2 263 ? 126.165 105.603 121.582 1.00 56.80  ? 263 ILE B O     1 
ATOM   4310 C  CB    . ILE B 2 263 ? 123.939 107.506 122.194 1.00 53.21  ? 263 ILE B CB    1 
ATOM   4311 C  CG1   . ILE B 2 263 ? 123.009 108.706 121.961 1.00 50.28  ? 263 ILE B CG1   1 
ATOM   4312 C  CG2   . ILE B 2 263 ? 123.885 106.983 123.630 1.00 52.99  ? 263 ILE B CG2   1 
ATOM   4313 C  CD1   . ILE B 2 263 ? 122.941 109.695 123.110 1.00 54.82  ? 263 ILE B CD1   1 
ATOM   4314 N  N     . LYS B 2 264 ? 127.323 106.970 122.955 1.00 56.14  ? 264 LYS B N     1 
ATOM   4315 C  CA    . LYS B 2 264 ? 128.264 105.937 123.373 1.00 55.40  ? 264 LYS B CA    1 
ATOM   4316 C  C     . LYS B 2 264 ? 128.804 106.229 124.768 1.00 57.35  ? 264 LYS B C     1 
ATOM   4317 O  O     . LYS B 2 264 ? 129.379 105.354 125.416 1.00 58.22  ? 264 LYS B O     1 
ATOM   4318 C  CB    . LYS B 2 264 ? 129.422 105.814 122.381 1.00 55.69  ? 264 LYS B CB    1 
ATOM   4319 C  CG    . LYS B 2 264 ? 129.867 107.124 121.763 1.00 56.31  ? 264 LYS B CG    1 
ATOM   4320 C  CD    . LYS B 2 264 ? 131.151 106.957 120.966 1.00 55.36  ? 264 LYS B CD    1 
ATOM   4321 C  CE    . LYS B 2 264 ? 132.275 106.413 121.832 1.00 55.08  ? 264 LYS B CE    1 
ATOM   4322 N  NZ    . LYS B 2 264 ? 133.525 106.209 121.051 1.00 59.02  ? 264 LYS B NZ    1 
ATOM   4323 O  OXT   . LYS B 2 264 ? 128.676 107.344 125.273 1.00 58.15  ? 264 LYS B OXT   1 
ATOM   4324 N  N     . MET C 1 27  ? 119.485 167.934 139.566 1.00 59.80  ? 1   MET C N     1 
ATOM   4325 C  CA    . MET C 1 27  ? 118.112 167.495 139.766 1.00 61.27  ? 1   MET C CA    1 
ATOM   4326 C  C     . MET C 1 27  ? 117.614 166.733 138.537 1.00 60.53  ? 1   MET C C     1 
ATOM   4327 O  O     . MET C 1 27  ? 116.766 165.849 138.646 1.00 59.19  ? 1   MET C O     1 
ATOM   4328 C  CB    . MET C 1 27  ? 117.177 168.679 140.085 1.00 61.77  ? 1   MET C CB    1 
ATOM   4329 C  CG    . MET C 1 27  ? 117.023 169.767 139.007 1.00 61.27  ? 1   MET C CG    1 
ATOM   4330 S  SD    . MET C 1 27  ? 118.478 170.277 138.063 1.00 75.19  ? 1   MET C SD    1 
ATOM   4331 C  CE    . MET C 1 27  ? 119.393 171.230 139.282 1.00 60.38  ? 1   MET C CE    1 
ATOM   4332 N  N     . SER C 1 28  ? 118.152 167.079 137.365 1.00 53.91  ? 2   SER C N     1 
ATOM   4333 C  CA    . SER C 1 28  ? 117.851 166.324 136.156 1.00 47.92  ? 2   SER C CA    1 
ATOM   4334 C  C     . SER C 1 28  ? 118.607 165.004 136.118 1.00 46.90  ? 2   SER C C     1 
ATOM   4335 O  O     . SER C 1 28  ? 118.134 164.042 135.502 1.00 52.66  ? 2   SER C O     1 
ATOM   4336 C  CB    . SER C 1 28  ? 118.182 167.159 134.918 1.00 53.91  ? 2   SER C CB    1 
ATOM   4337 O  OG    . SER C 1 28  ? 117.339 166.818 133.833 1.00 55.75  ? 2   SER C OG    1 
ATOM   4338 N  N     . ALA C 1 29  ? 119.775 164.949 136.766 1.00 44.23  ? 3   ALA C N     1 
ATOM   4339 C  CA    . ALA C 1 29  ? 120.535 163.707 136.863 1.00 39.19  ? 3   ALA C CA    1 
ATOM   4340 C  C     . ALA C 1 29  ? 119.791 162.665 137.686 1.00 43.20  ? 3   ALA C C     1 
ATOM   4341 O  O     . ALA C 1 29  ? 119.779 161.476 137.336 1.00 45.84  ? 3   ALA C O     1 
ATOM   4342 C  CB    . ALA C 1 29  ? 121.907 163.991 137.473 1.00 37.63  ? 3   ALA C CB    1 
ATOM   4343 N  N     . ILE C 1 30  ? 119.162 163.104 138.783 1.00 43.16  ? 4   ILE C N     1 
ATOM   4344 C  CA    . ILE C 1 30  ? 118.395 162.211 139.651 1.00 39.10  ? 4   ILE C CA    1 
ATOM   4345 C  C     . ILE C 1 30  ? 117.212 161.625 138.898 1.00 39.72  ? 4   ILE C C     1 
ATOM   4346 O  O     . ILE C 1 30  ? 116.976 160.412 138.927 1.00 47.33  ? 4   ILE C O     1 
ATOM   4347 C  CB    . ILE C 1 30  ? 117.932 162.964 140.909 1.00 44.40  ? 4   ILE C CB    1 
ATOM   4348 C  CG1   . ILE C 1 30  ? 119.135 163.563 141.629 1.00 42.36  ? 4   ILE C CG1   1 
ATOM   4349 C  CG2   . ILE C 1 30  ? 117.131 162.049 141.829 1.00 39.85  ? 4   ILE C CG2   1 
ATOM   4350 C  CD1   . ILE C 1 30  ? 120.013 162.532 142.229 1.00 43.55  ? 4   ILE C CD1   1 
ATOM   4351 N  N     . GLY C 1 31  ? 116.472 162.482 138.189 1.00 38.30  ? 5   GLY C N     1 
ATOM   4352 C  CA    . GLY C 1 31  ? 115.334 162.014 137.416 1.00 39.18  ? 5   GLY C CA    1 
ATOM   4353 C  C     . GLY C 1 31  ? 115.736 161.125 136.257 1.00 39.99  ? 5   GLY C C     1 
ATOM   4354 O  O     . GLY C 1 31  ? 115.041 160.158 135.940 1.00 44.09  ? 5   GLY C O     1 
ATOM   4355 N  N     . THR C 1 32  ? 116.885 161.417 135.637 1.00 38.55  ? 6   THR C N     1 
ATOM   4356 C  CA    . THR C 1 32  ? 117.368 160.600 134.527 1.00 37.21  ? 6   THR C CA    1 
ATOM   4357 C  C     . THR C 1 32  ? 117.751 159.198 134.989 1.00 38.55  ? 6   THR C C     1 
ATOM   4358 O  O     . THR C 1 32  ? 117.311 158.202 134.403 1.00 46.14  ? 6   THR C O     1 
ATOM   4359 C  CB    . THR C 1 32  ? 118.554 161.282 133.848 1.00 40.02  ? 6   THR C CB    1 
ATOM   4360 O  OG1   . THR C 1 32  ? 118.235 162.654 133.589 1.00 45.60  ? 6   THR C OG1   1 
ATOM   4361 C  CG2   . THR C 1 32  ? 118.879 160.589 132.538 1.00 35.72  ? 6   THR C CG2   1 
ATOM   4362 N  N     . VAL C 1 33  ? 118.552 159.104 136.058 1.00 36.04  ? 7   VAL C N     1 
ATOM   4363 C  CA    . VAL C 1 33  ? 118.982 157.800 136.564 1.00 31.03  ? 7   VAL C CA    1 
ATOM   4364 C  C     . VAL C 1 33  ? 117.794 157.026 137.133 1.00 33.98  ? 7   VAL C C     1 
ATOM   4365 O  O     . VAL C 1 33  ? 117.666 155.809 136.920 1.00 39.09  ? 7   VAL C O     1 
ATOM   4366 C  CB    . VAL C 1 33  ? 120.115 157.985 137.595 1.00 36.53  ? 7   VAL C CB    1 
ATOM   4367 C  CG1   . VAL C 1 33  ? 120.463 156.679 138.295 1.00 35.46  ? 7   VAL C CG1   1 
ATOM   4368 C  CG2   . VAL C 1 33  ? 121.350 158.555 136.915 1.00 30.18  ? 7   VAL C CG2   1 
ATOM   4369 N  N     . PHE C 1 34  ? 116.870 157.732 137.798 1.00 37.35  ? 8   PHE C N     1 
ATOM   4370 C  CA    . PHE C 1 34  ? 115.669 157.097 138.331 1.00 31.70  ? 8   PHE C CA    1 
ATOM   4371 C  C     . PHE C 1 34  ? 114.776 156.552 137.221 1.00 36.23  ? 8   PHE C C     1 
ATOM   4372 O  O     . PHE C 1 34  ? 114.253 155.437 137.334 1.00 45.55  ? 8   PHE C O     1 
ATOM   4373 C  CB    . PHE C 1 34  ? 114.901 158.093 139.200 1.00 34.97  ? 8   PHE C CB    1 
ATOM   4374 C  CG    . PHE C 1 34  ? 113.673 157.517 139.847 1.00 40.33  ? 8   PHE C CG    1 
ATOM   4375 C  CD1   . PHE C 1 34  ? 113.784 156.658 140.930 1.00 39.97  ? 8   PHE C CD1   1 
ATOM   4376 C  CD2   . PHE C 1 34  ? 112.409 157.842 139.379 1.00 38.62  ? 8   PHE C CD2   1 
ATOM   4377 C  CE1   . PHE C 1 34  ? 112.656 156.128 141.530 1.00 40.61  ? 8   PHE C CE1   1 
ATOM   4378 C  CE2   . PHE C 1 34  ? 111.277 157.315 139.975 1.00 40.75  ? 8   PHE C CE2   1 
ATOM   4379 C  CZ    . PHE C 1 34  ? 111.402 156.458 141.052 1.00 38.53  ? 8   PHE C CZ    1 
ATOM   4380 N  N     . LYS C 1 35  ? 114.617 157.300 136.121 1.00 38.90  ? 9   LYS C N     1 
ATOM   4381 C  CA    . LYS C 1 35  ? 113.759 156.803 135.053 1.00 36.57  ? 9   LYS C CA    1 
ATOM   4382 C  C     . LYS C 1 35  ? 114.424 155.652 134.301 1.00 40.49  ? 9   LYS C C     1 
ATOM   4383 O  O     . LYS C 1 35  ? 113.747 154.682 133.943 1.00 44.24  ? 9   LYS C O     1 
ATOM   4384 C  CB    . LYS C 1 35  ? 113.323 157.945 134.119 1.00 36.05  ? 9   LYS C CB    1 
ATOM   4385 C  CG    . LYS C 1 35  ? 114.161 158.241 132.879 1.00 44.10  ? 9   LYS C CG    1 
ATOM   4386 C  CD    . LYS C 1 35  ? 114.237 159.733 132.595 1.00 48.00  ? 9   LYS C CD    1 
ATOM   4387 C  CE    . LYS C 1 35  ? 115.271 160.036 131.522 1.00 49.04  ? 9   LYS C CE    1 
ATOM   4388 N  NZ    . LYS C 1 35  ? 115.446 161.498 131.320 1.00 46.55  ? 9   LYS C NZ    1 
ATOM   4389 N  N     . GLU C 1 36  ? 115.757 155.688 134.134 1.00 37.35  ? 10  GLU C N     1 
ATOM   4390 C  CA    . GLU C 1 36  ? 116.442 154.562 133.497 1.00 37.26  ? 10  GLU C CA    1 
ATOM   4391 C  C     . GLU C 1 36  ? 116.420 153.321 134.381 1.00 38.78  ? 10  GLU C C     1 
ATOM   4392 O  O     . GLU C 1 36  ? 116.550 152.196 133.885 1.00 47.60  ? 10  GLU C O     1 
ATOM   4393 C  CB    . GLU C 1 36  ? 117.884 154.919 133.138 1.00 36.15  ? 10  GLU C CB    1 
ATOM   4394 C  CG    . GLU C 1 36  ? 118.051 156.040 132.133 1.00 42.45  ? 10  GLU C CG    1 
ATOM   4395 C  CD    . GLU C 1 36  ? 119.480 156.164 131.642 1.00 47.65  ? 10  GLU C CD    1 
ATOM   4396 O  OE1   . GLU C 1 36  ? 119.695 156.121 130.413 1.00 51.29  ? 10  GLU C OE1   1 
ATOM   4397 O  OE2   . GLU C 1 36  ? 120.388 156.292 132.488 1.00 42.94  ? 10  GLU C OE2   1 
ATOM   4398 N  N     . HIS C 1 37  ? 116.258 153.501 135.691 1.00 34.67  ? 11  HIS C N     1 
ATOM   4399 C  CA    . HIS C 1 37  ? 116.111 152.336 136.553 1.00 30.63  ? 11  HIS C CA    1 
ATOM   4400 C  C     . HIS C 1 37  ? 114.672 151.828 136.587 1.00 32.71  ? 11  HIS C C     1 
ATOM   4401 O  O     . HIS C 1 37  ? 114.444 150.632 136.802 1.00 39.12  ? 11  HIS C O     1 
ATOM   4402 C  CB    . HIS C 1 37  ? 116.619 152.657 137.954 1.00 26.14  ? 11  HIS C CB    1 
ATOM   4403 C  CG    . HIS C 1 37  ? 118.090 152.449 138.113 1.00 23.44  ? 11  HIS C CG    1 
ATOM   4404 N  ND1   . HIS C 1 37  ? 119.019 153.385 137.720 1.00 30.50  ? 11  HIS C ND1   1 
ATOM   4405 C  CD2   . HIS C 1 37  ? 118.794 151.404 138.606 1.00 30.35  ? 11  HIS C CD2   1 
ATOM   4406 C  CE1   . HIS C 1 37  ? 120.232 152.930 137.970 1.00 27.25  ? 11  HIS C CE1   1 
ATOM   4407 N  NE2   . HIS C 1 37  ? 120.124 151.729 138.509 1.00 30.16  ? 11  HIS C NE2   1 
ATOM   4408 N  N     . VAL C 1 38  ? 113.683 152.703 136.376 1.00 38.17  ? 12  VAL C N     1 
ATOM   4409 C  CA    . VAL C 1 38  ? 112.308 152.215 136.498 1.00 33.27  ? 12  VAL C CA    1 
ATOM   4410 C  C     . VAL C 1 38  ? 111.699 151.706 135.191 1.00 39.19  ? 12  VAL C C     1 
ATOM   4411 O  O     . VAL C 1 38  ? 110.722 150.949 135.254 1.00 45.40  ? 12  VAL C O     1 
ATOM   4412 C  CB    . VAL C 1 38  ? 111.344 153.248 137.114 1.00 40.04  ? 12  VAL C CB    1 
ATOM   4413 C  CG1   . VAL C 1 38  ? 111.795 153.648 138.513 1.00 35.10  ? 12  VAL C CG1   1 
ATOM   4414 C  CG2   . VAL C 1 38  ? 111.167 154.451 136.213 1.00 42.71  ? 12  VAL C CG2   1 
ATOM   4415 N  N     . LYS C 1 39  ? 112.213 152.065 134.006 1.00 37.11  ? 13  LYS C N     1 
ATOM   4416 C  CA    . LYS C 1 39  ? 111.663 151.362 132.839 1.00 39.60  ? 13  LYS C CA    1 
ATOM   4417 C  C     . LYS C 1 39  ? 112.486 150.150 132.422 1.00 41.03  ? 13  LYS C C     1 
ATOM   4418 O  O     . LYS C 1 39  ? 112.187 149.553 131.383 1.00 47.49  ? 13  LYS C O     1 
ATOM   4419 C  CB    . LYS C 1 39  ? 111.481 152.247 131.589 1.00 44.69  ? 13  LYS C CB    1 
ATOM   4420 C  CG    . LYS C 1 39  ? 112.240 153.523 131.489 1.00 45.46  ? 13  LYS C CG    1 
ATOM   4421 C  CD    . LYS C 1 39  ? 112.055 154.201 130.145 1.00 47.27  ? 13  LYS C CD    1 
ATOM   4422 C  CE    . LYS C 1 39  ? 112.683 155.586 130.147 1.00 48.35  ? 13  LYS C CE    1 
ATOM   4423 N  NZ    . LYS C 1 39  ? 114.161 155.526 130.358 1.00 44.14  ? 13  LYS C NZ    1 
ATOM   4424 N  N     . ASN C 1 40  ? 113.507 149.769 133.183 1.00 37.54  ? 14  ASN C N     1 
ATOM   4425 C  CA    . ASN C 1 40  ? 114.377 148.660 132.805 1.00 33.30  ? 14  ASN C CA    1 
ATOM   4426 C  C     . ASN C 1 40  ? 114.510 147.655 133.936 1.00 32.92  ? 14  ASN C C     1 
ATOM   4427 O  O     . ASN C 1 40  ? 115.565 147.043 134.121 1.00 41.61  ? 14  ASN C O     1 
ATOM   4428 C  CB    . ASN C 1 40  ? 115.749 149.168 132.371 1.00 32.69  ? 14  ASN C CB    1 
ATOM   4429 C  CG    . ASN C 1 40  ? 115.668 150.162 131.234 1.00 33.88  ? 14  ASN C CG    1 
ATOM   4430 O  OD1   . ASN C 1 40  ? 115.482 149.786 130.080 1.00 41.02  ? 14  ASN C OD1   1 
ATOM   4431 N  ND2   . ASN C 1 40  ? 115.806 151.441 131.555 1.00 33.88  ? 14  ASN C ND2   1 
ATOM   4432 N  N     . PHE C 1 41  ? 113.430 147.452 134.693 1.00 33.86  ? 15  PHE C N     1 
ATOM   4433 C  CA    . PHE C 1 41  ? 113.455 146.539 135.836 1.00 32.81  ? 15  PHE C CA    1 
ATOM   4434 C  C     . PHE C 1 41  ? 113.600 145.085 135.388 1.00 34.43  ? 15  PHE C C     1 
ATOM   4435 O  O     . PHE C 1 41  ? 114.411 144.325 135.942 1.00 36.37  ? 15  PHE C O     1 
ATOM   4436 C  CB    . PHE C 1 41  ? 112.186 146.753 136.664 1.00 35.92  ? 15  PHE C CB    1 
ATOM   4437 C  CG    . PHE C 1 41  ? 112.122 145.935 137.917 1.00 38.76  ? 15  PHE C CG    1 
ATOM   4438 C  CD1   . PHE C 1 41  ? 112.972 146.196 138.980 1.00 38.26  ? 15  PHE C CD1   1 
ATOM   4439 C  CD2   . PHE C 1 41  ? 111.172 144.935 138.053 1.00 38.57  ? 15  PHE C CD2   1 
ATOM   4440 C  CE1   . PHE C 1 41  ? 112.903 145.448 140.140 1.00 35.18  ? 15  PHE C CE1   1 
ATOM   4441 C  CE2   . PHE C 1 41  ? 111.094 144.186 139.211 1.00 39.03  ? 15  PHE C CE2   1 
ATOM   4442 C  CZ    . PHE C 1 41  ? 111.960 144.442 140.255 1.00 37.10  ? 15  PHE C CZ    1 
ATOM   4443 N  N     . TYR C 1 42  ? 112.841 144.693 134.358 1.00 31.11  ? 16  TYR C N     1 
ATOM   4444 C  CA    . TYR C 1 42  ? 112.961 143.348 133.798 1.00 32.28  ? 16  TYR C CA    1 
ATOM   4445 C  C     . TYR C 1 42  ? 114.322 143.139 133.146 1.00 25.63  ? 16  TYR C C     1 
ATOM   4446 O  O     . TYR C 1 42  ? 114.893 142.044 133.225 1.00 38.47  ? 16  TYR C O     1 
ATOM   4447 C  CB    . TYR C 1 42  ? 111.840 143.096 132.788 1.00 28.18  ? 16  TYR C CB    1 
ATOM   4448 C  CG    . TYR C 1 42  ? 112.047 141.850 131.956 1.00 33.63  ? 16  TYR C CG    1 
ATOM   4449 C  CD1   . TYR C 1 42  ? 111.926 140.587 132.524 1.00 33.90  ? 16  TYR C CD1   1 
ATOM   4450 C  CD2   . TYR C 1 42  ? 112.377 141.933 130.607 1.00 36.74  ? 16  TYR C CD2   1 
ATOM   4451 C  CE1   . TYR C 1 42  ? 112.121 139.445 131.775 1.00 34.09  ? 16  TYR C CE1   1 
ATOM   4452 C  CE2   . TYR C 1 42  ? 112.577 140.793 129.850 1.00 35.60  ? 16  TYR C CE2   1 
ATOM   4453 C  CZ    . TYR C 1 42  ? 112.446 139.554 130.441 1.00 38.37  ? 16  TYR C CZ    1 
ATOM   4454 O  OH    . TYR C 1 42  ? 112.640 138.416 129.695 1.00 43.83  ? 16  TYR C OH    1 
ATOM   4455 N  N     . LEU C 1 43  ? 114.847 144.180 132.492 1.00 26.64  ? 17  LEU C N     1 
ATOM   4456 C  CA    . LEU C 1 43  ? 116.174 144.112 131.888 1.00 26.79  ? 17  LEU C CA    1 
ATOM   4457 C  C     . LEU C 1 43  ? 117.256 143.908 132.942 1.00 25.88  ? 17  LEU C C     1 
ATOM   4458 O  O     . LEU C 1 43  ? 118.172 143.102 132.745 1.00 35.37  ? 17  LEU C O     1 
ATOM   4459 C  CB    . LEU C 1 43  ? 116.442 145.384 131.082 1.00 27.25  ? 17  LEU C CB    1 
ATOM   4460 C  CG    . LEU C 1 43  ? 117.788 145.528 130.372 1.00 24.39  ? 17  LEU C CG    1 
ATOM   4461 C  CD1   . LEU C 1 43  ? 118.042 144.362 129.440 1.00 24.74  ? 17  LEU C CD1   1 
ATOM   4462 C  CD2   . LEU C 1 43  ? 117.845 146.837 129.612 1.00 27.02  ? 17  LEU C CD2   1 
ATOM   4463 N  N     . ILE C 1 44  ? 117.137 144.607 134.077 1.00 19.25  ? 18  ILE C N     1 
ATOM   4464 C  CA    . ILE C 1 44  ? 118.080 144.450 135.185 1.00 24.39  ? 18  ILE C CA    1 
ATOM   4465 C  C     . ILE C 1 44  ? 118.027 143.030 135.739 1.00 22.03  ? 18  ILE C C     1 
ATOM   4466 O  O     . ILE C 1 44  ? 119.068 142.392 135.947 1.00 32.38  ? 18  ILE C O     1 
ATOM   4467 C  CB    . ILE C 1 44  ? 117.798 145.503 136.277 1.00 33.34  ? 18  ILE C CB    1 
ATOM   4468 C  CG1   . ILE C 1 44  ? 118.327 146.873 135.857 1.00 31.40  ? 18  ILE C CG1   1 
ATOM   4469 C  CG2   . ILE C 1 44  ? 118.415 145.112 137.615 1.00 22.64  ? 18  ILE C CG2   1 
ATOM   4470 C  CD1   . ILE C 1 44  ? 117.656 148.027 136.570 1.00 22.91  ? 18  ILE C CD1   1 
ATOM   4471 N  N     . GLN C 1 45  ? 116.811 142.498 135.932 1.00 29.14  ? 19  GLN C N     1 
ATOM   4472 C  CA    . GLN C 1 45  ? 116.660 141.149 136.482 1.00 31.94  ? 19  GLN C CA    1 
ATOM   4473 C  C     . GLN C 1 45  ? 117.214 140.082 135.539 1.00 30.86  ? 19  GLN C C     1 
ATOM   4474 O  O     . GLN C 1 45  ? 117.921 139.160 135.970 1.00 34.84  ? 19  GLN C O     1 
ATOM   4475 C  CB    . GLN C 1 45  ? 115.189 140.866 136.787 1.00 32.26  ? 19  GLN C CB    1 
ATOM   4476 C  CG    . GLN C 1 45  ? 114.637 141.613 137.978 1.00 30.81  ? 19  GLN C CG    1 
ATOM   4477 C  CD    . GLN C 1 45  ? 113.125 141.646 137.974 1.00 44.19  ? 19  GLN C CD    1 
ATOM   4478 O  OE1   . GLN C 1 45  ? 112.508 142.211 137.072 1.00 44.36  ? 19  GLN C OE1   1 
ATOM   4479 N  NE2   . GLN C 1 45  ? 112.516 141.042 138.987 1.00 40.58  ? 19  GLN C NE2   1 
ATOM   4480 N  N     . ARG C 1 46  ? 116.923 140.205 134.241 1.00 25.44  ? 20  ARG C N     1 
ATOM   4481 C  CA    . ARG C 1 46  ? 117.368 139.198 133.282 1.00 24.65  ? 20  ARG C CA    1 
ATOM   4482 C  C     . ARG C 1 46  ? 118.876 139.261 133.058 1.00 22.49  ? 20  ARG C C     1 
ATOM   4483 O  O     . ARG C 1 46  ? 119.533 138.217 132.938 1.00 32.55  ? 20  ARG C O     1 
ATOM   4484 C  CB    . ARG C 1 46  ? 116.612 139.365 131.965 1.00 25.01  ? 20  ARG C CB    1 
ATOM   4485 C  CG    . ARG C 1 46  ? 116.449 138.079 131.179 1.00 30.94  ? 20  ARG C CG    1 
ATOM   4486 C  CD    . ARG C 1 46  ? 115.769 136.994 131.990 1.00 29.78  ? 20  ARG C CD    1 
ATOM   4487 N  NE    . ARG C 1 46  ? 115.629 135.767 131.216 1.00 32.08  ? 20  ARG C NE    1 
ATOM   4488 C  CZ    . ARG C 1 46  ? 116.490 134.759 131.253 1.00 34.11  ? 20  ARG C CZ    1 
ATOM   4489 N  NH1   . ARG C 1 46  ? 117.560 134.791 132.029 1.00 36.88  ? 20  ARG C NH1   1 
ATOM   4490 N  NH2   . ARG C 1 46  ? 116.271 133.693 130.489 1.00 31.35  ? 20  ARG C NH2   1 
ATOM   4491 N  N     . LEU C 1 47  ? 119.450 140.469 133.022 1.00 19.23  ? 21  LEU C N     1 
ATOM   4492 C  CA    . LEU C 1 47  ? 120.898 140.589 132.886 1.00 23.02  ? 21  LEU C CA    1 
ATOM   4493 C  C     . LEU C 1 47  ? 121.618 140.106 134.143 1.00 22.89  ? 21  LEU C C     1 
ATOM   4494 O  O     . LEU C 1 47  ? 122.719 139.551 134.053 1.00 29.07  ? 21  LEU C O     1 
ATOM   4495 C  CB    . LEU C 1 47  ? 121.281 142.032 132.557 1.00 26.07  ? 21  LEU C CB    1 
ATOM   4496 C  CG    . LEU C 1 47  ? 120.993 142.565 131.146 1.00 27.39  ? 21  LEU C CG    1 
ATOM   4497 C  CD1   . LEU C 1 47  ? 121.864 143.774 130.834 1.00 22.43  ? 21  LEU C CD1   1 
ATOM   4498 C  CD2   . LEU C 1 47  ? 121.147 141.497 130.075 1.00 25.74  ? 21  LEU C CD2   1 
ATOM   4499 N  N     . ALA C 1 48  ? 121.006 140.289 135.320 1.00 21.70  ? 22  ALA C N     1 
ATOM   4500 C  CA    . ALA C 1 48  ? 121.583 139.756 136.550 1.00 21.14  ? 22  ALA C CA    1 
ATOM   4501 C  C     . ALA C 1 48  ? 121.564 138.232 136.561 1.00 21.41  ? 22  ALA C C     1 
ATOM   4502 O  O     . ALA C 1 48  ? 122.527 137.595 137.008 1.00 37.58  ? 22  ALA C O     1 
ATOM   4503 C  CB    . ALA C 1 48  ? 120.833 140.308 137.760 1.00 23.22  ? 22  ALA C CB    1 
ATOM   4504 N  N     . GLN C 1 49  ? 120.474 137.632 136.066 1.00 25.94  ? 23  GLN C N     1 
ATOM   4505 C  CA    . GLN C 1 49  ? 120.407 136.177 135.940 1.00 22.46  ? 23  GLN C CA    1 
ATOM   4506 C  C     . GLN C 1 49  ? 121.455 135.652 134.964 1.00 28.13  ? 23  GLN C C     1 
ATOM   4507 O  O     . GLN C 1 49  ? 122.101 134.625 135.223 1.00 34.98  ? 23  GLN C O     1 
ATOM   4508 C  CB    . GLN C 1 49  ? 119.008 135.755 135.493 1.00 25.63  ? 23  GLN C CB    1 
ATOM   4509 C  CG    . GLN C 1 49  ? 117.957 135.815 136.580 1.00 28.40  ? 23  GLN C CG    1 
ATOM   4510 C  CD    . GLN C 1 49  ? 116.550 135.750 136.027 1.00 33.86  ? 23  GLN C CD    1 
ATOM   4511 O  OE1   . GLN C 1 49  ? 115.871 136.768 135.898 1.00 37.82  ? 23  GLN C OE1   1 
ATOM   4512 N  NE2   . GLN C 1 49  ? 116.106 134.548 135.688 1.00 33.82  ? 23  GLN C NE2   1 
ATOM   4513 N  N     . PHE C 1 50  ? 121.651 136.360 133.847 1.00 26.21  ? 24  PHE C N     1 
ATOM   4514 C  CA    . PHE C 1 50  ? 122.682 135.978 132.886 1.00 16.02  ? 24  PHE C CA    1 
ATOM   4515 C  C     . PHE C 1 50  ? 124.080 136.107 133.478 1.00 23.75  ? 24  PHE C C     1 
ATOM   4516 O  O     . PHE C 1 50  ? 124.952 135.282 133.197 1.00 33.55  ? 24  PHE C O     1 
ATOM   4517 C  CB    . PHE C 1 50  ? 122.559 136.821 131.620 1.00 23.72  ? 24  PHE C CB    1 
ATOM   4518 C  CG    . PHE C 1 50  ? 121.560 136.290 130.641 1.00 28.20  ? 24  PHE C CG    1 
ATOM   4519 C  CD1   . PHE C 1 50  ? 121.554 134.946 130.304 1.00 27.94  ? 24  PHE C CD1   1 
ATOM   4520 C  CD2   . PHE C 1 50  ? 120.620 137.127 130.065 1.00 27.63  ? 24  PHE C CD2   1 
ATOM   4521 C  CE1   . PHE C 1 50  ? 120.632 134.448 129.405 1.00 24.31  ? 24  PHE C CE1   1 
ATOM   4522 C  CE2   . PHE C 1 50  ? 119.695 136.635 129.167 1.00 29.98  ? 24  PHE C CE2   1 
ATOM   4523 C  CZ    . PHE C 1 50  ? 119.703 135.294 128.837 1.00 24.82  ? 24  PHE C CZ    1 
ATOM   4524 N  N     . GLN C 1 51  ? 124.311 137.132 134.304 1.00 22.27  ? 25  GLN C N     1 
ATOM   4525 C  CA    . GLN C 1 51  ? 125.612 137.290 134.952 1.00 21.13  ? 25  GLN C CA    1 
ATOM   4526 C  C     . GLN C 1 51  ? 125.876 136.173 135.958 1.00 24.47  ? 25  GLN C C     1 
ATOM   4527 O  O     . GLN C 1 51  ? 127.008 135.676 136.060 1.00 34.28  ? 25  GLN C O     1 
ATOM   4528 C  CB    . GLN C 1 51  ? 125.694 138.662 135.626 1.00 25.82  ? 25  GLN C CB    1 
ATOM   4529 C  CG    . GLN C 1 51  ? 127.018 138.956 136.316 1.00 29.01  ? 25  GLN C CG    1 
ATOM   4530 C  CD    . GLN C 1 51  ? 128.159 139.184 135.341 1.00 33.44  ? 25  GLN C CD    1 
ATOM   4531 O  OE1   . GLN C 1 51  ? 127.944 139.499 134.171 1.00 39.29  ? 25  GLN C OE1   1 
ATOM   4532 N  NE2   . GLN C 1 51  ? 129.384 139.028 135.823 1.00 33.05  ? 25  GLN C NE2   1 
ATOM   4533 N  N     . VAL C 1 52  ? 124.836 135.762 136.695 1.00 29.28  ? 26  VAL C N     1 
ATOM   4534 C  CA    . VAL C 1 52  ? 124.939 134.624 137.611 1.00 26.29  ? 26  VAL C CA    1 
ATOM   4535 C  C     . VAL C 1 52  ? 125.295 133.350 136.848 1.00 29.12  ? 26  VAL C C     1 
ATOM   4536 O  O     . VAL C 1 52  ? 126.165 132.578 137.272 1.00 38.82  ? 26  VAL C O     1 
ATOM   4537 C  CB    . VAL C 1 52  ? 123.629 134.466 138.410 1.00 27.81  ? 26  VAL C CB    1 
ATOM   4538 C  CG1   . VAL C 1 52  ? 123.559 133.116 139.113 1.00 30.59  ? 26  VAL C CG1   1 
ATOM   4539 C  CG2   . VAL C 1 52  ? 123.499 135.566 139.426 1.00 22.89  ? 26  VAL C CG2   1 
ATOM   4540 N  N     . LYS C 1 53  ? 124.659 133.134 135.693 1.00 35.49  ? 27  LYS C N     1 
ATOM   4541 C  CA    . LYS C 1 53  ? 124.992 131.964 134.880 1.00 25.33  ? 27  LYS C CA    1 
ATOM   4542 C  C     . LYS C 1 53  ? 126.388 132.067 134.265 1.00 31.12  ? 27  LYS C C     1 
ATOM   4543 O  O     . LYS C 1 53  ? 127.041 131.043 134.032 1.00 35.66  ? 27  LYS C O     1 
ATOM   4544 C  CB    . LYS C 1 53  ? 123.941 131.766 133.788 1.00 30.02  ? 27  LYS C CB    1 
ATOM   4545 C  CG    . LYS C 1 53  ? 122.546 131.503 134.320 1.00 37.05  ? 27  LYS C CG    1 
ATOM   4546 C  CD    . LYS C 1 53  ? 121.523 131.479 133.201 1.00 37.78  ? 27  LYS C CD    1 
ATOM   4547 C  CE    . LYS C 1 53  ? 121.867 130.424 132.171 1.00 36.98  ? 27  LYS C CE    1 
ATOM   4548 N  NZ    . LYS C 1 53  ? 121.913 129.057 132.758 1.00 40.46  ? 27  LYS C NZ    1 
ATOM   4549 N  N     . ILE C 1 54  ? 126.856 133.286 133.985 1.00 39.46  ? 28  ILE C N     1 
ATOM   4550 C  CA    . ILE C 1 54  ? 128.169 133.464 133.365 1.00 27.93  ? 28  ILE C CA    1 
ATOM   4551 C  C     . ILE C 1 54  ? 129.285 133.147 134.357 1.00 26.46  ? 28  ILE C C     1 
ATOM   4552 O  O     . ILE C 1 54  ? 130.222 132.406 134.039 1.00 39.53  ? 28  ILE C O     1 
ATOM   4553 C  CB    . ILE C 1 54  ? 128.297 134.886 132.779 1.00 28.42  ? 28  ILE C CB    1 
ATOM   4554 C  CG1   . ILE C 1 54  ? 127.655 134.953 131.395 1.00 25.46  ? 28  ILE C CG1   1 
ATOM   4555 C  CG2   . ILE C 1 54  ? 129.751 135.324 132.656 1.00 24.08  ? 28  ILE C CG2   1 
ATOM   4556 C  CD1   . ILE C 1 54  ? 127.257 136.350 130.972 1.00 25.66  ? 28  ILE C CD1   1 
ATOM   4557 N  N     . ILE C 1 55  ? 129.193 133.672 135.587 1.00 29.07  ? 29  ILE C N     1 
ATOM   4558 C  CA    . ILE C 1 55  ? 130.287 133.475 136.541 1.00 30.91  ? 29  ILE C CA    1 
ATOM   4559 C  C     . ILE C 1 55  ? 130.320 132.088 137.166 1.00 32.53  ? 29  ILE C C     1 
ATOM   4560 O  O     . ILE C 1 55  ? 131.298 131.756 137.848 1.00 34.39  ? 29  ILE C O     1 
ATOM   4561 C  CB    . ILE C 1 55  ? 130.272 134.528 137.671 1.00 28.72  ? 29  ILE C CB    1 
ATOM   4562 C  CG1   . ILE C 1 55  ? 129.227 134.182 138.734 1.00 31.56  ? 29  ILE C CG1   1 
ATOM   4563 C  CG2   . ILE C 1 55  ? 130.103 135.928 137.111 1.00 33.71  ? 29  ILE C CG2   1 
ATOM   4564 C  CD1   . ILE C 1 55  ? 129.542 134.746 140.095 1.00 34.92  ? 29  ILE C CD1   1 
ATOM   4565 N  N     . ASN C 1 56  ? 129.296 131.257 136.953 1.00 32.88  ? 30  ASN C N     1 
ATOM   4566 C  CA    . ASN C 1 56  ? 129.258 129.918 137.536 1.00 31.86  ? 30  ASN C CA    1 
ATOM   4567 C  C     . ASN C 1 56  ? 129.180 128.829 136.471 1.00 37.30  ? 30  ASN C C     1 
ATOM   4568 O  O     . ASN C 1 56  ? 128.670 127.740 136.750 1.00 36.19  ? 30  ASN C O     1 
ATOM   4569 C  CB    . ASN C 1 56  ? 128.075 129.780 138.499 1.00 32.85  ? 30  ASN C CB    1 
ATOM   4570 C  CG    . ASN C 1 56  ? 128.307 130.487 139.817 1.00 36.78  ? 30  ASN C CG    1 
ATOM   4571 O  OD1   . ASN C 1 56  ? 129.209 130.134 140.574 1.00 40.27  ? 30  ASN C OD1   1 
ATOM   4572 N  ND2   . ASN C 1 56  ? 127.488 131.492 140.099 1.00 32.50  ? 30  ASN C ND2   1 
ATOM   4573 N  N     . HIS C 1 57  ? 129.673 129.100 135.258 1.00 44.81  ? 31  HIS C N     1 
ATOM   4574 C  CA    . HIS C 1 57  ? 129.387 128.223 134.125 1.00 41.25  ? 31  HIS C CA    1 
ATOM   4575 C  C     . HIS C 1 57  ? 130.188 126.926 134.179 1.00 45.12  ? 31  HIS C C     1 
ATOM   4576 O  O     . HIS C 1 57  ? 129.649 125.849 133.899 1.00 47.12  ? 31  HIS C O     1 
ATOM   4577 C  CB    . HIS C 1 57  ? 129.655 128.957 132.813 1.00 36.69  ? 31  HIS C CB    1 
ATOM   4578 C  CG    . HIS C 1 57  ? 129.567 128.077 131.606 1.00 42.76  ? 31  HIS C CG    1 
ATOM   4579 N  ND1   . HIS C 1 57  ? 128.428 127.373 131.282 1.00 45.34  ? 31  HIS C ND1   1 
ATOM   4580 C  CD2   . HIS C 1 57  ? 130.477 127.781 130.649 1.00 38.20  ? 31  HIS C CD2   1 
ATOM   4581 C  CE1   . HIS C 1 57  ? 128.639 126.684 130.175 1.00 39.37  ? 31  HIS C CE1   1 
ATOM   4582 N  NE2   . HIS C 1 57  ? 129.875 126.916 129.771 1.00 43.61  ? 31  HIS C NE2   1 
ATOM   4583 N  N     . SER C 1 58  ? 131.472 127.002 134.529 1.00 40.00  ? 32  SER C N     1 
ATOM   4584 C  CA    . SER C 1 58  ? 132.324 125.820 134.482 1.00 34.43  ? 32  SER C CA    1 
ATOM   4585 C  C     . SER C 1 58  ? 132.272 124.989 135.756 1.00 41.32  ? 32  SER C C     1 
ATOM   4586 O  O     . SER C 1 58  ? 132.919 123.939 135.814 1.00 46.20  ? 32  SER C O     1 
ATOM   4587 C  CB    . SER C 1 58  ? 133.771 126.224 134.193 1.00 40.88  ? 32  SER C CB    1 
ATOM   4588 O  OG    . SER C 1 58  ? 133.880 126.845 132.925 1.00 46.89  ? 32  SER C OG    1 
ATOM   4589 N  N     . ASN C 1 59  ? 131.533 125.429 136.770 1.00 40.19  ? 33  ASN C N     1 
ATOM   4590 C  CA    . ASN C 1 59  ? 131.421 124.667 138.005 1.00 29.60  ? 33  ASN C CA    1 
ATOM   4591 C  C     . ASN C 1 59  ? 130.540 123.442 137.798 1.00 37.58  ? 33  ASN C C     1 
ATOM   4592 O  O     . ASN C 1 59  ? 129.549 123.494 137.061 1.00 39.96  ? 33  ASN C O     1 
ATOM   4593 C  CB    . ASN C 1 59  ? 130.852 125.542 139.119 1.00 34.38  ? 33  ASN C CB    1 
ATOM   4594 C  CG    . ASN C 1 59  ? 131.772 126.684 139.489 1.00 36.71  ? 33  ASN C CG    1 
ATOM   4595 O  OD1   . ASN C 1 59  ? 132.982 126.609 139.291 1.00 46.48  ? 33  ASN C OD1   1 
ATOM   4596 N  ND2   . ASN C 1 59  ? 131.203 127.748 140.040 1.00 35.68  ? 33  ASN C ND2   1 
ATOM   4597 N  N     . TYR C 1 60  ? 130.913 122.332 138.439 1.00 47.30  ? 34  TYR C N     1 
ATOM   4598 C  CA    . TYR C 1 60  ? 130.076 121.137 138.409 1.00 37.78  ? 34  TYR C CA    1 
ATOM   4599 C  C     . TYR C 1 60  ? 128.785 121.353 139.187 1.00 45.51  ? 34  TYR C C     1 
ATOM   4600 O  O     . TYR C 1 60  ? 127.718 120.880 138.780 1.00 50.55  ? 34  TYR C O     1 
ATOM   4601 C  CB    . TYR C 1 60  ? 130.841 119.939 138.970 1.00 43.02  ? 34  TYR C CB    1 
ATOM   4602 C  CG    . TYR C 1 60  ? 131.706 119.228 137.955 1.00 47.99  ? 34  TYR C CG    1 
ATOM   4603 C  CD1   . TYR C 1 60  ? 133.050 119.553 137.808 1.00 43.48  ? 34  TYR C CD1   1 
ATOM   4604 C  CD2   . TYR C 1 60  ? 131.179 118.230 137.143 1.00 48.05  ? 34  TYR C CD2   1 
ATOM   4605 C  CE1   . TYR C 1 60  ? 133.844 118.904 136.881 1.00 43.40  ? 34  TYR C CE1   1 
ATOM   4606 C  CE2   . TYR C 1 60  ? 131.963 117.577 136.213 1.00 47.38  ? 34  TYR C CE2   1 
ATOM   4607 C  CZ    . TYR C 1 60  ? 133.294 117.918 136.087 1.00 51.49  ? 34  TYR C CZ    1 
ATOM   4608 O  OH    . TYR C 1 60  ? 134.079 117.269 135.162 1.00 49.98  ? 34  TYR C OH    1 
ATOM   4609 N  N     . LEU C 1 61  ? 128.860 122.073 140.305 1.00 47.60  ? 35  LEU C N     1 
ATOM   4610 C  CA    . LEU C 1 61  ? 127.690 122.351 141.125 1.00 41.16  ? 35  LEU C CA    1 
ATOM   4611 C  C     . LEU C 1 61  ? 126.859 123.515 140.602 1.00 39.88  ? 35  LEU C C     1 
ATOM   4612 O  O     . LEU C 1 61  ? 125.756 123.741 141.110 1.00 48.90  ? 35  LEU C O     1 
ATOM   4613 C  CB    . LEU C 1 61  ? 128.118 122.616 142.571 1.00 41.64  ? 35  LEU C CB    1 
ATOM   4614 C  CG    . LEU C 1 61  ? 128.965 121.512 143.213 1.00 40.76  ? 35  LEU C CG    1 
ATOM   4615 C  CD1   . LEU C 1 61  ? 129.398 121.896 144.618 1.00 43.99  ? 35  LEU C CD1   1 
ATOM   4616 C  CD2   . LEU C 1 61  ? 128.212 120.192 143.226 1.00 39.59  ? 35  LEU C CD2   1 
ATOM   4617 N  N     . GLY C 1 62  ? 127.352 124.251 139.609 1.00 36.69  ? 36  GLY C N     1 
ATOM   4618 C  CA    . GLY C 1 62  ? 126.540 125.266 138.961 1.00 33.28  ? 36  GLY C CA    1 
ATOM   4619 C  C     . GLY C 1 62  ? 126.417 126.528 139.788 1.00 36.74  ? 36  GLY C C     1 
ATOM   4620 O  O     . GLY C 1 62  ? 127.387 127.020 140.374 1.00 42.16  ? 36  GLY C O     1 
ATOM   4621 N  N     . VAL C 1 63  ? 125.195 127.065 139.838 1.00 44.29  ? 37  VAL C N     1 
ATOM   4622 C  CA    . VAL C 1 63  ? 124.928 128.297 140.573 1.00 36.35  ? 37  VAL C CA    1 
ATOM   4623 C  C     . VAL C 1 63  ? 124.690 128.062 142.055 1.00 40.64  ? 37  VAL C C     1 
ATOM   4624 O  O     . VAL C 1 63  ? 124.333 129.003 142.771 1.00 44.14  ? 37  VAL C O     1 
ATOM   4625 C  CB    . VAL C 1 63  ? 123.720 129.041 139.972 1.00 34.58  ? 37  VAL C CB    1 
ATOM   4626 C  CG1   . VAL C 1 63  ? 123.989 129.399 138.520 1.00 34.99  ? 37  VAL C CG1   1 
ATOM   4627 C  CG2   . VAL C 1 63  ? 122.461 128.199 140.095 1.00 33.87  ? 37  VAL C CG2   1 
ATOM   4628 N  N     . ALA C 1 64  ? 124.878 126.831 142.535 1.00 41.90  ? 38  ALA C N     1 
ATOM   4629 C  CA    . ALA C 1 64  ? 124.773 126.555 143.961 1.00 36.41  ? 38  ALA C CA    1 
ATOM   4630 C  C     . ALA C 1 64  ? 125.966 127.086 144.744 1.00 41.38  ? 38  ALA C C     1 
ATOM   4631 O  O     . ALA C 1 64  ? 125.894 127.157 145.973 1.00 44.48  ? 38  ALA C O     1 
ATOM   4632 C  CB    . ALA C 1 64  ? 124.625 125.052 144.197 1.00 32.31  ? 38  ALA C CB    1 
ATOM   4633 N  N     . TRP C 1 65  ? 127.056 127.460 144.066 1.00 39.02  ? 39  TRP C N     1 
ATOM   4634 C  CA    . TRP C 1 65  ? 128.234 127.959 144.767 1.00 34.62  ? 39  TRP C CA    1 
ATOM   4635 C  C     . TRP C 1 65  ? 127.993 129.327 145.390 1.00 39.09  ? 39  TRP C C     1 
ATOM   4636 O  O     . TRP C 1 65  ? 128.611 129.649 146.413 1.00 45.85  ? 39  TRP C O     1 
ATOM   4637 C  CB    . TRP C 1 65  ? 129.431 127.999 143.823 1.00 41.53  ? 39  TRP C CB    1 
ATOM   4638 C  CG    . TRP C 1 65  ? 130.247 126.763 143.929 1.00 40.61  ? 39  TRP C CG    1 
ATOM   4639 C  CD1   . TRP C 1 65  ? 130.339 125.760 143.012 1.00 33.47  ? 39  TRP C CD1   1 
ATOM   4640 C  CD2   . TRP C 1 65  ? 131.061 126.372 145.037 1.00 43.00  ? 39  TRP C CD2   1 
ATOM   4641 N  NE1   . TRP C 1 65  ? 131.172 124.775 143.474 1.00 39.41  ? 39  TRP C NE1   1 
ATOM   4642 C  CE2   . TRP C 1 65  ? 131.631 125.127 144.717 1.00 42.40  ? 39  TRP C CE2   1 
ATOM   4643 C  CE3   . TRP C 1 65  ? 131.369 126.958 146.271 1.00 41.32  ? 39  TRP C CE3   1 
ATOM   4644 C  CZ2   . TRP C 1 65  ? 132.492 124.458 145.580 1.00 39.92  ? 39  TRP C CZ2   1 
ATOM   4645 C  CZ3   . TRP C 1 65  ? 132.228 126.295 147.121 1.00 42.31  ? 39  TRP C CZ3   1 
ATOM   4646 C  CH2   . TRP C 1 65  ? 132.776 125.057 146.774 1.00 38.87  ? 39  TRP C CH2   1 
ATOM   4647 N  N     . GLU C 1 66  ? 127.053 130.102 144.829 1.00 41.80  ? 40  GLU C N     1 
ATOM   4648 C  CA    . GLU C 1 66  ? 126.633 131.372 145.418 1.00 45.25  ? 40  GLU C CA    1 
ATOM   4649 C  C     . GLU C 1 66  ? 125.995 131.185 146.789 1.00 42.40  ? 40  GLU C C     1 
ATOM   4650 O  O     . GLU C 1 66  ? 125.935 132.129 147.584 1.00 47.07  ? 40  GLU C O     1 
ATOM   4651 C  CB    . GLU C 1 66  ? 125.650 132.079 144.482 1.00 42.88  ? 40  GLU C CB    1 
ATOM   4652 C  CG    . GLU C 1 66  ? 126.268 132.624 143.207 1.00 44.72  ? 40  GLU C CG    1 
ATOM   4653 C  CD    . GLU C 1 66  ? 125.891 134.071 142.946 1.00 55.44  ? 40  GLU C CD    1 
ATOM   4654 O  OE1   . GLU C 1 66  ? 126.687 134.787 142.303 1.00 54.09  ? 40  GLU C OE1   1 
ATOM   4655 O  OE2   . GLU C 1 66  ? 124.800 134.494 143.383 1.00 48.67  ? 40  GLU C OE2   1 
ATOM   4656 N  N     . LEU C 1 67  ? 125.496 129.984 147.070 1.00 37.31  ? 41  LEU C N     1 
ATOM   4657 C  CA    . LEU C 1 67  ? 124.996 129.567 148.369 1.00 32.84  ? 41  LEU C CA    1 
ATOM   4658 C  C     . LEU C 1 67  ? 126.049 128.849 149.203 1.00 37.76  ? 41  LEU C C     1 
ATOM   4659 O  O     . LEU C 1 67  ? 126.120 129.059 150.416 1.00 41.65  ? 41  LEU C O     1 
ATOM   4660 C  CB    . LEU C 1 67  ? 123.792 128.648 148.157 1.00 38.62  ? 41  LEU C CB    1 
ATOM   4661 C  CG    . LEU C 1 67  ? 122.499 128.844 148.934 1.00 44.22  ? 41  LEU C CG    1 
ATOM   4662 C  CD1   . LEU C 1 67  ? 121.909 130.208 148.642 1.00 42.98  ? 41  LEU C CD1   1 
ATOM   4663 C  CD2   . LEU C 1 67  ? 121.538 127.757 148.498 1.00 46.33  ? 41  LEU C CD2   1 
ATOM   4664 N  N     . ILE C 1 68  ? 126.876 128.014 148.565 1.00 39.47  ? 42  ILE C N     1 
ATOM   4665 C  CA    . ILE C 1 68  ? 127.789 127.136 149.298 1.00 38.24  ? 42  ILE C CA    1 
ATOM   4666 C  C     . ILE C 1 68  ? 128.968 127.920 149.871 1.00 39.13  ? 42  ILE C C     1 
ATOM   4667 O  O     . ILE C 1 68  ? 129.345 127.727 151.034 1.00 46.41  ? 42  ILE C O     1 
ATOM   4668 C  CB    . ILE C 1 68  ? 128.251 125.977 148.392 1.00 36.18  ? 42  ILE C CB    1 
ATOM   4669 C  CG1   . ILE C 1 68  ? 127.091 125.022 148.115 1.00 38.41  ? 42  ILE C CG1   1 
ATOM   4670 C  CG2   . ILE C 1 68  ? 129.375 125.178 149.033 1.00 37.06  ? 42  ILE C CG2   1 
ATOM   4671 C  CD1   . ILE C 1 68  ? 127.357 124.050 146.991 1.00 39.58  ? 42  ILE C CD1   1 
ATOM   4672 N  N     . ASN C 1 69  ? 129.568 128.810 149.071 1.00 39.95  ? 43  ASN C N     1 
ATOM   4673 C  CA    . ASN C 1 69  ? 130.745 129.558 149.522 1.00 38.36  ? 43  ASN C CA    1 
ATOM   4674 C  C     . ASN C 1 69  ? 130.481 130.501 150.704 1.00 37.65  ? 43  ASN C C     1 
ATOM   4675 O  O     . ASN C 1 69  ? 131.314 130.519 151.633 1.00 44.42  ? 43  ASN C O     1 
ATOM   4676 C  CB    . ASN C 1 69  ? 131.377 130.275 148.317 1.00 37.86  ? 43  ASN C CB    1 
ATOM   4677 C  CG    . ASN C 1 69  ? 132.496 131.216 148.711 1.00 46.27  ? 43  ASN C CG    1 
ATOM   4678 O  OD1   . ASN C 1 69  ? 132.344 132.435 148.652 1.00 42.91  ? 43  ASN C OD1   1 
ATOM   4679 N  ND2   . ASN C 1 69  ? 133.630 130.655 149.115 1.00 47.93  ? 43  ASN C ND2   1 
ATOM   4680 N  N     . PRO C 1 70  ? 129.386 131.295 150.754 1.00 40.81  ? 44  PRO C N     1 
ATOM   4681 C  CA    . PRO C 1 70  ? 129.090 132.009 152.009 1.00 37.16  ? 44  PRO C CA    1 
ATOM   4682 C  C     . PRO C 1 70  ? 128.844 131.108 153.205 1.00 35.79  ? 44  PRO C C     1 
ATOM   4683 O  O     . PRO C 1 70  ? 129.210 131.499 154.312 1.00 45.14  ? 44  PRO C O     1 
ATOM   4684 C  CB    . PRO C 1 70  ? 127.837 132.823 151.659 1.00 32.94  ? 44  PRO C CB    1 
ATOM   4685 C  CG    . PRO C 1 70  ? 127.964 133.068 150.236 1.00 34.85  ? 44  PRO C CG    1 
ATOM   4686 C  CD    . PRO C 1 70  ? 128.473 131.779 149.693 1.00 37.20  ? 44  PRO C CD    1 
ATOM   4687 N  N     . VAL C 1 71  ? 128.268 129.916 153.019 1.00 34.72  ? 45  VAL C N     1 
ATOM   4688 C  CA    . VAL C 1 71  ? 128.018 129.008 154.140 1.00 36.53  ? 45  VAL C CA    1 
ATOM   4689 C  C     . VAL C 1 71  ? 129.334 128.493 154.723 1.00 34.08  ? 45  VAL C C     1 
ATOM   4690 O  O     . VAL C 1 71  ? 129.506 128.423 155.949 1.00 39.84  ? 45  VAL C O     1 
ATOM   4691 C  CB    . VAL C 1 71  ? 127.086 127.864 153.686 1.00 37.95  ? 45  VAL C CB    1 
ATOM   4692 C  CG1   . VAL C 1 71  ? 127.203 126.630 154.579 1.00 33.93  ? 45  VAL C CG1   1 
ATOM   4693 C  CG2   . VAL C 1 71  ? 125.647 128.348 153.650 1.00 35.32  ? 45  VAL C CG2   1 
ATOM   4694 N  N     . MET C 1 72  ? 130.293 128.164 153.852 1.00 37.68  ? 46  MET C N     1 
ATOM   4695 C  CA    . MET C 1 72  ? 131.621 127.754 154.302 1.00 33.26  ? 46  MET C CA    1 
ATOM   4696 C  C     . MET C 1 72  ? 132.343 128.886 155.023 1.00 38.59  ? 46  MET C C     1 
ATOM   4697 O  O     . MET C 1 72  ? 132.985 128.660 156.060 1.00 41.60  ? 46  MET C O     1 
ATOM   4698 C  CB    . MET C 1 72  ? 132.444 127.274 153.110 1.00 35.44  ? 46  MET C CB    1 
ATOM   4699 C  CG    . MET C 1 72  ? 132.506 125.771 152.954 1.00 38.38  ? 46  MET C CG    1 
ATOM   4700 S  SD    . MET C 1 72  ? 132.601 125.324 151.216 1.00 56.93  ? 46  MET C SD    1 
ATOM   4701 C  CE    . MET C 1 72  ? 134.106 126.175 150.766 1.00 45.73  ? 46  MET C CE    1 
ATOM   4702 N  N     . GLN C 1 73  ? 132.225 130.114 154.503 1.00 37.81  ? 47  GLN C N     1 
ATOM   4703 C  CA    . GLN C 1 73  ? 132.813 131.264 155.188 1.00 27.52  ? 47  GLN C CA    1 
ATOM   4704 C  C     . GLN C 1 73  ? 132.141 131.520 156.537 1.00 26.10  ? 47  GLN C C     1 
ATOM   4705 O  O     . GLN C 1 73  ? 132.802 131.927 157.498 1.00 35.52  ? 47  GLN C O     1 
ATOM   4706 C  CB    . GLN C 1 73  ? 132.735 132.497 154.292 1.00 34.33  ? 47  GLN C CB    1 
ATOM   4707 C  CG    . GLN C 1 73  ? 133.663 132.424 153.093 1.00 38.02  ? 47  GLN C CG    1 
ATOM   4708 C  CD    . GLN C 1 73  ? 133.686 133.702 152.288 1.00 38.96  ? 47  GLN C CD    1 
ATOM   4709 O  OE1   . GLN C 1 73  ? 133.382 133.704 151.098 1.00 43.98  ? 47  GLN C OE1   1 
ATOM   4710 N  NE2   . GLN C 1 73  ? 134.048 134.801 152.936 1.00 41.76  ? 47  GLN C NE2   1 
ATOM   4711 N  N     . ILE C 1 74  ? 130.832 131.258 156.627 1.00 29.42  ? 48  ILE C N     1 
ATOM   4712 C  CA    . ILE C 1 74  ? 130.093 131.366 157.884 1.00 29.81  ? 48  ILE C CA    1 
ATOM   4713 C  C     . ILE C 1 74  ? 130.618 130.363 158.905 1.00 27.40  ? 48  ILE C C     1 
ATOM   4714 O  O     . ILE C 1 74  ? 130.790 130.691 160.087 1.00 31.69  ? 48  ILE C O     1 
ATOM   4715 C  CB    . ILE C 1 74  ? 128.585 131.172 157.616 1.00 40.67  ? 48  ILE C CB    1 
ATOM   4716 C  CG1   . ILE C 1 74  ? 127.964 132.459 157.094 1.00 32.42  ? 48  ILE C CG1   1 
ATOM   4717 C  CG2   . ILE C 1 74  ? 127.830 130.708 158.855 1.00 36.66  ? 48  ILE C CG2   1 
ATOM   4718 C  CD1   . ILE C 1 74  ? 126.649 132.263 156.378 1.00 35.81  ? 48  ILE C CD1   1 
ATOM   4719 N  N     . MET C 1 75  ? 130.888 129.132 158.459 1.00 35.94  ? 49  MET C N     1 
ATOM   4720 C  CA    . MET C 1 75  ? 131.457 128.114 159.344 1.00 34.74  ? 49  MET C CA    1 
ATOM   4721 C  C     . MET C 1 75  ? 132.843 128.515 159.838 1.00 34.35  ? 49  MET C C     1 
ATOM   4722 O  O     . MET C 1 75  ? 133.170 128.309 161.016 1.00 39.17  ? 49  MET C O     1 
ATOM   4723 C  CB    . MET C 1 75  ? 131.514 126.762 158.633 1.00 34.54  ? 49  MET C CB    1 
ATOM   4724 C  CG    . MET C 1 75  ? 130.156 126.189 158.273 1.00 38.04  ? 49  MET C CG    1 
ATOM   4725 S  SD    . MET C 1 75  ? 130.206 125.088 156.846 1.00 64.83  ? 49  MET C SD    1 
ATOM   4726 C  CE    . MET C 1 75  ? 131.597 124.042 157.264 1.00 42.98  ? 49  MET C CE    1 
ATOM   4727 N  N     . VAL C 1 76  ? 133.656 129.113 158.959 1.00 34.77  ? 50  VAL C N     1 
ATOM   4728 C  CA    . VAL C 1 76  ? 134.979 129.604 159.361 1.00 33.54  ? 50  VAL C CA    1 
ATOM   4729 C  C     . VAL C 1 76  ? 134.851 130.716 160.402 1.00 33.38  ? 50  VAL C C     1 
ATOM   4730 O  O     . VAL C 1 76  ? 135.539 130.710 161.434 1.00 37.14  ? 50  VAL C O     1 
ATOM   4731 C  CB    . VAL C 1 76  ? 135.772 130.075 158.128 1.00 33.28  ? 50  VAL C CB    1 
ATOM   4732 C  CG1   . VAL C 1 76  ? 137.089 130.717 158.540 1.00 31.01  ? 50  VAL C CG1   1 
ATOM   4733 C  CG2   . VAL C 1 76  ? 136.027 128.918 157.194 1.00 33.17  ? 50  VAL C CG2   1 
ATOM   4734 N  N     . TYR C 1 77  ? 133.944 131.668 160.159 1.00 30.42  ? 51  TYR C N     1 
ATOM   4735 C  CA    . TYR C 1 77  ? 133.786 132.804 161.064 1.00 20.17  ? 51  TYR C CA    1 
ATOM   4736 C  C     . TYR C 1 77  ? 133.192 132.382 162.404 1.00 23.44  ? 51  TYR C C     1 
ATOM   4737 O  O     . TYR C 1 77  ? 133.492 132.991 163.435 1.00 33.01  ? 51  TYR C O     1 
ATOM   4738 C  CB    . TYR C 1 77  ? 132.927 133.886 160.409 1.00 27.63  ? 51  TYR C CB    1 
ATOM   4739 C  CG    . TYR C 1 77  ? 133.673 134.735 159.401 1.00 31.30  ? 51  TYR C CG    1 
ATOM   4740 C  CD1   . TYR C 1 77  ? 134.907 135.290 159.710 1.00 30.17  ? 51  TYR C CD1   1 
ATOM   4741 C  CD2   . TYR C 1 77  ? 133.142 134.982 158.140 1.00 28.80  ? 51  TYR C CD2   1 
ATOM   4742 C  CE1   . TYR C 1 77  ? 135.591 136.065 158.794 1.00 25.99  ? 51  TYR C CE1   1 
ATOM   4743 C  CE2   . TYR C 1 77  ? 133.821 135.751 157.215 1.00 34.50  ? 51  TYR C CE2   1 
ATOM   4744 C  CZ    . TYR C 1 77  ? 135.044 136.291 157.549 1.00 34.91  ? 51  TYR C CZ    1 
ATOM   4745 O  OH    . TYR C 1 77  ? 135.720 137.061 156.634 1.00 37.90  ? 51  TYR C OH    1 
ATOM   4746 N  N     . TRP C 1 78  ? 132.361 131.338 162.417 1.00 29.39  ? 52  TRP C N     1 
ATOM   4747 C  CA    . TRP C 1 78  ? 131.830 130.857 163.687 1.00 30.89  ? 52  TRP C CA    1 
ATOM   4748 C  C     . TRP C 1 78  ? 132.876 130.050 164.448 1.00 34.71  ? 52  TRP C C     1 
ATOM   4749 O  O     . TRP C 1 78  ? 132.903 130.077 165.684 1.00 36.71  ? 52  TRP C O     1 
ATOM   4750 C  CB    . TRP C 1 78  ? 130.549 130.044 163.465 1.00 29.90  ? 52  TRP C CB    1 
ATOM   4751 C  CG    . TRP C 1 78  ? 130.172 129.128 164.609 1.00 32.16  ? 52  TRP C CG    1 
ATOM   4752 C  CD1   . TRP C 1 78  ? 129.317 129.416 165.630 1.00 29.52  ? 52  TRP C CD1   1 
ATOM   4753 C  CD2   . TRP C 1 78  ? 130.572 127.762 164.798 1.00 40.37  ? 52  TRP C CD2   1 
ATOM   4754 N  NE1   . TRP C 1 78  ? 129.199 128.339 166.470 1.00 32.63  ? 52  TRP C NE1   1 
ATOM   4755 C  CE2   . TRP C 1 78  ? 129.957 127.309 165.981 1.00 43.14  ? 52  TRP C CE2   1 
ATOM   4756 C  CE3   . TRP C 1 78  ? 131.417 126.893 164.103 1.00 39.96  ? 52  TRP C CE3   1 
ATOM   4757 C  CZ2   . TRP C 1 78  ? 130.149 126.021 166.475 1.00 40.11  ? 52  TRP C CZ2   1 
ATOM   4758 C  CZ3   . TRP C 1 78  ? 131.605 125.616 164.595 1.00 40.65  ? 52  TRP C CZ3   1 
ATOM   4759 C  CH2   . TRP C 1 78  ? 130.973 125.191 165.768 1.00 43.88  ? 52  TRP C CH2   1 
ATOM   4760 N  N     . MET C 1 79  ? 133.734 129.314 163.729 1.00 32.86  ? 53  MET C N     1 
ATOM   4761 C  CA    . MET C 1 79  ? 134.823 128.602 164.391 1.00 33.22  ? 53  MET C CA    1 
ATOM   4762 C  C     . MET C 1 79  ? 135.820 129.569 165.013 1.00 34.51  ? 53  MET C C     1 
ATOM   4763 O  O     . MET C 1 79  ? 136.380 129.296 166.080 1.00 39.03  ? 53  MET C O     1 
ATOM   4764 C  CB    . MET C 1 79  ? 135.535 127.678 163.403 1.00 38.86  ? 53  MET C CB    1 
ATOM   4765 C  CG    . MET C 1 79  ? 134.930 126.293 163.288 1.00 44.55  ? 53  MET C CG    1 
ATOM   4766 S  SD    . MET C 1 79  ? 135.863 125.215 162.186 1.00 58.75  ? 53  MET C SD    1 
ATOM   4767 C  CE    . MET C 1 79  ? 135.835 126.164 160.670 1.00 39.10  ? 53  MET C CE    1 
ATOM   4768 N  N     . VAL C 1 80  ? 136.049 130.710 164.366 1.00 33.27  ? 54  VAL C N     1 
ATOM   4769 C  CA    . VAL C 1 80  ? 137.047 131.650 164.870 1.00 29.61  ? 54  VAL C CA    1 
ATOM   4770 C  C     . VAL C 1 80  ? 136.446 132.578 165.919 1.00 27.67  ? 54  VAL C C     1 
ATOM   4771 O  O     . VAL C 1 80  ? 136.886 132.603 167.073 1.00 35.64  ? 54  VAL C O     1 
ATOM   4772 C  CB    . VAL C 1 80  ? 137.674 132.434 163.706 1.00 31.43  ? 54  VAL C CB    1 
ATOM   4773 C  CG1   . VAL C 1 80  ? 138.599 133.518 164.233 1.00 27.81  ? 54  VAL C CG1   1 
ATOM   4774 C  CG2   . VAL C 1 80  ? 138.419 131.478 162.807 1.00 34.74  ? 54  VAL C CG2   1 
ATOM   4775 N  N     . PHE C 1 81  ? 135.430 133.348 165.540 1.00 30.28  ? 55  PHE C N     1 
ATOM   4776 C  CA    . PHE C 1 81  ? 134.902 134.400 166.394 1.00 27.97  ? 55  PHE C CA    1 
ATOM   4777 C  C     . PHE C 1 81  ? 133.870 133.903 167.397 1.00 28.78  ? 55  PHE C C     1 
ATOM   4778 O  O     . PHE C 1 81  ? 133.486 134.664 168.292 1.00 39.65  ? 55  PHE C O     1 
ATOM   4779 C  CB    . PHE C 1 81  ? 134.299 135.515 165.530 1.00 28.53  ? 55  PHE C CB    1 
ATOM   4780 C  CG    . PHE C 1 81  ? 135.311 136.228 164.676 1.00 27.26  ? 55  PHE C CG    1 
ATOM   4781 C  CD1   . PHE C 1 81  ? 135.592 135.788 163.390 1.00 31.38  ? 55  PHE C CD1   1 
ATOM   4782 C  CD2   . PHE C 1 81  ? 135.997 137.326 165.167 1.00 20.96  ? 55  PHE C CD2   1 
ATOM   4783 C  CE1   . PHE C 1 81  ? 136.533 136.435 162.611 1.00 28.77  ? 55  PHE C CE1   1 
ATOM   4784 C  CE2   . PHE C 1 81  ? 136.938 137.976 164.391 1.00 26.62  ? 55  PHE C CE2   1 
ATOM   4785 C  CZ    . PHE C 1 81  ? 137.204 137.532 163.112 1.00 28.30  ? 55  PHE C CZ    1 
ATOM   4786 N  N     . GLY C 1 82  ? 133.411 132.661 167.275 1.00 34.29  ? 56  GLY C N     1 
ATOM   4787 C  CA    . GLY C 1 82  ? 132.488 132.108 168.245 1.00 27.57  ? 56  GLY C CA    1 
ATOM   4788 C  C     . GLY C 1 82  ? 133.138 131.231 169.289 1.00 35.31  ? 56  GLY C C     1 
ATOM   4789 O  O     . GLY C 1 82  ? 132.923 131.419 170.489 1.00 46.43  ? 56  GLY C O     1 
ATOM   4790 N  N     . LEU C 1 83  ? 133.949 130.272 168.846 1.00 38.39  ? 57  LEU C N     1 
ATOM   4791 C  CA    . LEU C 1 83  ? 134.606 129.340 169.751 1.00 37.88  ? 57  LEU C CA    1 
ATOM   4792 C  C     . LEU C 1 83  ? 135.916 129.896 170.296 1.00 43.62  ? 57  LEU C C     1 
ATOM   4793 O  O     . LEU C 1 83  ? 136.224 129.722 171.478 1.00 48.57  ? 57  LEU C O     1 
ATOM   4794 C  CB    . LEU C 1 83  ? 134.866 128.011 169.039 1.00 40.65  ? 57  LEU C CB    1 
ATOM   4795 C  CG    . LEU C 1 83  ? 133.730 126.992 169.012 1.00 45.85  ? 57  LEU C CG    1 
ATOM   4796 C  CD1   . LEU C 1 83  ? 133.822 126.163 167.750 1.00 44.35  ? 57  LEU C CD1   1 
ATOM   4797 C  CD2   . LEU C 1 83  ? 133.778 126.106 170.243 1.00 42.20  ? 57  LEU C CD2   1 
ATOM   4798 N  N     . GLY C 1 84  ? 136.698 130.560 169.444 1.00 44.36  ? 58  GLY C N     1 
ATOM   4799 C  CA    . GLY C 1 84  ? 138.007 131.024 169.871 1.00 42.69  ? 58  GLY C CA    1 
ATOM   4800 C  C     . GLY C 1 84  ? 137.950 132.271 170.733 1.00 47.05  ? 58  GLY C C     1 
ATOM   4801 O  O     . GLY C 1 84  ? 138.811 132.477 171.593 1.00 56.60  ? 58  GLY C O     1 
ATOM   4802 N  N     . ILE C 1 85  ? 136.945 133.115 170.522 1.00 39.91  ? 59  ILE C N     1 
ATOM   4803 C  CA    . ILE C 1 85  ? 136.889 134.403 171.207 1.00 42.93  ? 59  ILE C CA    1 
ATOM   4804 C  C     . ILE C 1 85  ? 136.004 134.341 172.445 1.00 47.31  ? 59  ILE C C     1 
ATOM   4805 O  O     . ILE C 1 85  ? 136.422 134.733 173.538 1.00 50.39  ? 59  ILE C O     1 
ATOM   4806 C  CB    . ILE C 1 85  ? 136.428 135.503 170.224 1.00 44.09  ? 59  ILE C CB    1 
ATOM   4807 C  CG1   . ILE C 1 85  ? 137.552 135.805 169.224 1.00 40.98  ? 59  ILE C CG1   1 
ATOM   4808 C  CG2   . ILE C 1 85  ? 135.977 136.759 170.979 1.00 41.56  ? 59  ILE C CG2   1 
ATOM   4809 C  CD1   . ILE C 1 85  ? 137.423 137.119 168.486 1.00 41.98  ? 59  ILE C CD1   1 
ATOM   4810 N  N     . ARG C 1 86  ? 134.776 133.839 172.313 1.00 42.42  ? 60  ARG C N     1 
ATOM   4811 C  CA    . ARG C 1 86  ? 133.828 133.851 173.420 1.00 39.14  ? 60  ARG C CA    1 
ATOM   4812 C  C     . ARG C 1 86  ? 133.326 132.465 173.803 1.00 41.97  ? 60  ARG C C     1 
ATOM   4813 O  O     . ARG C 1 86  ? 132.416 132.368 174.637 1.00 43.94  ? 60  ARG C O     1 
ATOM   4814 C  CB    . ARG C 1 86  ? 132.643 134.761 173.090 1.00 42.52  ? 60  ARG C CB    1 
ATOM   4815 C  CG    . ARG C 1 86  ? 131.893 134.377 171.836 1.00 37.99  ? 60  ARG C CG    1 
ATOM   4816 C  CD    . ARG C 1 86  ? 130.771 135.354 171.571 1.00 33.02  ? 60  ARG C CD    1 
ATOM   4817 N  NE    . ARG C 1 86  ? 129.752 135.314 172.611 1.00 35.64  ? 60  ARG C NE    1 
ATOM   4818 C  CZ    . ARG C 1 86  ? 129.448 136.333 173.400 1.00 38.35  ? 60  ARG C CZ    1 
ATOM   4819 N  NH1   . ARG C 1 86  ? 130.065 137.498 173.292 1.00 45.06  ? 60  ARG C NH1   1 
ATOM   4820 N  NH2   . ARG C 1 86  ? 128.502 136.182 174.322 1.00 36.90  ? 60  ARG C NH2   1 
ATOM   4821 N  N     . SER C 1 87  ? 133.911 131.401 173.233 1.00 44.15  ? 61  SER C N     1 
ATOM   4822 C  CA    . SER C 1 87  ? 133.581 129.993 173.515 1.00 44.82  ? 61  SER C CA    1 
ATOM   4823 C  C     . SER C 1 87  ? 132.098 129.686 173.303 1.00 46.58  ? 61  SER C C     1 
ATOM   4824 O  O     . SER C 1 87  ? 131.482 128.974 174.101 1.00 46.99  ? 61  SER C O     1 
ATOM   4825 C  CB    . SER C 1 87  ? 134.026 129.568 174.920 1.00 47.28  ? 61  SER C CB    1 
ATOM   4826 O  OG    . SER C 1 87  ? 133.340 130.269 175.944 1.00 51.41  ? 61  SER C OG    1 
ATOM   4827 N  N     . ASN C 1 88  ? 131.536 130.239 172.216 1.00 46.87  ? 62  ASN C N     1 
ATOM   4828 C  CA    . ASN C 1 88  ? 130.147 130.022 171.779 1.00 41.64  ? 62  ASN C CA    1 
ATOM   4829 C  C     . ASN C 1 88  ? 129.135 130.424 172.852 1.00 41.45  ? 62  ASN C C     1 
ATOM   4830 O  O     . ASN C 1 88  ? 128.119 129.756 173.055 1.00 47.25  ? 62  ASN C O     1 
ATOM   4831 C  CB    . ASN C 1 88  ? 129.922 128.574 171.327 1.00 41.66  ? 62  ASN C CB    1 
ATOM   4832 C  CG    . ASN C 1 88  ? 128.870 128.457 170.243 1.00 47.01  ? 62  ASN C CG    1 
ATOM   4833 O  OD1   . ASN C 1 88  ? 128.583 129.418 169.533 1.00 50.76  ? 62  ASN C OD1   1 
ATOM   4834 N  ND2   . ASN C 1 88  ? 128.289 127.272 170.110 1.00 47.85  ? 62  ASN C ND2   1 
ATOM   4835 N  N     . ALA C 1 89  ? 129.418 131.519 173.549 1.00 41.63  ? 63  ALA C N     1 
ATOM   4836 C  CA    . ALA C 1 89  ? 128.510 132.024 174.569 1.00 39.30  ? 63  ALA C CA    1 
ATOM   4837 C  C     . ALA C 1 89  ? 127.301 132.691 173.914 1.00 49.04  ? 63  ALA C C     1 
ATOM   4838 O  O     . ALA C 1 89  ? 127.439 133.323 172.863 1.00 47.83  ? 63  ALA C O     1 
ATOM   4839 C  CB    . ALA C 1 89  ? 129.225 133.017 175.480 1.00 37.69  ? 63  ALA C CB    1 
ATOM   4840 N  N     . PRO C 1 90  ? 126.111 132.551 174.498 1.00 51.25  ? 64  PRO C N     1 
ATOM   4841 C  CA    . PRO C 1 90  ? 124.924 133.190 173.920 1.00 42.34  ? 64  PRO C CA    1 
ATOM   4842 C  C     . PRO C 1 90  ? 124.957 134.704 174.057 1.00 42.72  ? 64  PRO C C     1 
ATOM   4843 O  O     . PRO C 1 90  ? 125.570 135.268 174.966 1.00 44.48  ? 64  PRO C O     1 
ATOM   4844 C  CB    . PRO C 1 90  ? 123.765 132.591 174.727 1.00 42.91  ? 64  PRO C CB    1 
ATOM   4845 C  CG    . PRO C 1 90  ? 124.329 131.377 175.387 1.00 44.41  ? 64  PRO C CG    1 
ATOM   4846 C  CD    . PRO C 1 90  ? 125.765 131.682 175.634 1.00 41.20  ? 64  PRO C CD    1 
ATOM   4847 N  N     . ILE C 1 91  ? 124.277 135.366 173.123 1.00 44.63  ? 65  ILE C N     1 
ATOM   4848 C  CA    . ILE C 1 91  ? 124.147 136.818 173.109 1.00 41.79  ? 65  ILE C CA    1 
ATOM   4849 C  C     . ILE C 1 91  ? 122.664 137.156 173.133 1.00 43.97  ? 65  ILE C C     1 
ATOM   4850 O  O     . ILE C 1 91  ? 121.921 136.738 172.235 1.00 47.54  ? 65  ILE C O     1 
ATOM   4851 C  CB    . ILE C 1 91  ? 124.822 137.452 171.881 1.00 37.43  ? 65  ILE C CB    1 
ATOM   4852 C  CG1   . ILE C 1 91  ? 126.326 137.172 171.889 1.00 43.70  ? 65  ILE C CG1   1 
ATOM   4853 C  CG2   . ILE C 1 91  ? 124.550 138.950 171.846 1.00 41.60  ? 65  ILE C CG2   1 
ATOM   4854 C  CD1   . ILE C 1 91  ? 127.119 137.941 170.852 1.00 40.49  ? 65  ILE C CD1   1 
ATOM   4855 N  N     . HIS C 1 92  ? 122.243 137.905 174.162 1.00 52.46  ? 66  HIS C N     1 
ATOM   4856 C  CA    . HIS C 1 92  ? 120.879 138.435 174.318 1.00 54.73  ? 66  HIS C CA    1 
ATOM   4857 C  C     . HIS C 1 92  ? 119.829 137.324 174.347 1.00 55.75  ? 66  HIS C C     1 
ATOM   4858 O  O     . HIS C 1 92  ? 118.721 137.472 173.830 1.00 57.63  ? 66  HIS C O     1 
ATOM   4859 C  CB    . HIS C 1 92  ? 120.551 139.463 173.229 1.00 55.36  ? 66  HIS C CB    1 
ATOM   4860 C  CG    . HIS C 1 92  ? 121.203 140.796 173.431 1.00 57.84  ? 66  HIS C CG    1 
ATOM   4861 N  ND1   . HIS C 1 92  ? 122.519 140.934 173.817 1.00 59.81  ? 66  HIS C ND1   1 
ATOM   4862 C  CD2   . HIS C 1 92  ? 120.720 142.053 173.291 1.00 58.13  ? 66  HIS C CD2   1 
ATOM   4863 C  CE1   . HIS C 1 92  ? 122.817 142.217 173.911 1.00 58.98  ? 66  HIS C CE1   1 
ATOM   4864 N  NE2   . HIS C 1 92  ? 121.743 142.917 173.596 1.00 61.00  ? 66  HIS C NE2   1 
ATOM   4865 N  N     . GLY C 1 93  ? 120.184 136.196 174.959 1.00 49.15  ? 67  GLY C N     1 
ATOM   4866 C  CA    . GLY C 1 93  ? 119.280 135.065 175.025 1.00 47.58  ? 67  GLY C CA    1 
ATOM   4867 C  C     . GLY C 1 93  ? 119.216 134.217 173.775 1.00 48.30  ? 67  GLY C C     1 
ATOM   4868 O  O     . GLY C 1 93  ? 118.432 133.266 173.728 1.00 55.48  ? 67  GLY C O     1 
ATOM   4869 N  N     . VAL C 1 94  ? 120.011 134.533 172.765 1.00 41.25  ? 68  VAL C N     1 
ATOM   4870 C  CA    . VAL C 1 94  ? 120.065 133.790 171.509 1.00 40.28  ? 68  VAL C CA    1 
ATOM   4871 C  C     . VAL C 1 94  ? 121.421 133.103 171.441 1.00 44.88  ? 68  VAL C C     1 
ATOM   4872 O  O     . VAL C 1 94  ? 122.426 133.717 171.816 1.00 46.74  ? 68  VAL C O     1 
ATOM   4873 C  CB    . VAL C 1 94  ? 119.860 134.717 170.292 1.00 39.73  ? 68  VAL C CB    1 
ATOM   4874 C  CG1   . VAL C 1 94  ? 119.767 133.925 168.996 1.00 39.27  ? 68  VAL C CG1   1 
ATOM   4875 C  CG2   . VAL C 1 94  ? 118.621 135.579 170.481 1.00 42.48  ? 68  VAL C CG2   1 
ATOM   4876 N  N     . PRO C 1 95  ? 121.495 131.837 171.021 1.00 41.39  ? 69  PRO C N     1 
ATOM   4877 C  CA    . PRO C 1 95  ? 122.802 131.207 170.788 1.00 40.98  ? 69  PRO C CA    1 
ATOM   4878 C  C     . PRO C 1 95  ? 123.572 131.908 169.677 1.00 38.47  ? 69  PRO C C     1 
ATOM   4879 O  O     . PRO C 1 95  ? 122.985 132.516 168.780 1.00 42.16  ? 69  PRO C O     1 
ATOM   4880 C  CB    . PRO C 1 95  ? 122.443 129.765 170.404 1.00 37.28  ? 69  PRO C CB    1 
ATOM   4881 C  CG    . PRO C 1 95  ? 120.970 129.768 170.142 1.00 35.73  ? 69  PRO C CG    1 
ATOM   4882 C  CD    . PRO C 1 95  ? 120.399 130.856 170.977 1.00 33.37  ? 69  PRO C CD    1 
ATOM   4883 N  N     . PHE C 1 96  ? 124.907 131.827 169.762 1.00 40.41  ? 70  PHE C N     1 
ATOM   4884 C  CA    . PHE C 1 96  ? 125.773 132.676 168.947 1.00 33.79  ? 70  PHE C CA    1 
ATOM   4885 C  C     . PHE C 1 96  ? 125.717 132.326 167.467 1.00 28.02  ? 70  PHE C C     1 
ATOM   4886 O  O     . PHE C 1 96  ? 125.940 133.203 166.623 1.00 29.35  ? 70  PHE C O     1 
ATOM   4887 C  CB    . PHE C 1 96  ? 127.223 132.596 169.437 1.00 34.38  ? 70  PHE C CB    1 
ATOM   4888 C  CG    . PHE C 1 96  ? 128.146 133.567 168.748 1.00 34.06  ? 70  PHE C CG    1 
ATOM   4889 C  CD1   . PHE C 1 96  ? 128.168 134.899 169.122 1.00 33.07  ? 70  PHE C CD1   1 
ATOM   4890 C  CD2   . PHE C 1 96  ? 128.970 133.156 167.706 1.00 27.07  ? 70  PHE C CD2   1 
ATOM   4891 C  CE1   . PHE C 1 96  ? 129.002 135.799 168.487 1.00 30.78  ? 70  PHE C CE1   1 
ATOM   4892 C  CE2   . PHE C 1 96  ? 129.793 134.059 167.060 1.00 25.61  ? 70  PHE C CE2   1 
ATOM   4893 C  CZ    . PHE C 1 96  ? 129.813 135.378 167.456 1.00 26.00  ? 70  PHE C CZ    1 
ATOM   4894 N  N     . VAL C 1 97  ? 125.442 131.062 167.132 1.00 32.93  ? 71  VAL C N     1 
ATOM   4895 C  CA    . VAL C 1 97  ? 125.464 130.635 165.734 1.00 31.32  ? 71  VAL C CA    1 
ATOM   4896 C  C     . VAL C 1 97  ? 124.335 131.303 164.949 1.00 35.42  ? 71  VAL C C     1 
ATOM   4897 O  O     . VAL C 1 97  ? 124.551 131.823 163.850 1.00 36.57  ? 71  VAL C O     1 
ATOM   4898 C  CB    . VAL C 1 97  ? 125.431 129.094 165.640 1.00 37.51  ? 71  VAL C CB    1 
ATOM   4899 C  CG1   . VAL C 1 97  ? 124.386 128.489 166.569 1.00 32.13  ? 71  VAL C CG1   1 
ATOM   4900 C  CG2   . VAL C 1 97  ? 125.214 128.630 164.205 1.00 31.70  ? 71  VAL C CG2   1 
ATOM   4901 N  N     . TYR C 1 98  ? 123.143 131.391 165.542 1.00 34.26  ? 72  TYR C N     1 
ATOM   4902 C  CA    . TYR C 1 98  ? 122.025 132.036 164.858 1.00 34.84  ? 72  TYR C CA    1 
ATOM   4903 C  C     . TYR C 1 98  ? 122.133 133.556 164.901 1.00 38.16  ? 72  TYR C C     1 
ATOM   4904 O  O     . TYR C 1 98  ? 121.705 134.228 163.958 1.00 39.81  ? 72  TYR C O     1 
ATOM   4905 C  CB    . TYR C 1 98  ? 120.709 131.552 165.465 1.00 32.49  ? 72  TYR C CB    1 
ATOM   4906 C  CG    . TYR C 1 98  ? 120.590 130.049 165.411 1.00 34.38  ? 72  TYR C CG    1 
ATOM   4907 C  CD1   . TYR C 1 98  ? 120.255 129.404 164.227 1.00 36.36  ? 72  TYR C CD1   1 
ATOM   4908 C  CD2   . TYR C 1 98  ? 120.845 129.273 166.534 1.00 39.60  ? 72  TYR C CD2   1 
ATOM   4909 C  CE1   . TYR C 1 98  ? 120.161 128.027 164.166 1.00 34.39  ? 72  TYR C CE1   1 
ATOM   4910 C  CE2   . TYR C 1 98  ? 120.758 127.897 166.483 1.00 37.18  ? 72  TYR C CE2   1 
ATOM   4911 C  CZ    . TYR C 1 98  ? 120.418 127.280 165.297 1.00 35.81  ? 72  TYR C CZ    1 
ATOM   4912 O  OH    . TYR C 1 98  ? 120.322 125.910 165.248 1.00 41.36  ? 72  TYR C OH    1 
ATOM   4913 N  N     . TRP C 1 99  ? 122.714 134.102 165.976 1.00 32.01  ? 73  TRP C N     1 
ATOM   4914 C  CA    . TRP C 1 99  ? 122.989 135.535 166.070 1.00 16.88  ? 73  TRP C CA    1 
ATOM   4915 C  C     . TRP C 1 99  ? 123.946 135.986 164.970 1.00 26.18  ? 73  TRP C C     1 
ATOM   4916 O  O     . TRP C 1 99  ? 123.680 136.963 164.256 1.00 34.06  ? 73  TRP C O     1 
ATOM   4917 C  CB    . TRP C 1 99  ? 123.563 135.830 167.457 1.00 23.83  ? 73  TRP C CB    1 
ATOM   4918 C  CG    . TRP C 1 99  ? 123.897 137.259 167.768 1.00 30.43  ? 73  TRP C CG    1 
ATOM   4919 C  CD1   . TRP C 1 99  ? 123.088 138.178 168.364 1.00 27.71  ? 73  TRP C CD1   1 
ATOM   4920 C  CD2   . TRP C 1 99  ? 125.148 137.919 167.537 1.00 28.00  ? 73  TRP C CD2   1 
ATOM   4921 N  NE1   . TRP C 1 99  ? 123.749 139.373 168.506 1.00 17.68  ? 73  TRP C NE1   1 
ATOM   4922 C  CE2   . TRP C 1 99  ? 125.017 139.240 168.003 1.00 26.78  ? 73  TRP C CE2   1 
ATOM   4923 C  CE3   . TRP C 1 99  ? 126.361 137.524 166.967 1.00 25.46  ? 73  TRP C CE3   1 
ATOM   4924 C  CZ2   . TRP C 1 99  ? 126.058 140.164 167.929 1.00 23.94  ? 73  TRP C CZ2   1 
ATOM   4925 C  CZ3   . TRP C 1 99  ? 127.388 138.446 166.885 1.00 21.32  ? 73  TRP C CZ3   1 
ATOM   4926 C  CH2   . TRP C 1 99  ? 127.230 139.750 167.362 1.00 20.45  ? 73  TRP C CH2   1 
ATOM   4927 N  N     . LEU C 1 100 ? 125.049 135.252 164.797 1.00 24.14  ? 74  LEU C N     1 
ATOM   4928 C  CA    . LEU C 1 100 ? 125.984 135.527 163.714 1.00 26.03  ? 74  LEU C CA    1 
ATOM   4929 C  C     . LEU C 1 100 ? 125.353 135.253 162.354 1.00 27.88  ? 74  LEU C C     1 
ATOM   4930 O  O     . LEU C 1 100 ? 125.595 135.999 161.401 1.00 34.48  ? 74  LEU C O     1 
ATOM   4931 C  CB    . LEU C 1 100 ? 127.254 134.694 163.900 1.00 28.30  ? 74  LEU C CB    1 
ATOM   4932 C  CG    . LEU C 1 100 ? 128.301 134.702 162.780 1.00 26.27  ? 74  LEU C CG    1 
ATOM   4933 C  CD1   . LEU C 1 100 ? 129.174 135.939 162.851 1.00 25.97  ? 74  LEU C CD1   1 
ATOM   4934 C  CD2   . LEU C 1 100 ? 129.147 133.449 162.831 1.00 25.05  ? 74  LEU C CD2   1 
ATOM   4935 N  N     . LEU C 1 101 ? 124.522 134.208 162.265 1.00 26.78  ? 75  LEU C N     1 
ATOM   4936 C  CA    . LEU C 1 101 ? 123.885 133.813 161.012 1.00 25.40  ? 75  LEU C CA    1 
ATOM   4937 C  C     . LEU C 1 101 ? 122.959 134.898 160.481 1.00 25.01  ? 75  LEU C C     1 
ATOM   4938 O  O     . LEU C 1 101 ? 122.978 135.215 159.286 1.00 29.01  ? 75  LEU C O     1 
ATOM   4939 C  CB    . LEU C 1 101 ? 123.114 132.511 161.237 1.00 30.87  ? 75  LEU C CB    1 
ATOM   4940 C  CG    . LEU C 1 101 ? 123.022 131.424 160.170 1.00 30.69  ? 75  LEU C CG    1 
ATOM   4941 C  CD1   . LEU C 1 101 ? 124.221 131.440 159.252 1.00 23.78  ? 75  LEU C CD1   1 
ATOM   4942 C  CD2   . LEU C 1 101 ? 122.879 130.068 160.839 1.00 28.06  ? 75  LEU C CD2   1 
ATOM   4943 N  N     . VAL C 1 102 ? 122.205 135.564 161.355 1.00 30.99  ? 76  VAL C N     1 
ATOM   4944 C  CA    . VAL C 1 102 ? 121.325 136.677 160.888 1.00 27.77  ? 76  VAL C CA    1 
ATOM   4945 C  C     . VAL C 1 102 ? 122.184 137.907 160.552 1.00 26.29  ? 76  VAL C C     1 
ATOM   4946 O  O     . VAL C 1 102 ? 121.930 138.522 159.504 1.00 37.46  ? 76  VAL C O     1 
ATOM   4947 C  CB    . VAL C 1 102 ? 120.195 136.992 161.886 1.00 27.98  ? 76  VAL C CB    1 
ATOM   4948 C  CG1   . VAL C 1 102 ? 119.365 138.189 161.454 1.00 27.14  ? 76  VAL C CG1   1 
ATOM   4949 C  CG2   . VAL C 1 102 ? 119.302 135.781 162.109 1.00 28.51  ? 76  VAL C CG2   1 
ATOM   4950 N  N     . GLY C 1 103 ? 123.163 138.240 161.393 1.00 32.99  ? 77  GLY C N     1 
ATOM   4951 C  CA    . GLY C 1 103 ? 124.057 139.393 161.169 1.00 23.22  ? 77  GLY C CA    1 
ATOM   4952 C  C     . GLY C 1 103 ? 124.939 139.324 159.934 1.00 20.97  ? 77  GLY C C     1 
ATOM   4953 O  O     . GLY C 1 103 ? 125.141 140.374 159.325 1.00 32.92  ? 77  GLY C O     1 
ATOM   4954 N  N     . ILE C 1 104 ? 125.506 138.169 159.601 1.00 33.53  ? 78  ILE C N     1 
ATOM   4955 C  CA    . ILE C 1 104 ? 126.469 138.045 158.460 1.00 27.63  ? 78  ILE C CA    1 
ATOM   4956 C  C     . ILE C 1 104 ? 125.734 137.773 157.139 1.00 37.22  ? 78  ILE C C     1 
ATOM   4957 O  O     . ILE C 1 104 ? 126.403 137.756 156.092 1.00 45.50  ? 78  ILE C O     1 
ATOM   4958 C  CB    . ILE C 1 104 ? 127.511 136.951 158.763 1.00 25.34  ? 78  ILE C CB    1 
ATOM   4959 C  CG1   . ILE C 1 104 ? 128.822 137.184 158.008 1.00 26.18  ? 78  ILE C CG1   1 
ATOM   4960 C  CG2   . ILE C 1 104 ? 126.938 135.558 158.502 1.00 28.45  ? 78  ILE C CG2   1 
ATOM   4961 C  CD1   . ILE C 1 104 ? 130.059 136.724 158.753 1.00 30.92  ? 78  ILE C CD1   1 
ATOM   4962 N  N     . SER C 1 105 ? 124.414 137.612 157.160 1.00 34.92  ? 79  SER C N     1 
ATOM   4963 C  CA    . SER C 1 105 ? 123.695 137.193 155.928 1.00 32.43  ? 79  SER C CA    1 
ATOM   4964 C  C     . SER C 1 105 ? 123.842 138.222 154.798 1.00 32.99  ? 79  SER C C     1 
ATOM   4965 O  O     . SER C 1 105 ? 124.009 137.796 153.642 1.00 38.29  ? 79  SER C O     1 
ATOM   4966 C  CB    . SER C 1 105 ? 122.240 136.924 156.225 1.00 35.74  ? 79  SER C CB    1 
ATOM   4967 O  OG    . SER C 1 105 ? 121.672 137.977 156.990 1.00 40.64  ? 79  SER C OG    1 
ATOM   4968 N  N     . MET C 1 106 ? 123.753 139.515 155.101 1.00 37.02  ? 80  MET C N     1 
ATOM   4969 C  CA    . MET C 1 106 ? 123.816 140.568 154.050 1.00 29.08  ? 80  MET C CA    1 
ATOM   4970 C  C     . MET C 1 106 ? 125.264 140.958 153.727 1.00 32.27  ? 80  MET C C     1 
ATOM   4971 O  O     . MET C 1 106 ? 125.458 141.583 152.682 1.00 36.17  ? 80  MET C O     1 
ATOM   4972 C  CB    . MET C 1 106 ? 123.020 141.798 154.496 1.00 23.60  ? 80  MET C CB    1 
ATOM   4973 C  CG    . MET C 1 106 ? 123.787 142.750 155.384 1.00 31.22  ? 80  MET C CG    1 
ATOM   4974 S  SD    . MET C 1 106 ? 124.063 142.160 157.065 1.00 52.92  ? 80  MET C SD    1 
ATOM   4975 C  CE    . MET C 1 106 ? 122.422 141.638 157.575 1.00 28.67  ? 80  MET C CE    1 
ATOM   4976 N  N     . TRP C 1 107 ? 126.234 140.535 154.536 1.00 29.14  ? 81  TRP C N     1 
ATOM   4977 C  CA    . TRP C 1 107 ? 127.639 140.980 154.363 1.00 27.68  ? 81  TRP C CA    1 
ATOM   4978 C  C     . TRP C 1 107 ? 128.207 140.527 153.027 1.00 20.61  ? 81  TRP C C     1 
ATOM   4979 O  O     . TRP C 1 107 ? 128.773 141.356 152.301 1.00 33.32  ? 81  TRP C O     1 
ATOM   4980 C  CB    . TRP C 1 107 ? 128.530 140.447 155.492 1.00 29.80  ? 81  TRP C CB    1 
ATOM   4981 C  CG    . TRP C 1 107 ? 129.986 140.608 155.152 1.00 26.40  ? 81  TRP C CG    1 
ATOM   4982 C  CD1   . TRP C 1 107 ? 130.902 139.622 154.937 1.00 19.85  ? 81  TRP C CD1   1 
ATOM   4983 C  CD2   . TRP C 1 107 ? 130.672 141.855 154.909 1.00 25.36  ? 81  TRP C CD2   1 
ATOM   4984 N  NE1   . TRP C 1 107 ? 132.109 140.166 154.598 1.00 25.86  ? 81  TRP C NE1   1 
ATOM   4985 C  CE2   . TRP C 1 107 ? 132.000 141.531 154.567 1.00 22.28  ? 81  TRP C CE2   1 
ATOM   4986 C  CE3   . TRP C 1 107 ? 130.296 143.203 154.949 1.00 19.27  ? 81  TRP C CE3   1 
ATOM   4987 C  CZ2   . TRP C 1 107 ? 132.948 142.505 154.273 1.00 25.91  ? 81  TRP C CZ2   1 
ATOM   4988 C  CZ3   . TRP C 1 107 ? 131.235 144.166 154.656 1.00 24.85  ? 81  TRP C CZ3   1 
ATOM   4989 C  CH2   . TRP C 1 107 ? 132.539 143.818 154.312 1.00 24.35  ? 81  TRP C CH2   1 
ATOM   4990 N  N     . PHE C 1 108 ? 128.084 139.244 152.735 1.00 23.00  ? 82  PHE C N     1 
ATOM   4991 C  CA    . PHE C 1 108 ? 128.677 138.699 151.516 1.00 22.58  ? 82  PHE C CA    1 
ATOM   4992 C  C     . PHE C 1 108 ? 128.124 139.389 150.277 1.00 28.46  ? 82  PHE C C     1 
ATOM   4993 O  O     . PHE C 1 108 ? 128.872 139.682 149.337 1.00 38.15  ? 82  PHE C O     1 
ATOM   4994 C  CB    . PHE C 1 108 ? 128.441 137.190 151.449 1.00 27.29  ? 82  PHE C CB    1 
ATOM   4995 C  CG    . PHE C 1 108 ? 128.956 136.446 152.648 1.00 35.25  ? 82  PHE C CG    1 
ATOM   4996 C  CD1   . PHE C 1 108 ? 130.318 136.263 152.835 1.00 26.46  ? 82  PHE C CD1   1 
ATOM   4997 C  CD2   . PHE C 1 108 ? 128.079 135.931 153.591 1.00 31.26  ? 82  PHE C CD2   1 
ATOM   4998 C  CE1   . PHE C 1 108 ? 130.797 135.583 153.939 1.00 21.41  ? 82  PHE C CE1   1 
ATOM   4999 C  CE2   . PHE C 1 108 ? 128.551 135.248 154.697 1.00 35.13  ? 82  PHE C CE2   1 
ATOM   5000 C  CZ    . PHE C 1 108 ? 129.911 135.073 154.871 1.00 28.98  ? 82  PHE C CZ    1 
ATOM   5001 N  N     . PHE C 1 109 ? 126.827 139.708 150.291 1.00 29.21  ? 83  PHE C N     1 
ATOM   5002 C  CA    . PHE C 1 109 ? 126.217 140.468 149.205 1.00 21.76  ? 83  PHE C CA    1 
ATOM   5003 C  C     . PHE C 1 109 ? 126.795 141.875 149.112 1.00 24.52  ? 83  PHE C C     1 
ATOM   5004 O  O     . PHE C 1 109 ? 127.106 142.346 148.016 1.00 28.06  ? 83  PHE C O     1 
ATOM   5005 C  CB    . PHE C 1 109 ? 124.702 140.525 149.398 1.00 26.58  ? 83  PHE C CB    1 
ATOM   5006 C  CG    . PHE C 1 109 ? 124.038 141.703 148.736 1.00 26.86  ? 83  PHE C CG    1 
ATOM   5007 C  CD1   . PHE C 1 109 ? 123.958 141.793 147.352 1.00 19.14  ? 83  PHE C CD1   1 
ATOM   5008 C  CD2   . PHE C 1 109 ? 123.479 142.715 149.501 1.00 21.43  ? 83  PHE C CD2   1 
ATOM   5009 C  CE1   . PHE C 1 109 ? 123.349 142.877 146.750 1.00 22.71  ? 83  PHE C CE1   1 
ATOM   5010 C  CE2   . PHE C 1 109 ? 122.868 143.799 148.902 1.00 19.16  ? 83  PHE C CE2   1 
ATOM   5011 C  CZ    . PHE C 1 109 ? 122.802 143.879 147.525 1.00 23.29  ? 83  PHE C CZ    1 
ATOM   5012 N  N     . ILE C 1 110 ? 126.944 142.554 150.256 1.00 22.19  ? 84  ILE C N     1 
ATOM   5013 C  CA    . ILE C 1 110 ? 127.448 143.929 150.270 1.00 24.08  ? 84  ILE C CA    1 
ATOM   5014 C  C     . ILE C 1 110 ? 128.887 143.974 149.772 1.00 29.21  ? 84  ILE C C     1 
ATOM   5015 O  O     . ILE C 1 110 ? 129.235 144.776 148.894 1.00 37.85  ? 84  ILE C O     1 
ATOM   5016 C  CB    . ILE C 1 110 ? 127.322 144.527 151.685 1.00 28.89  ? 84  ILE C CB    1 
ATOM   5017 C  CG1   . ILE C 1 110 ? 125.857 144.789 152.034 1.00 25.66  ? 84  ILE C CG1   1 
ATOM   5018 C  CG2   . ILE C 1 110 ? 128.139 145.807 151.822 1.00 23.17  ? 84  ILE C CG2   1 
ATOM   5019 C  CD1   . ILE C 1 110 ? 125.653 145.282 153.447 1.00 26.18  ? 84  ILE C CD1   1 
ATOM   5020 N  N     . ASN C 1 111 ? 129.720 143.065 150.284 1.00 26.59  ? 85  ASN C N     1 
ATOM   5021 C  CA    . ASN C 1 111 ? 131.128 142.999 149.908 1.00 27.24  ? 85  ASN C CA    1 
ATOM   5022 C  C     . ASN C 1 111 ? 131.298 142.649 148.434 1.00 27.82  ? 85  ASN C C     1 
ATOM   5023 O  O     . ASN C 1 111 ? 132.039 143.323 147.711 1.00 32.30  ? 85  ASN C O     1 
ATOM   5024 C  CB    . ASN C 1 111 ? 131.839 141.975 150.794 1.00 23.42  ? 85  ASN C CB    1 
ATOM   5025 C  CG    . ASN C 1 111 ? 133.336 141.966 150.598 1.00 29.72  ? 85  ASN C CG    1 
ATOM   5026 O  OD1   . ASN C 1 111 ? 134.006 142.974 150.807 1.00 35.58  ? 85  ASN C OD1   1 
ATOM   5027 N  ND2   . ASN C 1 111 ? 133.872 140.822 150.199 1.00 28.36  ? 85  ASN C ND2   1 
ATOM   5028 N  N     . GLN C 1 112 ? 130.570 141.632 147.959 1.00 28.17  ? 86  GLN C N     1 
ATOM   5029 C  CA    . GLN C 1 112 ? 130.713 141.196 146.575 1.00 24.95  ? 86  GLN C CA    1 
ATOM   5030 C  C     . GLN C 1 112 ? 130.129 142.213 145.601 1.00 29.97  ? 86  GLN C C     1 
ATOM   5031 O  O     . GLN C 1 112 ? 130.706 142.447 144.535 1.00 35.76  ? 86  GLN C O     1 
ATOM   5032 C  CB    . GLN C 1 112 ? 130.056 139.829 146.403 1.00 29.90  ? 86  GLN C CB    1 
ATOM   5033 C  CG    . GLN C 1 112 ? 131.027 138.670 146.513 1.00 36.87  ? 86  GLN C CG    1 
ATOM   5034 C  CD    . GLN C 1 112 ? 130.328 137.326 146.542 1.00 44.18  ? 86  GLN C CD    1 
ATOM   5035 O  OE1   . GLN C 1 112 ? 129.101 137.253 146.576 1.00 40.86  ? 86  GLN C OE1   1 
ATOM   5036 N  NE2   . GLN C 1 112 ? 131.109 136.254 146.526 1.00 38.08  ? 86  GLN C NE2   1 
ATOM   5037 N  N     . GLY C 1 113 ? 129.004 142.843 145.954 1.00 30.84  ? 87  GLY C N     1 
ATOM   5038 C  CA    . GLY C 1 113 ? 128.417 143.845 145.084 1.00 25.26  ? 87  GLY C CA    1 
ATOM   5039 C  C     . GLY C 1 113 ? 129.249 145.107 144.982 1.00 32.26  ? 87  GLY C C     1 
ATOM   5040 O  O     . GLY C 1 113 ? 129.405 145.666 143.894 1.00 40.36  ? 87  GLY C O     1 
ATOM   5041 N  N     . ILE C 1 114 ? 129.808 145.564 146.108 1.00 28.16  ? 88  ILE C N     1 
ATOM   5042 C  CA    . ILE C 1 114 ? 130.660 146.750 146.083 1.00 23.02  ? 88  ILE C CA    1 
ATOM   5043 C  C     . ILE C 1 114 ? 131.977 146.451 145.366 1.00 28.59  ? 88  ILE C C     1 
ATOM   5044 O  O     . ILE C 1 114 ? 132.478 147.286 144.603 1.00 38.34  ? 88  ILE C O     1 
ATOM   5045 C  CB    . ILE C 1 114 ? 130.857 147.282 147.518 1.00 29.76  ? 88  ILE C CB    1 
ATOM   5046 C  CG1   . ILE C 1 114 ? 129.553 147.909 148.018 1.00 25.45  ? 88  ILE C CG1   1 
ATOM   5047 C  CG2   . ILE C 1 114 ? 131.971 148.319 147.600 1.00 23.61  ? 88  ILE C CG2   1 
ATOM   5048 C  CD1   . ILE C 1 114 ? 129.612 148.439 149.431 1.00 33.72  ? 88  ILE C CD1   1 
ATOM   5049 N  N     . LEU C 1 115 ? 132.527 145.245 145.548 1.00 31.48  ? 89  LEU C N     1 
ATOM   5050 C  CA    . LEU C 1 115 ? 133.775 144.887 144.875 1.00 31.46  ? 89  LEU C CA    1 
ATOM   5051 C  C     . LEU C 1 115 ? 133.584 144.730 143.369 1.00 32.33  ? 89  LEU C C     1 
ATOM   5052 O  O     . LEU C 1 115 ? 134.349 145.291 142.577 1.00 33.15  ? 89  LEU C O     1 
ATOM   5053 C  CB    . LEU C 1 115 ? 134.342 143.599 145.472 1.00 31.29  ? 89  LEU C CB    1 
ATOM   5054 C  CG    . LEU C 1 115 ? 135.251 143.725 146.693 1.00 36.49  ? 89  LEU C CG    1 
ATOM   5055 C  CD1   . LEU C 1 115 ? 135.746 142.359 147.142 1.00 34.69  ? 89  LEU C CD1   1 
ATOM   5056 C  CD2   . LEU C 1 115 ? 136.417 144.660 146.412 1.00 34.33  ? 89  LEU C CD2   1 
ATOM   5057 N  N     . GLU C 1 116 ? 132.567 143.973 142.952 1.00 35.38  ? 90  GLU C N     1 
ATOM   5058 C  CA    . GLU C 1 116 ? 132.391 143.672 141.538 1.00 31.97  ? 90  GLU C CA    1 
ATOM   5059 C  C     . GLU C 1 116 ? 131.777 144.828 140.764 1.00 33.14  ? 90  GLU C C     1 
ATOM   5060 O  O     . GLU C 1 116 ? 132.108 145.021 139.590 1.00 43.69  ? 90  GLU C O     1 
ATOM   5061 C  CB    . GLU C 1 116 ? 131.527 142.421 141.374 1.00 33.87  ? 90  GLU C CB    1 
ATOM   5062 C  CG    . GLU C 1 116 ? 132.311 141.129 141.438 1.00 35.00  ? 90  GLU C CG    1 
ATOM   5063 C  CD    . GLU C 1 116 ? 131.620 140.075 142.275 1.00 46.51  ? 90  GLU C CD    1 
ATOM   5064 O  OE1   . GLU C 1 116 ? 132.248 139.568 143.229 1.00 47.50  ? 90  GLU C OE1   1 
ATOM   5065 O  OE2   . GLU C 1 116 ? 130.452 139.753 141.980 1.00 45.66  ? 90  GLU C OE2   1 
ATOM   5066 N  N     . GLY C 1 117 ? 130.881 145.593 141.382 1.00 23.85  ? 91  GLY C N     1 
ATOM   5067 C  CA    . GLY C 1 117 ? 130.250 146.667 140.651 1.00 28.59  ? 91  GLY C CA    1 
ATOM   5068 C  C     . GLY C 1 117 ? 131.007 147.974 140.622 1.00 29.32  ? 91  GLY C C     1 
ATOM   5069 O  O     . GLY C 1 117 ? 130.598 148.886 139.899 1.00 40.61  ? 91  GLY C O     1 
ATOM   5070 N  N     . THR C 1 118 ? 132.078 148.100 141.410 1.00 31.38  ? 92  THR C N     1 
ATOM   5071 C  CA    . THR C 1 118 ? 132.983 149.235 141.257 1.00 29.65  ? 92  THR C CA    1 
ATOM   5072 C  C     . THR C 1 118 ? 133.689 149.177 139.909 1.00 32.89  ? 92  THR C C     1 
ATOM   5073 O  O     . THR C 1 118 ? 133.910 150.208 139.263 1.00 40.60  ? 92  THR C O     1 
ATOM   5074 C  CB    . THR C 1 118 ? 133.995 149.253 142.408 1.00 32.28  ? 92  THR C CB    1 
ATOM   5075 O  OG1   . THR C 1 118 ? 133.294 149.274 143.656 1.00 37.11  ? 92  THR C OG1   1 
ATOM   5076 C  CG2   . THR C 1 118 ? 134.906 150.472 142.340 1.00 33.13  ? 92  THR C CG2   1 
ATOM   5077 N  N     . LYS C 1 119 ? 134.022 147.974 139.451 1.00 34.18  ? 93  LYS C N     1 
ATOM   5078 C  CA    . LYS C 1 119 ? 134.685 147.782 138.174 1.00 37.07  ? 93  LYS C CA    1 
ATOM   5079 C  C     . LYS C 1 119 ? 133.719 147.383 137.065 1.00 32.38  ? 93  LYS C C     1 
ATOM   5080 O  O     . LYS C 1 119 ? 134.169 146.921 136.017 1.00 37.61  ? 93  LYS C O     1 
ATOM   5081 C  CB    . LYS C 1 119 ? 135.791 146.736 138.313 1.00 39.22  ? 93  LYS C CB    1 
ATOM   5082 C  CG    . LYS C 1 119 ? 135.359 145.483 139.043 1.00 31.85  ? 93  LYS C CG    1 
ATOM   5083 C  CD    . LYS C 1 119 ? 136.449 144.430 139.032 1.00 40.29  ? 93  LYS C CD    1 
ATOM   5084 C  CE    . LYS C 1 119 ? 137.205 144.415 140.347 1.00 36.17  ? 93  LYS C CE    1 
ATOM   5085 N  NZ    . LYS C 1 119 ? 138.636 144.057 140.161 1.00 43.84  ? 93  LYS C NZ    1 
ATOM   5086 N  N     . ALA C 1 120 ? 132.409 147.561 137.274 1.00 33.22  ? 94  ALA C N     1 
ATOM   5087 C  CA    . ALA C 1 120 ? 131.413 147.037 136.339 1.00 30.86  ? 94  ALA C CA    1 
ATOM   5088 C  C     . ALA C 1 120 ? 131.448 147.768 135.002 1.00 39.99  ? 94  ALA C C     1 
ATOM   5089 O  O     . ALA C 1 120 ? 131.419 147.140 133.937 1.00 42.01  ? 94  ALA C O     1 
ATOM   5090 C  CB    . ALA C 1 120 ? 130.018 147.125 136.956 1.00 23.75  ? 94  ALA C CB    1 
ATOM   5091 N  N     . ILE C 1 121 ? 131.525 149.100 135.037 1.00 37.90  ? 95  ILE C N     1 
ATOM   5092 C  CA    . ILE C 1 121 ? 131.625 149.871 133.802 1.00 31.84  ? 95  ILE C CA    1 
ATOM   5093 C  C     . ILE C 1 121 ? 133.016 149.716 133.189 1.00 30.49  ? 95  ILE C C     1 
ATOM   5094 O  O     . ILE C 1 121 ? 133.203 149.900 131.983 1.00 41.57  ? 95  ILE C O     1 
ATOM   5095 C  CB    . ILE C 1 121 ? 131.257 151.345 134.075 1.00 35.93  ? 95  ILE C CB    1 
ATOM   5096 C  CG1   . ILE C 1 121 ? 129.969 151.426 134.897 1.00 35.27  ? 95  ILE C CG1   1 
ATOM   5097 C  CG2   . ILE C 1 121 ? 131.049 152.133 132.781 1.00 37.68  ? 95  ILE C CG2   1 
ATOM   5098 C  CD1   . ILE C 1 121 ? 129.513 152.839 135.199 1.00 33.83  ? 95  ILE C CD1   1 
ATOM   5099 N  N     . THR C 1 122 ? 134.009 149.335 133.997 1.00 36.71  ? 96  THR C N     1 
ATOM   5100 C  CA    . THR C 1 122 ? 135.356 149.139 133.468 1.00 39.61  ? 96  THR C CA    1 
ATOM   5101 C  C     . THR C 1 122 ? 135.443 147.928 132.538 1.00 37.60  ? 96  THR C C     1 
ATOM   5102 O  O     . THR C 1 122 ? 136.172 147.971 131.541 1.00 46.58  ? 96  THR C O     1 
ATOM   5103 C  CB    . THR C 1 122 ? 136.359 149.009 134.615 1.00 38.53  ? 96  THR C CB    1 
ATOM   5104 O  OG1   . THR C 1 122 ? 136.033 149.955 135.640 1.00 49.99  ? 96  THR C OG1   1 
ATOM   5105 C  CG2   . THR C 1 122 ? 137.767 149.281 134.128 1.00 38.49  ? 96  THR C CG2   1 
ATOM   5106 N  N     . GLN C 1 123 ? 134.700 146.855 132.818 1.00 38.61  ? 97  GLN C N     1 
ATOM   5107 C  CA    . GLN C 1 123 ? 134.734 145.677 131.959 1.00 43.63  ? 97  GLN C CA    1 
ATOM   5108 C  C     . GLN C 1 123 ? 133.439 145.437 131.195 1.00 39.51  ? 97  GLN C C     1 
ATOM   5109 O  O     . GLN C 1 123 ? 133.352 144.448 130.462 1.00 48.91  ? 97  GLN C O     1 
ATOM   5110 C  CB    . GLN C 1 123 ? 135.073 144.414 132.764 1.00 47.67  ? 97  GLN C CB    1 
ATOM   5111 C  CG    . GLN C 1 123 ? 134.477 144.361 134.147 1.00 40.18  ? 97  GLN C CG    1 
ATOM   5112 C  CD    . GLN C 1 123 ? 134.950 143.173 134.956 1.00 50.39  ? 97  GLN C CD    1 
ATOM   5113 O  OE1   . GLN C 1 123 ? 135.855 143.292 135.783 1.00 47.72  ? 97  GLN C OE1   1 
ATOM   5114 N  NE2   . GLN C 1 123 ? 134.336 142.018 134.728 1.00 49.27  ? 97  GLN C NE2   1 
ATOM   5115 N  N     . LYS C 1 124 ? 132.432 146.300 131.336 1.00 40.86  ? 98  LYS C N     1 
ATOM   5116 C  CA    . LYS C 1 124 ? 131.164 146.083 130.656 1.00 38.12  ? 98  LYS C CA    1 
ATOM   5117 C  C     . LYS C 1 124 ? 130.731 147.227 129.751 1.00 44.83  ? 98  LYS C C     1 
ATOM   5118 O  O     . LYS C 1 124 ? 129.670 147.122 129.126 1.00 49.09  ? 98  LYS C O     1 
ATOM   5119 C  CB    . LYS C 1 124 ? 130.056 145.804 131.681 1.00 42.16  ? 98  LYS C CB    1 
ATOM   5120 C  CG    . LYS C 1 124 ? 129.827 144.329 131.956 1.00 41.32  ? 98  LYS C CG    1 
ATOM   5121 C  CD    . LYS C 1 124 ? 130.432 143.919 133.285 1.00 50.54  ? 98  LYS C CD    1 
ATOM   5122 C  CE    . LYS C 1 124 ? 130.200 142.449 133.568 1.00 44.52  ? 98  LYS C CE    1 
ATOM   5123 N  NZ    . LYS C 1 124 ? 130.457 141.612 132.366 1.00 47.17  ? 98  LYS C NZ    1 
ATOM   5124 N  N     . PHE C 1 125 ? 131.503 148.312 129.658 1.00 44.29  ? 99  PHE C N     1 
ATOM   5125 C  CA    . PHE C 1 125 ? 131.092 149.435 128.817 1.00 43.06  ? 99  PHE C CA    1 
ATOM   5126 C  C     . PHE C 1 125 ? 131.265 149.118 127.339 1.00 46.96  ? 99  PHE C C     1 
ATOM   5127 O  O     . PHE C 1 125 ? 130.426 149.504 126.518 1.00 50.22  ? 99  PHE C O     1 
ATOM   5128 C  CB    . PHE C 1 125 ? 131.880 150.694 129.186 1.00 40.54  ? 99  PHE C CB    1 
ATOM   5129 C  CG    . PHE C 1 125 ? 131.649 151.860 128.267 1.00 42.80  ? 99  PHE C CG    1 
ATOM   5130 C  CD1   . PHE C 1 125 ? 130.472 152.588 128.333 1.00 42.29  ? 99  PHE C CD1   1 
ATOM   5131 C  CD2   . PHE C 1 125 ? 132.620 152.240 127.350 1.00 43.10  ? 99  PHE C CD2   1 
ATOM   5132 C  CE1   . PHE C 1 125 ? 130.262 153.666 127.489 1.00 42.21  ? 99  PHE C CE1   1 
ATOM   5133 C  CE2   . PHE C 1 125 ? 132.413 153.312 126.506 1.00 44.78  ? 99  PHE C CE2   1 
ATOM   5134 C  CZ    . PHE C 1 125 ? 131.233 154.027 126.576 1.00 40.01  ? 99  PHE C CZ    1 
ATOM   5135 N  N     . ASN C 1 126 ? 132.343 148.413 126.983 1.00 49.03  ? 100 ASN C N     1 
ATOM   5136 C  CA    . ASN C 1 126 ? 132.695 148.227 125.578 1.00 48.17  ? 100 ASN C CA    1 
ATOM   5137 C  C     . ASN C 1 126 ? 131.738 147.282 124.862 1.00 51.85  ? 100 ASN C C     1 
ATOM   5138 O  O     . ASN C 1 126 ? 131.603 147.357 123.636 1.00 55.49  ? 100 ASN C O     1 
ATOM   5139 C  CB    . ASN C 1 126 ? 134.128 147.711 125.463 1.00 47.85  ? 100 ASN C CB    1 
ATOM   5140 C  CG    . ASN C 1 126 ? 135.114 148.810 125.135 1.00 53.50  ? 100 ASN C CG    1 
ATOM   5141 O  OD1   . ASN C 1 126 ? 134.933 149.552 124.170 1.00 54.79  ? 100 ASN C OD1   1 
ATOM   5142 N  ND2   . ASN C 1 126 ? 136.164 148.923 125.939 1.00 53.13  ? 100 ASN C ND2   1 
ATOM   5143 N  N     . GLN C 1 127 ? 131.069 146.396 125.595 1.00 52.78  ? 101 GLN C N     1 
ATOM   5144 C  CA    . GLN C 1 127 ? 130.119 145.487 124.972 1.00 50.68  ? 101 GLN C CA    1 
ATOM   5145 C  C     . GLN C 1 127 ? 128.748 146.114 124.758 1.00 51.58  ? 101 GLN C C     1 
ATOM   5146 O  O     . GLN C 1 127 ? 127.914 145.508 124.077 1.00 54.08  ? 101 GLN C O     1 
ATOM   5147 C  CB    . GLN C 1 127 ? 129.981 144.214 125.811 1.00 53.33  ? 101 GLN C CB    1 
ATOM   5148 C  CG    . GLN C 1 127 ? 129.350 144.425 127.173 1.00 53.38  ? 101 GLN C CG    1 
ATOM   5149 C  CD    . GLN C 1 127 ? 129.372 143.170 128.023 1.00 58.56  ? 101 GLN C CD    1 
ATOM   5150 O  OE1   . GLN C 1 127 ? 128.326 142.670 128.438 1.00 57.63  ? 101 GLN C OE1   1 
ATOM   5151 N  NE2   . GLN C 1 127 ? 130.567 142.655 128.288 1.00 54.34  ? 101 GLN C NE2   1 
ATOM   5152 N  N     . VAL C 1 128 ? 128.487 147.297 125.316 1.00 51.40  ? 102 VAL C N     1 
ATOM   5153 C  CA    . VAL C 1 128 ? 127.200 147.967 125.144 1.00 53.81  ? 102 VAL C CA    1 
ATOM   5154 C  C     . VAL C 1 128 ? 127.407 149.400 124.670 1.00 54.16  ? 102 VAL C C     1 
ATOM   5155 O  O     . VAL C 1 128 ? 126.464 150.199 124.670 1.00 57.35  ? 102 VAL C O     1 
ATOM   5156 C  CB    . VAL C 1 128 ? 126.373 147.954 126.445 1.00 53.56  ? 102 VAL C CB    1 
ATOM   5157 C  CG1   . VAL C 1 128 ? 125.945 146.540 126.820 1.00 50.22  ? 102 VAL C CG1   1 
ATOM   5158 C  CG2   . VAL C 1 128 ? 127.145 148.614 127.577 1.00 50.15  ? 102 VAL C CG2   1 
ATOM   5159 N  N     . SER C 1 129 ? 128.640 149.740 124.276 1.00 50.67  ? 103 SER C N     1 
ATOM   5160 C  CA    . SER C 1 129 ? 128.942 151.117 123.887 1.00 51.57  ? 103 SER C CA    1 
ATOM   5161 C  C     . SER C 1 129 ? 128.296 151.481 122.557 1.00 55.93  ? 103 SER C C     1 
ATOM   5162 O  O     . SER C 1 129 ? 127.794 152.597 122.386 1.00 55.15  ? 103 SER C O     1 
ATOM   5163 C  CB    . SER C 1 129 ? 130.454 151.331 123.818 1.00 49.55  ? 103 SER C CB    1 
ATOM   5164 O  OG    . SER C 1 129 ? 131.068 150.371 122.978 1.00 57.85  ? 103 SER C OG    1 
ATOM   5165 N  N     . LYS C 1 130 ? 128.296 150.553 121.602 1.00 48.72  ? 104 LYS C N     1 
ATOM   5166 C  CA    . LYS C 1 130 ? 127.719 150.813 120.290 1.00 49.70  ? 104 LYS C CA    1 
ATOM   5167 C  C     . LYS C 1 130 ? 126.221 150.552 120.233 1.00 54.84  ? 104 LYS C C     1 
ATOM   5168 O  O     . LYS C 1 130 ? 125.608 150.795 119.188 1.00 58.59  ? 104 LYS C O     1 
ATOM   5169 C  CB    . LYS C 1 130 ? 128.441 149.981 119.229 1.00 47.50  ? 104 LYS C CB    1 
ATOM   5170 C  CG    . LYS C 1 130 ? 129.815 150.524 118.875 1.00 46.64  ? 104 LYS C CG    1 
ATOM   5171 C  CD    . LYS C 1 130 ? 130.763 149.426 118.437 1.00 53.40  ? 104 LYS C CD    1 
ATOM   5172 C  CE    . LYS C 1 130 ? 132.005 150.012 117.787 1.00 53.88  ? 104 LYS C CE    1 
ATOM   5173 N  NZ    . LYS C 1 130 ? 133.153 150.074 118.733 1.00 52.81  ? 104 LYS C NZ    1 
ATOM   5174 N  N     . MET C 1 131 ? 125.620 150.068 121.315 1.00 54.80  ? 105 MET C N     1 
ATOM   5175 C  CA    . MET C 1 131 ? 124.178 149.894 121.401 1.00 51.11  ? 105 MET C CA    1 
ATOM   5176 C  C     . MET C 1 131 ? 123.579 151.007 122.247 1.00 56.26  ? 105 MET C C     1 
ATOM   5177 O  O     . MET C 1 131 ? 124.224 151.517 123.167 1.00 57.32  ? 105 MET C O     1 
ATOM   5178 C  CB    . MET C 1 131 ? 123.818 148.537 122.007 1.00 51.74  ? 105 MET C CB    1 
ATOM   5179 C  CG    . MET C 1 131 ? 124.580 147.360 121.434 1.00 56.71  ? 105 MET C CG    1 
ATOM   5180 S  SD    . MET C 1 131 ? 124.997 146.156 122.707 1.00 66.83  ? 105 MET C SD    1 
ATOM   5181 C  CE    . MET C 1 131 ? 125.109 144.656 121.741 1.00 52.89  ? 105 MET C CE    1 
ATOM   5182 N  N     . ASN C 1 132 ? 122.342 151.385 121.929 1.00 66.15  ? 106 ASN C N     1 
ATOM   5183 C  CA    . ASN C 1 132 ? 121.628 152.361 122.741 1.00 62.91  ? 106 ASN C CA    1 
ATOM   5184 C  C     . ASN C 1 132 ? 121.171 151.700 124.035 1.00 63.66  ? 106 ASN C C     1 
ATOM   5185 O  O     . ASN C 1 132 ? 120.129 151.039 124.072 1.00 59.31  ? 106 ASN C O     1 
ATOM   5186 C  CB    . ASN C 1 132 ? 120.439 152.944 121.974 1.00 59.77  ? 106 ASN C CB    1 
ATOM   5187 C  CG    . ASN C 1 132 ? 120.464 154.459 121.931 1.00 62.68  ? 106 ASN C CG    1 
ATOM   5188 O  OD1   . ASN C 1 132 ? 121.530 155.071 121.875 1.00 59.94  ? 106 ASN C OD1   1 
ATOM   5189 N  ND2   . ASN C 1 132 ? 119.287 155.071 121.956 1.00 62.91  ? 106 ASN C ND2   1 
ATOM   5190 N  N     . PHE C 1 133 ? 121.955 151.873 125.097 1.00 50.46  ? 107 PHE C N     1 
ATOM   5191 C  CA    . PHE C 1 133 ? 121.762 151.155 126.343 1.00 47.34  ? 107 PHE C CA    1 
ATOM   5192 C  C     . PHE C 1 133 ? 121.691 152.135 127.507 1.00 49.79  ? 107 PHE C C     1 
ATOM   5193 O  O     . PHE C 1 133 ? 122.421 153.134 127.521 1.00 49.01  ? 107 PHE C O     1 
ATOM   5194 C  CB    . PHE C 1 133 ? 122.916 150.162 126.561 1.00 44.36  ? 107 PHE C CB    1 
ATOM   5195 C  CG    . PHE C 1 133 ? 122.664 149.159 127.647 1.00 45.21  ? 107 PHE C CG    1 
ATOM   5196 C  CD1   . PHE C 1 133 ? 121.914 148.021 127.395 1.00 47.41  ? 107 PHE C CD1   1 
ATOM   5197 C  CD2   . PHE C 1 133 ? 123.192 149.344 128.915 1.00 40.66  ? 107 PHE C CD2   1 
ATOM   5198 C  CE1   . PHE C 1 133 ? 121.686 147.090 128.391 1.00 44.69  ? 107 PHE C CE1   1 
ATOM   5199 C  CE2   . PHE C 1 133 ? 122.967 148.419 129.915 1.00 41.26  ? 107 PHE C CE2   1 
ATOM   5200 C  CZ    . PHE C 1 133 ? 122.213 147.291 129.653 1.00 45.55  ? 107 PHE C CZ    1 
ATOM   5201 N  N     . PRO C 1 134 ? 120.815 151.887 128.493 1.00 52.89  ? 108 PRO C N     1 
ATOM   5202 C  CA    . PRO C 1 134 ? 120.835 152.702 129.717 1.00 45.42  ? 108 PRO C CA    1 
ATOM   5203 C  C     . PRO C 1 134 ? 122.049 152.380 130.575 1.00 41.23  ? 108 PRO C C     1 
ATOM   5204 O  O     . PRO C 1 134 ? 122.107 151.327 131.214 1.00 48.12  ? 108 PRO C O     1 
ATOM   5205 C  CB    . PRO C 1 134 ? 119.523 152.327 130.416 1.00 38.04  ? 108 PRO C CB    1 
ATOM   5206 C  CG    . PRO C 1 134 ? 119.140 151.003 129.848 1.00 35.79  ? 108 PRO C CG    1 
ATOM   5207 C  CD    . PRO C 1 134 ? 119.671 150.959 128.452 1.00 37.36  ? 108 PRO C CD    1 
ATOM   5208 N  N     . LEU C 1 135 ? 123.022 153.293 130.604 1.00 28.92  ? 109 LEU C N     1 
ATOM   5209 C  CA    . LEU C 1 135 ? 124.336 152.958 131.143 1.00 29.59  ? 109 LEU C CA    1 
ATOM   5210 C  C     . LEU C 1 135 ? 124.354 152.929 132.667 1.00 36.95  ? 109 LEU C C     1 
ATOM   5211 O  O     . LEU C 1 135 ? 125.279 152.361 133.258 1.00 41.92  ? 109 LEU C O     1 
ATOM   5212 C  CB    . LEU C 1 135 ? 125.380 153.946 130.625 1.00 35.10  ? 109 LEU C CB    1 
ATOM   5213 C  CG    . LEU C 1 135 ? 125.937 153.665 129.229 1.00 41.91  ? 109 LEU C CG    1 
ATOM   5214 C  CD1   . LEU C 1 135 ? 126.566 154.916 128.637 1.00 38.89  ? 109 LEU C CD1   1 
ATOM   5215 C  CD2   . LEU C 1 135 ? 126.933 152.523 129.268 1.00 42.31  ? 109 LEU C CD2   1 
ATOM   5216 N  N     . SER C 1 136 ? 123.355 153.521 133.322 1.00 34.00  ? 110 SER C N     1 
ATOM   5217 C  CA    . SER C 1 136 ? 123.376 153.602 134.777 1.00 25.33  ? 110 SER C CA    1 
ATOM   5218 C  C     . SER C 1 136 ? 122.911 152.320 135.456 1.00 31.42  ? 110 SER C C     1 
ATOM   5219 O  O     . SER C 1 136 ? 123.022 152.218 136.681 1.00 42.08  ? 110 SER C O     1 
ATOM   5220 C  CB    . SER C 1 136 ? 122.520 154.779 135.253 1.00 27.91  ? 110 SER C CB    1 
ATOM   5221 O  OG    . SER C 1 136 ? 121.229 154.747 134.675 1.00 30.36  ? 110 SER C OG    1 
ATOM   5222 N  N     . ILE C 1 137 ? 122.402 151.338 134.702 1.00 35.34  ? 111 ILE C N     1 
ATOM   5223 C  CA    . ILE C 1 137 ? 121.881 150.115 135.302 1.00 26.45  ? 111 ILE C CA    1 
ATOM   5224 C  C     . ILE C 1 137 ? 122.885 148.971 135.289 1.00 28.26  ? 111 ILE C C     1 
ATOM   5225 O  O     . ILE C 1 137 ? 122.576 147.890 135.810 1.00 43.73  ? 111 ILE C O     1 
ATOM   5226 C  CB    . ILE C 1 137 ? 120.580 149.664 134.602 1.00 30.24  ? 111 ILE C CB    1 
ATOM   5227 C  CG1   . ILE C 1 137 ? 120.884 149.031 133.240 1.00 31.48  ? 111 ILE C CG1   1 
ATOM   5228 C  CG2   . ILE C 1 137 ? 119.622 150.830 134.457 1.00 22.52  ? 111 ILE C CG2   1 
ATOM   5229 C  CD1   . ILE C 1 137 ? 119.700 148.341 132.610 1.00 31.88  ? 111 ILE C CD1   1 
ATOM   5230 N  N     . ILE C 1 138 ? 124.066 149.167 134.708 1.00 24.43  ? 112 ILE C N     1 
ATOM   5231 C  CA    . ILE C 1 138 ? 125.120 148.148 134.690 1.00 25.35  ? 112 ILE C CA    1 
ATOM   5232 C  C     . ILE C 1 138 ? 125.604 147.796 136.103 1.00 26.62  ? 112 ILE C C     1 
ATOM   5233 O  O     . ILE C 1 138 ? 125.586 146.594 136.445 1.00 35.53  ? 112 ILE C O     1 
ATOM   5234 C  CB    . ILE C 1 138 ? 126.274 148.563 133.751 1.00 28.95  ? 112 ILE C CB    1 
ATOM   5235 C  CG1   . ILE C 1 138 ? 125.788 148.643 132.303 1.00 34.49  ? 112 ILE C CG1   1 
ATOM   5236 C  CG2   . ILE C 1 138 ? 127.449 147.608 133.873 1.00 29.36  ? 112 ILE C CG2   1 
ATOM   5237 C  CD1   . ILE C 1 138 ? 126.727 149.387 131.388 1.00 30.50  ? 112 ILE C CD1   1 
ATOM   5238 N  N     . PRO C 1 139 ? 125.987 148.749 136.988 1.00 34.38  ? 113 PRO C N     1 
ATOM   5239 C  CA    . PRO C 1 139 ? 126.307 148.325 138.362 1.00 27.41  ? 113 PRO C CA    1 
ATOM   5240 C  C     . PRO C 1 139 ? 125.104 147.815 139.136 1.00 25.78  ? 113 PRO C C     1 
ATOM   5241 O  O     . PRO C 1 139 ? 125.272 147.003 140.051 1.00 36.12  ? 113 PRO C O     1 
ATOM   5242 C  CB    . PRO C 1 139 ? 126.889 149.598 138.988 1.00 29.84  ? 113 PRO C CB    1 
ATOM   5243 C  CG    . PRO C 1 139 ? 126.230 150.677 138.290 1.00 24.07  ? 113 PRO C CG    1 
ATOM   5244 C  CD    . PRO C 1 139 ? 126.192 150.217 136.880 1.00 27.64  ? 113 PRO C CD    1 
ATOM   5245 N  N     . THR C 1 140 ? 123.890 148.232 138.761 1.00 20.63  ? 114 THR C N     1 
ATOM   5246 C  CA    . THR C 1 140 ? 122.692 147.758 139.444 1.00 21.67  ? 114 THR C CA    1 
ATOM   5247 C  C     . THR C 1 140 ? 122.429 146.280 139.168 1.00 26.57  ? 114 THR C C     1 
ATOM   5248 O  O     . THR C 1 140 ? 122.080 145.528 140.085 1.00 33.94  ? 114 THR C O     1 
ATOM   5249 C  CB    . THR C 1 140 ? 121.489 148.609 139.038 1.00 26.57  ? 114 THR C CB    1 
ATOM   5250 O  OG1   . THR C 1 140 ? 121.870 149.989 139.026 1.00 36.80  ? 114 THR C OG1   1 
ATOM   5251 C  CG2   . THR C 1 140 ? 120.347 148.422 140.023 1.00 26.53  ? 114 THR C CG2   1 
ATOM   5252 N  N     . TYR C 1 141 ? 122.608 145.830 137.920 1.00 26.98  ? 115 TYR C N     1 
ATOM   5253 C  CA    . TYR C 1 141 ? 122.413 144.404 137.662 1.00 24.64  ? 115 TYR C CA    1 
ATOM   5254 C  C     . TYR C 1 141 ? 123.589 143.581 138.174 1.00 28.72  ? 115 TYR C C     1 
ATOM   5255 O  O     . TYR C 1 141 ? 123.397 142.420 138.568 1.00 38.64  ? 115 TYR C O     1 
ATOM   5256 C  CB    . TYR C 1 141 ? 122.109 144.146 136.170 1.00 28.43  ? 115 TYR C CB    1 
ATOM   5257 C  CG    . TYR C 1 141 ? 123.262 143.888 135.202 1.00 28.83  ? 115 TYR C CG    1 
ATOM   5258 C  CD1   . TYR C 1 141 ? 123.821 142.617 135.042 1.00 28.29  ? 115 TYR C CD1   1 
ATOM   5259 C  CD2   . TYR C 1 141 ? 123.729 144.903 134.386 1.00 27.02  ? 115 TYR C CD2   1 
ATOM   5260 C  CE1   . TYR C 1 141 ? 124.850 142.393 134.150 1.00 31.31  ? 115 TYR C CE1   1 
ATOM   5261 C  CE2   . TYR C 1 141 ? 124.755 144.689 133.487 1.00 25.58  ? 115 TYR C CE2   1 
ATOM   5262 C  CZ    . TYR C 1 141 ? 125.310 143.434 133.372 1.00 33.33  ? 115 TYR C CZ    1 
ATOM   5263 O  OH    . TYR C 1 141 ? 126.328 143.222 132.475 1.00 39.98  ? 115 TYR C OH    1 
ATOM   5264 N  N     . ILE C 1 142 ? 124.796 144.167 138.213 1.00 26.68  ? 116 ILE C N     1 
ATOM   5265 C  CA    . ILE C 1 142 ? 125.918 143.480 138.859 1.00 23.75  ? 116 ILE C CA    1 
ATOM   5266 C  C     . ILE C 1 142 ? 125.649 143.290 140.357 1.00 29.54  ? 116 ILE C C     1 
ATOM   5267 O  O     . ILE C 1 142 ? 125.964 142.238 140.931 1.00 40.92  ? 116 ILE C O     1 
ATOM   5268 C  CB    . ILE C 1 142 ? 127.234 144.240 138.584 1.00 32.42  ? 116 ILE C CB    1 
ATOM   5269 C  CG1   . ILE C 1 142 ? 127.598 144.144 137.101 1.00 29.80  ? 116 ILE C CG1   1 
ATOM   5270 C  CG2   . ILE C 1 142 ? 128.390 143.691 139.402 1.00 31.02  ? 116 ILE C CG2   1 
ATOM   5271 C  CD1   . ILE C 1 142 ? 127.907 142.741 136.623 1.00 26.26  ? 116 ILE C CD1   1 
ATOM   5272 N  N     . VAL C 1 143 ? 125.009 144.274 140.997 1.00 25.48  ? 117 VAL C N     1 
ATOM   5273 C  CA    . VAL C 1 143 ? 124.622 144.146 142.403 1.00 23.35  ? 117 VAL C CA    1 
ATOM   5274 C  C     . VAL C 1 143 ? 123.485 143.131 142.573 1.00 20.93  ? 117 VAL C C     1 
ATOM   5275 O  O     . VAL C 1 143 ? 123.488 142.324 143.516 1.00 38.38  ? 117 VAL C O     1 
ATOM   5276 C  CB    . VAL C 1 143 ? 124.264 145.541 142.963 1.00 30.28  ? 117 VAL C CB    1 
ATOM   5277 C  CG1   . VAL C 1 143 ? 123.381 145.468 144.201 1.00 24.19  ? 117 VAL C CG1   1 
ATOM   5278 C  CG2   . VAL C 1 143 ? 125.532 146.319 143.283 1.00 23.83  ? 117 VAL C CG2   1 
ATOM   5279 N  N     . THR C 1 144 ? 122.516 143.127 141.648 1.00 11.75  ? 118 THR C N     1 
ATOM   5280 C  CA    . THR C 1 144 ? 121.372 142.214 141.741 1.00 27.74  ? 118 THR C CA    1 
ATOM   5281 C  C     . THR C 1 144 ? 121.783 140.752 141.572 1.00 25.33  ? 118 THR C C     1 
ATOM   5282 O  O     . THR C 1 144 ? 121.141 139.851 142.148 1.00 35.77  ? 118 THR C O     1 
ATOM   5283 C  CB    . THR C 1 144 ? 120.320 142.592 140.695 1.00 23.04  ? 118 THR C CB    1 
ATOM   5284 O  OG1   . THR C 1 144 ? 120.291 144.015 140.536 1.00 29.66  ? 118 THR C OG1   1 
ATOM   5285 C  CG2   . THR C 1 144 ? 118.940 142.114 141.117 1.00 23.40  ? 118 THR C CG2   1 
ATOM   5286 N  N     . SER C 1 145 ? 122.860 140.504 140.815 1.00 22.48  ? 119 SER C N     1 
ATOM   5287 C  CA    . SER C 1 145 ? 123.389 139.149 140.668 1.00 19.68  ? 119 SER C CA    1 
ATOM   5288 C  C     . SER C 1 145 ? 123.880 138.570 141.997 1.00 31.40  ? 119 SER C C     1 
ATOM   5289 O  O     . SER C 1 145 ? 123.864 137.350 142.193 1.00 37.16  ? 119 SER C O     1 
ATOM   5290 C  CB    . SER C 1 145 ? 124.514 139.142 139.630 1.00 19.15  ? 119 SER C CB    1 
ATOM   5291 O  OG    . SER C 1 145 ? 125.542 140.050 139.980 1.00 29.01  ? 119 SER C OG    1 
ATOM   5292 N  N     . ARG C 1 146 ? 124.312 139.425 142.925 1.00 29.42  ? 120 ARG C N     1 
ATOM   5293 C  CA    . ARG C 1 146 ? 124.636 138.984 144.278 1.00 17.86  ? 120 ARG C CA    1 
ATOM   5294 C  C     . ARG C 1 146 ? 123.434 139.047 145.213 1.00 25.37  ? 120 ARG C C     1 
ATOM   5295 O  O     . ARG C 1 146 ? 123.378 138.307 146.210 1.00 36.04  ? 120 ARG C O     1 
ATOM   5296 C  CB    . ARG C 1 146 ? 125.780 139.831 144.842 1.00 29.21  ? 120 ARG C CB    1 
ATOM   5297 C  CG    . ARG C 1 146 ? 127.091 139.707 144.076 1.00 27.71  ? 120 ARG C CG    1 
ATOM   5298 C  CD    . ARG C 1 146 ? 127.454 138.251 143.831 1.00 30.41  ? 120 ARG C CD    1 
ATOM   5299 N  NE    . ARG C 1 146 ? 128.762 138.101 143.207 1.00 32.29  ? 120 ARG C NE    1 
ATOM   5300 C  CZ    . ARG C 1 146 ? 129.451 136.969 143.175 1.00 36.12  ? 120 ARG C CZ    1 
ATOM   5301 N  NH1   . ARG C 1 146 ? 128.978 135.857 143.715 1.00 34.69  ? 120 ARG C NH1   1 
ATOM   5302 N  NH2   . ARG C 1 146 ? 130.644 136.949 142.588 1.00 31.06  ? 120 ARG C NH2   1 
ATOM   5303 N  N     . PHE C 1 147 ? 122.473 139.920 144.898 1.00 26.60  ? 121 PHE C N     1 
ATOM   5304 C  CA    . PHE C 1 147 ? 121.253 140.022 145.694 1.00 15.91  ? 121 PHE C CA    1 
ATOM   5305 C  C     . PHE C 1 147 ? 120.416 138.750 145.627 1.00 21.87  ? 121 PHE C C     1 
ATOM   5306 O  O     . PHE C 1 147 ? 119.708 138.428 146.592 1.00 36.88  ? 121 PHE C O     1 
ATOM   5307 C  CB    . PHE C 1 147 ? 120.430 141.220 145.231 1.00 22.57  ? 121 PHE C CB    1 
ATOM   5308 C  CG    . PHE C 1 147 ? 119.301 141.571 146.152 1.00 27.54  ? 121 PHE C CG    1 
ATOM   5309 C  CD1   . PHE C 1 147 ? 119.546 141.903 147.475 1.00 24.83  ? 121 PHE C CD1   1 
ATOM   5310 C  CD2   . PHE C 1 147 ? 117.993 141.572 145.693 1.00 26.66  ? 121 PHE C CD2   1 
ATOM   5311 C  CE1   . PHE C 1 147 ? 118.507 142.227 148.324 1.00 27.42  ? 121 PHE C CE1   1 
ATOM   5312 C  CE2   . PHE C 1 147 ? 116.949 141.897 146.538 1.00 25.72  ? 121 PHE C CE2   1 
ATOM   5313 C  CZ    . PHE C 1 147 ? 117.208 142.225 147.853 1.00 27.65  ? 121 PHE C CZ    1 
ATOM   5314 N  N     . TYR C 1 148 ? 120.478 138.026 144.503 1.00 24.66  ? 122 TYR C N     1 
ATOM   5315 C  CA    . TYR C 1 148 ? 119.792 136.731 144.401 1.00 27.06  ? 122 TYR C CA    1 
ATOM   5316 C  C     . TYR C 1 148 ? 120.312 135.734 145.440 1.00 31.29  ? 122 TYR C C     1 
ATOM   5317 O  O     . TYR C 1 148 ? 119.529 135.076 146.150 1.00 26.77  ? 122 TYR C O     1 
ATOM   5318 C  CB    . TYR C 1 148 ? 119.964 136.155 142.997 1.00 28.04  ? 122 TYR C CB    1 
ATOM   5319 C  CG    . TYR C 1 148 ? 119.152 136.838 141.927 1.00 33.64  ? 122 TYR C CG    1 
ATOM   5320 C  CD1   . TYR C 1 148 ? 117.830 137.201 142.156 1.00 30.17  ? 122 TYR C CD1   1 
ATOM   5321 C  CD2   . TYR C 1 148 ? 119.703 137.112 140.680 1.00 29.44  ? 122 TYR C CD2   1 
ATOM   5322 C  CE1   . TYR C 1 148 ? 117.083 137.825 141.176 1.00 30.04  ? 122 TYR C CE1   1 
ATOM   5323 C  CE2   . TYR C 1 148 ? 118.965 137.735 139.695 1.00 26.44  ? 122 TYR C CE2   1 
ATOM   5324 C  CZ    . TYR C 1 148 ? 117.655 138.088 139.949 1.00 26.78  ? 122 TYR C CZ    1 
ATOM   5325 O  OH    . TYR C 1 148 ? 116.913 138.707 138.973 1.00 36.66  ? 122 TYR C OH    1 
ATOM   5326 N  N     . GLY C 1 149 ? 121.639 135.622 145.548 1.00 27.75  ? 123 GLY C N     1 
ATOM   5327 C  CA    . GLY C 1 149 ? 122.227 134.745 146.545 1.00 18.09  ? 123 GLY C CA    1 
ATOM   5328 C  C     . GLY C 1 149 ? 121.981 135.220 147.962 1.00 27.98  ? 123 GLY C C     1 
ATOM   5329 O  O     . GLY C 1 149 ? 121.856 134.408 148.884 1.00 39.83  ? 123 GLY C O     1 
ATOM   5330 N  N     . HIS C 1 150 ? 121.899 136.544 148.153 1.00 26.46  ? 124 HIS C N     1 
ATOM   5331 C  CA    . HIS C 1 150 ? 121.529 137.087 149.460 1.00 23.47  ? 124 HIS C CA    1 
ATOM   5332 C  C     . HIS C 1 150 ? 120.121 136.668 149.868 1.00 30.05  ? 124 HIS C C     1 
ATOM   5333 O  O     . HIS C 1 150 ? 119.883 136.307 151.026 1.00 33.32  ? 124 HIS C O     1 
ATOM   5334 C  CB    . HIS C 1 150 ? 121.627 138.610 149.454 1.00 22.99  ? 124 HIS C CB    1 
ATOM   5335 C  CG    . HIS C 1 150 ? 120.980 139.255 150.640 1.00 29.34  ? 124 HIS C CG    1 
ATOM   5336 N  ND1   . HIS C 1 150 ? 121.276 138.893 151.937 1.00 28.84  ? 124 HIS C ND1   1 
ATOM   5337 C  CD2   . HIS C 1 150 ? 120.039 140.223 150.727 1.00 30.52  ? 124 HIS C CD2   1 
ATOM   5338 C  CE1   . HIS C 1 150 ? 120.553 139.617 152.771 1.00 28.68  ? 124 HIS C CE1   1 
ATOM   5339 N  NE2   . HIS C 1 150 ? 119.794 140.434 152.062 1.00 31.06  ? 124 HIS C NE2   1 
ATOM   5340 N  N     . LEU C 1 151 ? 119.171 136.722 148.927 1.00 30.71  ? 125 LEU C N     1 
ATOM   5341 C  CA    . LEU C 1 151 ? 117.797 136.319 149.223 1.00 28.11  ? 125 LEU C CA    1 
ATOM   5342 C  C     . LEU C 1 151 ? 117.705 134.830 149.545 1.00 30.95  ? 125 LEU C C     1 
ATOM   5343 O  O     . LEU C 1 151 ? 116.992 134.431 150.481 1.00 38.33  ? 125 LEU C O     1 
ATOM   5344 C  CB    . LEU C 1 151 ? 116.880 136.666 148.050 1.00 34.40  ? 125 LEU C CB    1 
ATOM   5345 C  CG    . LEU C 1 151 ? 116.607 138.148 147.789 1.00 33.63  ? 125 LEU C CG    1 
ATOM   5346 C  CD1   . LEU C 1 151 ? 115.881 138.325 146.466 1.00 32.71  ? 125 LEU C CD1   1 
ATOM   5347 C  CD2   . LEU C 1 151 ? 115.820 138.770 148.929 1.00 31.50  ? 125 LEU C CD2   1 
ATOM   5348 N  N     . GLY C 1 152 ? 118.436 133.999 148.791 1.00 28.73  ? 126 GLY C N     1 
ATOM   5349 C  CA    . GLY C 1 152 ? 118.461 132.569 149.089 1.00 23.47  ? 126 GLY C CA    1 
ATOM   5350 C  C     . GLY C 1 152 ? 119.069 132.253 150.445 1.00 27.27  ? 126 GLY C C     1 
ATOM   5351 O  O     . GLY C 1 152 ? 118.543 131.425 151.204 1.00 31.34  ? 126 GLY C O     1 
ATOM   5352 N  N     . LEU C 1 153 ? 120.174 132.932 150.778 1.00 30.75  ? 127 LEU C N     1 
ATOM   5353 C  CA    . LEU C 1 153 ? 120.816 132.745 152.075 1.00 26.13  ? 127 LEU C CA    1 
ATOM   5354 C  C     . LEU C 1 153 ? 119.921 133.213 153.218 1.00 31.49  ? 127 LEU C C     1 
ATOM   5355 O  O     . LEU C 1 153 ? 119.876 132.573 154.271 1.00 37.99  ? 127 LEU C O     1 
ATOM   5356 C  CB    . LEU C 1 153 ? 122.155 133.483 152.105 1.00 30.44  ? 127 LEU C CB    1 
ATOM   5357 C  CG    . LEU C 1 153 ? 122.983 133.403 153.391 1.00 34.38  ? 127 LEU C CG    1 
ATOM   5358 C  CD1   . LEU C 1 153 ? 123.230 131.958 153.793 1.00 28.11  ? 127 LEU C CD1   1 
ATOM   5359 C  CD2   . LEU C 1 153 ? 124.294 134.151 153.233 1.00 28.13  ? 127 LEU C CD2   1 
ATOM   5360 N  N     . LEU C 1 154 ? 119.193 134.318 153.023 1.00 36.11  ? 128 LEU C N     1 
ATOM   5361 C  CA    . LEU C 1 154 ? 118.297 134.817 154.065 1.00 31.64  ? 128 LEU C CA    1 
ATOM   5362 C  C     . LEU C 1 154 ? 117.128 133.867 154.304 1.00 31.10  ? 128 LEU C C     1 
ATOM   5363 O  O     . LEU C 1 154 ? 116.708 133.666 155.454 1.00 35.82  ? 128 LEU C O     1 
ATOM   5364 C  CB    . LEU C 1 154 ? 117.794 136.212 153.695 1.00 32.20  ? 128 LEU C CB    1 
ATOM   5365 C  CG    . LEU C 1 154 ? 116.912 136.919 154.725 1.00 32.33  ? 128 LEU C CG    1 
ATOM   5366 C  CD1   . LEU C 1 154 ? 117.679 137.162 156.012 1.00 31.74  ? 128 LEU C CD1   1 
ATOM   5367 C  CD2   . LEU C 1 154 ? 116.377 138.222 154.164 1.00 33.72  ? 128 LEU C CD2   1 
ATOM   5368 N  N     . LEU C 1 155 ? 116.595 133.270 153.229 1.00 33.80  ? 129 LEU C N     1 
ATOM   5369 C  CA    . LEU C 1 155 ? 115.547 132.260 153.386 1.00 37.27  ? 129 LEU C CA    1 
ATOM   5370 C  C     . LEU C 1 155 ? 116.057 131.037 154.146 1.00 41.53  ? 129 LEU C C     1 
ATOM   5371 O  O     . LEU C 1 155 ? 115.365 130.518 155.038 1.00 40.76  ? 129 LEU C O     1 
ATOM   5372 C  CB    . LEU C 1 155 ? 115.002 131.854 152.018 1.00 39.97  ? 129 LEU C CB    1 
ATOM   5373 C  CG    . LEU C 1 155 ? 113.830 130.869 152.029 1.00 42.41  ? 129 LEU C CG    1 
ATOM   5374 C  CD1   . LEU C 1 155 ? 112.565 131.542 152.540 1.00 34.76  ? 129 LEU C CD1   1 
ATOM   5375 C  CD2   . LEU C 1 155 ? 113.608 130.285 150.645 1.00 39.55  ? 129 LEU C CD2   1 
ATOM   5376 N  N     . LEU C 1 156 ? 117.280 130.586 153.834 1.00 39.34  ? 130 LEU C N     1 
ATOM   5377 C  CA    . LEU C 1 156 ? 117.858 129.465 154.575 1.00 31.31  ? 130 LEU C CA    1 
ATOM   5378 C  C     . LEU C 1 156 ? 118.138 129.824 156.030 1.00 35.53  ? 130 LEU C C     1 
ATOM   5379 O  O     . LEU C 1 156 ? 118.025 128.970 156.914 1.00 40.17  ? 130 LEU C O     1 
ATOM   5380 C  CB    . LEU C 1 156 ? 119.141 128.980 153.912 1.00 38.48  ? 130 LEU C CB    1 
ATOM   5381 C  CG    . LEU C 1 156 ? 119.024 128.277 152.569 1.00 41.50  ? 130 LEU C CG    1 
ATOM   5382 C  CD1   . LEU C 1 156 ? 120.397 128.222 151.968 1.00 43.05  ? 130 LEU C CD1   1 
ATOM   5383 C  CD2   . LEU C 1 156 ? 118.448 126.885 152.737 1.00 37.47  ? 130 LEU C CD2   1 
ATOM   5384 N  N     . VAL C 1 157 ? 118.508 131.079 156.296 1.00 37.76  ? 131 VAL C N     1 
ATOM   5385 C  CA    . VAL C 1 157 ? 118.778 131.520 157.662 1.00 32.75  ? 131 VAL C CA    1 
ATOM   5386 C  C     . VAL C 1 157 ? 117.494 131.528 158.489 1.00 35.03  ? 131 VAL C C     1 
ATOM   5387 O  O     . VAL C 1 157 ? 117.486 131.093 159.649 1.00 35.83  ? 131 VAL C O     1 
ATOM   5388 C  CB    . VAL C 1 157 ? 119.475 132.898 157.634 1.00 35.85  ? 131 VAL C CB    1 
ATOM   5389 C  CG1   . VAL C 1 157 ? 119.283 133.669 158.932 1.00 34.50  ? 131 VAL C CG1   1 
ATOM   5390 C  CG2   . VAL C 1 157 ? 120.959 132.730 157.350 1.00 28.09  ? 131 VAL C CG2   1 
ATOM   5391 N  N     . ILE C 1 158 ? 116.384 131.983 157.895 1.00 40.14  ? 132 ILE C N     1 
ATOM   5392 C  CA    . ILE C 1 158 ? 115.092 131.966 158.585 1.00 38.32  ? 132 ILE C CA    1 
ATOM   5393 C  C     . ILE C 1 158 ? 114.629 130.530 158.845 1.00 42.51  ? 132 ILE C C     1 
ATOM   5394 O  O     . ILE C 1 158 ? 114.137 130.204 159.939 1.00 44.54  ? 132 ILE C O     1 
ATOM   5395 C  CB    . ILE C 1 158 ? 114.058 132.777 157.777 1.00 40.60  ? 132 ILE C CB    1 
ATOM   5396 C  CG1   . ILE C 1 158 ? 114.424 134.263 157.800 1.00 41.80  ? 132 ILE C CG1   1 
ATOM   5397 C  CG2   . ILE C 1 158 ? 112.648 132.594 158.317 1.00 38.29  ? 132 ILE C CG2   1 
ATOM   5398 C  CD1   . ILE C 1 158 ? 113.630 135.107 156.834 1.00 37.43  ? 132 ILE C CD1   1 
ATOM   5399 N  N     . ILE C 1 159 ? 114.826 129.640 157.864 1.00 42.99  ? 133 ILE C N     1 
ATOM   5400 C  CA    . ILE C 1 159 ? 114.456 128.232 158.037 1.00 37.84  ? 133 ILE C CA    1 
ATOM   5401 C  C     . ILE C 1 159 ? 115.328 127.561 159.104 1.00 41.55  ? 133 ILE C C     1 
ATOM   5402 O  O     . ILE C 1 159 ? 114.842 126.757 159.910 1.00 45.08  ? 133 ILE C O     1 
ATOM   5403 C  CB    . ILE C 1 159 ? 114.520 127.507 156.676 1.00 43.55  ? 133 ILE C CB    1 
ATOM   5404 C  CG1   . ILE C 1 159 ? 113.360 127.962 155.789 1.00 43.31  ? 133 ILE C CG1   1 
ATOM   5405 C  CG2   . ILE C 1 159 ? 114.473 125.989 156.819 1.00 44.19  ? 133 ILE C CG2   1 
ATOM   5406 C  CD1   . ILE C 1 159 ? 113.556 127.654 154.326 1.00 45.69  ? 133 ILE C CD1   1 
ATOM   5407 N  N     . ALA C 1 160 ? 116.615 127.918 159.161 1.00 40.41  ? 134 ALA C N     1 
ATOM   5408 C  CA    . ALA C 1 160 ? 117.499 127.364 160.183 1.00 38.83  ? 134 ALA C CA    1 
ATOM   5409 C  C     . ALA C 1 160 ? 117.161 127.904 161.569 1.00 43.05  ? 134 ALA C C     1 
ATOM   5410 O  O     . ALA C 1 160 ? 117.320 127.199 162.572 1.00 52.10  ? 134 ALA C O     1 
ATOM   5411 C  CB    . ALA C 1 160 ? 118.956 127.663 159.836 1.00 38.19  ? 134 ALA C CB    1 
ATOM   5412 N  N     . CYS C 1 161 ? 116.699 129.155 161.645 1.00 49.44  ? 135 CYS C N     1 
ATOM   5413 C  CA    . CYS C 1 161 ? 116.243 129.706 162.916 1.00 44.30  ? 135 CYS C CA    1 
ATOM   5414 C  C     . CYS C 1 161 ? 114.934 129.082 163.377 1.00 49.95  ? 135 CYS C C     1 
ATOM   5415 O  O     . CYS C 1 161 ? 114.654 129.082 164.580 1.00 51.07  ? 135 CYS C O     1 
ATOM   5416 C  CB    . CYS C 1 161 ? 116.085 131.224 162.812 1.00 42.42  ? 135 CYS C CB    1 
ATOM   5417 S  SG    . CYS C 1 161 ? 117.635 132.150 162.861 1.00 60.69  ? 135 CYS C SG    1 
ATOM   5418 N  N     . MET C 1 162 ? 114.122 128.569 162.443 1.00 56.96  ? 136 MET C N     1 
ATOM   5419 C  CA    . MET C 1 162 ? 112.919 127.823 162.815 1.00 53.14  ? 136 MET C CA    1 
ATOM   5420 C  C     . MET C 1 162 ? 113.228 126.548 163.597 1.00 56.08  ? 136 MET C C     1 
ATOM   5421 O  O     . MET C 1 162 ? 112.396 126.113 164.399 1.00 59.07  ? 136 MET C O     1 
ATOM   5422 C  CB    . MET C 1 162 ? 112.118 127.432 161.572 1.00 53.06  ? 136 MET C CB    1 
ATOM   5423 C  CG    . MET C 1 162 ? 110.938 128.314 161.225 1.00 48.28  ? 136 MET C CG    1 
ATOM   5424 S  SD    . MET C 1 162 ? 110.695 128.316 159.438 1.00 65.30  ? 136 MET C SD    1 
ATOM   5425 C  CE    . MET C 1 162 ? 109.292 129.411 159.265 1.00 55.96  ? 136 MET C CE    1 
ATOM   5426 N  N     . PHE C 1 163 ? 114.398 125.944 163.384 1.00 57.53  ? 137 PHE C N     1 
ATOM   5427 C  CA    . PHE C 1 163 ? 114.728 124.638 163.947 1.00 55.68  ? 137 PHE C CA    1 
ATOM   5428 C  C     . PHE C 1 163 ? 115.098 124.681 165.425 1.00 58.51  ? 137 PHE C C     1 
ATOM   5429 O  O     . PHE C 1 163 ? 115.220 123.619 166.043 1.00 62.68  ? 137 PHE C O     1 
ATOM   5430 C  CB    . PHE C 1 163 ? 115.875 124.005 163.154 1.00 57.28  ? 137 PHE C CB    1 
ATOM   5431 C  CG    . PHE C 1 163 ? 115.421 123.138 162.016 1.00 59.13  ? 137 PHE C CG    1 
ATOM   5432 C  CD1   . PHE C 1 163 ? 114.631 123.659 161.000 1.00 60.05  ? 137 PHE C CD1   1 
ATOM   5433 C  CD2   . PHE C 1 163 ? 115.783 121.800 161.959 1.00 59.49  ? 137 PHE C CD2   1 
ATOM   5434 C  CE1   . PHE C 1 163 ? 114.211 122.863 159.950 1.00 60.96  ? 137 PHE C CE1   1 
ATOM   5435 C  CE2   . PHE C 1 163 ? 115.366 120.997 160.911 1.00 60.49  ? 137 PHE C CE2   1 
ATOM   5436 C  CZ    . PHE C 1 163 ? 114.579 121.531 159.905 1.00 60.82  ? 137 PHE C CZ    1 
ATOM   5437 N  N     . THR C 1 164 ? 115.290 125.866 166.004 1.00 56.72  ? 138 THR C N     1 
ATOM   5438 C  CA    . THR C 1 164 ? 115.590 126.000 167.422 1.00 56.55  ? 138 THR C CA    1 
ATOM   5439 C  C     . THR C 1 164 ? 114.364 126.314 168.266 1.00 58.12  ? 138 THR C C     1 
ATOM   5440 O  O     . THR C 1 164 ? 114.234 125.776 169.369 1.00 61.78  ? 138 THR C O     1 
ATOM   5441 C  CB    . THR C 1 164 ? 116.635 127.108 167.634 1.00 55.18  ? 138 THR C CB    1 
ATOM   5442 O  OG1   . THR C 1 164 ? 117.707 126.917 166.711 1.00 56.44  ? 138 THR C OG1   1 
ATOM   5443 C  CG2   . THR C 1 164 ? 117.202 127.077 169.047 1.00 55.07  ? 138 THR C CG2   1 
ATOM   5444 N  N     . GLY C 1 165 ? 113.452 127.133 167.754 1.00 49.87  ? 139 GLY C N     1 
ATOM   5445 C  CA    . GLY C 1 165 ? 112.337 127.657 168.519 1.00 50.55  ? 139 GLY C CA    1 
ATOM   5446 C  C     . GLY C 1 165 ? 112.069 129.118 168.254 1.00 51.93  ? 139 GLY C C     1 
ATOM   5447 O  O     . GLY C 1 165 ? 111.126 129.677 168.831 1.00 58.83  ? 139 GLY C O     1 
ATOM   5448 N  N     . ILE C 1 166 ? 112.870 129.760 167.406 1.00 44.15  ? 140 ILE C N     1 
ATOM   5449 C  CA    . ILE C 1 166 ? 112.657 131.144 167.004 1.00 45.66  ? 140 ILE C CA    1 
ATOM   5450 C  C     . ILE C 1 166 ? 111.798 131.105 165.746 1.00 43.32  ? 140 ILE C C     1 
ATOM   5451 O  O     . ILE C 1 166 ? 112.286 130.822 164.651 1.00 47.95  ? 140 ILE C O     1 
ATOM   5452 C  CB    . ILE C 1 166 ? 113.981 131.873 166.771 1.00 46.04  ? 140 ILE C CB    1 
ATOM   5453 C  CG1   . ILE C 1 166 ? 114.947 131.593 167.924 1.00 45.37  ? 140 ILE C CG1   1 
ATOM   5454 C  CG2   . ILE C 1 166 ? 113.747 133.364 166.613 1.00 44.97  ? 140 ILE C CG2   1 
ATOM   5455 C  CD1   . ILE C 1 166 ? 116.350 132.095 167.688 1.00 45.42  ? 140 ILE C CD1   1 
ATOM   5456 N  N     . TYR C 1 167 ? 110.515 131.382 165.905 1.00 47.34  ? 141 TYR C N     1 
ATOM   5457 C  CA    . TYR C 1 167 ? 109.568 131.327 164.809 1.00 47.96  ? 141 TYR C CA    1 
ATOM   5458 C  C     . TYR C 1 167 ? 109.205 132.735 164.350 1.00 50.49  ? 141 TYR C C     1 
ATOM   5459 O  O     . TYR C 1 167 ? 109.265 133.680 165.143 1.00 53.07  ? 141 TYR C O     1 
ATOM   5460 C  CB    . TYR C 1 167 ? 108.302 130.572 165.233 1.00 46.54  ? 141 TYR C CB    1 
ATOM   5461 C  CG    . TYR C 1 167 ? 108.567 129.130 165.598 1.00 48.59  ? 141 TYR C CG    1 
ATOM   5462 C  CD1   . TYR C 1 167 ? 108.911 128.201 164.625 1.00 48.39  ? 141 TYR C CD1   1 
ATOM   5463 C  CD2   . TYR C 1 167 ? 108.493 128.703 166.919 1.00 50.01  ? 141 TYR C CD2   1 
ATOM   5464 C  CE1   . TYR C 1 167 ? 109.161 126.882 164.954 1.00 51.37  ? 141 TYR C CE1   1 
ATOM   5465 C  CE2   . TYR C 1 167 ? 108.742 127.387 167.257 1.00 48.85  ? 141 TYR C CE2   1 
ATOM   5466 C  CZ    . TYR C 1 167 ? 109.077 126.481 166.271 1.00 53.41  ? 141 TYR C CZ    1 
ATOM   5467 O  OH    . TYR C 1 167 ? 109.324 125.170 166.604 1.00 54.74  ? 141 TYR C OH    1 
ATOM   5468 N  N     . PRO C 1 168 ? 108.861 132.917 163.060 1.00 41.33  ? 142 PRO C N     1 
ATOM   5469 C  CA    . PRO C 1 168 ? 108.465 134.246 162.574 1.00 37.90  ? 142 PRO C CA    1 
ATOM   5470 C  C     . PRO C 1 168 ? 107.198 134.787 163.215 1.00 42.55  ? 142 PRO C C     1 
ATOM   5471 O  O     . PRO C 1 168 ? 106.121 134.192 163.110 1.00 48.31  ? 142 PRO C O     1 
ATOM   5472 C  CB    . PRO C 1 168 ? 108.265 134.022 161.071 1.00 35.96  ? 142 PRO C CB    1 
ATOM   5473 C  CG    . PRO C 1 168 ? 109.124 132.862 160.751 1.00 39.80  ? 142 PRO C CG    1 
ATOM   5474 C  CD    . PRO C 1 168 ? 109.063 131.970 161.950 1.00 40.95  ? 142 PRO C CD    1 
ATOM   5475 N  N     . SER C 1 169 ? 107.336 135.917 163.898 1.00 39.08  ? 143 SER C N     1 
ATOM   5476 C  CA    . SER C 1 169 ? 106.218 136.637 164.482 1.00 38.20  ? 143 SER C CA    1 
ATOM   5477 C  C     . SER C 1 169 ? 105.738 137.701 163.498 1.00 36.42  ? 143 SER C C     1 
ATOM   5478 O  O     . SER C 1 169 ? 106.086 137.691 162.315 1.00 38.43  ? 143 SER C O     1 
ATOM   5479 C  CB    . SER C 1 169 ? 106.620 137.235 165.829 1.00 39.24  ? 143 SER C CB    1 
ATOM   5480 O  OG    . SER C 1 169 ? 107.707 138.130 165.688 1.00 38.08  ? 143 SER C OG    1 
ATOM   5481 N  N     . ILE C 1 170 ? 104.917 138.636 163.985 1.00 41.44  ? 144 ILE C N     1 
ATOM   5482 C  CA    . ILE C 1 170 ? 104.460 139.750 163.164 1.00 35.43  ? 144 ILE C CA    1 
ATOM   5483 C  C     . ILE C 1 170 ? 105.592 140.739 162.874 1.00 30.40  ? 144 ILE C C     1 
ATOM   5484 O  O     . ILE C 1 170 ? 105.501 141.524 161.927 1.00 38.21  ? 144 ILE C O     1 
ATOM   5485 C  CB    . ILE C 1 170 ? 103.252 140.423 163.858 1.00 37.03  ? 144 ILE C CB    1 
ATOM   5486 C  CG1   . ILE C 1 170 ? 102.459 141.327 162.903 1.00 35.37  ? 144 ILE C CG1   1 
ATOM   5487 C  CG2   . ILE C 1 170 ? 103.693 141.200 165.092 1.00 33.22  ? 144 ILE C CG2   1 
ATOM   5488 C  CD1   . ILE C 1 170 ? 102.205 140.727 161.533 1.00 34.38  ? 144 ILE C CD1   1 
ATOM   5489 N  N     . HIS C 1 171 ? 106.689 140.685 163.632 1.00 37.89  ? 145 HIS C N     1 
ATOM   5490 C  CA    . HIS C 1 171 ? 107.796 141.615 163.454 1.00 35.38  ? 145 HIS C CA    1 
ATOM   5491 C  C     . HIS C 1 171 ? 108.650 141.317 162.226 1.00 29.80  ? 145 HIS C C     1 
ATOM   5492 O  O     . HIS C 1 171 ? 109.544 142.109 161.917 1.00 40.48  ? 145 HIS C O     1 
ATOM   5493 C  CB    . HIS C 1 171 ? 108.677 141.611 164.703 1.00 28.83  ? 145 HIS C CB    1 
ATOM   5494 C  CG    . HIS C 1 171 ? 107.928 141.885 165.968 1.00 30.34  ? 145 HIS C CG    1 
ATOM   5495 N  ND1   . HIS C 1 171 ? 107.278 140.897 166.677 1.00 34.86  ? 145 HIS C ND1   1 
ATOM   5496 C  CD2   . HIS C 1 171 ? 107.720 143.035 166.652 1.00 31.78  ? 145 HIS C CD2   1 
ATOM   5497 C  CE1   . HIS C 1 171 ? 106.704 141.427 167.742 1.00 36.76  ? 145 HIS C CE1   1 
ATOM   5498 N  NE2   . HIS C 1 171 ? 106.958 142.723 167.750 1.00 31.56  ? 145 HIS C NE2   1 
ATOM   5499 N  N     . ILE C 1 172 ? 108.406 140.208 161.522 1.00 33.15  ? 146 ILE C N     1 
ATOM   5500 C  CA    . ILE C 1 172 ? 109.236 139.849 160.378 1.00 36.42  ? 146 ILE C CA    1 
ATOM   5501 C  C     . ILE C 1 172 ? 108.854 140.594 159.103 1.00 35.66  ? 146 ILE C C     1 
ATOM   5502 O  O     . ILE C 1 172 ? 109.610 140.550 158.125 1.00 42.92  ? 146 ILE C O     1 
ATOM   5503 C  CB    . ILE C 1 172 ? 109.200 138.318 160.170 1.00 37.24  ? 146 ILE C CB    1 
ATOM   5504 C  CG1   . ILE C 1 172 ? 110.528 137.821 159.577 1.00 36.33  ? 146 ILE C CG1   1 
ATOM   5505 C  CG2   . ILE C 1 172 ? 108.005 137.902 159.321 1.00 33.45  ? 146 ILE C CG2   1 
ATOM   5506 C  CD1   . ILE C 1 172 ? 110.898 136.414 159.962 1.00 38.98  ? 146 ILE C CD1   1 
ATOM   5507 N  N     . ILE C 1 173 ? 107.733 141.323 159.086 1.00 34.41  ? 147 ILE C N     1 
ATOM   5508 C  CA    . ILE C 1 173 ? 107.395 142.107 157.898 1.00 34.13  ? 147 ILE C CA    1 
ATOM   5509 C  C     . ILE C 1 173 ? 108.214 143.387 157.778 1.00 37.61  ? 147 ILE C C     1 
ATOM   5510 O  O     . ILE C 1 173 ? 108.068 144.112 156.788 1.00 41.04  ? 147 ILE C O     1 
ATOM   5511 C  CB    . ILE C 1 173 ? 105.858 142.319 157.806 1.00 37.60  ? 147 ILE C CB    1 
ATOM   5512 C  CG1   . ILE C 1 173 ? 105.150 142.960 159.034 1.00 32.44  ? 147 ILE C CG1   1 
ATOM   5513 C  CG2   . ILE C 1 173 ? 105.167 141.006 157.455 1.00 42.89  ? 147 ILE C CG2   1 
ATOM   5514 C  CD1   . ILE C 1 173 ? 105.563 144.326 159.593 1.00 33.79  ? 147 ILE C CD1   1 
ATOM   5515 N  N     . GLN C 1 174 ? 109.067 143.681 158.764 1.00 38.02  ? 148 GLN C N     1 
ATOM   5516 C  CA    . GLN C 1 174 ? 110.054 144.747 158.639 1.00 29.96  ? 148 GLN C CA    1 
ATOM   5517 C  C     . GLN C 1 174 ? 111.156 144.404 157.642 1.00 27.37  ? 148 GLN C C     1 
ATOM   5518 O  O     . GLN C 1 174 ? 111.896 145.302 157.225 1.00 38.68  ? 148 GLN C O     1 
ATOM   5519 C  CB    . GLN C 1 174 ? 110.679 145.041 159.999 1.00 29.60  ? 148 GLN C CB    1 
ATOM   5520 C  CG    . GLN C 1 174 ? 109.703 145.345 161.109 1.00 33.08  ? 148 GLN C CG    1 
ATOM   5521 C  CD    . GLN C 1 174 ? 110.394 145.482 162.450 1.00 35.53  ? 148 GLN C CD    1 
ATOM   5522 O  OE1   . GLN C 1 174 ? 110.933 146.537 162.778 1.00 36.90  ? 148 GLN C OE1   1 
ATOM   5523 N  NE2   . GLN C 1 174 ? 110.391 144.409 163.230 1.00 33.75  ? 148 GLN C NE2   1 
ATOM   5524 N  N     . LEU C 1 175 ? 111.286 143.128 157.264 1.00 28.83  ? 149 LEU C N     1 
ATOM   5525 C  CA    . LEU C 1 175 ? 112.242 142.742 156.233 1.00 29.56  ? 149 LEU C CA    1 
ATOM   5526 C  C     . LEU C 1 175 ? 111.879 143.339 154.880 1.00 32.35  ? 149 LEU C C     1 
ATOM   5527 O  O     . LEU C 1 175 ? 112.774 143.644 154.087 1.00 43.34  ? 149 LEU C O     1 
ATOM   5528 C  CB    . LEU C 1 175 ? 112.330 141.218 156.145 1.00 32.29  ? 149 LEU C CB    1 
ATOM   5529 C  CG    . LEU C 1 175 ? 113.084 140.499 157.268 1.00 34.65  ? 149 LEU C CG    1 
ATOM   5530 C  CD1   . LEU C 1 175 ? 113.352 139.051 156.894 1.00 30.03  ? 149 LEU C CD1   1 
ATOM   5531 C  CD2   . LEU C 1 175 ? 114.385 141.213 157.617 1.00 29.50  ? 149 LEU C CD2   1 
ATOM   5532 N  N     . LEU C 1 176 ? 110.586 143.588 154.638 1.00 34.52  ? 150 LEU C N     1 
ATOM   5533 C  CA    . LEU C 1 176 ? 110.136 144.265 153.425 1.00 35.01  ? 150 LEU C CA    1 
ATOM   5534 C  C     . LEU C 1 176 ? 110.623 145.708 153.337 1.00 36.26  ? 150 LEU C C     1 
ATOM   5535 O  O     . LEU C 1 176 ? 110.600 146.293 152.249 1.00 41.82  ? 150 LEU C O     1 
ATOM   5536 C  CB    . LEU C 1 176 ? 108.609 144.235 153.348 1.00 38.63  ? 150 LEU C CB    1 
ATOM   5537 C  CG    . LEU C 1 176 ? 107.950 142.882 153.078 1.00 37.79  ? 150 LEU C CG    1 
ATOM   5538 C  CD1   . LEU C 1 176 ? 106.447 143.041 152.944 1.00 37.60  ? 150 LEU C CD1   1 
ATOM   5539 C  CD2   . LEU C 1 176 ? 108.533 142.234 151.835 1.00 36.62  ? 150 LEU C CD2   1 
ATOM   5540 N  N     . ILE C 1 177 ? 111.043 146.297 154.451 1.00 37.76  ? 151 ILE C N     1 
ATOM   5541 C  CA    . ILE C 1 177 ? 111.714 147.587 154.457 1.00 36.59  ? 151 ILE C CA    1 
ATOM   5542 C  C     . ILE C 1 177 ? 113.230 147.426 154.480 1.00 34.54  ? 151 ILE C C     1 
ATOM   5543 O  O     . ILE C 1 177 ? 113.946 148.139 153.778 1.00 38.04  ? 151 ILE C O     1 
ATOM   5544 C  CB    . ILE C 1 177 ? 111.218 148.422 155.659 1.00 35.05  ? 151 ILE C CB    1 
ATOM   5545 C  CG1   . ILE C 1 177 ? 109.697 148.602 155.591 1.00 39.61  ? 151 ILE C CG1   1 
ATOM   5546 C  CG2   . ILE C 1 177 ? 111.927 149.773 155.740 1.00 34.52  ? 151 ILE C CG2   1 
ATOM   5547 C  CD1   . ILE C 1 177 ? 109.230 149.596 154.543 1.00 40.86  ? 151 ILE C CD1   1 
ATOM   5548 N  N     . TYR C 1 178 ? 113.727 146.454 155.248 1.00 30.28  ? 152 TYR C N     1 
ATOM   5549 C  CA    . TYR C 1 178 ? 115.155 146.403 155.551 1.00 26.79  ? 152 TYR C CA    1 
ATOM   5550 C  C     . TYR C 1 178 ? 115.980 145.755 154.441 1.00 26.81  ? 152 TYR C C     1 
ATOM   5551 O  O     . TYR C 1 178 ? 117.089 146.217 154.155 1.00 38.23  ? 152 TYR C O     1 
ATOM   5552 C  CB    . TYR C 1 178 ? 115.375 145.683 156.883 1.00 32.50  ? 152 TYR C CB    1 
ATOM   5553 C  CG    . TYR C 1 178 ? 114.827 146.447 158.071 1.00 25.07  ? 152 TYR C CG    1 
ATOM   5554 C  CD1   . TYR C 1 178 ? 114.743 147.836 158.049 1.00 31.29  ? 152 TYR C CD1   1 
ATOM   5555 C  CD2   . TYR C 1 178 ? 114.389 145.782 159.208 1.00 27.22  ? 152 TYR C CD2   1 
ATOM   5556 C  CE1   . TYR C 1 178 ? 114.243 148.539 159.127 1.00 29.92  ? 152 TYR C CE1   1 
ATOM   5557 C  CE2   . TYR C 1 178 ? 113.891 146.481 160.294 1.00 27.94  ? 152 TYR C CE2   1 
ATOM   5558 C  CZ    . TYR C 1 178 ? 113.817 147.856 160.244 1.00 33.48  ? 152 TYR C CZ    1 
ATOM   5559 O  OH    . TYR C 1 178 ? 113.319 148.551 161.320 1.00 43.26  ? 152 TYR C OH    1 
ATOM   5560 N  N     . VAL C 1 179 ? 115.489 144.669 153.829 1.00 30.43  ? 153 VAL C N     1 
ATOM   5561 C  CA    . VAL C 1 179 ? 116.205 144.063 152.699 1.00 36.47  ? 153 VAL C CA    1 
ATOM   5562 C  C     . VAL C 1 179 ? 116.262 144.972 151.467 1.00 30.56  ? 153 VAL C C     1 
ATOM   5563 O  O     . VAL C 1 179 ? 117.345 145.079 150.859 1.00 39.84  ? 153 VAL C O     1 
ATOM   5564 C  CB    . VAL C 1 179 ? 115.638 142.662 152.401 1.00 34.41  ? 153 VAL C CB    1 
ATOM   5565 C  CG1   . VAL C 1 179 ? 116.525 141.914 151.425 1.00 34.49  ? 153 VAL C CG1   1 
ATOM   5566 C  CG2   . VAL C 1 179 ? 115.475 141.863 153.686 1.00 21.99  ? 153 VAL C CG2   1 
ATOM   5567 N  N     . PRO C 1 180 ? 115.165 145.644 151.035 1.00 38.84  ? 154 PRO C N     1 
ATOM   5568 C  CA    . PRO C 1 180 ? 115.338 146.665 149.984 1.00 32.38  ? 154 PRO C CA    1 
ATOM   5569 C  C     . PRO C 1 180 ? 116.243 147.815 150.375 1.00 30.20  ? 154 PRO C C     1 
ATOM   5570 O  O     . PRO C 1 180 ? 116.895 148.381 149.492 1.00 36.80  ? 154 PRO C O     1 
ATOM   5571 C  CB    . PRO C 1 180 ? 113.906 147.147 149.726 1.00 24.84  ? 154 PRO C CB    1 
ATOM   5572 C  CG    . PRO C 1 180 ? 113.084 146.008 150.050 1.00 29.17  ? 154 PRO C CG    1 
ATOM   5573 C  CD    . PRO C 1 180 ? 113.716 145.444 151.270 1.00 29.03  ? 154 PRO C CD    1 
ATOM   5574 N  N     . PHE C 1 181 ? 116.314 148.172 151.661 1.00 26.49  ? 155 PHE C N     1 
ATOM   5575 C  CA    . PHE C 1 181 ? 117.250 149.209 152.086 1.00 25.53  ? 155 PHE C CA    1 
ATOM   5576 C  C     . PHE C 1 181 ? 118.696 148.772 151.881 1.00 28.93  ? 155 PHE C C     1 
ATOM   5577 O  O     . PHE C 1 181 ? 119.539 149.579 151.469 1.00 32.35  ? 155 PHE C O     1 
ATOM   5578 C  CB    . PHE C 1 181 ? 117.027 149.580 153.553 1.00 24.01  ? 155 PHE C CB    1 
ATOM   5579 C  CG    . PHE C 1 181 ? 118.104 150.462 154.101 1.00 35.51  ? 155 PHE C CG    1 
ATOM   5580 C  CD1   . PHE C 1 181 ? 118.177 151.788 153.715 1.00 33.03  ? 155 PHE C CD1   1 
ATOM   5581 C  CD2   . PHE C 1 181 ? 119.075 149.961 154.960 1.00 38.35  ? 155 PHE C CD2   1 
ATOM   5582 C  CE1   . PHE C 1 181 ? 119.175 152.601 154.191 1.00 31.80  ? 155 PHE C CE1   1 
ATOM   5583 C  CE2   . PHE C 1 181 ? 120.083 150.770 155.421 1.00 37.23  ? 155 PHE C CE2   1 
ATOM   5584 C  CZ    . PHE C 1 181 ? 120.130 152.088 155.039 1.00 35.30  ? 155 PHE C CZ    1 
ATOM   5585 N  N     . CYS C 1 182 ? 119.007 147.512 152.200 1.00 29.14  ? 156 CYS C N     1 
ATOM   5586 C  CA    . CYS C 1 182 ? 120.350 146.984 151.980 1.00 28.82  ? 156 CYS C CA    1 
ATOM   5587 C  C     . CYS C 1 182 ? 120.695 146.961 150.497 1.00 24.77  ? 156 CYS C C     1 
ATOM   5588 O  O     . CYS C 1 182 ? 121.809 147.346 150.101 1.00 32.38  ? 156 CYS C O     1 
ATOM   5589 C  CB    . CYS C 1 182 ? 120.457 145.584 152.587 1.00 32.74  ? 156 CYS C CB    1 
ATOM   5590 S  SG    . CYS C 1 182 ? 122.086 144.823 152.492 1.00 51.08  ? 156 CYS C SG    1 
ATOM   5591 N  N     . PHE C 1 183 ? 119.727 146.555 149.661 1.00 26.91  ? 157 PHE C N     1 
ATOM   5592 C  CA    . PHE C 1 183 ? 119.921 146.588 148.212 1.00 25.16  ? 157 PHE C CA    1 
ATOM   5593 C  C     . PHE C 1 183 ? 120.155 148.011 147.705 1.00 26.22  ? 157 PHE C C     1 
ATOM   5594 O  O     . PHE C 1 183 ? 121.034 148.239 146.868 1.00 31.98  ? 157 PHE C O     1 
ATOM   5595 C  CB    . PHE C 1 183 ? 118.719 145.962 147.502 1.00 22.73  ? 157 PHE C CB    1 
ATOM   5596 C  CG    . PHE C 1 183 ? 118.836 145.964 146.002 1.00 21.97  ? 157 PHE C CG    1 
ATOM   5597 C  CD1   . PHE C 1 183 ? 119.653 145.048 145.360 1.00 28.35  ? 157 PHE C CD1   1 
ATOM   5598 C  CD2   . PHE C 1 183 ? 118.138 146.886 145.236 1.00 25.40  ? 157 PHE C CD2   1 
ATOM   5599 C  CE1   . PHE C 1 183 ? 119.768 145.049 143.983 1.00 25.63  ? 157 PHE C CE1   1 
ATOM   5600 C  CE2   . PHE C 1 183 ? 118.253 146.895 143.860 1.00 29.21  ? 157 PHE C CE2   1 
ATOM   5601 C  CZ    . PHE C 1 183 ? 119.069 145.973 143.233 1.00 27.59  ? 157 PHE C CZ    1 
ATOM   5602 N  N     . PHE C 1 184 ? 119.394 148.981 148.220 1.00 31.59  ? 158 PHE C N     1 
ATOM   5603 C  CA    . PHE C 1 184 ? 119.497 150.353 147.729 1.00 22.21  ? 158 PHE C CA    1 
ATOM   5604 C  C     . PHE C 1 184 ? 120.780 151.027 148.202 1.00 27.58  ? 158 PHE C C     1 
ATOM   5605 O  O     . PHE C 1 184 ? 121.361 151.833 147.468 1.00 34.16  ? 158 PHE C O     1 
ATOM   5606 C  CB    . PHE C 1 184 ? 118.270 151.155 148.160 1.00 25.91  ? 158 PHE C CB    1 
ATOM   5607 C  CG    . PHE C 1 184 ? 117.021 150.800 147.403 1.00 34.88  ? 158 PHE C CG    1 
ATOM   5608 C  CD1   . PHE C 1 184 ? 117.093 150.339 146.097 1.00 34.60  ? 158 PHE C CD1   1 
ATOM   5609 C  CD2   . PHE C 1 184 ? 115.773 150.929 147.995 1.00 36.91  ? 158 PHE C CD2   1 
ATOM   5610 C  CE1   . PHE C 1 184 ? 115.947 150.009 145.397 1.00 35.12  ? 158 PHE C CE1   1 
ATOM   5611 C  CE2   . PHE C 1 184 ? 114.623 150.599 147.302 1.00 36.53  ? 158 PHE C CE2   1 
ATOM   5612 C  CZ    . PHE C 1 184 ? 114.711 150.140 146.000 1.00 34.35  ? 158 PHE C CZ    1 
ATOM   5613 N  N     . LEU C 1 185 ? 121.236 150.706 149.419 1.00 27.45  ? 159 LEU C N     1 
ATOM   5614 C  CA    . LEU C 1 185 ? 122.530 151.196 149.893 1.00 26.62  ? 159 LEU C CA    1 
ATOM   5615 C  C     . LEU C 1 185 ? 123.668 150.670 149.031 1.00 23.39  ? 159 LEU C C     1 
ATOM   5616 O  O     . LEU C 1 185 ? 124.548 151.438 148.609 1.00 35.70  ? 159 LEU C O     1 
ATOM   5617 C  CB    . LEU C 1 185 ? 122.752 150.793 151.353 1.00 29.88  ? 159 LEU C CB    1 
ATOM   5618 C  CG    . LEU C 1 185 ? 124.160 151.106 151.883 1.00 36.42  ? 159 LEU C CG    1 
ATOM   5619 C  CD1   . LEU C 1 185 ? 124.255 152.491 152.504 1.00 29.52  ? 159 LEU C CD1   1 
ATOM   5620 C  CD2   . LEU C 1 185 ? 124.653 150.043 152.846 1.00 32.78  ? 159 LEU C CD2   1 
ATOM   5621 N  N     . THR C 1 186 ? 123.655 149.357 148.753 1.00 26.32  ? 160 THR C N     1 
ATOM   5622 C  CA    . THR C 1 186 ? 124.688 148.765 147.905 1.00 29.93  ? 160 THR C CA    1 
ATOM   5623 C  C     . THR C 1 186 ? 124.646 149.343 146.495 1.00 22.31  ? 160 THR C C     1 
ATOM   5624 O  O     . THR C 1 186 ? 125.693 149.655 145.918 1.00 25.99  ? 160 THR C O     1 
ATOM   5625 C  CB    . THR C 1 186 ? 124.535 147.243 147.872 1.00 29.80  ? 160 THR C CB    1 
ATOM   5626 O  OG1   . THR C 1 186 ? 124.241 146.765 149.189 1.00 37.36  ? 160 THR C OG1   1 
ATOM   5627 C  CG2   . THR C 1 186 ? 125.814 146.586 147.381 1.00 17.05  ? 160 THR C CG2   1 
ATOM   5628 N  N     . ALA C 1 187 ? 123.442 149.562 145.958 1.00 26.27  ? 161 ALA C N     1 
ATOM   5629 C  CA    . ALA C 1 187 ? 123.298 150.102 144.609 1.00 23.37  ? 161 ALA C CA    1 
ATOM   5630 C  C     . ALA C 1 187 ? 123.755 151.557 144.520 1.00 29.83  ? 161 ALA C C     1 
ATOM   5631 O  O     . ALA C 1 187 ? 124.369 151.949 143.526 1.00 38.25  ? 161 ALA C O     1 
ATOM   5632 C  CB    . ALA C 1 187 ? 121.849 149.962 144.147 1.00 21.94  ? 161 ALA C CB    1 
ATOM   5633 N  N     . SER C 1 188 ? 123.486 152.367 145.549 1.00 26.72  ? 162 SER C N     1 
ATOM   5634 C  CA    . SER C 1 188 ? 123.898 153.770 145.522 1.00 23.34  ? 162 SER C CA    1 
ATOM   5635 C  C     . SER C 1 188 ? 125.412 153.914 145.661 1.00 28.75  ? 162 SER C C     1 
ATOM   5636 O  O     . SER C 1 188 ? 126.045 154.694 144.926 1.00 41.81  ? 162 SER C O     1 
ATOM   5637 C  CB    . SER C 1 188 ? 123.183 154.544 146.629 1.00 27.50  ? 162 SER C CB    1 
ATOM   5638 O  OG    . SER C 1 188 ? 121.779 154.394 146.528 1.00 43.87  ? 162 SER C OG    1 
ATOM   5639 N  N     . VAL C 1 189 ? 126.006 153.162 146.599 1.00 31.21  ? 163 VAL C N     1 
ATOM   5640 C  CA    . VAL C 1 189 ? 127.461 153.159 146.765 1.00 31.84  ? 163 VAL C CA    1 
ATOM   5641 C  C     . VAL C 1 189 ? 128.138 152.651 145.497 1.00 27.99  ? 163 VAL C C     1 
ATOM   5642 O  O     . VAL C 1 189 ? 129.143 153.213 145.040 1.00 36.22  ? 163 VAL C O     1 
ATOM   5643 C  CB    . VAL C 1 189 ? 127.847 152.324 148.002 1.00 28.76  ? 163 VAL C CB    1 
ATOM   5644 C  CG1   . VAL C 1 189 ? 129.347 152.073 148.065 1.00 26.26  ? 163 VAL C CG1   1 
ATOM   5645 C  CG2   . VAL C 1 189 ? 127.380 153.014 149.271 1.00 27.44  ? 163 VAL C CG2   1 
ATOM   5646 N  N     . THR C 1 190 ? 127.556 151.625 144.878 1.00 32.74  ? 164 THR C N     1 
ATOM   5647 C  CA    . THR C 1 190 ? 128.100 151.057 143.654 1.00 29.51  ? 164 THR C CA    1 
ATOM   5648 C  C     . THR C 1 190 ? 127.966 152.017 142.473 1.00 31.24  ? 164 THR C C     1 
ATOM   5649 O  O     . THR C 1 190 ? 128.864 152.091 141.628 1.00 36.35  ? 164 THR C O     1 
ATOM   5650 C  CB    . THR C 1 190 ? 127.391 149.735 143.382 1.00 26.02  ? 164 THR C CB    1 
ATOM   5651 O  OG1   . THR C 1 190 ? 127.398 148.946 144.578 1.00 40.78  ? 164 THR C OG1   1 
ATOM   5652 C  CG2   . THR C 1 190 ? 128.101 148.980 142.356 1.00 33.18  ? 164 THR C CG2   1 
ATOM   5653 N  N     . LEU C 1 191 ? 126.864 152.774 142.416 1.00 29.34  ? 165 LEU C N     1 
ATOM   5654 C  CA    . LEU C 1 191 ? 126.670 153.763 141.359 1.00 25.04  ? 165 LEU C CA    1 
ATOM   5655 C  C     . LEU C 1 191 ? 127.694 154.887 141.454 1.00 34.07  ? 165 LEU C C     1 
ATOM   5656 O  O     . LEU C 1 191 ? 128.184 155.375 140.428 1.00 37.42  ? 165 LEU C O     1 
ATOM   5657 C  CB    . LEU C 1 191 ? 125.246 154.322 141.425 1.00 25.26  ? 165 LEU C CB    1 
ATOM   5658 C  CG    . LEU C 1 191 ? 124.894 155.553 140.585 1.00 28.92  ? 165 LEU C CG    1 
ATOM   5659 C  CD1   . LEU C 1 191 ? 124.748 155.191 139.114 1.00 25.30  ? 165 LEU C CD1   1 
ATOM   5660 C  CD2   . LEU C 1 191 ? 123.632 156.221 141.104 1.00 24.20  ? 165 LEU C CD2   1 
ATOM   5661 N  N     . LEU C 1 192 ? 128.032 155.312 142.675 1.00 37.15  ? 166 LEU C N     1 
ATOM   5662 C  CA    . LEU C 1 192 ? 129.106 156.297 142.814 1.00 25.05  ? 166 LEU C CA    1 
ATOM   5663 C  C     . LEU C 1 192 ? 130.468 155.696 142.461 1.00 30.23  ? 166 LEU C C     1 
ATOM   5664 O  O     . LEU C 1 192 ? 131.237 156.281 141.680 1.00 32.75  ? 166 LEU C O     1 
ATOM   5665 C  CB    . LEU C 1 192 ? 129.127 156.872 144.230 1.00 30.87  ? 166 LEU C CB    1 
ATOM   5666 C  CG    . LEU C 1 192 ? 130.277 157.848 144.510 1.00 31.99  ? 166 LEU C CG    1 
ATOM   5667 C  CD1   . LEU C 1 192 ? 130.215 159.063 143.594 1.00 32.51  ? 166 LEU C CD1   1 
ATOM   5668 C  CD2   . LEU C 1 192 ? 130.289 158.281 145.961 1.00 29.83  ? 166 LEU C CD2   1 
ATOM   5669 N  N     . THR C 1 193 ? 130.781 154.518 143.013 1.00 34.13  ? 167 THR C N     1 
ATOM   5670 C  CA    . THR C 1 193 ? 132.131 153.983 142.891 1.00 22.73  ? 167 THR C CA    1 
ATOM   5671 C  C     . THR C 1 193 ? 132.435 153.431 141.505 1.00 29.07  ? 167 THR C C     1 
ATOM   5672 O  O     . THR C 1 193 ? 133.610 153.342 141.150 1.00 32.70  ? 167 THR C O     1 
ATOM   5673 C  CB    . THR C 1 193 ? 132.384 152.895 143.937 1.00 30.79  ? 167 THR C CB    1 
ATOM   5674 O  OG1   . THR C 1 193 ? 131.335 151.923 143.891 1.00 33.30  ? 167 THR C OG1   1 
ATOM   5675 C  CG2   . THR C 1 193 ? 132.462 153.501 145.331 1.00 28.22  ? 167 THR C CG2   1 
ATOM   5676 N  N     . SER C 1 194 ? 131.422 153.083 140.706 1.00 34.99  ? 168 SER C N     1 
ATOM   5677 C  CA    . SER C 1 194 ? 131.689 152.643 139.338 1.00 25.46  ? 168 SER C CA    1 
ATOM   5678 C  C     . SER C 1 194 ? 132.182 153.797 138.471 1.00 27.96  ? 168 SER C C     1 
ATOM   5679 O  O     . SER C 1 194 ? 133.166 153.652 137.733 1.00 38.71  ? 168 SER C O     1 
ATOM   5680 C  CB    . SER C 1 194 ? 130.436 152.005 138.740 1.00 24.83  ? 168 SER C CB    1 
ATOM   5681 O  OG    . SER C 1 194 ? 129.395 152.952 138.594 1.00 33.86  ? 168 SER C OG    1 
ATOM   5682 N  N     . THR C 1 195 ? 131.567 154.971 138.569 1.00 27.29  ? 169 THR C N     1 
ATOM   5683 C  CA    . THR C 1 195 ? 132.012 156.163 137.820 1.00 26.80  ? 169 THR C CA    1 
ATOM   5684 C  C     . THR C 1 195 ? 133.383 156.620 138.270 1.00 26.69  ? 169 THR C C     1 
ATOM   5685 O  O     . THR C 1 195 ? 134.187 156.941 137.417 1.00 34.50  ? 169 THR C O     1 
ATOM   5686 C  CB    . THR C 1 195 ? 130.957 157.272 137.904 1.00 33.88  ? 169 THR C CB    1 
ATOM   5687 O  OG1   . THR C 1 195 ? 129.850 156.761 137.177 1.00 39.31  ? 169 THR C OG1   1 
ATOM   5688 C  CG2   . THR C 1 195 ? 131.415 158.573 137.273 1.00 26.19  ? 169 THR C CG2   1 
ATOM   5689 N  N     . LEU C 1 196 ? 133.644 156.652 139.561 1.00 32.15  ? 170 LEU C N     1 
ATOM   5690 C  CA    . LEU C 1 196 ? 134.958 157.034 140.133 1.00 28.94  ? 170 LEU C CA    1 
ATOM   5691 C  C     . LEU C 1 196 ? 136.029 156.033 139.670 1.00 24.98  ? 170 LEU C C     1 
ATOM   5692 O  O     . LEU C 1 196 ? 137.096 156.484 139.347 1.00 27.32  ? 170 LEU C O     1 
ATOM   5693 C  CB    . LEU C 1 196 ? 134.868 157.138 141.656 1.00 31.85  ? 170 LEU C CB    1 
ATOM   5694 C  CG    . LEU C 1 196 ? 134.245 158.401 142.246 1.00 31.63  ? 170 LEU C CG    1 
ATOM   5695 C  CD1   . LEU C 1 196 ? 134.433 158.317 143.741 1.00 32.06  ? 170 LEU C CD1   1 
ATOM   5696 C  CD2   . LEU C 1 196 ? 134.892 159.642 141.686 1.00 26.66  ? 170 LEU C CD2   1 
ATOM   5697 N  N     . GLY C 1 197 ? 135.742 154.743 139.608 1.00 29.33  ? 171 GLY C N     1 
ATOM   5698 C  CA    . GLY C 1 197 ? 136.684 153.736 139.101 1.00 30.47  ? 171 GLY C CA    1 
ATOM   5699 C  C     . GLY C 1 197 ? 137.049 153.925 137.657 1.00 31.27  ? 171 GLY C C     1 
ATOM   5700 O  O     . GLY C 1 197 ? 138.185 153.633 137.318 1.00 40.75  ? 171 GLY C O     1 
ATOM   5701 N  N     . VAL C 1 198 ? 136.112 154.270 136.798 1.00 35.27  ? 172 VAL C N     1 
ATOM   5702 C  CA    . VAL C 1 198 ? 136.476 154.610 135.395 1.00 35.37  ? 172 VAL C CA    1 
ATOM   5703 C  C     . VAL C 1 198 ? 137.366 155.864 135.309 1.00 33.37  ? 172 VAL C C     1 
ATOM   5704 O  O     . VAL C 1 198 ? 138.341 155.824 134.601 1.00 35.74  ? 172 VAL C O     1 
ATOM   5705 C  CB    . VAL C 1 198 ? 135.138 154.785 134.639 1.00 31.78  ? 172 VAL C CB    1 
ATOM   5706 C  CG1   . VAL C 1 198 ? 135.331 155.362 133.246 1.00 35.97  ? 172 VAL C CG1   1 
ATOM   5707 C  CG2   . VAL C 1 198 ? 134.350 153.492 134.567 1.00 35.90  ? 172 VAL C CG2   1 
ATOM   5708 N  N     . LEU C 1 199 ? 137.041 156.934 136.013 1.00 34.55  ? 173 LEU C N     1 
ATOM   5709 C  CA    . LEU C 1 199 ? 137.874 158.152 136.029 1.00 28.23  ? 173 LEU C CA    1 
ATOM   5710 C  C     . LEU C 1 199 ? 139.236 157.932 136.697 1.00 36.54  ? 173 LEU C C     1 
ATOM   5711 O  O     . LEU C 1 199 ? 140.209 158.380 136.105 1.00 41.70  ? 173 LEU C O     1 
ATOM   5712 C  CB    . LEU C 1 199 ? 137.044 159.221 136.734 1.00 31.53  ? 173 LEU C CB    1 
ATOM   5713 C  CG    . LEU C 1 199 ? 135.670 159.552 136.150 1.00 33.83  ? 173 LEU C CG    1 
ATOM   5714 C  CD1   . LEU C 1 199 ? 134.940 160.437 137.135 1.00 38.92  ? 173 LEU C CD1   1 
ATOM   5715 C  CD2   . LEU C 1 199 ? 135.796 160.258 134.830 1.00 34.59  ? 173 LEU C CD2   1 
ATOM   5716 N  N     . VAL C 1 200 ? 139.304 157.268 137.854 1.00 36.70  ? 174 VAL C N     1 
ATOM   5717 C  CA    . VAL C 1 200 ? 140.592 156.922 138.524 1.00 27.72  ? 174 VAL C CA    1 
ATOM   5718 C  C     . VAL C 1 200 ? 140.534 155.432 138.865 1.00 30.83  ? 174 VAL C C     1 
ATOM   5719 O  O     . VAL C 1 200 ? 139.804 155.100 139.747 1.00 44.51  ? 174 VAL C O     1 
ATOM   5720 C  CB    . VAL C 1 200 ? 140.903 157.818 139.749 1.00 32.45  ? 174 VAL C CB    1 
ATOM   5721 C  CG1   . VAL C 1 200 ? 142.271 157.553 140.353 1.00 31.26  ? 174 VAL C CG1   1 
ATOM   5722 C  CG2   . VAL C 1 200 ? 140.739 159.297 139.434 1.00 34.72  ? 174 VAL C CG2   1 
ATOM   5723 N  N     . ARG C 1 201 ? 141.385 154.616 138.282 1.00 33.25  ? 175 ARG C N     1 
ATOM   5724 C  CA    . ARG C 1 201 ? 141.451 153.149 138.519 1.00 36.01  ? 175 ARG C CA    1 
ATOM   5725 C  C     . ARG C 1 201 ? 141.923 152.884 139.953 1.00 37.21  ? 175 ARG C C     1 
ATOM   5726 O  O     . ARG C 1 201 ? 141.614 151.803 140.433 1.00 42.68  ? 175 ARG C O     1 
ATOM   5727 C  CB    . ARG C 1 201 ? 142.219 152.443 137.391 1.00 35.99  ? 175 ARG C CB    1 
ATOM   5728 C  CG    . ARG C 1 201 ? 141.837 150.999 137.108 1.00 33.19  ? 175 ARG C CG    1 
ATOM   5729 C  CD    . ARG C 1 201 ? 140.615 150.779 136.230 1.00 37.11  ? 175 ARG C CD    1 
ATOM   5730 N  NE    . ARG C 1 201 ? 140.051 151.994 135.637 1.00 42.13  ? 175 ARG C NE    1 
ATOM   5731 C  CZ    . ARG C 1 201 ? 140.145 152.348 134.369 1.00 40.81  ? 175 ARG C CZ    1 
ATOM   5732 N  NH1   . ARG C 1 201 ? 140.540 151.477 133.468 1.00 34.84  ? 175 ARG C NH1   1 
ATOM   5733 N  NH2   . ARG C 1 201 ? 139.854 153.577 134.007 1.00 39.73  ? 175 ARG C NH2   1 
ATOM   5734 N  N     . ASP C 1 202 ? 142.662 153.806 140.563 1.00 36.49  ? 176 ASP C N     1 
ATOM   5735 C  CA    . ASP C 1 202 ? 143.253 153.672 141.922 1.00 32.91  ? 176 ASP C CA    1 
ATOM   5736 C  C     . ASP C 1 202 ? 142.111 153.475 142.921 1.00 37.12  ? 176 ASP C C     1 
ATOM   5737 O  O     . ASP C 1 202 ? 142.338 152.783 143.876 1.00 49.78  ? 176 ASP C O     1 
ATOM   5738 C  CB    . ASP C 1 202 ? 144.184 154.849 142.151 1.00 39.13  ? 176 ASP C CB    1 
ATOM   5739 C  CG    . ASP C 1 202 ? 145.145 155.171 141.021 1.00 38.59  ? 176 ASP C CG    1 
ATOM   5740 O  OD1   . ASP C 1 202 ? 144.675 155.345 139.885 1.00 37.01  ? 176 ASP C OD1   1 
ATOM   5741 O  OD2   . ASP C 1 202 ? 146.350 155.257 141.290 1.00 39.31  ? 176 ASP C OD2   1 
ATOM   5742 N  N     . THR C 1 203 ? 140.976 154.128 142.747 1.00 41.01  ? 177 THR C N     1 
ATOM   5743 C  CA    . THR C 1 203 ? 139.746 154.004 143.546 1.00 39.34  ? 177 THR C CA    1 
ATOM   5744 C  C     . THR C 1 203 ? 139.328 152.566 143.800 1.00 37.81  ? 177 THR C C     1 
ATOM   5745 O  O     . THR C 1 203 ? 138.977 152.289 144.930 1.00 47.78  ? 177 THR C O     1 
ATOM   5746 C  CB    . THR C 1 203 ? 138.711 154.812 142.756 1.00 39.89  ? 177 THR C CB    1 
ATOM   5747 O  OG1   . THR C 1 203 ? 138.902 156.160 143.170 1.00 39.76  ? 177 THR C OG1   1 
ATOM   5748 C  CG2   . THR C 1 203 ? 137.282 154.371 143.026 1.00 43.26  ? 177 THR C CG2   1 
ATOM   5749 N  N     . GLN C 1 204 ? 139.357 151.684 142.819 1.00 29.54  ? 178 GLN C N     1 
ATOM   5750 C  CA    . GLN C 1 204 ? 139.080 150.245 142.992 1.00 37.94  ? 178 GLN C CA    1 
ATOM   5751 C  C     . GLN C 1 204 ? 140.075 149.577 143.953 1.00 38.48  ? 178 GLN C C     1 
ATOM   5752 O  O     . GLN C 1 204 ? 139.685 148.583 144.549 1.00 46.50  ? 178 GLN C O     1 
ATOM   5753 C  CB    . GLN C 1 204 ? 139.168 149.626 141.598 1.00 40.86  ? 178 GLN C CB    1 
ATOM   5754 C  CG    . GLN C 1 204 ? 138.368 150.329 140.508 1.00 42.32  ? 178 GLN C CG    1 
ATOM   5755 C  CD    . GLN C 1 204 ? 138.349 149.547 139.215 1.00 45.02  ? 178 GLN C CD    1 
ATOM   5756 O  OE1   . GLN C 1 204 ? 139.058 148.549 139.064 1.00 48.54  ? 178 GLN C OE1   1 
ATOM   5757 N  NE2   . GLN C 1 204 ? 137.548 149.990 138.261 1.00 43.48  ? 178 GLN C NE2   1 
ATOM   5758 N  N     . MET C 1 205 ? 141.326 150.011 144.032 1.00 48.83  ? 179 MET C N     1 
ATOM   5759 C  CA    . MET C 1 205 ? 142.322 149.560 144.995 1.00 40.73  ? 179 MET C CA    1 
ATOM   5760 C  C     . MET C 1 205 ? 141.990 150.012 146.414 1.00 43.04  ? 179 MET C C     1 
ATOM   5761 O  O     . MET C 1 205 ? 142.328 149.314 147.375 1.00 49.28  ? 179 MET C O     1 
ATOM   5762 C  CB    . MET C 1 205 ? 143.704 150.070 144.589 1.00 46.00  ? 179 MET C CB    1 
ATOM   5763 C  CG    . MET C 1 205 ? 144.249 149.480 143.297 1.00 43.98  ? 179 MET C CG    1 
ATOM   5764 S  SD    . MET C 1 205 ? 144.344 147.681 143.310 1.00 60.96  ? 179 MET C SD    1 
ATOM   5765 C  CE    . MET C 1 205 ? 145.459 147.408 144.682 1.00 46.85  ? 179 MET C CE    1 
ATOM   5766 N  N     . LEU C 1 206 ? 141.345 151.175 146.554 1.00 45.28  ? 180 LEU C N     1 
ATOM   5767 C  CA    . LEU C 1 206 ? 140.953 151.673 147.878 1.00 41.82  ? 180 LEU C CA    1 
ATOM   5768 C  C     . LEU C 1 206 ? 139.863 150.809 148.518 1.00 41.37  ? 180 LEU C C     1 
ATOM   5769 O  O     . LEU C 1 206 ? 139.767 150.725 149.758 1.00 42.97  ? 180 LEU C O     1 
ATOM   5770 C  CB    . LEU C 1 206 ? 140.468 153.120 147.762 1.00 45.74  ? 180 LEU C CB    1 
ATOM   5771 C  CG    . LEU C 1 206 ? 140.972 154.220 148.697 1.00 46.78  ? 180 LEU C CG    1 
ATOM   5772 C  CD1   . LEU C 1 206 ? 142.464 154.422 148.568 1.00 46.04  ? 180 LEU C CD1   1 
ATOM   5773 C  CD2   . LEU C 1 206 ? 140.230 155.518 148.428 1.00 44.58  ? 180 LEU C CD2   1 
ATOM   5774 N  N     . MET C 1 207 ? 139.010 150.188 147.685 1.00 39.61  ? 181 MET C N     1 
ATOM   5775 C  CA    . MET C 1 207 ? 137.838 149.470 148.209 1.00 41.72  ? 181 MET C CA    1 
ATOM   5776 C  C     . MET C 1 207 ? 138.194 148.269 149.087 1.00 45.28  ? 181 MET C C     1 
ATOM   5777 O  O     . MET C 1 207 ? 137.397 147.902 149.958 1.00 50.50  ? 181 MET C O     1 
ATOM   5778 C  CB    . MET C 1 207 ? 136.904 148.998 147.086 1.00 48.25  ? 181 MET C CB    1 
ATOM   5779 C  CG    . MET C 1 207 ? 136.502 150.017 146.028 1.00 44.89  ? 181 MET C CG    1 
ATOM   5780 S  SD    . MET C 1 207 ? 135.753 151.599 146.514 1.00 58.93  ? 181 MET C SD    1 
ATOM   5781 C  CE    . MET C 1 207 ? 134.642 151.168 147.857 1.00 46.95  ? 181 MET C CE    1 
ATOM   5782 N  N     . GLN C 1 208 ? 139.368 147.654 148.885 1.00 40.85  ? 182 GLN C N     1 
ATOM   5783 C  CA    . GLN C 1 208 ? 139.779 146.526 149.726 1.00 42.86  ? 182 GLN C CA    1 
ATOM   5784 C  C     . GLN C 1 208 ? 139.963 146.930 151.185 1.00 44.70  ? 182 GLN C C     1 
ATOM   5785 O  O     . GLN C 1 208 ? 139.521 146.212 152.087 1.00 47.44  ? 182 GLN C O     1 
ATOM   5786 C  CB    . GLN C 1 208 ? 141.063 145.891 149.193 1.00 50.88  ? 182 GLN C CB    1 
ATOM   5787 C  CG    . GLN C 1 208 ? 140.861 144.870 148.087 1.00 53.16  ? 182 GLN C CG    1 
ATOM   5788 C  CD    . GLN C 1 208 ? 140.853 145.485 146.715 1.00 57.83  ? 182 GLN C CD    1 
ATOM   5789 O  OE1   . GLN C 1 208 ? 139.949 146.240 146.378 1.00 54.40  ? 182 GLN C OE1   1 
ATOM   5790 N  NE2   . GLN C 1 208 ? 141.865 145.174 145.914 1.00 55.61  ? 182 GLN C NE2   1 
ATOM   5791 N  N     . ALA C 1 209 ? 140.599 148.072 151.441 1.00 46.75  ? 183 ALA C N     1 
ATOM   5792 C  CA    . ALA C 1 209 ? 140.735 148.528 152.820 1.00 42.35  ? 183 ALA C CA    1 
ATOM   5793 C  C     . ALA C 1 209 ? 139.421 149.080 153.359 1.00 39.77  ? 183 ALA C C     1 
ATOM   5794 O  O     . ALA C 1 209 ? 139.108 148.899 154.549 1.00 45.46  ? 183 ALA C O     1 
ATOM   5795 C  CB    . ALA C 1 209 ? 141.840 149.577 152.924 1.00 43.14  ? 183 ALA C CB    1 
ATOM   5796 N  N     . ILE C 1 210 ? 138.640 149.743 152.489 1.00 33.81  ? 184 ILE C N     1 
ATOM   5797 C  CA    . ILE C 1 210 ? 137.370 150.335 152.921 1.00 40.47  ? 184 ILE C CA    1 
ATOM   5798 C  C     . ILE C 1 210 ? 136.390 149.254 153.384 1.00 37.07  ? 184 ILE C C     1 
ATOM   5799 O  O     . ILE C 1 210 ? 135.728 149.396 154.422 1.00 29.06  ? 184 ILE C O     1 
ATOM   5800 C  CB    . ILE C 1 210 ? 136.786 151.207 151.791 1.00 42.36  ? 184 ILE C CB    1 
ATOM   5801 C  CG1   . ILE C 1 210 ? 137.642 152.459 151.599 1.00 36.21  ? 184 ILE C CG1   1 
ATOM   5802 C  CG2   . ILE C 1 210 ? 135.346 151.615 152.083 1.00 36.92  ? 184 ILE C CG2   1 
ATOM   5803 C  CD1   . ILE C 1 210 ? 137.234 153.304 150.417 1.00 38.90  ? 184 ILE C CD1   1 
ATOM   5804 N  N     . LEU C 1 211 ? 136.329 148.131 152.661 1.00 37.42  ? 185 LEU C N     1 
ATOM   5805 C  CA    . LEU C 1 211 ? 135.384 147.080 153.024 1.00 38.37  ? 185 LEU C CA    1 
ATOM   5806 C  C     . LEU C 1 211 ? 135.807 146.326 154.281 1.00 31.58  ? 185 LEU C C     1 
ATOM   5807 O  O     . LEU C 1 211 ? 134.946 145.852 155.026 1.00 37.76  ? 185 LEU C O     1 
ATOM   5808 C  CB    . LEU C 1 211 ? 135.197 146.122 151.850 1.00 37.97  ? 185 LEU C CB    1 
ATOM   5809 C  CG    . LEU C 1 211 ? 134.177 146.653 150.840 1.00 34.57  ? 185 LEU C CG    1 
ATOM   5810 C  CD1   . LEU C 1 211 ? 134.383 146.028 149.480 1.00 37.06  ? 185 LEU C CD1   1 
ATOM   5811 C  CD2   . LEU C 1 211 ? 132.759 146.418 151.334 1.00 30.49  ? 185 LEU C CD2   1 
ATOM   5812 N  N     . ARG C 1 212 ? 137.110 146.228 154.557 1.00 31.35  ? 186 ARG C N     1 
ATOM   5813 C  CA    . ARG C 1 212 ? 137.542 145.627 155.818 1.00 30.36  ? 186 ARG C CA    1 
ATOM   5814 C  C     . ARG C 1 212 ? 137.232 146.541 156.998 1.00 32.58  ? 186 ARG C C     1 
ATOM   5815 O  O     . ARG C 1 212 ? 136.905 146.058 158.095 1.00 29.68  ? 186 ARG C O     1 
ATOM   5816 C  CB    . ARG C 1 212 ? 139.031 145.296 155.764 1.00 38.86  ? 186 ARG C CB    1 
ATOM   5817 C  CG    . ARG C 1 212 ? 139.373 144.291 154.689 1.00 35.96  ? 186 ARG C CG    1 
ATOM   5818 C  CD    . ARG C 1 212 ? 140.373 143.255 155.149 1.00 37.31  ? 186 ARG C CD    1 
ATOM   5819 N  NE    . ARG C 1 212 ? 140.090 141.942 154.579 1.00 42.17  ? 186 ARG C NE    1 
ATOM   5820 C  CZ    . ARG C 1 212 ? 140.410 141.564 153.349 1.00 43.68  ? 186 ARG C CZ    1 
ATOM   5821 N  NH1   . ARG C 1 212 ? 141.046 142.373 152.518 1.00 39.14  ? 186 ARG C NH1   1 
ATOM   5822 N  NH2   . ARG C 1 212 ? 140.087 140.340 152.941 1.00 42.66  ? 186 ARG C NH2   1 
ATOM   5823 N  N     . ILE C 1 213 ? 137.331 147.862 156.784 1.00 40.42  ? 187 ILE C N     1 
ATOM   5824 C  CA    . ILE C 1 213 ? 136.874 148.833 157.782 1.00 27.63  ? 187 ILE C CA    1 
ATOM   5825 C  C     . ILE C 1 213 ? 135.386 148.643 158.064 1.00 35.67  ? 187 ILE C C     1 
ATOM   5826 O  O     . ILE C 1 213 ? 134.951 148.616 159.223 1.00 38.39  ? 187 ILE C O     1 
ATOM   5827 C  CB    . ILE C 1 213 ? 137.184 150.268 157.310 1.00 37.32  ? 187 ILE C CB    1 
ATOM   5828 C  CG1   . ILE C 1 213 ? 138.664 150.590 157.507 1.00 38.05  ? 187 ILE C CG1   1 
ATOM   5829 C  CG2   . ILE C 1 213 ? 136.322 151.304 158.039 1.00 38.10  ? 187 ILE C CG2   1 
ATOM   5830 C  CD1   . ILE C 1 213 ? 139.042 152.028 157.209 1.00 32.93  ? 187 ILE C CD1   1 
ATOM   5831 N  N     . LEU C 1 214 ? 134.590 148.473 157.005 1.00 41.02  ? 188 LEU C N     1 
ATOM   5832 C  CA    . LEU C 1 214 ? 133.151 148.273 157.180 1.00 29.67  ? 188 LEU C CA    1 
ATOM   5833 C  C     . LEU C 1 214 ? 132.824 146.922 157.812 1.00 28.81  ? 188 LEU C C     1 
ATOM   5834 O  O     . LEU C 1 214 ? 131.802 146.789 158.494 1.00 31.74  ? 188 LEU C O     1 
ATOM   5835 C  CB    . LEU C 1 214 ? 132.432 148.412 155.838 1.00 30.43  ? 188 LEU C CB    1 
ATOM   5836 C  CG    . LEU C 1 214 ? 132.515 149.770 155.138 1.00 31.89  ? 188 LEU C CG    1 
ATOM   5837 C  CD1   . LEU C 1 214 ? 131.663 149.772 153.882 1.00 32.62  ? 188 LEU C CD1   1 
ATOM   5838 C  CD2   . LEU C 1 214 ? 132.112 150.898 156.071 1.00 26.32  ? 188 LEU C CD2   1 
ATOM   5839 N  N     . PHE C 1 215 ? 133.669 145.911 157.597 1.00 34.62  ? 189 PHE C N     1 
ATOM   5840 C  CA    . PHE C 1 215 ? 133.399 144.584 158.140 1.00 16.67  ? 189 PHE C CA    1 
ATOM   5841 C  C     . PHE C 1 215 ? 133.705 144.513 159.629 1.00 28.66  ? 189 PHE C C     1 
ATOM   5842 O  O     . PHE C 1 215 ? 132.846 144.125 160.430 1.00 28.11  ? 189 PHE C O     1 
ATOM   5843 C  CB    . PHE C 1 215 ? 134.215 143.531 157.395 1.00 21.59  ? 189 PHE C CB    1 
ATOM   5844 C  CG    . PHE C 1 215 ? 133.934 142.121 157.835 1.00 29.35  ? 189 PHE C CG    1 
ATOM   5845 C  CD1   . PHE C 1 215 ? 132.633 141.649 157.912 1.00 31.22  ? 189 PHE C CD1   1 
ATOM   5846 C  CD2   . PHE C 1 215 ? 134.973 141.266 158.172 1.00 24.34  ? 189 PHE C CD2   1 
ATOM   5847 C  CE1   . PHE C 1 215 ? 132.371 140.351 158.308 1.00 23.63  ? 189 PHE C CE1   1 
ATOM   5848 C  CE2   . PHE C 1 215 ? 134.717 139.968 158.572 1.00 25.91  ? 189 PHE C CE2   1 
ATOM   5849 C  CZ    . PHE C 1 215 ? 133.415 139.511 158.639 1.00 17.63  ? 189 PHE C CZ    1 
ATOM   5850 N  N     . TYR C 1 216 ? 134.932 144.864 160.019 1.00 34.34  ? 190 TYR C N     1 
ATOM   5851 C  CA    . TYR C 1 216 ? 135.347 144.613 161.395 1.00 22.48  ? 190 TYR C CA    1 
ATOM   5852 C  C     . TYR C 1 216 ? 134.760 145.624 162.374 1.00 23.12  ? 190 TYR C C     1 
ATOM   5853 O  O     . TYR C 1 216 ? 134.497 145.284 163.532 1.00 29.36  ? 190 TYR C O     1 
ATOM   5854 C  CB    . TYR C 1 216 ? 136.867 144.607 161.489 1.00 24.92  ? 190 TYR C CB    1 
ATOM   5855 C  CG    . TYR C 1 216 ? 137.533 143.403 160.874 1.00 28.25  ? 190 TYR C CG    1 
ATOM   5856 C  CD1   . TYR C 1 216 ? 137.325 142.129 161.391 1.00 24.86  ? 190 TYR C CD1   1 
ATOM   5857 C  CD2   . TYR C 1 216 ? 138.377 143.541 159.783 1.00 28.76  ? 190 TYR C CD2   1 
ATOM   5858 C  CE1   . TYR C 1 216 ? 137.942 141.026 160.829 1.00 27.84  ? 190 TYR C CE1   1 
ATOM   5859 C  CE2   . TYR C 1 216 ? 138.994 142.449 159.216 1.00 30.07  ? 190 TYR C CE2   1 
ATOM   5860 C  CZ    . TYR C 1 216 ? 138.774 141.195 159.742 1.00 28.48  ? 190 TYR C CZ    1 
ATOM   5861 O  OH    . TYR C 1 216 ? 139.394 140.109 159.173 1.00 33.81  ? 190 TYR C OH    1 
ATOM   5862 N  N     . PHE C 1 217 ? 134.556 146.866 161.939 1.00 32.63  ? 191 PHE C N     1 
ATOM   5863 C  CA    . PHE C 1 217 ? 133.946 147.879 162.794 1.00 36.51  ? 191 PHE C CA    1 
ATOM   5864 C  C     . PHE C 1 217 ? 132.428 147.819 162.689 1.00 37.71  ? 191 PHE C C     1 
ATOM   5865 O  O     . PHE C 1 217 ? 131.788 148.778 162.245 1.00 44.66  ? 191 PHE C O     1 
ATOM   5866 C  CB    . PHE C 1 217 ? 134.457 149.272 162.425 1.00 38.70  ? 191 PHE C CB    1 
ATOM   5867 C  CG    . PHE C 1 217 ? 134.552 150.211 163.589 1.00 42.70  ? 191 PHE C CG    1 
ATOM   5868 C  CD1   . PHE C 1 217 ? 135.145 149.810 164.775 1.00 44.68  ? 191 PHE C CD1   1 
ATOM   5869 C  CD2   . PHE C 1 217 ? 134.043 151.499 163.499 1.00 47.19  ? 191 PHE C CD2   1 
ATOM   5870 C  CE1   . PHE C 1 217 ? 135.232 150.676 165.852 1.00 47.64  ? 191 PHE C CE1   1 
ATOM   5871 C  CE2   . PHE C 1 217 ? 134.126 152.371 164.571 1.00 44.56  ? 191 PHE C CE2   1 
ATOM   5872 C  CZ    . PHE C 1 217 ? 134.723 151.957 165.748 1.00 47.43  ? 191 PHE C CZ    1 
ATOM   5873 N  N     . SER C 1 218 ? 131.859 146.703 163.137 1.00 32.64  ? 192 SER C N     1 
ATOM   5874 C  CA    . SER C 1 218 ? 130.406 146.478 162.996 1.00 24.31  ? 192 SER C CA    1 
ATOM   5875 C  C     . SER C 1 218 ? 129.964 145.487 164.080 1.00 32.82  ? 192 SER C C     1 
ATOM   5876 O  O     . SER C 1 218 ? 130.838 144.939 164.769 1.00 34.50  ? 192 SER C O     1 
ATOM   5877 C  CB    . SER C 1 218 ? 130.112 145.968 161.607 1.00 23.76  ? 192 SER C CB    1 
ATOM   5878 O  OG    . SER C 1 218 ? 130.517 144.615 161.471 1.00 34.71  ? 192 SER C OG    1 
ATOM   5879 N  N     . PRO C 1 219 ? 128.652 145.211 164.243 1.00 38.15  ? 193 PRO C N     1 
ATOM   5880 C  CA    . PRO C 1 219 ? 128.124 144.274 165.269 1.00 29.44  ? 193 PRO C CA    1 
ATOM   5881 C  C     . PRO C 1 219 ? 128.009 142.846 164.737 1.00 29.75  ? 193 PRO C C     1 
ATOM   5882 O  O     . PRO C 1 219 ? 127.376 142.042 165.444 1.00 40.81  ? 193 PRO C O     1 
ATOM   5883 C  CB    . PRO C 1 219 ? 126.820 144.949 165.669 1.00 34.41  ? 193 PRO C CB    1 
ATOM   5884 C  CG    . PRO C 1 219 ? 126.298 145.452 164.340 1.00 23.31  ? 193 PRO C CG    1 
ATOM   5885 C  CD    . PRO C 1 219 ? 127.496 145.874 163.554 1.00 30.60  ? 193 PRO C CD    1 
ATOM   5886 N  N     . ILE C 1 220 ? 128.453 142.562 163.514 1.00 24.63  ? 194 ILE C N     1 
ATOM   5887 C  CA    . ILE C 1 220 ? 128.310 141.215 162.880 1.00 26.78  ? 194 ILE C CA    1 
ATOM   5888 C  C     . ILE C 1 220 ? 129.054 140.087 163.627 1.00 37.12  ? 194 ILE C C     1 
ATOM   5889 O  O     . ILE C 1 220 ? 128.425 139.021 163.768 1.00 41.54  ? 194 ILE C O     1 
ATOM   5890 C  CB    . ILE C 1 220 ? 128.804 141.286 161.420 1.00 34.72  ? 194 ILE C CB    1 
ATOM   5891 C  CG1   . ILE C 1 220 ? 127.963 142.228 160.568 1.00 33.20  ? 194 ILE C CG1   1 
ATOM   5892 C  CG2   . ILE C 1 220 ? 128.904 139.898 160.789 1.00 24.53  ? 194 ILE C CG2   1 
ATOM   5893 C  CD1   . ILE C 1 220 ? 128.370 142.240 159.107 1.00 33.37  ? 194 ILE C CD1   1 
ATOM   5894 N  N     . LEU C 1 221 ? 130.284 140.285 164.125 1.00 29.80  ? 195 LEU C N     1 
ATOM   5895 C  CA    . LEU C 1 221 ? 131.090 139.169 164.708 1.00 29.32  ? 195 LEU C CA    1 
ATOM   5896 C  C     . LEU C 1 221 ? 131.214 139.304 166.223 1.00 30.40  ? 195 LEU C C     1 
ATOM   5897 O  O     . LEU C 1 221 ? 131.564 138.304 166.867 1.00 41.71  ? 195 LEU C O     1 
ATOM   5898 C  CB    . LEU C 1 221 ? 132.488 139.170 164.089 1.00 32.10  ? 195 LEU C CB    1 
ATOM   5899 C  CG    . LEU C 1 221 ? 132.601 139.061 162.567 1.00 27.67  ? 195 LEU C CG    1 
ATOM   5900 C  CD1   . LEU C 1 221 ? 133.987 139.564 162.208 1.00 30.05  ? 195 LEU C CD1   1 
ATOM   5901 C  CD2   . LEU C 1 221 ? 132.440 137.619 162.128 1.00 27.95  ? 195 LEU C CD2   1 
ATOM   5902 N  N     . TRP C 1 222 ? 130.916 140.475 166.763 1.00 27.02  ? 196 TRP C N     1 
ATOM   5903 C  CA    . TRP C 1 222 ? 131.118 140.788 168.170 1.00 25.46  ? 196 TRP C CA    1 
ATOM   5904 C  C     . TRP C 1 222 ? 130.278 141.992 168.562 1.00 33.01  ? 196 TRP C C     1 
ATOM   5905 O  O     . TRP C 1 222 ? 129.863 142.789 167.721 1.00 41.25  ? 196 TRP C O     1 
ATOM   5906 C  CB    . TRP C 1 222 ? 132.604 141.029 168.477 1.00 31.33  ? 196 TRP C CB    1 
ATOM   5907 C  CG    . TRP C 1 222 ? 133.336 141.873 167.456 1.00 30.18  ? 196 TRP C CG    1 
ATOM   5908 C  CD1   . TRP C 1 222 ? 132.886 143.002 166.833 1.00 28.49  ? 196 TRP C CD1   1 
ATOM   5909 C  CD2   . TRP C 1 222 ? 134.658 141.644 166.955 1.00 32.82  ? 196 TRP C CD2   1 
ATOM   5910 N  NE1   . TRP C 1 222 ? 133.838 143.480 165.970 1.00 28.29  ? 196 TRP C NE1   1 
ATOM   5911 C  CE2   . TRP C 1 222 ? 134.937 142.666 166.029 1.00 29.39  ? 196 TRP C CE2   1 
ATOM   5912 C  CE3   . TRP C 1 222 ? 135.633 140.673 167.202 1.00 31.94  ? 196 TRP C CE3   1 
ATOM   5913 C  CZ2   . TRP C 1 222 ? 136.150 142.746 165.349 1.00 32.65  ? 196 TRP C CZ2   1 
ATOM   5914 C  CZ3   . TRP C 1 222 ? 136.836 140.755 166.528 1.00 31.82  ? 196 TRP C CZ3   1 
ATOM   5915 C  CH2   . TRP C 1 222 ? 137.084 141.782 165.612 1.00 27.86  ? 196 TRP C CH2   1 
ATOM   5916 N  N     . LEU C 1 223 ? 130.035 142.105 169.862 1.00 55.74  ? 197 LEU C N     1 
ATOM   5917 C  CA    . LEU C 1 223 ? 129.402 143.282 170.452 1.00 51.86  ? 197 LEU C CA    1 
ATOM   5918 C  C     . LEU C 1 223 ? 130.360 143.861 171.480 1.00 60.62  ? 197 LEU C C     1 
ATOM   5919 O  O     . LEU C 1 223 ? 130.679 143.178 172.473 1.00 66.82  ? 197 LEU C O     1 
ATOM   5920 C  CB    . LEU C 1 223 ? 128.069 142.921 171.106 1.00 51.53  ? 197 LEU C CB    1 
ATOM   5921 C  CG    . LEU C 1 223 ? 126.807 142.971 170.245 1.00 57.23  ? 197 LEU C CG    1 
ATOM   5922 C  CD1   . LEU C 1 223 ? 125.601 142.551 171.067 1.00 58.18  ? 197 LEU C CD1   1 
ATOM   5923 C  CD2   . LEU C 1 223 ? 126.600 144.355 169.652 1.00 58.01  ? 197 LEU C CD2   1 
ATOM   5924 N  N     . PRO C 1 224 ? 130.853 145.091 171.308 1.00 70.55  ? 198 PRO C N     1 
ATOM   5925 C  CA    . PRO C 1 224 ? 131.794 145.652 172.290 1.00 72.03  ? 198 PRO C CA    1 
ATOM   5926 C  C     . PRO C 1 224 ? 131.129 146.227 173.534 1.00 75.30  ? 198 PRO C C     1 
ATOM   5927 O  O     . PRO C 1 224 ? 131.456 147.339 173.960 1.00 78.52  ? 198 PRO C O     1 
ATOM   5928 C  CB    . PRO C 1 224 ? 132.515 146.750 171.493 1.00 73.20  ? 198 PRO C CB    1 
ATOM   5929 C  CG    . PRO C 1 224 ? 132.199 146.468 170.048 1.00 71.41  ? 198 PRO C CG    1 
ATOM   5930 C  CD    . PRO C 1 224 ? 130.833 145.877 170.066 1.00 71.78  ? 198 PRO C CD    1 
ATOM   5931 N  N     . LYS C 1 225 ? 130.202 145.480 174.129 1.00 81.20  ? 199 LYS C N     1 
ATOM   5932 C  CA    . LYS C 1 225 ? 129.570 145.831 175.395 1.00 80.68  ? 199 LYS C CA    1 
ATOM   5933 C  C     . LYS C 1 225 ? 130.044 144.963 176.546 1.00 80.94  ? 199 LYS C C     1 
ATOM   5934 O  O     . LYS C 1 225 ? 130.248 145.468 177.652 1.00 82.62  ? 199 LYS C O     1 
ATOM   5935 C  CB    . LYS C 1 225 ? 128.044 145.714 175.273 1.00 82.80  ? 199 LYS C CB    1 
ATOM   5936 C  CG    . LYS C 1 225 ? 127.351 146.937 174.690 1.00 84.33  ? 199 LYS C CG    1 
ATOM   5937 C  CD    . LYS C 1 225 ? 127.848 148.221 175.328 1.00 84.35  ? 199 LYS C CD    1 
ATOM   5938 C  CE    . LYS C 1 225 ? 126.699 149.155 175.674 1.00 83.04  ? 199 LYS C CE    1 
ATOM   5939 N  NZ    . LYS C 1 225 ? 127.036 150.038 176.825 1.00 80.72  ? 199 LYS C NZ    1 
ATOM   5940 N  N     . ASN C 1 226 ? 130.226 143.667 176.305 1.00 79.81  ? 200 ASN C N     1 
ATOM   5941 C  CA    . ASN C 1 226 ? 130.730 142.741 177.308 1.00 82.30  ? 200 ASN C CA    1 
ATOM   5942 C  C     . ASN C 1 226 ? 132.228 142.492 177.186 1.00 82.05  ? 200 ASN C C     1 
ATOM   5943 O  O     . ASN C 1 226 ? 132.759 141.644 177.914 1.00 79.79  ? 200 ASN C O     1 
ATOM   5944 C  CB    . ASN C 1 226 ? 129.982 141.408 177.212 1.00 80.83  ? 200 ASN C CB    1 
ATOM   5945 C  CG    . ASN C 1 226 ? 129.843 140.916 175.783 1.00 80.88  ? 200 ASN C CG    1 
ATOM   5946 O  OD1   . ASN C 1 226 ? 129.218 141.570 174.947 1.00 80.06  ? 200 ASN C OD1   1 
ATOM   5947 N  ND2   . ASN C 1 226 ? 130.425 139.758 175.497 1.00 79.37  ? 200 ASN C ND2   1 
ATOM   5948 N  N     . HIS C 1 227 ? 132.916 143.197 176.290 1.00 80.71  ? 201 HIS C N     1 
ATOM   5949 C  CA    . HIS C 1 227 ? 134.342 142.995 176.063 1.00 80.45  ? 201 HIS C CA    1 
ATOM   5950 C  C     . HIS C 1 227 ? 135.188 144.193 176.462 1.00 82.25  ? 201 HIS C C     1 
ATOM   5951 O  O     . HIS C 1 227 ? 136.113 144.046 177.271 1.00 78.97  ? 201 HIS C O     1 
ATOM   5952 C  CB    . HIS C 1 227 ? 134.595 142.652 174.587 1.00 78.91  ? 201 HIS C CB    1 
ATOM   5953 C  CG    . HIS C 1 227 ? 134.072 141.312 174.173 1.00 80.18  ? 201 HIS C CG    1 
ATOM   5954 N  ND1   . HIS C 1 227 ? 133.900 140.272 175.061 1.00 78.96  ? 201 HIS C ND1   1 
ATOM   5955 C  CD2   . HIS C 1 227 ? 133.685 140.840 172.964 1.00 80.09  ? 201 HIS C CD2   1 
ATOM   5956 C  CE1   . HIS C 1 227 ? 133.435 139.217 174.417 1.00 78.40  ? 201 HIS C CE1   1 
ATOM   5957 N  NE2   . HIS C 1 227 ? 133.292 139.537 173.143 1.00 79.66  ? 201 HIS C NE2   1 
ATOM   5958 N  N     . GLY C 1 228 ? 134.908 145.373 175.927 1.00 90.77  ? 202 GLY C N     1 
ATOM   5959 C  CA    . GLY C 1 228 ? 135.776 146.524 176.105 1.00 87.84  ? 202 GLY C CA    1 
ATOM   5960 C  C     . GLY C 1 228 ? 135.028 147.835 176.205 1.00 88.12  ? 202 GLY C C     1 
ATOM   5961 O  O     . GLY C 1 228 ? 133.973 147.920 176.841 1.00 88.18  ? 202 GLY C O     1 
ATOM   5962 N  N     . ILE C 1 229 ? 135.586 148.867 175.569 1.00 91.18  ? 203 ILE C N     1 
ATOM   5963 C  CA    . ILE C 1 229 ? 135.090 150.228 175.729 1.00 90.86  ? 203 ILE C CA    1 
ATOM   5964 C  C     . ILE C 1 229 ? 133.847 150.429 174.873 1.00 89.82  ? 203 ILE C C     1 
ATOM   5965 O  O     . ILE C 1 229 ? 133.837 150.114 173.676 1.00 86.66  ? 203 ILE C O     1 
ATOM   5966 C  CB    . ILE C 1 229 ? 136.186 151.242 175.364 1.00 91.05  ? 203 ILE C CB    1 
ATOM   5967 C  CG1   . ILE C 1 229 ? 137.420 151.039 176.246 1.00 89.88  ? 203 ILE C CG1   1 
ATOM   5968 C  CG2   . ILE C 1 229 ? 135.680 152.674 175.501 1.00 87.74  ? 203 ILE C CG2   1 
ATOM   5969 C  CD1   . ILE C 1 229 ? 138.581 151.936 175.883 1.00 88.88  ? 203 ILE C CD1   1 
ATOM   5970 N  N     . SER C 1 230 ? 132.788 150.954 175.488 1.00 91.58  ? 204 SER C N     1 
ATOM   5971 C  CA    . SER C 1 230 ? 131.563 151.307 174.783 1.00 90.68  ? 204 SER C CA    1 
ATOM   5972 C  C     . SER C 1 230 ? 131.466 152.782 174.430 1.00 89.90  ? 204 SER C C     1 
ATOM   5973 O  O     . SER C 1 230 ? 130.708 153.136 173.524 1.00 90.99  ? 204 SER C O     1 
ATOM   5974 C  CB    . SER C 1 230 ? 130.338 150.924 175.621 1.00 90.78  ? 204 SER C CB    1 
ATOM   5975 O  OG    . SER C 1 230 ? 130.036 151.926 176.576 1.00 90.90  ? 204 SER C OG    1 
ATOM   5976 N  N     . GLY C 1 231 ? 132.209 153.649 175.119 1.00 89.56  ? 205 GLY C N     1 
ATOM   5977 C  CA    . GLY C 1 231 ? 132.105 155.076 174.876 1.00 91.28  ? 205 GLY C CA    1 
ATOM   5978 C  C     . GLY C 1 231 ? 132.780 155.546 173.605 1.00 91.81  ? 205 GLY C C     1 
ATOM   5979 O  O     . GLY C 1 231 ? 132.453 156.629 173.109 1.00 91.97  ? 205 GLY C O     1 
ATOM   5980 N  N     . LEU C 1 232 ? 133.718 154.766 173.072 1.00 85.81  ? 206 LEU C N     1 
ATOM   5981 C  CA    . LEU C 1 232 ? 134.428 155.137 171.855 1.00 85.87  ? 206 LEU C CA    1 
ATOM   5982 C  C     . LEU C 1 232 ? 134.233 154.138 170.728 1.00 84.94  ? 206 LEU C C     1 
ATOM   5983 O  O     . LEU C 1 232 ? 133.950 154.540 169.594 1.00 87.40  ? 206 LEU C O     1 
ATOM   5984 C  CB    . LEU C 1 232 ? 135.927 155.308 172.149 1.00 85.59  ? 206 LEU C CB    1 
ATOM   5985 C  CG    . LEU C 1 232 ? 136.659 156.322 171.270 1.00 86.29  ? 206 LEU C CG    1 
ATOM   5986 C  CD1   . LEU C 1 232 ? 136.011 157.695 171.381 1.00 85.44  ? 206 LEU C CD1   1 
ATOM   5987 C  CD2   . LEU C 1 232 ? 138.132 156.390 171.638 1.00 85.60  ? 206 LEU C CD2   1 
ATOM   5988 N  N     . ILE C 1 233 ? 134.395 152.842 171.002 1.00 76.51  ? 207 ILE C N     1 
ATOM   5989 C  CA    . ILE C 1 233 ? 134.286 151.837 169.948 1.00 76.76  ? 207 ILE C CA    1 
ATOM   5990 C  C     . ILE C 1 233 ? 132.830 151.637 169.545 1.00 77.49  ? 207 ILE C C     1 
ATOM   5991 O  O     . ILE C 1 233 ? 132.490 151.671 168.356 1.00 75.69  ? 207 ILE C O     1 
ATOM   5992 C  CB    . ILE C 1 233 ? 134.940 150.519 170.406 1.00 78.64  ? 207 ILE C CB    1 
ATOM   5993 C  CG1   . ILE C 1 233 ? 136.463 150.674 170.468 1.00 78.94  ? 207 ILE C CG1   1 
ATOM   5994 C  CG2   . ILE C 1 233 ? 134.556 149.365 169.486 1.00 76.20  ? 207 ILE C CG2   1 
ATOM   5995 C  CD1   . ILE C 1 233 ? 137.134 150.805 169.114 1.00 77.70  ? 207 ILE C CD1   1 
ATOM   5996 N  N     . HIS C 1 234 ? 131.943 151.450 170.525 1.00 76.33  ? 208 HIS C N     1 
ATOM   5997 C  CA    . HIS C 1 234 ? 130.544 151.167 170.227 1.00 71.87  ? 208 HIS C CA    1 
ATOM   5998 C  C     . HIS C 1 234 ? 129.791 152.404 169.755 1.00 72.44  ? 208 HIS C C     1 
ATOM   5999 O  O     . HIS C 1 234 ? 128.829 152.280 168.989 1.00 71.99  ? 208 HIS C O     1 
ATOM   6000 C  CB    . HIS C 1 234 ? 129.856 150.571 171.456 1.00 71.47  ? 208 HIS C CB    1 
ATOM   6001 C  CG    . HIS C 1 234 ? 128.510 149.982 171.169 1.00 76.16  ? 208 HIS C CG    1 
ATOM   6002 N  ND1   . HIS C 1 234 ? 127.361 150.741 171.120 1.00 75.68  ? 208 HIS C ND1   1 
ATOM   6003 C  CD2   . HIS C 1 234 ? 128.130 148.707 170.914 1.00 76.02  ? 208 HIS C CD2   1 
ATOM   6004 C  CE1   . HIS C 1 234 ? 126.331 149.959 170.848 1.00 73.41  ? 208 HIS C CE1   1 
ATOM   6005 N  NE2   . HIS C 1 234 ? 126.771 148.721 170.719 1.00 76.46  ? 208 HIS C NE2   1 
ATOM   6006 N  N     . GLU C 1 235 ? 130.202 153.594 170.199 1.00 75.71  ? 209 GLU C N     1 
ATOM   6007 C  CA    . GLU C 1 235 ? 129.533 154.819 169.772 1.00 71.30  ? 209 GLU C CA    1 
ATOM   6008 C  C     . GLU C 1 235 ? 129.881 155.165 168.330 1.00 70.25  ? 209 GLU C C     1 
ATOM   6009 O  O     . GLU C 1 235 ? 129.033 155.653 167.576 1.00 71.64  ? 209 GLU C O     1 
ATOM   6010 C  CB    . GLU C 1 235 ? 129.900 155.972 170.709 1.00 73.60  ? 209 GLU C CB    1 
ATOM   6011 C  CG    . GLU C 1 235 ? 129.108 156.001 172.006 1.00 76.74  ? 209 GLU C CG    1 
ATOM   6012 C  CD    . GLU C 1 235 ? 127.626 155.757 171.796 1.00 77.58  ? 209 GLU C CD    1 
ATOM   6013 O  OE1   . GLU C 1 235 ? 126.986 156.546 171.069 1.00 76.13  ? 209 GLU C OE1   1 
ATOM   6014 O  OE2   . GLU C 1 235 ? 127.098 154.775 172.361 1.00 76.16  ? 209 GLU C OE2   1 
ATOM   6015 N  N     . MET C 1 236 ? 131.131 154.921 167.930 1.00 65.24  ? 210 MET C N     1 
ATOM   6016 C  CA    . MET C 1 236 ? 131.543 155.195 166.558 1.00 63.38  ? 210 MET C CA    1 
ATOM   6017 C  C     . MET C 1 236 ? 131.073 154.123 165.585 1.00 65.35  ? 210 MET C C     1 
ATOM   6018 O  O     . MET C 1 236 ? 131.163 154.325 164.370 1.00 65.37  ? 210 MET C O     1 
ATOM   6019 C  CB    . MET C 1 236 ? 133.064 155.333 166.480 1.00 64.01  ? 210 MET C CB    1 
ATOM   6020 C  CG    . MET C 1 236 ? 133.557 156.771 166.473 1.00 68.29  ? 210 MET C CG    1 
ATOM   6021 S  SD    . MET C 1 236 ? 133.662 157.452 164.806 1.00 83.73  ? 210 MET C SD    1 
ATOM   6022 C  CE    . MET C 1 236 ? 133.192 159.156 165.101 1.00 67.26  ? 210 MET C CE    1 
ATOM   6023 N  N     . MET C 1 237 ? 130.576 152.992 166.089 1.00 57.41  ? 211 MET C N     1 
ATOM   6024 C  CA    . MET C 1 237 ? 130.083 151.942 165.205 1.00 50.92  ? 211 MET C CA    1 
ATOM   6025 C  C     . MET C 1 237 ? 128.717 152.289 164.630 1.00 51.23  ? 211 MET C C     1 
ATOM   6026 O  O     . MET C 1 237 ? 128.316 151.717 163.612 1.00 53.19  ? 211 MET C O     1 
ATOM   6027 C  CB    . MET C 1 237 ? 130.022 150.612 165.957 1.00 48.23  ? 211 MET C CB    1 
ATOM   6028 C  CG    . MET C 1 237 ? 131.118 149.634 165.577 1.00 50.12  ? 211 MET C CG    1 
ATOM   6029 S  SD    . MET C 1 237 ? 131.396 148.377 166.836 1.00 61.38  ? 211 MET C SD    1 
ATOM   6030 C  CE    . MET C 1 237 ? 129.809 147.556 166.840 1.00 49.12  ? 211 MET C CE    1 
ATOM   6031 N  N     . LYS C 1 238 ? 127.996 153.222 165.262 1.00 44.03  ? 212 LYS C N     1 
ATOM   6032 C  CA    . LYS C 1 238 ? 126.676 153.637 164.792 1.00 39.95  ? 212 LYS C CA    1 
ATOM   6033 C  C     . LYS C 1 238 ? 126.722 154.337 163.440 1.00 43.78  ? 212 LYS C C     1 
ATOM   6034 O  O     . LYS C 1 238 ? 125.737 154.286 162.698 1.00 48.23  ? 212 LYS C O     1 
ATOM   6035 C  CB    . LYS C 1 238 ? 126.011 154.568 165.809 1.00 47.19  ? 212 LYS C CB    1 
ATOM   6036 C  CG    . LYS C 1 238 ? 125.072 153.904 166.813 1.00 44.59  ? 212 LYS C CG    1 
ATOM   6037 C  CD    . LYS C 1 238 ? 125.785 152.959 167.758 1.00 46.69  ? 212 LYS C CD    1 
ATOM   6038 C  CE    . LYS C 1 238 ? 124.965 152.739 169.016 1.00 50.21  ? 212 LYS C CE    1 
ATOM   6039 N  NZ    . LYS C 1 238 ? 124.689 154.016 169.731 1.00 52.72  ? 212 LYS C NZ    1 
ATOM   6040 N  N     . TYR C 1 239 ? 127.839 154.986 163.104 1.00 42.82  ? 213 TYR C N     1 
ATOM   6041 C  CA    . TYR C 1 239 ? 127.977 155.660 161.819 1.00 39.75  ? 213 TYR C CA    1 
ATOM   6042 C  C     . TYR C 1 239 ? 128.163 154.690 160.660 1.00 40.74  ? 213 TYR C C     1 
ATOM   6043 O  O     . TYR C 1 239 ? 128.063 155.110 159.503 1.00 43.09  ? 213 TYR C O     1 
ATOM   6044 C  CB    . TYR C 1 239 ? 129.145 156.645 161.872 1.00 43.98  ? 213 TYR C CB    1 
ATOM   6045 C  CG    . TYR C 1 239 ? 128.904 157.800 162.815 1.00 41.89  ? 213 TYR C CG    1 
ATOM   6046 C  CD1   . TYR C 1 239 ? 129.359 157.759 164.128 1.00 42.78  ? 213 TYR C CD1   1 
ATOM   6047 C  CD2   . TYR C 1 239 ? 128.208 158.927 162.395 1.00 37.92  ? 213 TYR C CD2   1 
ATOM   6048 C  CE1   . TYR C 1 239 ? 129.135 158.813 164.994 1.00 44.47  ? 213 TYR C CE1   1 
ATOM   6049 C  CE2   . TYR C 1 239 ? 127.979 159.985 163.253 1.00 47.47  ? 213 TYR C CE2   1 
ATOM   6050 C  CZ    . TYR C 1 239 ? 128.444 159.923 164.551 1.00 49.80  ? 213 TYR C CZ    1 
ATOM   6051 O  OH    . TYR C 1 239 ? 128.217 160.975 165.407 1.00 47.83  ? 213 TYR C OH    1 
ATOM   6052 N  N     . ASN C 1 240 ? 128.439 153.426 160.941 1.00 34.47  ? 214 ASN C N     1 
ATOM   6053 C  CA    . ASN C 1 240 ? 128.467 152.399 159.913 1.00 32.14  ? 214 ASN C CA    1 
ATOM   6054 C  C     . ASN C 1 240 ? 127.038 152.025 159.531 1.00 30.13  ? 214 ASN C C     1 
ATOM   6055 O  O     . ASN C 1 240 ? 126.223 151.764 160.422 1.00 34.98  ? 214 ASN C O     1 
ATOM   6056 C  CB    . ASN C 1 240 ? 129.221 151.177 160.425 1.00 31.66  ? 214 ASN C CB    1 
ATOM   6057 C  CG    . ASN C 1 240 ? 129.755 150.306 159.313 1.00 30.18  ? 214 ASN C CG    1 
ATOM   6058 O  OD1   . ASN C 1 240 ? 129.508 150.555 158.138 1.00 38.83  ? 214 ASN C OD1   1 
ATOM   6059 N  ND2   . ASN C 1 240 ? 130.495 149.272 159.681 1.00 27.94  ? 214 ASN C ND2   1 
ATOM   6060 N  N     . PRO C 1 241 ? 126.641 152.036 158.227 1.00 35.49  ? 215 PRO C N     1 
ATOM   6061 C  CA    . PRO C 1 241 ? 125.294 151.547 157.789 1.00 35.18  ? 215 PRO C CA    1 
ATOM   6062 C  C     . PRO C 1 241 ? 125.147 150.059 158.077 1.00 32.34  ? 215 PRO C C     1 
ATOM   6063 O  O     . PRO C 1 241 ? 124.006 149.597 158.273 1.00 37.32  ? 215 PRO C O     1 
ATOM   6064 C  CB    . PRO C 1 241 ? 125.256 151.872 156.303 1.00 33.84  ? 215 PRO C CB    1 
ATOM   6065 C  CG    . PRO C 1 241 ? 126.218 153.028 156.154 1.00 31.33  ? 215 PRO C CG    1 
ATOM   6066 C  CD    . PRO C 1 241 ? 127.345 152.633 157.035 1.00 32.27  ? 215 PRO C CD    1 
ATOM   6067 N  N     . VAL C 1 242 ? 126.264 149.344 158.150 1.00 31.98  ? 216 VAL C N     1 
ATOM   6068 C  CA    . VAL C 1 242 ? 126.266 147.880 158.438 1.00 27.09  ? 216 VAL C CA    1 
ATOM   6069 C  C     . VAL C 1 242 ? 125.671 147.687 159.841 1.00 28.78  ? 216 VAL C C     1 
ATOM   6070 O  O     . VAL C 1 242 ? 124.961 146.692 160.045 1.00 39.02  ? 216 VAL C O     1 
ATOM   6071 C  CB    . VAL C 1 242 ? 127.657 147.235 158.288 1.00 27.74  ? 216 VAL C CB    1 
ATOM   6072 C  CG1   . VAL C 1 242 ? 127.621 145.730 158.505 1.00 31.63  ? 216 VAL C CG1   1 
ATOM   6073 C  CG2   . VAL C 1 242 ? 128.288 147.563 156.942 1.00 23.28  ? 216 VAL C CG2   1 
ATOM   6074 N  N     . TYR C 1 243 ? 125.971 148.591 160.774 1.00 28.29  ? 217 TYR C N     1 
ATOM   6075 C  CA    . TYR C 1 243 ? 125.452 148.378 162.138 1.00 31.87  ? 217 TYR C CA    1 
ATOM   6076 C  C     . TYR C 1 243 ? 123.936 148.364 162.102 1.00 31.74  ? 217 TYR C C     1 
ATOM   6077 O  O     . TYR C 1 243 ? 123.343 147.444 162.672 1.00 36.79  ? 217 TYR C O     1 
ATOM   6078 C  CB    . TYR C 1 243 ? 125.918 149.556 162.999 1.00 31.04  ? 217 TYR C CB    1 
ATOM   6079 C  CG    . TYR C 1 243 ? 125.446 149.522 164.445 1.00 32.67  ? 217 TYR C CG    1 
ATOM   6080 C  CD1   . TYR C 1 243 ? 124.175 149.955 164.799 1.00 31.14  ? 217 TYR C CD1   1 
ATOM   6081 C  CD2   . TYR C 1 243 ? 126.274 149.051 165.456 1.00 29.91  ? 217 TYR C CD2   1 
ATOM   6082 C  CE1   . TYR C 1 243 ? 123.735 149.906 166.108 1.00 38.46  ? 217 TYR C CE1   1 
ATOM   6083 C  CE2   . TYR C 1 243 ? 125.848 149.005 166.771 1.00 33.83  ? 217 TYR C CE2   1 
ATOM   6084 C  CZ    . TYR C 1 243 ? 124.576 149.437 167.098 1.00 39.96  ? 217 TYR C CZ    1 
ATOM   6085 O  OH    . TYR C 1 243 ? 124.142 149.399 168.389 1.00 44.74  ? 217 TYR C OH    1 
ATOM   6086 N  N     . PHE C 1 244 ? 123.325 149.301 161.378 1.00 34.56  ? 218 PHE C N     1 
ATOM   6087 C  CA    . PHE C 1 244 ? 121.847 149.337 161.268 1.00 22.00  ? 218 PHE C CA    1 
ATOM   6088 C  C     . PHE C 1 244 ? 121.325 148.101 160.561 1.00 26.54  ? 218 PHE C C     1 
ATOM   6089 O  O     . PHE C 1 244 ? 120.346 147.527 161.040 1.00 33.28  ? 218 PHE C O     1 
ATOM   6090 C  CB    . PHE C 1 244 ? 121.449 150.609 160.515 1.00 29.70  ? 218 PHE C CB    1 
ATOM   6091 C  CG    . PHE C 1 244 ? 119.978 150.701 160.140 1.00 31.55  ? 218 PHE C CG    1 
ATOM   6092 C  CD1   . PHE C 1 244 ? 119.006 150.909 161.112 1.00 30.30  ? 218 PHE C CD1   1 
ATOM   6093 C  CD2   . PHE C 1 244 ? 119.571 150.573 158.819 1.00 27.04  ? 218 PHE C CD2   1 
ATOM   6094 C  CE1   . PHE C 1 244 ? 117.668 150.980 160.768 1.00 31.51  ? 218 PHE C CE1   1 
ATOM   6095 C  CE2   . PHE C 1 244 ? 118.230 150.649 158.482 1.00 32.58  ? 218 PHE C CE2   1 
ATOM   6096 C  CZ    . PHE C 1 244 ? 117.284 150.851 159.456 1.00 33.26  ? 218 PHE C CZ    1 
ATOM   6097 N  N     . ILE C 1 245 ? 121.963 147.696 159.462 1.00 25.37  ? 219 ILE C N     1 
ATOM   6098 C  CA    . ILE C 1 245 ? 121.404 146.545 158.701 1.00 25.24  ? 219 ILE C CA    1 
ATOM   6099 C  C     . ILE C 1 245 ? 121.460 145.251 159.529 1.00 26.13  ? 219 ILE C C     1 
ATOM   6100 O  O     . ILE C 1 245 ? 120.437 144.556 159.581 1.00 37.06  ? 219 ILE C O     1 
ATOM   6101 C  CB    . ILE C 1 245 ? 122.107 146.395 157.338 1.00 28.98  ? 219 ILE C CB    1 
ATOM   6102 C  CG1   . ILE C 1 245 ? 122.047 147.688 156.533 1.00 36.02  ? 219 ILE C CG1   1 
ATOM   6103 C  CG2   . ILE C 1 245 ? 121.530 145.226 156.542 1.00 23.52  ? 219 ILE C CG2   1 
ATOM   6104 C  CD1   . ILE C 1 245 ? 122.997 147.724 155.351 1.00 29.74  ? 219 ILE C CD1   1 
ATOM   6105 N  N     . ALA C 1 246 ? 122.586 144.976 160.196 1.00 28.27  ? 220 ALA C N     1 
ATOM   6106 C  CA    . ALA C 1 246 ? 122.683 143.759 161.029 1.00 30.31  ? 220 ALA C CA    1 
ATOM   6107 C  C     . ALA C 1 246 ? 121.717 143.827 162.209 1.00 32.00  ? 220 ALA C C     1 
ATOM   6108 O  O     . ALA C 1 246 ? 121.011 142.844 162.473 1.00 40.15  ? 220 ALA C O     1 
ATOM   6109 C  CB    . ALA C 1 246 ? 124.108 143.550 161.482 1.00 50.00  ? 220 ALA C CB    1 
ATOM   6110 N  N     . GLU C 1 247 ? 121.663 144.980 162.867 1.00 31.20  ? 221 GLU C N     1 
ATOM   6111 C  CA    . GLU C 1 247 ? 120.778 145.145 164.046 1.00 28.03  ? 221 GLU C CA    1 
ATOM   6112 C  C     . GLU C 1 247 ? 119.303 145.036 163.645 1.00 26.02  ? 221 GLU C C     1 
ATOM   6113 O  O     . GLU C 1 247 ? 118.543 144.401 164.391 1.00 29.84  ? 221 GLU C O     1 
ATOM   6114 C  CB    . GLU C 1 247 ? 121.190 146.441 164.744 1.00 35.30  ? 221 GLU C CB    1 
ATOM   6115 C  CG    . GLU C 1 247 ? 122.460 146.292 165.576 1.00 31.17  ? 221 GLU C CG    1 
ATOM   6116 C  CD    . GLU C 1 247 ? 122.539 145.003 166.374 1.00 40.98  ? 221 GLU C CD    1 
ATOM   6117 O  OE1   . GLU C 1 247 ? 123.296 144.092 165.983 1.00 35.15  ? 221 GLU C OE1   1 
ATOM   6118 O  OE2   . GLU C 1 247 ? 121.835 144.914 167.398 1.00 44.50  ? 221 GLU C OE2   1 
ATOM   6119 N  N     . SER C 1 248 ? 118.932 145.646 162.523 1.00 33.44  ? 222 SER C N     1 
ATOM   6120 C  CA    . SER C 1 248 ? 117.533 145.630 162.036 1.00 23.65  ? 222 SER C CA    1 
ATOM   6121 C  C     . SER C 1 248 ? 117.073 144.216 161.675 1.00 29.22  ? 222 SER C C     1 
ATOM   6122 O  O     . SER C 1 248 ? 115.938 143.879 162.036 1.00 38.58  ? 222 SER C O     1 
ATOM   6123 C  CB    . SER C 1 248 ? 117.407 146.562 160.874 1.00 22.57  ? 222 SER C CB    1 
ATOM   6124 O  OG    . SER C 1 248 ? 118.039 146.037 159.717 1.00 33.90  ? 222 SER C OG    1 
ATOM   6125 N  N     . TYR C 1 249 ? 117.915 143.431 160.997 1.00 28.63  ? 223 TYR C N     1 
ATOM   6126 C  CA    . TYR C 1 249 ? 117.587 142.023 160.649 1.00 21.74  ? 223 TYR C CA    1 
ATOM   6127 C  C     . TYR C 1 249 ? 117.444 141.201 161.917 1.00 29.37  ? 223 TYR C C     1 
ATOM   6128 O  O     . TYR C 1 249 ? 116.501 140.417 162.004 1.00 37.02  ? 223 TYR C O     1 
ATOM   6129 C  CB    . TYR C 1 249 ? 118.703 141.446 159.778 1.00 29.46  ? 223 TYR C CB    1 
ATOM   6130 C  CG    . TYR C 1 249 ? 118.695 141.726 158.281 1.00 29.55  ? 223 TYR C CG    1 
ATOM   6131 C  CD1   . TYR C 1 249 ? 118.454 142.996 157.776 1.00 28.13  ? 223 TYR C CD1   1 
ATOM   6132 C  CD2   . TYR C 1 249 ? 118.966 140.712 157.374 1.00 32.01  ? 223 TYR C CD2   1 
ATOM   6133 C  CE1   . TYR C 1 249 ? 118.475 143.248 156.415 1.00 28.49  ? 223 TYR C CE1   1 
ATOM   6134 C  CE2   . TYR C 1 249 ? 118.988 140.949 156.011 1.00 30.35  ? 223 TYR C CE2   1 
ATOM   6135 C  CZ    . TYR C 1 249 ? 118.742 142.220 155.531 1.00 32.33  ? 223 TYR C CZ    1 
ATOM   6136 O  OH    . TYR C 1 249 ? 118.766 142.453 154.191 1.00 36.17  ? 223 TYR C OH    1 
ATOM   6137 N  N     . ARG C 1 250 ? 118.330 141.402 162.891 1.00 30.45  ? 224 ARG C N     1 
ATOM   6138 C  CA    . ARG C 1 250 ? 118.297 140.678 164.186 1.00 21.33  ? 224 ARG C CA    1 
ATOM   6139 C  C     . ARG C 1 250 ? 117.013 141.021 164.950 1.00 19.67  ? 224 ARG C C     1 
ATOM   6140 O  O     . ARG C 1 250 ? 116.460 140.133 165.606 1.00 28.51  ? 224 ARG C O     1 
ATOM   6141 C  CB    . ARG C 1 250 ? 119.592 140.990 164.942 1.00 27.96  ? 224 ARG C CB    1 
ATOM   6142 C  CG    . ARG C 1 250 ? 120.764 140.111 164.534 1.00 27.73  ? 224 ARG C CG    1 
ATOM   6143 C  CD    . ARG C 1 250 ? 121.971 140.327 165.423 1.00 26.32  ? 224 ARG C CD    1 
ATOM   6144 N  NE    . ARG C 1 250 ? 123.177 139.729 164.841 1.00 29.37  ? 224 ARG C NE    1 
ATOM   6145 C  CZ    . ARG C 1 250 ? 124.323 140.366 164.670 1.00 31.40  ? 224 ARG C CZ    1 
ATOM   6146 N  NH1   . ARG C 1 250 ? 124.393 141.667 164.866 1.00 30.04  ? 224 ARG C NH1   1 
ATOM   6147 N  NH2   . ARG C 1 250 ? 125.396 139.698 164.301 1.00 20.72  ? 224 ARG C NH2   1 
ATOM   6148 N  N     . ALA C 1 251 ? 116.598 142.280 164.911 1.00 38.60  ? 225 ALA C N     1 
ATOM   6149 C  CA    . ALA C 1 251 ? 115.371 142.698 165.615 1.00 28.45  ? 225 ALA C CA    1 
ATOM   6150 C  C     . ALA C 1 251 ? 114.161 142.192 164.837 1.00 35.23  ? 225 ALA C C     1 
ATOM   6151 O  O     . ALA C 1 251 ? 113.158 141.836 165.476 1.00 44.79  ? 225 ALA C O     1 
ATOM   6152 C  CB    . ALA C 1 251 ? 115.350 144.191 165.751 1.00 31.35  ? 225 ALA C CB    1 
ATOM   6153 N  N     . ALA C 1 252 ? 114.264 142.126 163.505 1.00 35.90  ? 226 ALA C N     1 
ATOM   6154 C  CA    . ALA C 1 252 ? 113.134 141.587 162.758 1.00 26.89  ? 226 ALA C CA    1 
ATOM   6155 C  C     . ALA C 1 252 ? 113.027 140.074 162.914 1.00 28.76  ? 226 ALA C C     1 
ATOM   6156 O  O     . ALA C 1 252 ? 111.921 139.535 163.032 1.00 41.17  ? 226 ALA C O     1 
ATOM   6157 C  CB    . ALA C 1 252 ? 113.251 141.965 161.283 1.00 27.50  ? 226 ALA C CB    1 
ATOM   6158 N  N     . ILE C 1 253 ? 114.156 139.373 162.925 1.00 30.69  ? 227 ILE C N     1 
ATOM   6159 C  CA    . ILE C 1 253 ? 114.161 137.917 162.873 1.00 23.21  ? 227 ILE C CA    1 
ATOM   6160 C  C     . ILE C 1 253 ? 114.297 137.293 164.258 1.00 26.79  ? 227 ILE C C     1 
ATOM   6161 O  O     . ILE C 1 253 ? 113.514 136.415 164.621 1.00 40.30  ? 227 ILE C O     1 
ATOM   6162 C  CB    . ILE C 1 253 ? 115.275 137.429 161.922 1.00 30.04  ? 227 ILE C CB    1 
ATOM   6163 C  CG1   . ILE C 1 253 ? 115.010 137.933 160.502 1.00 26.74  ? 227 ILE C CG1   1 
ATOM   6164 C  CG2   . ILE C 1 253 ? 115.377 135.912 161.930 1.00 30.17  ? 227 ILE C CG2   1 
ATOM   6165 C  CD1   . ILE C 1 253 ? 116.192 137.815 159.572 1.00 27.02  ? 227 ILE C CD1   1 
ATOM   6166 N  N     . LEU C 1 254 ? 115.267 137.738 165.057 1.00 34.72  ? 228 LEU C N     1 
ATOM   6167 C  CA    . LEU C 1 254 ? 115.584 137.056 166.311 1.00 29.22  ? 228 LEU C CA    1 
ATOM   6168 C  C     . LEU C 1 254 ? 114.835 137.641 167.506 1.00 33.12  ? 228 LEU C C     1 
ATOM   6169 O  O     . LEU C 1 254 ? 114.137 136.916 168.222 1.00 40.93  ? 228 LEU C O     1 
ATOM   6170 C  CB    . LEU C 1 254 ? 117.093 137.106 166.569 1.00 31.48  ? 228 LEU C CB    1 
ATOM   6171 C  CG    . LEU C 1 254 ? 118.003 136.407 165.565 1.00 31.41  ? 228 LEU C CG    1 
ATOM   6172 C  CD1   . LEU C 1 254 ? 119.447 136.797 165.807 1.00 27.36  ? 228 LEU C CD1   1 
ATOM   6173 C  CD2   . LEU C 1 254 ? 117.833 134.904 165.635 1.00 29.24  ? 228 LEU C CD2   1 
ATOM   6174 N  N     . TYR C 1 255 ? 114.977 138.946 167.736 1.00 41.33  ? 229 TYR C N     1 
ATOM   6175 C  CA    . TYR C 1 255 ? 114.532 139.544 168.989 1.00 32.97  ? 229 TYR C CA    1 
ATOM   6176 C  C     . TYR C 1 255 ? 113.036 139.819 169.034 1.00 39.09  ? 229 TYR C C     1 
ATOM   6177 O  O     . TYR C 1 255 ? 112.506 140.028 170.133 1.00 46.56  ? 229 TYR C O     1 
ATOM   6178 C  CB    . TYR C 1 255 ? 115.298 140.842 169.250 1.00 36.03  ? 229 TYR C CB    1 
ATOM   6179 C  CG    . TYR C 1 255 ? 116.798 140.671 169.295 1.00 36.51  ? 229 TYR C CG    1 
ATOM   6180 C  CD1   . TYR C 1 255 ? 117.372 139.571 169.922 1.00 42.36  ? 229 TYR C CD1   1 
ATOM   6181 C  CD2   . TYR C 1 255 ? 117.639 141.609 168.713 1.00 35.30  ? 229 TYR C CD2   1 
ATOM   6182 C  CE1   . TYR C 1 255 ? 118.745 139.409 169.964 1.00 44.66  ? 229 TYR C CE1   1 
ATOM   6183 C  CE2   . TYR C 1 255 ? 119.011 141.458 168.751 1.00 36.43  ? 229 TYR C CE2   1 
ATOM   6184 C  CZ    . TYR C 1 255 ? 119.557 140.357 169.377 1.00 42.85  ? 229 TYR C CZ    1 
ATOM   6185 O  OH    . TYR C 1 255 ? 120.922 140.205 169.417 1.00 52.69  ? 229 TYR C OH    1 
ATOM   6186 N  N     . HIS C 1 256 ? 112.365 139.821 167.878 1.00 41.92  ? 230 HIS C N     1 
ATOM   6187 C  CA    . HIS C 1 256 ? 110.922 140.055 167.730 1.00 35.54  ? 230 HIS C CA    1 
ATOM   6188 C  C     . HIS C 1 256 ? 110.504 141.402 168.324 1.00 42.70  ? 230 HIS C C     1 
ATOM   6189 O  O     . HIS C 1 256 ? 109.643 141.493 169.199 1.00 44.51  ? 230 HIS C O     1 
ATOM   6190 C  CB    . HIS C 1 256 ? 110.102 138.909 168.336 1.00 36.93  ? 230 HIS C CB    1 
ATOM   6191 C  CG    . HIS C 1 256 ? 110.535 137.550 167.882 1.00 40.85  ? 230 HIS C CG    1 
ATOM   6192 N  ND1   . HIS C 1 256 ? 110.922 136.563 168.762 1.00 43.60  ? 230 HIS C ND1   1 
ATOM   6193 C  CD2   . HIS C 1 256 ? 110.638 137.014 166.644 1.00 41.49  ? 230 HIS C CD2   1 
ATOM   6194 C  CE1   . HIS C 1 256 ? 111.248 135.476 168.084 1.00 46.77  ? 230 HIS C CE1   1 
ATOM   6195 N  NE2   . HIS C 1 256 ? 111.084 135.724 166.797 1.00 45.70  ? 230 HIS C NE2   1 
ATOM   6196 N  N     . GLU C 1 257 ? 111.142 142.458 167.828 1.00 41.32  ? 231 GLU C N     1 
ATOM   6197 C  CA    . GLU C 1 257 ? 110.834 143.813 168.257 1.00 33.75  ? 231 GLU C CA    1 
ATOM   6198 C  C     . GLU C 1 257 ? 110.781 144.723 167.041 1.00 38.20  ? 231 GLU C C     1 
ATOM   6199 O  O     . GLU C 1 257 ? 111.395 144.449 166.007 1.00 40.12  ? 231 GLU C O     1 
ATOM   6200 C  CB    . GLU C 1 257 ? 111.866 144.338 169.262 1.00 38.53  ? 231 GLU C CB    1 
ATOM   6201 C  CG    . GLU C 1 257 ? 113.295 143.958 168.931 1.00 40.94  ? 231 GLU C CG    1 
ATOM   6202 C  CD    . GLU C 1 257 ? 114.307 144.926 169.507 1.00 51.45  ? 231 GLU C CD    1 
ATOM   6203 O  OE1   . GLU C 1 257 ? 114.989 144.558 170.488 1.00 49.67  ? 231 GLU C OE1   1 
ATOM   6204 O  OE2   . GLU C 1 257 ? 114.423 146.053 168.981 1.00 51.16  ? 231 GLU C OE2   1 
ATOM   6205 N  N     . TRP C 1 258 ? 110.025 145.809 167.173 1.00 41.29  ? 232 TRP C N     1 
ATOM   6206 C  CA    . TRP C 1 258 ? 109.992 146.850 166.152 1.00 35.08  ? 232 TRP C CA    1 
ATOM   6207 C  C     . TRP C 1 258 ? 111.225 147.721 166.333 1.00 35.27  ? 232 TRP C C     1 
ATOM   6208 O  O     . TRP C 1 258 ? 111.354 148.429 167.337 1.00 45.41  ? 232 TRP C O     1 
ATOM   6209 C  CB    . TRP C 1 258 ? 108.709 147.670 166.251 1.00 31.87  ? 232 TRP C CB    1 
ATOM   6210 C  CG    . TRP C 1 258 ? 107.459 146.849 166.258 1.00 41.03  ? 232 TRP C CG    1 
ATOM   6211 C  CD1   . TRP C 1 258 ? 106.639 146.614 167.320 1.00 39.26  ? 232 TRP C CD1   1 
ATOM   6212 C  CD2   . TRP C 1 258 ? 106.882 146.156 165.144 1.00 40.77  ? 232 TRP C CD2   1 
ATOM   6213 N  NE1   . TRP C 1 258 ? 105.587 145.816 166.939 1.00 37.13  ? 232 TRP C NE1   1 
ATOM   6214 C  CE2   . TRP C 1 258 ? 105.712 145.522 165.608 1.00 37.51  ? 232 TRP C CE2   1 
ATOM   6215 C  CE3   . TRP C 1 258 ? 107.239 146.011 163.801 1.00 33.73  ? 232 TRP C CE3   1 
ATOM   6216 C  CZ2   . TRP C 1 258 ? 104.901 144.753 164.777 1.00 34.51  ? 232 TRP C CZ2   1 
ATOM   6217 C  CZ3   . TRP C 1 258 ? 106.436 145.250 162.980 1.00 33.96  ? 232 TRP C CZ3   1 
ATOM   6218 C  CH2   . TRP C 1 258 ? 105.279 144.630 163.469 1.00 36.29  ? 232 TRP C CH2   1 
ATOM   6219 N  N     . TYR C 1 259 ? 112.136 147.667 165.361 1.00 33.76  ? 233 TYR C N     1 
ATOM   6220 C  CA    . TYR C 1 259 ? 113.440 148.299 165.524 1.00 37.51  ? 233 TYR C CA    1 
ATOM   6221 C  C     . TYR C 1 259 ? 113.355 149.816 165.385 1.00 37.87  ? 233 TYR C C     1 
ATOM   6222 O  O     . TYR C 1 259 ? 114.236 150.537 165.865 1.00 39.88  ? 233 TYR C O     1 
ATOM   6223 C  CB    . TYR C 1 259 ? 114.424 147.710 164.511 1.00 33.95  ? 233 TYR C CB    1 
ATOM   6224 C  CG    . TYR C 1 259 ? 115.857 148.133 164.725 1.00 34.35  ? 233 TYR C CG    1 
ATOM   6225 C  CD1   . TYR C 1 259 ? 116.558 147.734 165.857 1.00 38.23  ? 233 TYR C CD1   1 
ATOM   6226 C  CD2   . TYR C 1 259 ? 116.506 148.933 163.797 1.00 34.56  ? 233 TYR C CD2   1 
ATOM   6227 C  CE1   . TYR C 1 259 ? 117.868 148.125 166.056 1.00 30.73  ? 233 TYR C CE1   1 
ATOM   6228 C  CE2   . TYR C 1 259 ? 117.813 149.328 163.989 1.00 34.28  ? 233 TYR C CE2   1 
ATOM   6229 C  CZ    . TYR C 1 259 ? 118.489 148.921 165.117 1.00 34.07  ? 233 TYR C CZ    1 
ATOM   6230 O  OH    . TYR C 1 259 ? 119.790 149.319 165.305 1.00 45.37  ? 233 TYR C OH    1 
ATOM   6231 N  N     . PHE C 1 260 ? 112.296 150.323 164.750 1.00 46.85  ? 234 PHE C N     1 
ATOM   6232 C  CA    . PHE C 1 260 ? 112.229 151.750 164.461 1.00 42.45  ? 234 PHE C CA    1 
ATOM   6233 C  C     . PHE C 1 260 ? 111.635 152.569 165.603 1.00 41.51  ? 234 PHE C C     1 
ATOM   6234 O  O     . PHE C 1 260 ? 111.578 153.797 165.495 1.00 52.89  ? 234 PHE C O     1 
ATOM   6235 C  CB    . PHE C 1 260 ? 111.438 151.994 163.172 1.00 40.04  ? 234 PHE C CB    1 
ATOM   6236 C  CG    . PHE C 1 260 ? 110.221 151.125 163.019 1.00 42.35  ? 234 PHE C CG    1 
ATOM   6237 C  CD1   . PHE C 1 260 ? 109.045 151.434 163.681 1.00 40.66  ? 234 PHE C CD1   1 
ATOM   6238 C  CD2   . PHE C 1 260 ? 110.246 150.017 162.188 1.00 43.97  ? 234 PHE C CD2   1 
ATOM   6239 C  CE1   . PHE C 1 260 ? 107.923 150.641 163.540 1.00 41.95  ? 234 PHE C CE1   1 
ATOM   6240 C  CE2   . PHE C 1 260 ? 109.125 149.221 162.039 1.00 43.09  ? 234 PHE C CE2   1 
ATOM   6241 C  CZ    . PHE C 1 260 ? 107.964 149.536 162.716 1.00 43.00  ? 234 PHE C CZ    1 
ATOM   6242 N  N     . MET C 1 261 ? 111.182 151.929 166.684 1.00 47.85  ? 235 MET C N     1 
ATOM   6243 C  CA    . MET C 1 261 ? 110.703 152.694 167.833 1.00 49.19  ? 235 MET C CA    1 
ATOM   6244 C  C     . MET C 1 261 ? 111.854 153.346 168.588 1.00 54.23  ? 235 MET C C     1 
ATOM   6245 O  O     . MET C 1 261 ? 111.744 154.498 169.023 1.00 58.40  ? 235 MET C O     1 
ATOM   6246 C  CB    . MET C 1 261 ? 109.890 151.803 168.771 1.00 50.36  ? 235 MET C CB    1 
ATOM   6247 C  CG    . MET C 1 261 ? 108.914 150.879 168.078 1.00 54.30  ? 235 MET C CG    1 
ATOM   6248 S  SD    . MET C 1 261 ? 107.806 151.775 166.976 1.00 68.81  ? 235 MET C SD    1 
ATOM   6249 C  CE    . MET C 1 261 ? 106.314 151.833 167.962 1.00 52.10  ? 235 MET C CE    1 
ATOM   6250 N  N     . ASP C 1 262 ? 112.963 152.632 168.753 1.00 51.75  ? 236 ASP C N     1 
ATOM   6251 C  CA    . ASP C 1 262 ? 114.088 153.138 169.524 1.00 49.57  ? 236 ASP C CA    1 
ATOM   6252 C  C     . ASP C 1 262 ? 115.242 153.628 168.662 1.00 53.40  ? 236 ASP C C     1 
ATOM   6253 O  O     . ASP C 1 262 ? 116.155 154.272 169.189 1.00 60.30  ? 236 ASP C O     1 
ATOM   6254 C  CB    . ASP C 1 262 ? 114.598 152.052 170.477 1.00 52.19  ? 236 ASP C CB    1 
ATOM   6255 C  CG    . ASP C 1 262 ? 113.474 151.332 171.192 1.00 60.02  ? 236 ASP C CG    1 
ATOM   6256 O  OD1   . ASP C 1 262 ? 113.037 150.273 170.694 1.00 63.55  ? 236 ASP C OD1   1 
ATOM   6257 O  OD2   . ASP C 1 262 ? 113.026 151.823 172.249 1.00 57.93  ? 236 ASP C OD2   1 
ATOM   6258 N  N     . HIS C 1 263 ? 115.228 153.349 167.361 1.00 43.95  ? 237 HIS C N     1 
ATOM   6259 C  CA    . HIS C 1 263 ? 116.345 153.662 166.477 1.00 46.52  ? 237 HIS C CA    1 
ATOM   6260 C  C     . HIS C 1 263 ? 115.858 154.364 165.218 1.00 47.86  ? 237 HIS C C     1 
ATOM   6261 O  O     . HIS C 1 263 ? 116.311 154.089 164.106 1.00 56.41  ? 237 HIS C O     1 
ATOM   6262 C  CB    . HIS C 1 263 ? 117.120 152.396 166.123 1.00 39.61  ? 237 HIS C CB    1 
ATOM   6263 C  CG    . HIS C 1 263 ? 117.642 151.656 167.313 1.00 46.75  ? 237 HIS C CG    1 
ATOM   6264 N  ND1   . HIS C 1 263 ? 116.916 150.680 167.960 1.00 49.28  ? 237 HIS C ND1   1 
ATOM   6265 C  CD2   . HIS C 1 263 ? 118.818 151.750 167.976 1.00 45.69  ? 237 HIS C CD2   1 
ATOM   6266 C  CE1   . HIS C 1 263 ? 117.622 150.203 168.969 1.00 47.19  ? 237 HIS C CE1   1 
ATOM   6267 N  NE2   . HIS C 1 263 ? 118.781 150.836 169.001 1.00 48.57  ? 237 HIS C NE2   1 
ATOM   6268 N  N     . TRP C 1 264 ? 114.913 155.294 165.380 1.00 42.87  ? 238 TRP C N     1 
ATOM   6269 C  CA    . TRP C 1 264 ? 114.406 156.030 164.226 1.00 46.73  ? 238 TRP C CA    1 
ATOM   6270 C  C     . TRP C 1 264 ? 115.398 157.082 163.744 1.00 50.05  ? 238 TRP C C     1 
ATOM   6271 O  O     . TRP C 1 264 ? 115.452 157.373 162.542 1.00 52.68  ? 238 TRP C O     1 
ATOM   6272 C  CB    . TRP C 1 264 ? 113.059 156.672 164.562 1.00 46.41  ? 238 TRP C CB    1 
ATOM   6273 C  CG    . TRP C 1 264 ? 113.110 157.663 165.683 1.00 49.57  ? 238 TRP C CG    1 
ATOM   6274 C  CD1   . TRP C 1 264 ? 113.043 157.395 167.018 1.00 49.51  ? 238 TRP C CD1   1 
ATOM   6275 C  CD2   . TRP C 1 264 ? 113.234 159.084 165.563 1.00 51.94  ? 238 TRP C CD2   1 
ATOM   6276 N  NE1   . TRP C 1 264 ? 113.121 158.562 167.739 1.00 54.66  ? 238 TRP C NE1   1 
ATOM   6277 C  CE2   . TRP C 1 264 ? 113.238 159.614 166.870 1.00 53.51  ? 238 TRP C CE2   1 
ATOM   6278 C  CE3   . TRP C 1 264 ? 113.342 159.962 164.481 1.00 49.06  ? 238 TRP C CE3   1 
ATOM   6279 C  CZ2   . TRP C 1 264 ? 113.347 160.980 167.120 1.00 49.56  ? 238 TRP C CZ2   1 
ATOM   6280 C  CZ3   . TRP C 1 264 ? 113.451 161.317 164.731 1.00 54.04  ? 238 TRP C CZ3   1 
ATOM   6281 C  CH2   . TRP C 1 264 ? 113.452 161.812 166.042 1.00 51.75  ? 238 TRP C CH2   1 
ATOM   6282 N  N     . LYS C 1 265 ? 116.188 157.657 164.657 1.00 46.42  ? 239 LYS C N     1 
ATOM   6283 C  CA    . LYS C 1 265 ? 117.203 158.632 164.266 1.00 41.63  ? 239 LYS C CA    1 
ATOM   6284 C  C     . LYS C 1 265 ? 118.320 157.977 163.464 1.00 42.70  ? 239 LYS C C     1 
ATOM   6285 O  O     . LYS C 1 265 ? 118.828 158.561 162.500 1.00 52.65  ? 239 LYS C O     1 
ATOM   6286 C  CB    . LYS C 1 265 ? 117.768 159.322 165.506 1.00 45.32  ? 239 LYS C CB    1 
ATOM   6287 C  CG    . LYS C 1 265 ? 117.151 160.677 165.801 1.00 48.34  ? 239 LYS C CG    1 
ATOM   6288 C  CD    . LYS C 1 265 ? 117.810 161.329 167.004 1.00 50.54  ? 239 LYS C CD    1 
ATOM   6289 C  CE    . LYS C 1 265 ? 116.834 161.478 168.159 1.00 49.43  ? 239 LYS C CE    1 
ATOM   6290 N  NZ    . LYS C 1 265 ? 117.524 161.457 169.477 1.00 48.55  ? 239 LYS C NZ    1 
ATOM   6291 N  N     . LEU C 1 266 ? 118.706 156.758 163.850 1.00 39.53  ? 240 LEU C N     1 
ATOM   6292 C  CA    . LEU C 1 266 ? 119.698 156.001 163.091 1.00 37.26  ? 240 LEU C CA    1 
ATOM   6293 C  C     . LEU C 1 266 ? 119.175 155.635 161.706 1.00 36.29  ? 240 LEU C C     1 
ATOM   6294 O  O     . LEU C 1 266 ? 119.923 155.679 160.723 1.00 42.14  ? 240 LEU C O     1 
ATOM   6295 C  CB    . LEU C 1 266 ? 120.092 154.746 163.866 1.00 40.69  ? 240 LEU C CB    1 
ATOM   6296 C  CG    . LEU C 1 266 ? 121.418 154.079 163.506 1.00 41.47  ? 240 LEU C CG    1 
ATOM   6297 C  CD1   . LEU C 1 266 ? 122.572 155.054 163.648 1.00 38.24  ? 240 LEU C CD1   1 
ATOM   6298 C  CD2   . LEU C 1 266 ? 121.634 152.855 164.373 1.00 39.59  ? 240 LEU C CD2   1 
ATOM   6299 N  N     . MET C 1 267 ? 117.888 155.285 161.613 1.00 38.33  ? 241 MET C N     1 
ATOM   6300 C  CA    . MET C 1 267 ? 117.282 154.984 160.319 1.00 39.97  ? 241 MET C CA    1 
ATOM   6301 C  C     . MET C 1 267 ? 117.231 156.223 159.429 1.00 42.51  ? 241 MET C C     1 
ATOM   6302 O  O     . MET C 1 267 ? 117.469 156.136 158.219 1.00 49.19  ? 241 MET C O     1 
ATOM   6303 C  CB    . MET C 1 267 ? 115.875 154.421 160.515 1.00 40.48  ? 241 MET C CB    1 
ATOM   6304 C  CG    . MET C 1 267 ? 115.224 153.981 159.219 1.00 47.62  ? 241 MET C CG    1 
ATOM   6305 S  SD    . MET C 1 267 ? 113.797 152.912 159.415 1.00 56.89  ? 241 MET C SD    1 
ATOM   6306 C  CE    . MET C 1 267 ? 112.757 153.988 160.390 1.00 47.29  ? 241 MET C CE    1 
ATOM   6307 N  N     . LEU C 1 268 ? 116.922 157.385 160.017 1.00 38.48  ? 242 LEU C N     1 
ATOM   6308 C  CA    . LEU C 1 268 ? 116.922 158.639 159.264 1.00 36.41  ? 242 LEU C CA    1 
ATOM   6309 C  C     . LEU C 1 268 ? 118.321 159.000 158.777 1.00 35.51  ? 242 LEU C C     1 
ATOM   6310 O  O     . LEU C 1 268 ? 118.490 159.464 157.641 1.00 42.63  ? 242 LEU C O     1 
ATOM   6311 C  CB    . LEU C 1 268 ? 116.352 159.765 160.124 1.00 39.14  ? 242 LEU C CB    1 
ATOM   6312 C  CG    . LEU C 1 268 ? 114.831 159.837 160.252 1.00 42.29  ? 242 LEU C CG    1 
ATOM   6313 C  CD1   . LEU C 1 268 ? 114.428 161.015 161.120 1.00 42.14  ? 242 LEU C CD1   1 
ATOM   6314 C  CD2   . LEU C 1 268 ? 114.184 159.933 158.883 1.00 44.88  ? 242 LEU C CD2   1 
ATOM   6315 N  N     . TYR C 1 269 ? 119.334 158.785 159.624 1.00 31.73  ? 243 TYR C N     1 
ATOM   6316 C  CA    . TYR C 1 269 ? 120.721 159.017 159.228 1.00 32.88  ? 243 TYR C CA    1 
ATOM   6317 C  C     . TYR C 1 269 ? 121.139 158.087 158.095 1.00 31.78  ? 243 TYR C C     1 
ATOM   6318 O  O     . TYR C 1 269 ? 121.838 158.503 157.163 1.00 41.39  ? 243 TYR C O     1 
ATOM   6319 C  CB    . TYR C 1 269 ? 121.634 158.843 160.445 1.00 31.48  ? 243 TYR C CB    1 
ATOM   6320 C  CG    . TYR C 1 269 ? 123.077 158.525 160.125 1.00 36.87  ? 243 TYR C CG    1 
ATOM   6321 C  CD1   . TYR C 1 269 ? 123.932 159.506 159.639 1.00 36.58  ? 243 TYR C CD1   1 
ATOM   6322 C  CD2   . TYR C 1 269 ? 123.589 157.248 160.325 1.00 35.03  ? 243 TYR C CD2   1 
ATOM   6323 C  CE1   . TYR C 1 269 ? 125.253 159.224 159.349 1.00 31.23  ? 243 TYR C CE1   1 
ATOM   6324 C  CE2   . TYR C 1 269 ? 124.908 156.955 160.034 1.00 30.61  ? 243 TYR C CE2   1 
ATOM   6325 C  CZ    . TYR C 1 269 ? 125.734 157.948 159.549 1.00 35.62  ? 243 TYR C CZ    1 
ATOM   6326 O  OH    . TYR C 1 269 ? 127.048 157.663 159.262 1.00 42.52  ? 243 TYR C OH    1 
ATOM   6327 N  N     . ASN C 1 270 ? 120.697 156.831 158.148 1.00 37.11  ? 244 ASN C N     1 
ATOM   6328 C  CA    . ASN C 1 270 ? 121.020 155.870 157.099 1.00 29.25  ? 244 ASN C CA    1 
ATOM   6329 C  C     . ASN C 1 270 ? 120.321 156.206 155.782 1.00 38.39  ? 244 ASN C C     1 
ATOM   6330 O  O     . ASN C 1 270 ? 120.914 156.062 154.702 1.00 42.95  ? 244 ASN C O     1 
ATOM   6331 C  CB    . ASN C 1 270 ? 120.652 154.470 157.575 1.00 32.58  ? 244 ASN C CB    1 
ATOM   6332 C  CG    . ASN C 1 270 ? 121.676 153.894 158.522 1.00 34.48  ? 244 ASN C CG    1 
ATOM   6333 O  OD1   . ASN C 1 270 ? 122.614 153.234 158.098 1.00 37.93  ? 244 ASN C OD1   1 
ATOM   6334 N  ND2   . ASN C 1 270 ? 121.502 154.143 159.811 1.00 36.32  ? 244 ASN C ND2   1 
ATOM   6335 N  N     . PHE C 1 271 ? 119.062 156.658 155.853 1.00 38.34  ? 245 PHE C N     1 
ATOM   6336 C  CA    . PHE C 1 271 ? 118.358 157.119 154.656 1.00 31.24  ? 245 PHE C CA    1 
ATOM   6337 C  C     . PHE C 1 271 ? 119.031 158.345 154.052 1.00 39.77  ? 245 PHE C C     1 
ATOM   6338 O  O     . PHE C 1 271 ? 119.115 158.474 152.823 1.00 45.01  ? 245 PHE C O     1 
ATOM   6339 C  CB    . PHE C 1 271 ? 116.895 157.433 154.975 1.00 34.03  ? 245 PHE C CB    1 
ATOM   6340 C  CG    . PHE C 1 271 ? 116.042 156.223 155.236 1.00 40.05  ? 245 PHE C CG    1 
ATOM   6341 C  CD1   . PHE C 1 271 ? 116.441 154.960 154.823 1.00 46.41  ? 245 PHE C CD1   1 
ATOM   6342 C  CD2   . PHE C 1 271 ? 114.814 156.359 155.863 1.00 43.17  ? 245 PHE C CD2   1 
ATOM   6343 C  CE1   . PHE C 1 271 ? 115.642 153.852 155.059 1.00 38.68  ? 245 PHE C CE1   1 
ATOM   6344 C  CE2   . PHE C 1 271 ? 114.009 155.259 156.094 1.00 43.57  ? 245 PHE C CE2   1 
ATOM   6345 C  CZ    . PHE C 1 271 ? 114.425 154.005 155.692 1.00 40.06  ? 245 PHE C CZ    1 
ATOM   6346 N  N     . GLY C 1 272 ? 119.517 159.256 154.902 1.00 33.79  ? 246 GLY C N     1 
ATOM   6347 C  CA    . GLY C 1 272 ? 120.264 160.401 154.405 1.00 31.48  ? 246 GLY C CA    1 
ATOM   6348 C  C     . GLY C 1 272 ? 121.577 160.012 153.751 1.00 32.87  ? 246 GLY C C     1 
ATOM   6349 O  O     . GLY C 1 272 ? 121.979 160.613 152.752 1.00 41.41  ? 246 GLY C O     1 
ATOM   6350 N  N     . ILE C 1 273 ? 122.252 158.996 154.300 1.00 30.51  ? 247 ILE C N     1 
ATOM   6351 C  CA    . ILE C 1 273 ? 123.491 158.487 153.705 1.00 34.26  ? 247 ILE C CA    1 
ATOM   6352 C  C     . ILE C 1 273 ? 123.221 157.898 152.322 1.00 32.11  ? 247 ILE C C     1 
ATOM   6353 O  O     . ILE C 1 273 ? 123.959 158.159 151.359 1.00 35.47  ? 247 ILE C O     1 
ATOM   6354 C  CB    . ILE C 1 273 ? 124.150 157.462 154.653 1.00 36.38  ? 247 ILE C CB    1 
ATOM   6355 C  CG1   . ILE C 1 273 ? 124.836 158.181 155.825 1.00 33.00  ? 247 ILE C CG1   1 
ATOM   6356 C  CG2   . ILE C 1 273 ? 125.094 156.501 153.910 1.00 34.57  ? 247 ILE C CG2   1 
ATOM   6357 C  CD1   . ILE C 1 273 ? 126.302 158.521 155.611 1.00 38.07  ? 247 ILE C CD1   1 
ATOM   6358 N  N     . VAL C 1 274 ? 122.133 157.124 152.202 1.00 34.14  ? 248 VAL C N     1 
ATOM   6359 C  CA    . VAL C 1 274 ? 121.742 156.534 150.920 1.00 35.68  ? 248 VAL C CA    1 
ATOM   6360 C  C     . VAL C 1 274 ? 121.395 157.619 149.903 1.00 35.63  ? 248 VAL C C     1 
ATOM   6361 O  O     . VAL C 1 274 ? 121.820 157.560 148.740 1.00 38.95  ? 248 VAL C O     1 
ATOM   6362 C  CB    . VAL C 1 274 ? 120.576 155.545 151.130 1.00 40.88  ? 248 VAL C CB    1 
ATOM   6363 C  CG1   . VAL C 1 274 ? 119.775 155.315 149.848 1.00 33.43  ? 248 VAL C CG1   1 
ATOM   6364 C  CG2   . VAL C 1 274 ? 121.098 154.232 151.644 1.00 34.51  ? 248 VAL C CG2   1 
ATOM   6365 N  N     . ALA C 1 275 ? 120.651 158.644 150.338 1.00 39.54  ? 249 ALA C N     1 
ATOM   6366 C  CA    . ALA C 1 275 ? 120.267 159.737 149.447 1.00 34.08  ? 249 ALA C CA    1 
ATOM   6367 C  C     . ALA C 1 275 ? 121.474 160.546 148.985 1.00 32.01  ? 249 ALA C C     1 
ATOM   6368 O  O     . ALA C 1 275 ? 121.549 160.940 147.815 1.00 42.82  ? 249 ALA C O     1 
ATOM   6369 C  CB    . ALA C 1 275 ? 119.251 160.643 150.142 1.00 33.08  ? 249 ALA C CB    1 
ATOM   6370 N  N     . ILE C 1 276 ? 122.435 160.787 149.883 1.00 36.16  ? 250 ILE C N     1 
ATOM   6371 C  CA    . ILE C 1 276 ? 123.641 161.534 149.531 1.00 35.39  ? 250 ILE C CA    1 
ATOM   6372 C  C     . ILE C 1 276 ? 124.497 160.749 148.539 1.00 32.80  ? 250 ILE C C     1 
ATOM   6373 O  O     . ILE C 1 276 ? 124.997 161.310 147.549 1.00 41.10  ? 250 ILE C O     1 
ATOM   6374 C  CB    . ILE C 1 276 ? 124.415 161.899 150.816 1.00 37.29  ? 250 ILE C CB    1 
ATOM   6375 C  CG1   . ILE C 1 276 ? 123.780 163.115 151.491 1.00 37.19  ? 250 ILE C CG1   1 
ATOM   6376 C  CG2   . ILE C 1 276 ? 125.889 162.174 150.544 1.00 37.79  ? 250 ILE C CG2   1 
ATOM   6377 C  CD1   . ILE C 1 276 ? 124.078 163.220 152.968 1.00 39.13  ? 250 ILE C CD1   1 
ATOM   6378 N  N     . PHE C 1 277 ? 124.655 159.440 148.776 1.00 36.52  ? 251 PHE C N     1 
ATOM   6379 C  CA    . PHE C 1 277 ? 125.416 158.586 147.865 1.00 33.36  ? 251 PHE C CA    1 
ATOM   6380 C  C     . PHE C 1 277 ? 124.766 158.523 146.487 1.00 32.65  ? 251 PHE C C     1 
ATOM   6381 O  O     . PHE C 1 277 ? 125.452 158.631 145.463 1.00 43.23  ? 251 PHE C O     1 
ATOM   6382 C  CB    . PHE C 1 277 ? 125.549 157.183 148.456 1.00 34.74  ? 251 PHE C CB    1 
ATOM   6383 C  CG    . PHE C 1 277 ? 126.869 156.928 149.123 1.00 35.37  ? 251 PHE C CG    1 
ATOM   6384 C  CD1   . PHE C 1 277 ? 128.018 156.752 148.369 1.00 35.77  ? 251 PHE C CD1   1 
ATOM   6385 C  CD2   . PHE C 1 277 ? 126.961 156.868 150.505 1.00 34.39  ? 251 PHE C CD2   1 
ATOM   6386 C  CE1   . PHE C 1 277 ? 129.237 156.517 148.982 1.00 35.90  ? 251 PHE C CE1   1 
ATOM   6387 C  CE2   . PHE C 1 277 ? 128.174 156.635 151.122 1.00 37.79  ? 251 PHE C CE2   1 
ATOM   6388 C  CZ    . PHE C 1 277 ? 129.314 156.460 150.360 1.00 36.04  ? 251 PHE C CZ    1 
ATOM   6389 N  N     . PHE C 1 278 ? 123.434 158.393 146.451 1.00 31.80  ? 252 PHE C N     1 
ATOM   6390 C  CA    . PHE C 1 278 ? 122.709 158.368 145.185 1.00 30.29  ? 252 PHE C CA    1 
ATOM   6391 C  C     . PHE C 1 278 ? 122.818 159.695 144.445 1.00 34.81  ? 252 PHE C C     1 
ATOM   6392 O  O     . PHE C 1 278 ? 122.978 159.712 143.220 1.00 38.14  ? 252 PHE C O     1 
ATOM   6393 C  CB    . PHE C 1 278 ? 121.240 158.015 145.424 1.00 33.95  ? 252 PHE C CB    1 
ATOM   6394 C  CG    . PHE C 1 278 ? 120.423 157.945 144.166 1.00 37.34  ? 252 PHE C CG    1 
ATOM   6395 C  CD1   . PHE C 1 278 ? 120.570 156.885 143.285 1.00 36.96  ? 252 PHE C CD1   1 
ATOM   6396 C  CD2   . PHE C 1 278 ? 119.509 158.943 143.861 1.00 35.31  ? 252 PHE C CD2   1 
ATOM   6397 C  CE1   . PHE C 1 278 ? 119.820 156.821 142.123 1.00 33.38  ? 252 PHE C CE1   1 
ATOM   6398 C  CE2   . PHE C 1 278 ? 118.756 158.883 142.701 1.00 33.25  ? 252 PHE C CE2   1 
ATOM   6399 C  CZ    . PHE C 1 278 ? 118.914 157.820 141.833 1.00 27.43  ? 252 PHE C CZ    1 
ATOM   6400 N  N     . ALA C 1 279 ? 122.758 160.815 145.175 1.00 36.71  ? 253 ALA C N     1 
ATOM   6401 C  CA    . ALA C 1 279 ? 122.816 162.130 144.543 1.00 29.85  ? 253 ALA C CA    1 
ATOM   6402 C  C     . ALA C 1 279 ? 124.180 162.396 143.921 1.00 32.88  ? 253 ALA C C     1 
ATOM   6403 O  O     . ALA C 1 279 ? 124.274 162.803 142.754 1.00 36.91  ? 253 ALA C O     1 
ATOM   6404 C  CB    . ALA C 1 279 ? 122.464 163.216 145.561 1.00 31.82  ? 253 ALA C CB    1 
ATOM   6405 N  N     . ILE C 1 280 ? 125.253 162.131 144.677 1.00 31.77  ? 254 ILE C N     1 
ATOM   6406 C  CA    . ILE C 1 280 ? 126.601 162.372 144.167 1.00 28.92  ? 254 ILE C CA    1 
ATOM   6407 C  C     . ILE C 1 280 ? 126.931 161.401 143.034 1.00 31.74  ? 254 ILE C C     1 
ATOM   6408 O  O     . ILE C 1 280 ? 127.524 161.792 142.017 1.00 40.39  ? 254 ILE C O     1 
ATOM   6409 C  CB    . ILE C 1 280 ? 127.625 162.301 145.318 1.00 33.50  ? 254 ILE C CB    1 
ATOM   6410 C  CG1   . ILE C 1 280 ? 127.294 163.361 146.372 1.00 29.71  ? 254 ILE C CG1   1 
ATOM   6411 C  CG2   . ILE C 1 280 ? 129.042 162.515 144.809 1.00 29.57  ? 254 ILE C CG2   1 
ATOM   6412 C  CD1   . ILE C 1 280 ? 128.273 163.423 147.526 1.00 35.74  ? 254 ILE C CD1   1 
ATOM   6413 N  N     . GLY C 1 281 ? 126.503 160.137 143.161 1.00 35.57  ? 255 GLY C N     1 
ATOM   6414 C  CA    . GLY C 1 281 ? 126.756 159.165 142.110 1.00 24.59  ? 255 GLY C CA    1 
ATOM   6415 C  C     . GLY C 1 281 ? 126.010 159.462 140.823 1.00 25.65  ? 255 GLY C C     1 
ATOM   6416 O  O     . GLY C 1 281 ? 126.572 159.337 139.733 1.00 32.54  ? 255 GLY C O     1 
ATOM   6417 N  N     . ALA C 1 282 ? 124.742 159.878 140.931 1.00 31.42  ? 256 ALA C N     1 
ATOM   6418 C  CA    . ALA C 1 282 ? 123.964 160.226 139.746 1.00 29.62  ? 256 ALA C CA    1 
ATOM   6419 C  C     . ALA C 1 282 ? 124.508 161.478 139.071 1.00 32.18  ? 256 ALA C C     1 
ATOM   6420 O  O     . ALA C 1 282 ? 124.553 161.543 137.835 1.00 36.00  ? 256 ALA C O     1 
ATOM   6421 C  CB    . ALA C 1 282 ? 122.493 160.412 140.118 1.00 32.05  ? 256 ALA C CB    1 
ATOM   6422 N  N     . TYR C 1 283 ? 124.981 162.482 139.781 1.00 36.16  ? 257 TYR C N     1 
ATOM   6423 C  CA    . TYR C 1 283 ? 125.581 163.664 139.122 1.00 30.38  ? 257 TYR C CA    1 
ATOM   6424 C  C     . TYR C 1 283 ? 126.868 163.309 138.387 1.00 28.01  ? 257 TYR C C     1 
ATOM   6425 O  O     . TYR C 1 283 ? 127.045 163.777 137.282 1.00 37.40  ? 257 TYR C O     1 
ATOM   6426 C  CB    . TYR C 1 283 ? 125.745 164.716 140.216 1.00 35.80  ? 257 TYR C CB    1 
ATOM   6427 C  CG    . TYR C 1 283 ? 126.601 165.900 139.800 1.00 42.32  ? 257 TYR C CG    1 
ATOM   6428 C  CD1   . TYR C 1 283 ? 126.034 166.988 139.152 1.00 36.09  ? 257 TYR C CD1   1 
ATOM   6429 C  CD2   . TYR C 1 283 ? 127.971 165.911 140.021 1.00 39.38  ? 257 TYR C CD2   1 
ATOM   6430 C  CE1   . TYR C 1 283 ? 126.804 168.060 138.746 1.00 34.74  ? 257 TYR C CE1   1 
ATOM   6431 C  CE2   . TYR C 1 283 ? 128.753 166.973 139.608 1.00 38.28  ? 257 TYR C CE2   1 
ATOM   6432 C  CZ    . TYR C 1 283 ? 128.166 168.051 138.974 1.00 38.61  ? 257 TYR C CZ    1 
ATOM   6433 O  OH    . TYR C 1 283 ? 128.926 169.109 138.580 1.00 44.71  ? 257 TYR C OH    1 
ATOM   6434 N  N     . LEU C 1 284 ? 127.761 162.563 139.017 1.00 26.18  ? 258 LEU C N     1 
ATOM   6435 C  CA    . LEU C 1 284 ? 129.059 162.224 138.398 1.00 27.24  ? 258 LEU C CA    1 
ATOM   6436 C  C     . LEU C 1 284 ? 128.887 161.376 137.143 1.00 31.07  ? 258 LEU C C     1 
ATOM   6437 O  O     . LEU C 1 284 ? 129.582 161.637 136.186 1.00 33.33  ? 258 LEU C O     1 
ATOM   6438 C  CB    . LEU C 1 284 ? 129.949 161.552 139.433 1.00 33.44  ? 258 LEU C CB    1 
ATOM   6439 C  CG    . LEU C 1 284 ? 130.797 162.500 140.279 1.00 35.69  ? 258 LEU C CG    1 
ATOM   6440 C  CD1   . LEU C 1 284 ? 131.856 161.681 140.968 1.00 40.99  ? 258 LEU C CD1   1 
ATOM   6441 C  CD2   . LEU C 1 284 ? 131.429 163.572 139.411 1.00 35.45  ? 258 LEU C CD2   1 
ATOM   6442 N  N     . HIS C 1 285 ? 127.986 160.405 137.157 1.00 33.28  ? 259 HIS C N     1 
ATOM   6443 C  CA    . HIS C 1 285 ? 127.709 159.524 136.006 1.00 31.29  ? 259 HIS C CA    1 
ATOM   6444 C  C     . HIS C 1 285 ? 127.168 160.321 134.815 1.00 32.28  ? 259 HIS C C     1 
ATOM   6445 O  O     . HIS C 1 285 ? 127.655 160.127 133.730 1.00 36.29  ? 259 HIS C O     1 
ATOM   6446 C  CB    . HIS C 1 285 ? 126.738 158.443 136.492 1.00 26.49  ? 259 HIS C CB    1 
ATOM   6447 C  CG    . HIS C 1 285 ? 126.265 157.496 135.442 1.00 28.30  ? 259 HIS C CG    1 
ATOM   6448 N  ND1   . HIS C 1 285 ? 126.927 156.337 135.113 1.00 25.35  ? 259 HIS C ND1   1 
ATOM   6449 C  CD2   . HIS C 1 285 ? 125.207 157.555 134.637 1.00 32.80  ? 259 HIS C CD2   1 
ATOM   6450 C  CE1   . HIS C 1 285 ? 126.283 155.735 134.136 1.00 29.31  ? 259 HIS C CE1   1 
ATOM   6451 N  NE2   . HIS C 1 285 ? 125.243 156.460 133.828 1.00 34.46  ? 259 HIS C NE2   1 
ATOM   6452 N  N     . MET C 1 286 ? 126.241 161.235 135.024 1.00 27.89  ? 260 MET C N     1 
ATOM   6453 C  CA    . MET C 1 286 ? 125.680 162.083 133.956 1.00 28.38  ? 260 MET C CA    1 
ATOM   6454 C  C     . MET C 1 286 ? 126.741 163.011 133.351 1.00 31.77  ? 260 MET C C     1 
ATOM   6455 O  O     . MET C 1 286 ? 126.707 163.151 132.132 1.00 39.11  ? 260 MET C O     1 
ATOM   6456 C  CB    . MET C 1 286 ? 124.423 162.771 134.492 1.00 36.85  ? 260 MET C CB    1 
ATOM   6457 C  CG    . MET C 1 286 ? 123.296 161.820 134.846 1.00 34.98  ? 260 MET C CG    1 
ATOM   6458 S  SD    . MET C 1 286 ? 122.884 160.573 133.614 1.00 49.54  ? 260 MET C SD    1 
ATOM   6459 C  CE    . MET C 1 286 ? 122.509 161.607 132.195 1.00 38.69  ? 260 MET C CE    1 
ATOM   6460 N  N     . LYS C 1 287 ? 127.630 163.597 134.143 1.00 38.48  ? 261 LYS C N     1 
ATOM   6461 C  CA    . LYS C 1 287 ? 128.756 164.433 133.659 1.00 32.88  ? 261 LYS C CA    1 
ATOM   6462 C  C     . LYS C 1 287 ? 129.790 163.673 132.799 1.00 38.19  ? 261 LYS C C     1 
ATOM   6463 O  O     . LYS C 1 287 ? 130.293 164.293 131.853 1.00 47.15  ? 261 LYS C O     1 
ATOM   6464 C  CB    . LYS C 1 287 ? 129.345 165.060 134.916 1.00 34.91  ? 261 LYS C CB    1 
ATOM   6465 C  CG    . LYS C 1 287 ? 130.531 165.970 134.736 1.00 37.11  ? 261 LYS C CG    1 
ATOM   6466 C  CD    . LYS C 1 287 ? 130.877 166.688 136.030 1.00 41.39  ? 261 LYS C CD    1 
ATOM   6467 C  CE    . LYS C 1 287 ? 131.499 168.010 135.750 1.00 44.46  ? 261 LYS C CE    1 
ATOM   6468 N  NZ    . LYS C 1 287 ? 132.923 167.978 136.078 1.00 46.03  ? 261 LYS C NZ    1 
ATOM   6469 N  N     . TYR C 1 288 ? 130.171 162.453 133.148 1.00 36.48  ? 262 TYR C N     1 
ATOM   6470 C  CA    . TYR C 1 288 ? 131.235 161.718 132.428 1.00 35.71  ? 262 TYR C CA    1 
ATOM   6471 C  C     . TYR C 1 288 ? 130.777 160.609 131.529 1.00 32.80  ? 262 TYR C C     1 
ATOM   6472 O  O     . TYR C 1 288 ? 131.643 160.164 130.826 1.00 34.80  ? 262 TYR C O     1 
ATOM   6473 C  CB    . TYR C 1 288 ? 132.175 161.257 133.544 1.00 36.36  ? 262 TYR C CB    1 
ATOM   6474 C  CG    . TYR C 1 288 ? 132.857 162.398 134.275 1.00 36.38  ? 262 TYR C CG    1 
ATOM   6475 C  CD1   . TYR C 1 288 ? 133.835 163.159 133.654 1.00 33.44  ? 262 TYR C CD1   1 
ATOM   6476 C  CD2   . TYR C 1 288 ? 132.527 162.699 135.585 1.00 32.61  ? 262 TYR C CD2   1 
ATOM   6477 C  CE1   . TYR C 1 288 ? 134.467 164.190 134.319 1.00 36.94  ? 262 TYR C CE1   1 
ATOM   6478 C  CE2   . TYR C 1 288 ? 133.144 163.734 136.255 1.00 39.63  ? 262 TYR C CE2   1 
ATOM   6479 C  CZ    . TYR C 1 288 ? 134.116 164.480 135.622 1.00 41.96  ? 262 TYR C CZ    1 
ATOM   6480 O  OH    . TYR C 1 288 ? 134.719 165.493 136.293 1.00 44.25  ? 262 TYR C OH    1 
ATOM   6481 N  N     . ARG C 1 289 ? 129.501 160.296 131.423 1.00 38.54  ? 263 ARG C N     1 
ATOM   6482 C  CA    . ARG C 1 289 ? 129.038 159.099 130.663 1.00 37.62  ? 263 ARG C CA    1 
ATOM   6483 C  C     . ARG C 1 289 ? 129.388 159.174 129.162 1.00 41.72  ? 263 ARG C C     1 
ATOM   6484 O  O     . ARG C 1 289 ? 129.656 158.112 128.592 1.00 40.29  ? 263 ARG C O     1 
ATOM   6485 C  CB    . ARG C 1 289 ? 127.575 158.755 130.970 1.00 36.71  ? 263 ARG C CB    1 
ATOM   6486 C  CG    . ARG C 1 289 ? 126.481 159.753 130.628 1.00 34.60  ? 263 ARG C CG    1 
ATOM   6487 C  CD    . ARG C 1 289 ? 125.199 159.083 130.186 1.00 42.03  ? 263 ARG C CD    1 
ATOM   6488 N  NE    . ARG C 1 289 ? 124.618 158.142 131.148 1.00 47.84  ? 263 ARG C NE    1 
ATOM   6489 C  CZ    . ARG C 1 289 ? 123.353 157.737 131.128 1.00 44.44  ? 263 ARG C CZ    1 
ATOM   6490 N  NH1   . ARG C 1 289 ? 122.989 156.663 131.794 1.00 41.45  ? 263 ARG C NH1   1 
ATOM   6491 N  NH2   . ARG C 1 289 ? 122.450 158.409 130.445 1.00 41.44  ? 263 ARG C NH2   1 
ATOM   6492 N  N     . ASP C 1 290 ? 129.285 160.332 128.524 1.00 44.73  ? 264 ASP C N     1 
ATOM   6493 C  CA    . ASP C 1 290 ? 129.670 160.547 127.101 1.00 40.47  ? 264 ASP C CA    1 
ATOM   6494 C  C     . ASP C 1 290 ? 131.173 160.351 126.900 1.00 41.67  ? 264 ASP C C     1 
ATOM   6495 O  O     . ASP C 1 290 ? 131.539 160.113 125.767 1.00 48.95  ? 264 ASP C O     1 
ATOM   6496 C  CB    . ASP C 1 290 ? 129.126 161.863 126.583 1.00 42.72  ? 264 ASP C CB    1 
ATOM   6497 C  CG    . ASP C 1 290 ? 127.613 162.014 126.613 1.00 52.61  ? 264 ASP C CG    1 
ATOM   6498 O  OD1   . ASP C 1 290 ? 126.935 161.080 127.078 1.00 52.67  ? 264 ASP C OD1   1 
ATOM   6499 O  OD2   . ASP C 1 290 ? 127.123 163.075 126.175 1.00 54.51  ? 264 ASP C OD2   1 
ATOM   6500 N  N     . GLN C 1 291 ? 132.004 160.640 127.890 1.00 40.36  ? 265 GLN C N     1 
ATOM   6501 C  CA    . GLN C 1 291 ? 133.480 160.585 127.827 1.00 34.76  ? 265 GLN C CA    1 
ATOM   6502 C  C     . GLN C 1 291 ? 134.067 159.280 128.364 1.00 37.90  ? 265 GLN C C     1 
ATOM   6503 O  O     . GLN C 1 291 ? 135.253 159.254 128.475 1.00 39.02  ? 265 GLN C O     1 
ATOM   6504 C  CB    . GLN C 1 291 ? 133.903 161.847 128.560 1.00 35.47  ? 265 GLN C CB    1 
ATOM   6505 C  CG    . GLN C 1 291 ? 133.336 163.129 127.966 1.00 43.18  ? 265 GLN C CG    1 
ATOM   6506 C  CD    . GLN C 1 291 ? 132.291 163.779 128.845 1.00 49.56  ? 265 GLN C CD    1 
ATOM   6507 O  OE1   . GLN C 1 291 ? 131.095 163.761 128.535 1.00 49.21  ? 265 GLN C OE1   1 
ATOM   6508 N  NE2   . GLN C 1 291 ? 132.735 164.360 129.952 1.00 44.04  ? 265 GLN C NE2   1 
ATOM   6509 N  N     . PHE C 1 292 ? 133.296 158.250 128.669 1.00 40.90  ? 266 PHE C N     1 
ATOM   6510 C  CA    . PHE C 1 292 ? 133.739 156.985 129.324 1.00 33.34  ? 266 PHE C CA    1 
ATOM   6511 C  C     . PHE C 1 292 ? 134.751 156.255 128.458 1.00 39.01  ? 266 PHE C C     1 
ATOM   6512 O  O     . PHE C 1 292 ? 135.672 155.709 129.052 1.00 45.53  ? 266 PHE C O     1 
ATOM   6513 C  CB    . PHE C 1 292 ? 132.553 156.086 129.678 1.00 34.97  ? 266 PHE C CB    1 
ATOM   6514 C  CG    . PHE C 1 292 ? 131.864 156.352 131.009 1.00 37.06  ? 266 PHE C CG    1 
ATOM   6515 C  CD1   . PHE C 1 292 ? 130.633 155.778 131.302 1.00 38.27  ? 266 PHE C CD1   1 
ATOM   6516 C  CD2   . PHE C 1 292 ? 132.441 157.177 131.966 1.00 35.35  ? 266 PHE C CD2   1 
ATOM   6517 C  CE1   . PHE C 1 292 ? 130.005 156.023 132.511 1.00 34.07  ? 266 PHE C CE1   1 
ATOM   6518 C  CE2   . PHE C 1 292 ? 131.806 157.413 133.171 1.00 29.55  ? 266 PHE C CE2   1 
ATOM   6519 C  CZ    . PHE C 1 292 ? 130.590 156.845 133.441 1.00 33.18  ? 266 PHE C CZ    1 
ATOM   6520 N  N     . ALA C 1 293 ? 134.613 156.269 127.144 1.00 43.30  ? 267 ALA C N     1 
ATOM   6521 C  CA    . ALA C 1 293 ? 135.542 155.663 126.175 1.00 39.54  ? 267 ALA C CA    1 
ATOM   6522 C  C     . ALA C 1 293 ? 136.908 156.309 126.341 1.00 42.29  ? 267 ALA C C     1 
ATOM   6523 O  O     . ALA C 1 293 ? 137.899 155.580 126.227 1.00 49.92  ? 267 ALA C O     1 
ATOM   6524 C  CB    . ALA C 1 293 ? 134.992 155.906 124.816 1.00 39.36  ? 267 ALA C CB    1 
ATOM   6525 N  N     . ASP C 1 294 ? 136.962 157.603 126.624 1.00 40.22  ? 268 ASP C N     1 
ATOM   6526 C  CA    . ASP C 1 294 ? 138.223 158.334 126.906 1.00 40.55  ? 268 ASP C CA    1 
ATOM   6527 C  C     . ASP C 1 294 ? 138.962 157.804 128.139 1.00 46.61  ? 268 ASP C C     1 
ATOM   6528 O  O     . ASP C 1 294 ? 140.191 157.868 128.135 1.00 54.88  ? 268 ASP C O     1 
ATOM   6529 C  CB    . ASP C 1 294 ? 137.956 159.809 127.121 1.00 45.61  ? 268 ASP C CB    1 
ATOM   6530 C  CG    . ASP C 1 294 ? 137.163 160.508 126.029 1.00 52.91  ? 268 ASP C CG    1 
ATOM   6531 O  OD1   . ASP C 1 294 ? 136.876 159.855 125.007 1.00 50.32  ? 268 ASP C OD1   1 
ATOM   6532 O  OD2   . ASP C 1 294 ? 136.839 161.699 126.215 1.00 54.26  ? 268 ASP C OD2   1 
ATOM   6533 N  N     . PHE C 1 295 ? 138.269 157.412 129.202 1.00 45.33  ? 269 PHE C N     1 
ATOM   6534 C  CA    . PHE C 1 295 ? 138.907 156.997 130.471 1.00 41.04  ? 269 PHE C CA    1 
ATOM   6535 C  C     . PHE C 1 295 ? 139.141 155.535 130.511 1.00 41.83  ? 269 PHE C C     1 
ATOM   6536 O  O     . PHE C 1 295 ? 139.697 155.051 131.493 1.00 45.06  ? 269 PHE C O     1 
ATOM   6537 C  CB    . PHE C 1 295 ? 137.895 157.441 131.520 1.00 42.27  ? 269 PHE C CB    1 
ATOM   6538 C  CG    . PHE C 1 295 ? 137.745 158.938 131.693 1.00 41.06  ? 269 PHE C CG    1 
ATOM   6539 C  CD1   . PHE C 1 295 ? 138.673 159.658 132.426 1.00 35.86  ? 269 PHE C CD1   1 
ATOM   6540 C  CD2   . PHE C 1 295 ? 136.663 159.609 131.144 1.00 42.41  ? 269 PHE C CD2   1 
ATOM   6541 C  CE1   . PHE C 1 295 ? 138.521 161.016 132.587 1.00 45.61  ? 269 PHE C CE1   1 
ATOM   6542 C  CE2   . PHE C 1 295 ? 136.523 160.971 131.303 1.00 43.93  ? 269 PHE C CE2   1 
ATOM   6543 C  CZ    . PHE C 1 295 ? 137.449 161.669 132.026 1.00 43.85  ? 269 PHE C CZ    1 
ATOM   6544 N  N     . LEU C 1 296 ? 138.756 154.825 129.472 1.00 44.83  ? 270 LEU C N     1 
ATOM   6545 C  CA    . LEU C 1 296 ? 138.803 153.350 129.534 1.00 44.44  ? 270 LEU C CA    1 
ATOM   6546 C  C     . LEU C 1 296 ? 140.020 152.886 128.759 1.00 49.27  ? 270 LEU C C     1 
ATOM   6547 O  O     . LEU C 1 296 ? 140.402 151.724 128.841 1.00 57.01  ? 270 LEU C O     1 
ATOM   6548 C  CB    . LEU C 1 296 ? 137.508 152.754 128.997 1.00 46.19  ? 270 LEU C CB    1 
ATOM   6549 C  CG    . LEU C 1 296 ? 136.377 152.641 130.021 1.00 45.24  ? 270 LEU C CG    1 
ATOM   6550 C  CD1   . LEU C 1 296 ? 135.392 151.577 129.623 1.00 44.46  ? 270 LEU C CD1   1 
ATOM   6551 C  CD2   . LEU C 1 296 ? 136.913 152.387 131.418 1.00 43.49  ? 270 LEU C CD2   1 
ATOM   6552 O  OXT   . LEU C 1 296 ? 140.575 153.748 128.085 1.00 50.00  ? 270 LEU C OXT   1 
ATOM   6553 N  N     . MET D 2 1   ? 117.311 164.549 99.789  1.00 83.17  ? 1   MET D N     1 
ATOM   6554 C  CA    . MET D 2 1   ? 117.270 166.003 99.892  1.00 85.77  ? 1   MET D CA    1 
ATOM   6555 C  C     . MET D 2 1   ? 117.278 166.443 101.352 1.00 85.64  ? 1   MET D C     1 
ATOM   6556 O  O     . MET D 2 1   ? 117.566 167.598 101.661 1.00 84.60  ? 1   MET D O     1 
ATOM   6557 C  CB    . MET D 2 1   ? 116.034 166.559 99.181  1.00 86.07  ? 1   MET D CB    1 
ATOM   6558 C  CG    . MET D 2 1   ? 116.016 166.307 97.682  1.00 86.41  ? 1   MET D CG    1 
ATOM   6559 S  SD    . MET D 2 1   ? 116.935 167.549 96.753  1.00 94.13  ? 1   MET D SD    1 
ATOM   6560 C  CE    . MET D 2 1   ? 115.683 168.098 95.596  1.00 85.82  ? 1   MET D CE    1 
ATOM   6561 N  N     . ASN D 2 2   ? 116.962 165.510 102.245 1.00 71.68  ? 2   ASN D N     1 
ATOM   6562 C  CA    . ASN D 2 2   ? 116.948 165.767 103.679 1.00 70.89  ? 2   ASN D CA    1 
ATOM   6563 C  C     . ASN D 2 2   ? 118.219 165.212 104.306 1.00 67.51  ? 2   ASN D C     1 
ATOM   6564 O  O     . ASN D 2 2   ? 118.613 164.077 104.025 1.00 66.47  ? 2   ASN D O     1 
ATOM   6565 C  CB    . ASN D 2 2   ? 115.716 165.143 104.334 1.00 72.08  ? 2   ASN D CB    1 
ATOM   6566 C  CG    . ASN D 2 2   ? 114.850 166.165 105.040 1.00 75.44  ? 2   ASN D CG    1 
ATOM   6567 O  OD1   . ASN D 2 2   ? 115.336 167.198 105.498 1.00 74.34  ? 2   ASN D OD1   1 
ATOM   6568 N  ND2   . ASN D 2 2   ? 113.556 165.878 105.133 1.00 72.92  ? 2   ASN D ND2   1 
ATOM   6569 N  N     . VAL D 2 3   ? 118.855 166.018 105.156 1.00 60.48  ? 3   VAL D N     1 
ATOM   6570 C  CA    . VAL D 2 3   ? 120.116 165.625 105.769 1.00 56.76  ? 3   VAL D CA    1 
ATOM   6571 C  C     . VAL D 2 3   ? 119.842 164.676 106.928 1.00 55.53  ? 3   VAL D C     1 
ATOM   6572 O  O     . VAL D 2 3   ? 119.076 164.995 107.846 1.00 64.00  ? 3   VAL D O     1 
ATOM   6573 C  CB    . VAL D 2 3   ? 120.893 166.867 106.232 1.00 56.03  ? 3   VAL D CB    1 
ATOM   6574 C  CG1   . VAL D 2 3   ? 122.070 166.478 107.113 1.00 54.54  ? 3   VAL D CG1   1 
ATOM   6575 C  CG2   . VAL D 2 3   ? 121.360 167.676 105.034 1.00 57.16  ? 3   VAL D CG2   1 
ATOM   6576 N  N     . SER D 2 4   ? 120.466 163.500 106.889 1.00 44.32  ? 4   SER D N     1 
ATOM   6577 C  CA    . SER D 2 4   ? 120.339 162.511 107.953 1.00 45.32  ? 4   SER D CA    1 
ATOM   6578 C  C     . SER D 2 4   ? 121.464 162.593 108.973 1.00 47.50  ? 4   SER D C     1 
ATOM   6579 O  O     . SER D 2 4   ? 121.205 162.536 110.178 1.00 50.54  ? 4   SER D O     1 
ATOM   6580 C  CB    . SER D 2 4   ? 120.290 161.102 107.359 1.00 48.85  ? 4   SER D CB    1 
ATOM   6581 O  OG    . SER D 2 4   ? 121.574 160.688 106.937 1.00 51.54  ? 4   SER D OG    1 
ATOM   6582 N  N     . VAL D 2 5   ? 122.709 162.713 108.520 1.00 50.91  ? 5   VAL D N     1 
ATOM   6583 C  CA    . VAL D 2 5   ? 123.867 162.884 109.390 1.00 46.67  ? 5   VAL D CA    1 
ATOM   6584 C  C     . VAL D 2 5   ? 124.563 164.177 108.991 1.00 42.34  ? 5   VAL D C     1 
ATOM   6585 O  O     . VAL D 2 5   ? 124.861 164.385 107.811 1.00 49.17  ? 5   VAL D O     1 
ATOM   6586 C  CB    . VAL D 2 5   ? 124.846 161.695 109.296 1.00 44.31  ? 5   VAL D CB    1 
ATOM   6587 C  CG1   . VAL D 2 5   ? 126.001 161.875 110.266 1.00 40.49  ? 5   VAL D CG1   1 
ATOM   6588 C  CG2   . VAL D 2 5   ? 124.131 160.379 109.561 1.00 43.28  ? 5   VAL D CG2   1 
ATOM   6589 N  N     . ASN D 2 6   ? 124.815 165.048 109.968 1.00 43.71  ? 6   ASN D N     1 
ATOM   6590 C  CA    . ASN D 2 6   ? 125.510 166.309 109.729 1.00 46.31  ? 6   ASN D CA    1 
ATOM   6591 C  C     . ASN D 2 6   ? 126.702 166.381 110.672 1.00 47.33  ? 6   ASN D C     1 
ATOM   6592 O  O     . ASN D 2 6   ? 126.529 166.515 111.888 1.00 48.39  ? 6   ASN D O     1 
ATOM   6593 C  CB    . ASN D 2 6   ? 124.576 167.505 109.929 1.00 47.33  ? 6   ASN D CB    1 
ATOM   6594 C  CG    . ASN D 2 6   ? 125.059 168.756 109.212 1.00 46.97  ? 6   ASN D CG    1 
ATOM   6595 O  OD1   . ASN D 2 6   ? 126.256 168.956 109.013 1.00 49.83  ? 6   ASN D OD1   1 
ATOM   6596 N  ND2   . ASN D 2 6   ? 124.119 169.605 108.819 1.00 53.41  ? 6   ASN D ND2   1 
ATOM   6597 N  N     . ILE D 2 7   ? 127.903 166.298 110.111 1.00 49.73  ? 7   ILE D N     1 
ATOM   6598 C  CA    . ILE D 2 7   ? 129.149 166.380 110.864 1.00 47.39  ? 7   ILE D CA    1 
ATOM   6599 C  C     . ILE D 2 7   ? 129.755 167.750 110.593 1.00 43.53  ? 7   ILE D C     1 
ATOM   6600 O  O     . ILE D 2 7   ? 130.022 168.097 109.437 1.00 47.71  ? 7   ILE D O     1 
ATOM   6601 C  CB    . ILE D 2 7   ? 130.118 165.255 110.472 1.00 45.63  ? 7   ILE D CB    1 
ATOM   6602 C  CG1   . ILE D 2 7   ? 129.530 163.892 110.840 1.00 48.65  ? 7   ILE D CG1   1 
ATOM   6603 C  CG2   . ILE D 2 7   ? 131.466 165.452 111.129 1.00 44.11  ? 7   ILE D CG2   1 
ATOM   6604 C  CD1   . ILE D 2 7   ? 129.657 162.864 109.743 1.00 46.24  ? 7   ILE D CD1   1 
ATOM   6605 N  N     . LYS D 2 8   ? 129.958 168.533 111.650 1.00 41.52  ? 8   LYS D N     1 
ATOM   6606 C  CA    . LYS D 2 8   ? 130.454 169.902 111.534 1.00 44.92  ? 8   LYS D CA    1 
ATOM   6607 C  C     . LYS D 2 8   ? 131.697 170.060 112.397 1.00 50.75  ? 8   LYS D C     1 
ATOM   6608 O  O     . LYS D 2 8   ? 131.593 170.096 113.628 1.00 55.64  ? 8   LYS D O     1 
ATOM   6609 C  CB    . LYS D 2 8   ? 129.383 170.913 111.943 1.00 46.59  ? 8   LYS D CB    1 
ATOM   6610 C  CG    . LYS D 2 8   ? 128.092 170.825 111.146 1.00 52.39  ? 8   LYS D CG    1 
ATOM   6611 C  CD    . LYS D 2 8   ? 126.871 171.100 112.011 1.00 49.95  ? 8   LYS D CD    1 
ATOM   6612 C  CE    . LYS D 2 8   ? 126.861 170.237 113.264 1.00 52.73  ? 8   LYS D CE    1 
ATOM   6613 N  NZ    . LYS D 2 8   ? 126.078 168.986 113.081 1.00 52.75  ? 8   LYS D NZ    1 
ATOM   6614 N  N     . ASN D 2 9   ? 132.860 170.153 111.737 1.00 45.80  ? 9   ASN D N     1 
ATOM   6615 C  CA    . ASN D 2 9   ? 134.142 170.543 112.342 1.00 40.37  ? 9   ASN D CA    1 
ATOM   6616 C  C     . ASN D 2 9   ? 134.561 169.609 113.475 1.00 40.04  ? 9   ASN D C     1 
ATOM   6617 O  O     . ASN D 2 9   ? 135.060 170.044 114.514 1.00 47.49  ? 9   ASN D O     1 
ATOM   6618 C  CB    . ASN D 2 9   ? 134.098 171.993 112.828 1.00 42.07  ? 9   ASN D CB    1 
ATOM   6619 C  CG    . ASN D 2 9   ? 133.835 172.977 111.708 1.00 45.74  ? 9   ASN D CG    1 
ATOM   6620 O  OD1   . ASN D 2 9   ? 132.844 173.705 111.726 1.00 44.33  ? 9   ASN D OD1   1 
ATOM   6621 N  ND2   . ASN D 2 9   ? 134.728 173.007 110.725 1.00 50.56  ? 9   ASN D ND2   1 
ATOM   6622 N  N     . VAL D 2 10  ? 134.356 168.311 113.276 1.00 35.83  ? 10  VAL D N     1 
ATOM   6623 C  CA    . VAL D 2 10  ? 134.622 167.335 114.326 1.00 37.94  ? 10  VAL D CA    1 
ATOM   6624 C  C     . VAL D 2 10  ? 136.124 167.096 114.421 1.00 40.31  ? 10  VAL D C     1 
ATOM   6625 O  O     . VAL D 2 10  ? 136.795 166.825 113.417 1.00 44.04  ? 10  VAL D O     1 
ATOM   6626 C  CB    . VAL D 2 10  ? 133.837 166.034 114.072 1.00 39.11  ? 10  VAL D CB    1 
ATOM   6627 C  CG1   . VAL D 2 10  ? 134.525 164.819 114.690 1.00 38.74  ? 10  VAL D CG1   1 
ATOM   6628 C  CG2   . VAL D 2 10  ? 132.434 166.172 114.633 1.00 38.85  ? 10  VAL D CG2   1 
ATOM   6629 N  N     . THR D 2 11  ? 136.666 167.237 115.635 1.00 36.91  ? 11  THR D N     1 
ATOM   6630 C  CA    . THR D 2 11  ? 138.091 167.031 115.922 1.00 33.84  ? 11  THR D CA    1 
ATOM   6631 C  C     . THR D 2 11  ? 138.170 166.089 117.083 1.00 32.89  ? 11  THR D C     1 
ATOM   6632 O  O     . THR D 2 11  ? 137.354 166.212 117.947 1.00 48.92  ? 11  THR D O     1 
ATOM   6633 C  CB    . THR D 2 11  ? 138.793 168.361 116.220 1.00 39.15  ? 11  THR D CB    1 
ATOM   6634 O  OG1   . THR D 2 11  ? 139.076 169.014 114.992 1.00 47.60  ? 11  THR D OG1   1 
ATOM   6635 C  CG2   . THR D 2 11  ? 140.115 168.182 116.938 1.00 37.54  ? 11  THR D CG2   1 
ATOM   6636 N  N     . LYS D 2 12  ? 139.030 165.096 117.027 1.00 32.11  ? 12  LYS D N     1 
ATOM   6637 C  CA    . LYS D 2 12  ? 139.278 164.193 118.155 1.00 31.66  ? 12  LYS D CA    1 
ATOM   6638 C  C     . LYS D 2 12  ? 140.761 164.327 118.482 1.00 33.22  ? 12  LYS D C     1 
ATOM   6639 O  O     . LYS D 2 12  ? 141.548 164.051 117.605 1.00 41.82  ? 12  LYS D O     1 
ATOM   6640 C  CB    . LYS D 2 12  ? 138.929 162.731 117.863 1.00 32.80  ? 12  LYS D CB    1 
ATOM   6641 C  CG    . LYS D 2 12  ? 139.113 161.746 118.991 1.00 27.45  ? 12  LYS D CG    1 
ATOM   6642 C  CD    . LYS D 2 12  ? 137.928 161.752 119.939 1.00 28.39  ? 12  LYS D CD    1 
ATOM   6643 C  CE    . LYS D 2 12  ? 138.333 161.522 121.343 1.00 26.97  ? 12  LYS D CE    1 
ATOM   6644 N  NZ    . LYS D 2 12  ? 137.163 161.427 122.204 1.00 30.41  ? 12  LYS D NZ    1 
ATOM   6645 N  N     . GLU D 2 13  ? 141.089 164.619 119.726 1.00 42.31  ? 13  GLU D N     1 
ATOM   6646 C  CA    . GLU D 2 13  ? 142.478 164.826 120.177 1.00 37.29  ? 13  GLU D CA    1 
ATOM   6647 C  C     . GLU D 2 13  ? 142.752 163.836 121.298 1.00 36.93  ? 13  GLU D C     1 
ATOM   6648 O  O     . GLU D 2 13  ? 141.836 163.541 122.024 1.00 37.11  ? 13  GLU D O     1 
ATOM   6649 C  CB    . GLU D 2 13  ? 142.727 166.250 120.656 1.00 35.34  ? 13  GLU D CB    1 
ATOM   6650 C  CG    . GLU D 2 13  ? 142.112 167.308 119.755 1.00 45.35  ? 13  GLU D CG    1 
ATOM   6651 C  CD    . GLU D 2 13  ? 142.443 168.720 120.193 1.00 52.34  ? 13  GLU D CD    1 
ATOM   6652 O  OE1   . GLU D 2 13  ? 143.452 168.876 120.903 1.00 52.19  ? 13  GLU D OE1   1 
ATOM   6653 O  OE2   . GLU D 2 13  ? 141.705 169.660 119.827 1.00 54.41  ? 13  GLU D OE2   1 
ATOM   6654 N  N     . TYR D 2 14  ? 143.943 163.269 121.332 1.00 33.28  ? 14  TYR D N     1 
ATOM   6655 C  CA    . TYR D 2 14  ? 144.340 162.352 122.421 1.00 27.51  ? 14  TYR D CA    1 
ATOM   6656 C  C     . TYR D 2 14  ? 145.625 162.828 123.021 1.00 30.44  ? 14  TYR D C     1 
ATOM   6657 O  O     . TYR D 2 14  ? 146.539 163.163 122.288 1.00 31.94  ? 14  TYR D O     1 
ATOM   6658 C  CB    . TYR D 2 14  ? 144.479 160.926 121.904 1.00 28.95  ? 14  TYR D CB    1 
ATOM   6659 C  CG    . TYR D 2 14  ? 143.207 160.224 121.484 1.00 26.16  ? 14  TYR D CG    1 
ATOM   6660 C  CD1   . TYR D 2 14  ? 142.294 159.789 122.429 1.00 22.72  ? 14  TYR D CD1   1 
ATOM   6661 C  CD2   . TYR D 2 14  ? 142.964 159.946 120.148 1.00 26.53  ? 14  TYR D CD2   1 
ATOM   6662 C  CE1   . TYR D 2 14  ? 141.146 159.125 122.052 1.00 24.35  ? 14  TYR D CE1   1 
ATOM   6663 C  CE2   . TYR D 2 14  ? 141.825 159.274 119.760 1.00 20.77  ? 14  TYR D CE2   1 
ATOM   6664 C  CZ    . TYR D 2 14  ? 140.921 158.861 120.717 1.00 22.72  ? 14  TYR D CZ    1 
ATOM   6665 O  OH    . TYR D 2 14  ? 139.804 158.196 120.343 1.00 32.00  ? 14  TYR D OH    1 
ATOM   6666 N  N     . ARG D 2 15  ? 145.683 162.927 124.338 1.00 48.65  ? 15  ARG D N     1 
ATOM   6667 C  CA    . ARG D 2 15  ? 146.963 163.287 125.019 1.00 42.94  ? 15  ARG D CA    1 
ATOM   6668 C  C     . ARG D 2 15  ? 147.897 162.076 124.999 1.00 37.79  ? 15  ARG D C     1 
ATOM   6669 O  O     . ARG D 2 15  ? 147.446 160.979 125.241 1.00 42.56  ? 15  ARG D O     1 
ATOM   6670 C  CB    . ARG D 2 15  ? 146.739 164.009 126.356 1.00 43.81  ? 15  ARG D CB    1 
ATOM   6671 C  CG    . ARG D 2 15  ? 145.980 165.322 126.273 1.00 47.19  ? 15  ARG D CG    1 
ATOM   6672 C  CD    . ARG D 2 15  ? 146.866 166.488 125.929 1.00 43.34  ? 15  ARG D CD    1 
ATOM   6673 N  NE    . ARG D 2 15  ? 146.909 167.484 127.003 1.00 54.79  ? 15  ARG D NE    1 
ATOM   6674 C  CZ    . ARG D 2 15  ? 147.465 168.677 126.873 1.00 55.91  ? 15  ARG D CZ    1 
ATOM   6675 N  NH1   . ARG D 2 15  ? 147.230 169.394 125.788 1.00 51.56  ? 15  ARG D NH1   1 
ATOM   6676 N  NH2   . ARG D 2 15  ? 148.255 169.149 127.818 1.00 49.38  ? 15  ARG D NH2   1 
ATOM   6677 N  N     . ILE D 2 16  ? 149.159 162.309 124.726 1.00 41.13  ? 16  ILE D N     1 
ATOM   6678 C  CA    . ILE D 2 16  ? 150.129 161.203 124.520 1.00 39.57  ? 16  ILE D CA    1 
ATOM   6679 C  C     . ILE D 2 16  ? 151.189 161.245 125.623 1.00 38.12  ? 16  ILE D C     1 
ATOM   6680 O  O     . ILE D 2 16  ? 151.868 162.270 125.738 1.00 43.13  ? 16  ILE D O     1 
ATOM   6681 C  CB    . ILE D 2 16  ? 150.733 161.283 123.095 1.00 41.17  ? 16  ILE D CB    1 
ATOM   6682 C  CG1   . ILE D 2 16  ? 149.702 161.010 122.001 1.00 38.66  ? 16  ILE D CG1   1 
ATOM   6683 C  CG2   . ILE D 2 16  ? 151.953 160.378 122.943 1.00 38.80  ? 16  ILE D CG2   1 
ATOM   6684 C  CD1   . ILE D 2 16  ? 149.107 159.616 122.023 1.00 38.99  ? 16  ILE D CD1   1 
ATOM   6685 N  N     . TYR D 2 17  ? 151.351 160.163 126.361 1.00 41.46  ? 17  TYR D N     1 
ATOM   6686 C  CA    . TYR D 2 17  ? 152.256 160.069 127.496 1.00 43.98  ? 17  TYR D CA    1 
ATOM   6687 C  C     . TYR D 2 17  ? 153.200 158.891 127.313 1.00 46.14  ? 17  TYR D C     1 
ATOM   6688 O  O     . TYR D 2 17  ? 152.849 157.880 126.699 1.00 50.57  ? 17  TYR D O     1 
ATOM   6689 C  CB    . TYR D 2 17  ? 151.507 159.902 128.828 1.00 41.83  ? 17  TYR D CB    1 
ATOM   6690 C  CG    . TYR D 2 17  ? 150.392 160.889 129.055 1.00 43.34  ? 17  TYR D CG    1 
ATOM   6691 C  CD1   . TYR D 2 17  ? 150.659 162.246 129.186 1.00 44.22  ? 17  TYR D CD1   1 
ATOM   6692 C  CD2   . TYR D 2 17  ? 149.073 160.466 129.149 1.00 39.91  ? 17  TYR D CD2   1 
ATOM   6693 C  CE1   . TYR D 2 17  ? 149.642 163.154 129.395 1.00 40.60  ? 17  TYR D CE1   1 
ATOM   6694 C  CE2   . TYR D 2 17  ? 148.049 161.367 129.358 1.00 36.86  ? 17  TYR D CE2   1 
ATOM   6695 C  CZ    . TYR D 2 17  ? 148.341 162.708 129.483 1.00 40.94  ? 17  TYR D CZ    1 
ATOM   6696 O  OH    . TYR D 2 17  ? 147.325 163.610 129.694 1.00 53.41  ? 17  TYR D OH    1 
ATOM   6697 N  N     . ARG D 2 18  ? 154.405 159.032 127.860 1.00 48.86  ? 18  ARG D N     1 
ATOM   6698 C  CA    . ARG D 2 18  ? 155.369 157.944 127.911 1.00 52.71  ? 18  ARG D CA    1 
ATOM   6699 C  C     . ARG D 2 18  ? 155.556 157.371 129.306 1.00 54.62  ? 18  ARG D C     1 
ATOM   6700 O  O     . ARG D 2 18  ? 155.701 156.155 129.445 1.00 54.01  ? 18  ARG D O     1 
ATOM   6701 C  CB    . ARG D 2 18  ? 156.729 158.408 127.376 1.00 52.80  ? 18  ARG D CB    1 
ATOM   6702 C  CG    . ARG D 2 18  ? 156.655 159.093 126.023 1.00 51.51  ? 18  ARG D CG    1 
ATOM   6703 C  CD    . ARG D 2 18  ? 156.736 158.090 124.884 1.00 49.84  ? 18  ARG D CD    1 
ATOM   6704 N  NE    . ARG D 2 18  ? 158.111 157.844 124.467 1.00 55.09  ? 18  ARG D NE    1 
ATOM   6705 C  CZ    . ARG D 2 18  ? 158.640 158.282 123.333 1.00 54.47  ? 18  ARG D CZ    1 
ATOM   6706 N  NH1   . ARG D 2 18  ? 157.936 159.001 122.475 1.00 50.96  ? 18  ARG D NH1   1 
ATOM   6707 N  NH2   . ARG D 2 18  ? 159.906 157.992 123.052 1.00 51.26  ? 18  ARG D NH2   1 
ATOM   6708 N  N     . THR D 2 19  ? 155.557 158.212 130.337 1.00 57.63  ? 19  THR D N     1 
ATOM   6709 C  CA    . THR D 2 19  ? 155.695 157.772 131.717 1.00 56.09  ? 19  THR D CA    1 
ATOM   6710 C  C     . THR D 2 19  ? 154.433 158.124 132.493 1.00 55.94  ? 19  THR D C     1 
ATOM   6711 O  O     . THR D 2 19  ? 153.566 158.857 132.013 1.00 60.94  ? 19  THR D O     1 
ATOM   6712 C  CB    . THR D 2 19  ? 156.913 158.413 132.410 1.00 59.75  ? 19  THR D CB    1 
ATOM   6713 O  OG1   . THR D 2 19  ? 156.569 159.724 132.868 1.00 60.89  ? 19  THR D OG1   1 
ATOM   6714 C  CG2   . THR D 2 19  ? 158.096 158.512 131.458 1.00 55.65  ? 19  THR D CG2   1 
ATOM   6715 N  N     . ASN D 2 20  ? 154.338 157.581 133.711 1.00 53.36  ? 20  ASN D N     1 
ATOM   6716 C  CA    . ASN D 2 20  ? 153.237 157.940 134.599 1.00 52.83  ? 20  ASN D CA    1 
ATOM   6717 C  C     . ASN D 2 20  ? 153.426 159.332 135.186 1.00 55.94  ? 20  ASN D C     1 
ATOM   6718 O  O     . ASN D 2 20  ? 152.449 159.964 135.611 1.00 58.44  ? 20  ASN D O     1 
ATOM   6719 C  CB    . ASN D 2 20  ? 153.107 156.909 135.720 1.00 54.51  ? 20  ASN D CB    1 
ATOM   6720 C  CG    . ASN D 2 20  ? 151.853 156.070 135.599 1.00 57.16  ? 20  ASN D CG    1 
ATOM   6721 O  OD1   . ASN D 2 20  ? 150.771 156.585 135.324 1.00 57.92  ? 20  ASN D OD1   1 
ATOM   6722 N  ND2   . ASN D 2 20  ? 151.993 154.766 135.807 1.00 56.91  ? 20  ASN D ND2   1 
ATOM   6723 N  N     . LYS D 2 21  ? 154.671 159.815 135.225 1.00 56.44  ? 21  LYS D N     1 
ATOM   6724 C  CA    . LYS D 2 21  ? 154.953 161.151 135.742 1.00 57.13  ? 21  LYS D CA    1 
ATOM   6725 C  C     . LYS D 2 21  ? 154.371 162.230 134.835 1.00 59.25  ? 21  LYS D C     1 
ATOM   6726 O  O     . LYS D 2 21  ? 153.836 163.233 135.321 1.00 59.34  ? 21  LYS D O     1 
ATOM   6727 C  CB    . LYS D 2 21  ? 156.465 161.324 135.908 1.00 60.29  ? 21  LYS D CB    1 
ATOM   6728 C  CG    . LYS D 2 21  ? 156.929 162.726 136.266 1.00 59.92  ? 21  LYS D CG    1 
ATOM   6729 C  CD    . LYS D 2 21  ? 158.378 162.937 135.857 1.00 61.17  ? 21  LYS D CD    1 
ATOM   6730 C  CE    . LYS D 2 21  ? 158.541 164.189 135.013 1.00 65.38  ? 21  LYS D CE    1 
ATOM   6731 N  NZ    . LYS D 2 21  ? 158.033 163.999 133.626 1.00 62.78  ? 21  LYS D NZ    1 
ATOM   6732 N  N     . GLU D 2 22  ? 154.446 162.028 133.515 1.00 58.28  ? 22  GLU D N     1 
ATOM   6733 C  CA    . GLU D 2 22  ? 153.854 162.978 132.574 1.00 54.87  ? 22  GLU D CA    1 
ATOM   6734 C  C     . GLU D 2 22  ? 152.334 162.991 132.677 1.00 54.38  ? 22  GLU D C     1 
ATOM   6735 O  O     . GLU D 2 22  ? 151.710 164.054 132.585 1.00 57.41  ? 22  GLU D O     1 
ATOM   6736 C  CB    . GLU D 2 22  ? 154.284 162.644 131.145 1.00 58.05  ? 22  GLU D CB    1 
ATOM   6737 C  CG    . GLU D 2 22  ? 155.762 162.341 130.985 1.00 58.51  ? 22  GLU D CG    1 
ATOM   6738 C  CD    . GLU D 2 22  ? 156.096 161.790 129.613 1.00 60.91  ? 22  GLU D CD    1 
ATOM   6739 O  OE1   . GLU D 2 22  ? 155.156 161.456 128.862 1.00 59.75  ? 22  GLU D OE1   1 
ATOM   6740 O  OE2   . GLU D 2 22  ? 157.296 161.688 129.286 1.00 60.20  ? 22  GLU D OE2   1 
ATOM   6741 N  N     . ARG D 2 23  ? 151.746 161.796 132.753 1.00 46.05  ? 23  ARG D N     1 
ATOM   6742 C  CA    . ARG D 2 23  ? 150.280 161.661 132.917 1.00 46.22  ? 23  ARG D CA    1 
ATOM   6743 C  C     . ARG D 2 23  ? 149.811 162.402 134.175 1.00 52.93  ? 23  ARG D C     1 
ATOM   6744 O  O     . ARG D 2 23  ? 148.801 163.108 134.065 1.00 58.16  ? 23  ARG D O     1 
ATOM   6745 C  CB    . ARG D 2 23  ? 149.923 160.177 132.892 1.00 48.12  ? 23  ARG D CB    1 
ATOM   6746 C  CG    . ARG D 2 23  ? 148.437 159.888 132.798 1.00 50.21  ? 23  ARG D CG    1 
ATOM   6747 C  CD    . ARG D 2 23  ? 148.238 158.415 132.582 1.00 52.33  ? 23  ARG D CD    1 
ATOM   6748 N  NE    . ARG D 2 23  ? 148.074 157.792 133.897 1.00 54.93  ? 23  ARG D NE    1 
ATOM   6749 C  CZ    . ARG D 2 23  ? 147.135 156.922 134.209 1.00 53.66  ? 23  ARG D CZ    1 
ATOM   6750 N  NH1   . ARG D 2 23  ? 145.864 157.203 133.995 1.00 48.18  ? 23  ARG D NH1   1 
ATOM   6751 N  NH2   . ARG D 2 23  ? 147.485 155.761 134.719 1.00 54.74  ? 23  ARG D NH2   1 
ATOM   6752 N  N     . MET D 2 24  ? 150.471 162.205 135.317 1.00 59.95  ? 24  MET D N     1 
ATOM   6753 C  CA    . MET D 2 24  ? 150.168 162.887 136.605 1.00 59.22  ? 24  MET D CA    1 
ATOM   6754 C  C     . MET D 2 24  ? 150.388 164.405 136.546 1.00 59.39  ? 24  MET D C     1 
ATOM   6755 O  O     . MET D 2 24  ? 149.507 165.121 137.018 1.00 60.14  ? 24  MET D O     1 
ATOM   6756 C  CB    . MET D 2 24  ? 151.033 162.328 137.727 1.00 60.81  ? 24  MET D CB    1 
ATOM   6757 C  CG    . MET D 2 24  ? 150.540 162.703 139.101 1.00 63.90  ? 24  MET D CG    1 
ATOM   6758 S  SD    . MET D 2 24  ? 149.557 161.381 139.830 1.00 74.27  ? 24  MET D SD    1 
ATOM   6759 C  CE    . MET D 2 24  ? 150.886 160.201 140.092 1.00 60.48  ? 24  MET D CE    1 
ATOM   6760 N  N     . LYS D 2 25  ? 151.452 164.881 135.901 1.00 58.16  ? 25  LYS D N     1 
ATOM   6761 C  CA    . LYS D 2 25  ? 151.576 166.354 135.764 1.00 61.22  ? 25  LYS D CA    1 
ATOM   6762 C  C     . LYS D 2 25  ? 150.414 166.941 134.938 1.00 63.12  ? 25  LYS D C     1 
ATOM   6763 O  O     . LYS D 2 25  ? 149.903 167.986 135.321 1.00 63.81  ? 25  LYS D O     1 
ATOM   6764 C  CB    . LYS D 2 25  ? 152.909 166.746 135.127 1.00 60.77  ? 25  LYS D CB    1 
ATOM   6765 C  CG    . LYS D 2 25  ? 154.008 167.040 136.126 1.00 63.09  ? 25  LYS D CG    1 
ATOM   6766 C  CD    . LYS D 2 25  ? 155.220 166.145 135.911 1.00 63.53  ? 25  LYS D CD    1 
ATOM   6767 C  CE    . LYS D 2 25  ? 155.656 166.180 134.489 1.00 66.09  ? 25  LYS D CE    1 
ATOM   6768 N  NZ    . LYS D 2 25  ? 156.846 167.024 134.356 1.00 64.80  ? 25  LYS D NZ    1 
ATOM   6769 N  N     . ASP D 2 26  ? 150.009 166.292 133.856 1.00 59.22  ? 26  ASP D N     1 
ATOM   6770 C  CA    . ASP D 2 26  ? 148.923 166.828 133.006 1.00 61.37  ? 26  ASP D CA    1 
ATOM   6771 C  C     . ASP D 2 26  ? 147.627 166.878 133.804 1.00 60.01  ? 26  ASP D C     1 
ATOM   6772 O  O     . ASP D 2 26  ? 146.892 167.865 133.668 1.00 58.66  ? 26  ASP D O     1 
ATOM   6773 C  CB    . ASP D 2 26  ? 148.818 166.032 131.713 1.00 59.93  ? 26  ASP D CB    1 
ATOM   6774 C  CG    . ASP D 2 26  ? 148.163 166.738 130.542 1.00 60.12  ? 26  ASP D CG    1 
ATOM   6775 O  OD1   . ASP D 2 26  ? 148.888 167.368 129.769 1.00 61.08  ? 26  ASP D OD1   1 
ATOM   6776 O  OD2   . ASP D 2 26  ? 146.936 166.639 130.414 1.00 63.20  ? 26  ASP D OD2   1 
ATOM   6777 N  N     . ALA D 2 27  ? 147.357 165.843 134.590 1.00 65.28  ? 27  ALA D N     1 
ATOM   6778 C  CA    . ALA D 2 27  ? 146.157 165.789 135.454 1.00 65.59  ? 27  ALA D CA    1 
ATOM   6779 C  C     . ALA D 2 27  ? 146.173 166.863 136.535 1.00 67.32  ? 27  ALA D C     1 
ATOM   6780 O  O     . ALA D 2 27  ? 145.122 167.466 136.788 1.00 66.36  ? 27  ALA D O     1 
ATOM   6781 C  CB    . ALA D 2 27  ? 146.088 164.426 136.059 1.00 62.65  ? 27  ALA D CB    1 
ATOM   6782 N  N     . LEU D 2 28  ? 147.329 167.123 137.128 1.00 73.59  ? 28  LEU D N     1 
ATOM   6783 C  CA    . LEU D 2 28  ? 147.379 168.003 138.321 1.00 71.38  ? 28  LEU D CA    1 
ATOM   6784 C  C     . LEU D 2 28  ? 147.722 169.462 138.029 1.00 73.66  ? 28  LEU D C     1 
ATOM   6785 O  O     . LEU D 2 28  ? 147.579 170.264 138.960 1.00 77.16  ? 28  LEU D O     1 
ATOM   6786 C  CB    . LEU D 2 28  ? 148.433 167.344 139.210 1.00 71.84  ? 28  LEU D CB    1 
ATOM   6787 C  CG    . LEU D 2 28  ? 148.002 166.037 139.879 1.00 72.85  ? 28  LEU D CG    1 
ATOM   6788 C  CD1   . LEU D 2 28  ? 148.937 165.644 141.003 1.00 72.28  ? 28  LEU D CD1   1 
ATOM   6789 C  CD2   . LEU D 2 28  ? 146.570 166.111 140.371 1.00 70.04  ? 28  LEU D CD2   1 
ATOM   6790 N  N     . ILE D 2 29  ? 148.155 169.811 136.828 1.00 76.98  ? 29  ILE D N     1 
ATOM   6791 C  CA    . ILE D 2 29  ? 148.620 171.210 136.560 1.00 77.72  ? 29  ILE D CA    1 
ATOM   6792 C  C     . ILE D 2 29  ? 147.670 171.813 135.525 1.00 80.22  ? 29  ILE D C     1 
ATOM   6793 O  O     . ILE D 2 29  ? 147.518 171.211 134.446 1.00 78.55  ? 29  ILE D O     1 
ATOM   6794 C  CB    . ILE D 2 29  ? 150.097 171.248 136.145 1.00 75.30  ? 29  ILE D CB    1 
ATOM   6795 C  CG1   . ILE D 2 29  ? 150.993 170.602 137.193 1.00 74.22  ? 29  ILE D CG1   1 
ATOM   6796 C  CG2   . ILE D 2 29  ? 150.545 172.669 135.810 1.00 76.09  ? 29  ILE D CG2   1 
ATOM   6797 C  CD1   . ILE D 2 29  ? 152.452 170.529 136.786 1.00 77.95  ? 29  ILE D CD1   1 
ATOM   6798 N  N     . PRO D 2 30  ? 147.027 172.964 135.806 1.00 86.60  ? 30  PRO D N     1 
ATOM   6799 C  CA    . PRO D 2 30  ? 145.957 173.512 134.952 1.00 85.76  ? 30  PRO D CA    1 
ATOM   6800 C  C     . PRO D 2 30  ? 146.427 173.988 133.586 1.00 85.48  ? 30  PRO D C     1 
ATOM   6801 O  O     . PRO D 2 30  ? 145.619 174.032 132.650 1.00 85.73  ? 30  PRO D O     1 
ATOM   6802 C  CB    . PRO D 2 30  ? 145.409 174.679 135.790 1.00 84.80  ? 30  PRO D CB    1 
ATOM   6803 C  CG    . PRO D 2 30  ? 145.872 174.411 137.190 1.00 85.44  ? 30  PRO D CG    1 
ATOM   6804 C  CD    . PRO D 2 30  ? 147.200 173.746 137.040 1.00 83.93  ? 30  PRO D CD    1 
ATOM   6805 N  N     . LYS D 2 31  ? 147.699 174.346 133.437 1.00 80.59  ? 31  LYS D N     1 
ATOM   6806 C  CA    . LYS D 2 31  ? 148.226 174.862 132.175 1.00 81.70  ? 31  LYS D CA    1 
ATOM   6807 C  C     . LYS D 2 31  ? 149.455 174.071 131.746 1.00 82.66  ? 31  LYS D C     1 
ATOM   6808 O  O     . LYS D 2 31  ? 150.470 174.625 131.322 1.00 82.34  ? 31  LYS D O     1 
ATOM   6809 C  CB    . LYS D 2 31  ? 148.551 176.349 132.285 1.00 82.86  ? 31  LYS D CB    1 
ATOM   6810 C  CG    . LYS D 2 31  ? 147.329 177.254 132.306 1.00 83.75  ? 31  LYS D CG    1 
ATOM   6811 C  CD    . LYS D 2 31  ? 147.487 178.373 133.323 1.00 81.81  ? 31  LYS D CD    1 
ATOM   6812 C  CE    . LYS D 2 31  ? 146.217 179.202 133.436 1.00 82.72  ? 31  LYS D CE    1 
ATOM   6813 N  NZ    . LYS D 2 31  ? 145.767 179.720 132.114 1.00 81.72  ? 31  LYS D NZ    1 
ATOM   6814 N  N     . HIS D 2 32  ? 149.369 172.748 131.851 1.00 70.77  ? 32  HIS D N     1 
ATOM   6815 C  CA    . HIS D 2 32  ? 150.469 171.883 131.450 1.00 66.44  ? 32  HIS D CA    1 
ATOM   6816 C  C     . HIS D 2 32  ? 150.438 171.661 129.943 1.00 66.79  ? 32  HIS D C     1 
ATOM   6817 O  O     . HIS D 2 32  ? 149.383 171.375 129.370 1.00 67.84  ? 32  HIS D O     1 
ATOM   6818 C  CB    . HIS D 2 32  ? 150.391 170.545 132.186 1.00 66.37  ? 32  HIS D CB    1 
ATOM   6819 C  CG    . HIS D 2 32  ? 151.496 169.598 131.839 1.00 66.25  ? 32  HIS D CG    1 
ATOM   6820 N  ND1   . HIS D 2 32  ? 152.775 169.736 132.331 1.00 70.07  ? 32  HIS D ND1   1 
ATOM   6821 C  CD2   . HIS D 2 32  ? 151.511 168.494 131.055 1.00 63.79  ? 32  HIS D CD2   1 
ATOM   6822 C  CE1   . HIS D 2 32  ? 153.533 168.761 131.860 1.00 67.75  ? 32  HIS D CE1   1 
ATOM   6823 N  NE2   . HIS D 2 32  ? 152.789 167.993 131.085 1.00 64.48  ? 32  HIS D NE2   1 
ATOM   6824 N  N     . LYS D 2 33  ? 151.597 171.799 129.305 1.00 64.30  ? 33  LYS D N     1 
ATOM   6825 C  CA    . LYS D 2 33  ? 151.722 171.587 127.870 1.00 61.47  ? 33  LYS D CA    1 
ATOM   6826 C  C     . LYS D 2 33  ? 152.230 170.174 127.613 1.00 60.31  ? 33  LYS D C     1 
ATOM   6827 O  O     . LYS D 2 33  ? 153.195 169.730 128.244 1.00 61.70  ? 33  LYS D O     1 
ATOM   6828 C  CB    . LYS D 2 33  ? 152.665 172.621 127.253 1.00 60.85  ? 33  LYS D CB    1 
ATOM   6829 C  CG    . LYS D 2 33  ? 152.022 173.981 127.038 1.00 60.81  ? 33  LYS D CG    1 
ATOM   6830 C  CD    . LYS D 2 33  ? 151.899 174.312 125.563 1.00 63.74  ? 33  LYS D CD    1 
ATOM   6831 C  CE    . LYS D 2 33  ? 151.707 175.803 125.346 1.00 65.03  ? 33  LYS D CE    1 
ATOM   6832 N  NZ    . LYS D 2 33  ? 150.853 176.415 126.401 1.00 64.64  ? 33  LYS D NZ    1 
ATOM   6833 N  N     . ASN D 2 34  ? 151.580 169.475 126.688 1.00 58.85  ? 34  ASN D N     1 
ATOM   6834 C  CA    . ASN D 2 34  ? 151.842 168.061 126.463 1.00 54.29  ? 34  ASN D CA    1 
ATOM   6835 C  C     . ASN D 2 34  ? 151.660 167.741 124.988 1.00 53.06  ? 34  ASN D C     1 
ATOM   6836 O  O     . ASN D 2 34  ? 151.050 168.504 124.234 1.00 51.63  ? 34  ASN D O     1 
ATOM   6837 C  CB    . ASN D 2 34  ? 150.917 167.189 127.322 1.00 51.41  ? 34  ASN D CB    1 
ATOM   6838 C  CG    . ASN D 2 34  ? 151.487 165.814 127.591 1.00 51.64  ? 34  ASN D CG    1 
ATOM   6839 O  OD1   . ASN D 2 34  ? 151.226 164.868 126.852 1.00 51.46  ? 34  ASN D OD1   1 
ATOM   6840 N  ND2   . ASN D 2 34  ? 152.276 165.697 128.650 1.00 56.51  ? 34  ASN D ND2   1 
ATOM   6841 N  N     . LYS D 2 35  ? 152.208 166.597 124.582 1.00 49.41  ? 35  LYS D N     1 
ATOM   6842 C  CA    . LYS D 2 35  ? 152.045 166.127 123.214 1.00 47.00  ? 35  LYS D CA    1 
ATOM   6843 C  C     . LYS D 2 35  ? 150.610 165.676 122.976 1.00 47.83  ? 35  LYS D C     1 
ATOM   6844 O  O     . LYS D 2 35  ? 150.047 164.909 123.762 1.00 48.13  ? 35  LYS D O     1 
ATOM   6845 C  CB    . LYS D 2 35  ? 153.013 164.980 122.934 1.00 42.41  ? 35  LYS D CB    1 
ATOM   6846 C  CG    . LYS D 2 35  ? 153.001 164.501 121.498 1.00 45.60  ? 35  LYS D CG    1 
ATOM   6847 C  CD    . LYS D 2 35  ? 154.340 164.736 120.835 1.00 48.17  ? 35  LYS D CD    1 
ATOM   6848 C  CE    . LYS D 2 35  ? 155.268 163.564 121.071 1.00 49.92  ? 35  LYS D CE    1 
ATOM   6849 N  NZ    . LYS D 2 35  ? 156.672 163.873 120.688 1.00 49.99  ? 35  LYS D NZ    1 
ATOM   6850 N  N     . THR D 2 36  ? 150.022 166.154 121.885 1.00 43.13  ? 36  THR D N     1 
ATOM   6851 C  CA    . THR D 2 36  ? 148.643 165.848 121.541 1.00 37.81  ? 36  THR D CA    1 
ATOM   6852 C  C     . THR D 2 36  ? 148.589 165.264 120.137 1.00 40.52  ? 36  THR D C     1 
ATOM   6853 O  O     . THR D 2 36  ? 149.239 165.770 119.220 1.00 42.11  ? 36  THR D O     1 
ATOM   6854 C  CB    . THR D 2 36  ? 147.758 167.099 121.637 1.00 44.09  ? 36  THR D CB    1 
ATOM   6855 O  OG1   . THR D 2 36  ? 148.067 167.807 122.843 1.00 49.27  ? 36  THR D OG1   1 
ATOM   6856 C  CG2   . THR D 2 36  ? 146.287 166.723 121.651 1.00 37.10  ? 36  THR D CG2   1 
ATOM   6857 N  N     . PHE D 2 37  ? 147.812 164.196 119.980 1.00 37.07  ? 37  PHE D N     1 
ATOM   6858 C  CA    . PHE D 2 37  ? 147.663 163.498 118.712 1.00 27.63  ? 37  PHE D CA    1 
ATOM   6859 C  C     . PHE D 2 37  ? 146.271 163.759 118.158 1.00 28.52  ? 37  PHE D C     1 
ATOM   6860 O  O     . PHE D 2 37  ? 145.276 163.591 118.870 1.00 27.54  ? 37  PHE D O     1 
ATOM   6861 C  CB    . PHE D 2 37  ? 147.897 161.996 118.888 1.00 28.94  ? 37  PHE D CB    1 
ATOM   6862 C  CG    . PHE D 2 37  ? 147.637 161.191 117.652 1.00 31.98  ? 37  PHE D CG    1 
ATOM   6863 C  CD1   . PHE D 2 37  ? 148.489 161.278 116.563 1.00 27.81  ? 37  PHE D CD1   1 
ATOM   6864 C  CD2   . PHE D 2 37  ? 146.547 160.337 117.581 1.00 30.43  ? 37  PHE D CD2   1 
ATOM   6865 C  CE1   . PHE D 2 37  ? 148.257 160.533 115.424 1.00 25.12  ? 37  PHE D CE1   1 
ATOM   6866 C  CE2   . PHE D 2 37  ? 146.310 159.591 116.445 1.00 32.19  ? 37  PHE D CE2   1 
ATOM   6867 C  CZ    . PHE D 2 37  ? 147.165 159.689 115.367 1.00 28.57  ? 37  PHE D CZ    1 
ATOM   6868 N  N     . PHE D 2 38  ? 146.202 164.170 116.894 1.00 36.10  ? 38  PHE D N     1 
ATOM   6869 C  CA    . PHE D 2 38  ? 144.931 164.421 116.218 1.00 31.37  ? 38  PHE D CA    1 
ATOM   6870 C  C     . PHE D 2 38  ? 144.513 163.140 115.505 1.00 31.05  ? 38  PHE D C     1 
ATOM   6871 O  O     . PHE D 2 38  ? 145.013 162.816 114.428 1.00 35.79  ? 38  PHE D O     1 
ATOM   6872 C  CB    . PHE D 2 38  ? 145.048 165.581 115.236 1.00 32.63  ? 38  PHE D CB    1 
ATOM   6873 C  CG    . PHE D 2 38  ? 144.968 166.932 115.878 1.00 32.27  ? 38  PHE D CG    1 
ATOM   6874 C  CD1   . PHE D 2 38  ? 143.772 167.399 116.396 1.00 39.22  ? 38  PHE D CD1   1 
ATOM   6875 C  CD2   . PHE D 2 38  ? 146.084 167.748 115.941 1.00 39.52  ? 38  PHE D CD2   1 
ATOM   6876 C  CE1   . PHE D 2 38  ? 143.698 168.650 116.983 1.00 42.74  ? 38  PHE D CE1   1 
ATOM   6877 C  CE2   . PHE D 2 38  ? 146.009 168.999 116.523 1.00 43.17  ? 38  PHE D CE2   1 
ATOM   6878 C  CZ    . PHE D 2 38  ? 144.818 169.448 117.046 1.00 40.97  ? 38  PHE D CZ    1 
ATOM   6879 N  N     . ALA D 2 39  ? 143.594 162.397 116.124 1.00 32.87  ? 39  ALA D N     1 
ATOM   6880 C  CA    . ALA D 2 39  ? 142.977 161.273 115.432 1.00 29.82  ? 39  ALA D CA    1 
ATOM   6881 C  C     . ALA D 2 39  ? 142.081 161.761 114.302 1.00 32.49  ? 39  ALA D C     1 
ATOM   6882 O  O     . ALA D 2 39  ? 142.052 161.165 113.220 1.00 36.58  ? 39  ALA D O     1 
ATOM   6883 C  CB    . ALA D 2 39  ? 142.190 160.412 116.417 1.00 24.38  ? 39  ALA D CB    1 
ATOM   6884 N  N     . LEU D 2 40  ? 141.349 162.848 114.537 1.00 32.70  ? 40  LEU D N     1 
ATOM   6885 C  CA    . LEU D 2 40  ? 140.569 163.537 113.521 1.00 26.80  ? 40  LEU D CA    1 
ATOM   6886 C  C     . LEU D 2 40  ? 140.849 165.027 113.639 1.00 26.54  ? 40  LEU D C     1 
ATOM   6887 O  O     . LEU D 2 40  ? 141.127 165.525 114.733 1.00 39.25  ? 40  LEU D O     1 
ATOM   6888 C  CB    . LEU D 2 40  ? 139.071 163.261 113.681 1.00 32.13  ? 40  LEU D CB    1 
ATOM   6889 C  CG    . LEU D 2 40  ? 138.586 161.856 113.318 1.00 30.13  ? 40  LEU D CG    1 
ATOM   6890 C  CD1   . LEU D 2 40  ? 137.090 161.752 113.525 1.00 30.67  ? 40  LEU D CD1   1 
ATOM   6891 C  CD2   . LEU D 2 40  ? 138.955 161.501 111.888 1.00 24.53  ? 40  LEU D CD2   1 
ATOM   6892 N  N     . ASP D 2 41  ? 140.785 165.737 112.516 1.00 31.32  ? 41  ASP D N     1 
ATOM   6893 C  CA    . ASP D 2 41  ? 141.126 167.159 112.473 1.00 37.79  ? 41  ASP D CA    1 
ATOM   6894 C  C     . ASP D 2 41  ? 140.163 167.887 111.540 1.00 44.30  ? 41  ASP D C     1 
ATOM   6895 O  O     . ASP D 2 41  ? 140.380 167.909 110.324 1.00 45.32  ? 41  ASP D O     1 
ATOM   6896 C  CB    . ASP D 2 41  ? 142.573 167.354 112.032 1.00 41.49  ? 41  ASP D CB    1 
ATOM   6897 C  CG    . ASP D 2 41  ? 143.074 168.763 112.278 1.00 50.31  ? 41  ASP D CG    1 
ATOM   6898 O  OD1   . ASP D 2 41  ? 143.210 169.528 111.300 1.00 52.05  ? 41  ASP D OD1   1 
ATOM   6899 O  OD2   . ASP D 2 41  ? 143.331 169.109 113.449 1.00 47.70  ? 41  ASP D OD2   1 
ATOM   6900 N  N     . ASP D 2 42  ? 139.111 168.471 112.130 1.00 43.69  ? 42  ASP D N     1 
ATOM   6901 C  CA    . ASP D 2 42  ? 138.151 169.361 111.464 1.00 41.38  ? 42  ASP D CA    1 
ATOM   6902 C  C     . ASP D 2 42  ? 137.442 168.670 110.294 1.00 45.30  ? 42  ASP D C     1 
ATOM   6903 O  O     . ASP D 2 42  ? 137.565 169.065 109.132 1.00 53.31  ? 42  ASP D O     1 
ATOM   6904 C  CB    . ASP D 2 42  ? 138.829 170.661 111.016 1.00 41.16  ? 42  ASP D CB    1 
ATOM   6905 C  CG    . ASP D 2 42  ? 137.865 171.826 110.941 1.00 51.69  ? 42  ASP D CG    1 
ATOM   6906 O  OD1   . ASP D 2 42  ? 137.010 171.837 110.031 1.00 53.68  ? 42  ASP D OD1   1 
ATOM   6907 O  OD2   . ASP D 2 42  ? 137.965 172.736 111.790 1.00 54.32  ? 42  ASP D OD2   1 
ATOM   6908 N  N     . ILE D 2 43  ? 136.692 167.626 110.623 1.00 41.15  ? 43  ILE D N     1 
ATOM   6909 C  CA    . ILE D 2 43  ? 135.938 166.863 109.636 1.00 41.13  ? 43  ILE D CA    1 
ATOM   6910 C  C     . ILE D 2 43  ? 134.575 167.516 109.443 1.00 41.77  ? 43  ILE D C     1 
ATOM   6911 O  O     . ILE D 2 43  ? 133.849 167.758 110.413 1.00 42.94  ? 43  ILE D O     1 
ATOM   6912 C  CB    . ILE D 2 43  ? 135.791 165.396 110.070 1.00 44.34  ? 43  ILE D CB    1 
ATOM   6913 C  CG1   . ILE D 2 43  ? 137.161 164.795 110.401 1.00 37.12  ? 43  ILE D CG1   1 
ATOM   6914 C  CG2   . ILE D 2 43  ? 135.054 164.588 109.004 1.00 42.84  ? 43  ILE D CG2   1 
ATOM   6915 C  CD1   . ILE D 2 43  ? 137.987 164.416 109.191 1.00 44.38  ? 43  ILE D CD1   1 
ATOM   6916 N  N     . SER D 2 44  ? 134.226 167.801 108.190 1.00 43.51  ? 44  SER D N     1 
ATOM   6917 C  CA    . SER D 2 44  ? 132.937 168.401 107.861 1.00 41.70  ? 44  SER D CA    1 
ATOM   6918 C  C     . SER D 2 44  ? 132.370 167.700 106.634 1.00 42.62  ? 44  SER D C     1 
ATOM   6919 O  O     . SER D 2 44  ? 132.841 167.925 105.516 1.00 51.53  ? 44  SER D O     1 
ATOM   6920 C  CB    . SER D 2 44  ? 133.070 169.904 107.614 1.00 44.12  ? 44  SER D CB    1 
ATOM   6921 O  OG    . SER D 2 44  ? 133.179 170.612 108.834 1.00 44.75  ? 44  SER D OG    1 
ATOM   6922 N  N     . LEU D 2 45  ? 131.369 166.848 106.844 1.00 41.24  ? 45  LEU D N     1 
ATOM   6923 C  CA    . LEU D 2 45  ? 130.623 166.244 105.751 1.00 47.37  ? 45  LEU D CA    1 
ATOM   6924 C  C     . LEU D 2 45  ? 129.195 166.005 106.217 1.00 44.60  ? 45  LEU D C     1 
ATOM   6925 O  O     . LEU D 2 45  ? 128.948 165.758 107.398 1.00 46.64  ? 45  LEU D O     1 
ATOM   6926 C  CB    . LEU D 2 45  ? 131.268 164.935 105.265 1.00 48.43  ? 45  LEU D CB    1 
ATOM   6927 C  CG    . LEU D 2 45  ? 131.268 163.694 106.163 1.00 45.57  ? 45  LEU D CG    1 
ATOM   6928 C  CD1   . LEU D 2 45  ? 130.252 162.666 105.684 1.00 45.80  ? 45  LEU D CD1   1 
ATOM   6929 C  CD2   . LEU D 2 45  ? 132.655 163.081 106.221 1.00 48.12  ? 45  LEU D CD2   1 
ATOM   6930 N  N     . LYS D 2 46  ? 128.254 166.094 105.282 1.00 49.45  ? 46  LYS D N     1 
ATOM   6931 C  CA    . LYS D 2 46  ? 126.851 165.877 105.596 1.00 50.02  ? 46  LYS D CA    1 
ATOM   6932 C  C     . LYS D 2 46  ? 126.296 164.757 104.730 1.00 45.61  ? 46  LYS D C     1 
ATOM   6933 O  O     . LYS D 2 46  ? 126.588 164.674 103.534 1.00 42.57  ? 46  LYS D O     1 
ATOM   6934 C  CB    . LYS D 2 46  ? 126.022 167.162 105.421 1.00 45.79  ? 46  LYS D CB    1 
ATOM   6935 C  CG    . LYS D 2 46  ? 126.208 167.887 104.104 1.00 51.26  ? 46  LYS D CG    1 
ATOM   6936 C  CD    . LYS D 2 46  ? 125.238 169.053 103.985 1.00 53.85  ? 46  LYS D CD    1 
ATOM   6937 C  CE    . LYS D 2 46  ? 125.411 170.037 105.131 1.00 52.02  ? 46  LYS D CE    1 
ATOM   6938 N  NZ    . LYS D 2 46  ? 124.190 170.854 105.355 1.00 52.89  ? 46  LYS D NZ    1 
ATOM   6939 N  N     . ALA D 2 47  ? 125.504 163.890 105.351 1.00 50.60  ? 47  ALA D N     1 
ATOM   6940 C  CA    . ALA D 2 47  ? 124.920 162.732 104.695 1.00 45.88  ? 47  ALA D CA    1 
ATOM   6941 C  C     . ALA D 2 47  ? 123.424 162.938 104.516 1.00 46.45  ? 47  ALA D C     1 
ATOM   6942 O  O     . ALA D 2 47  ? 122.748 163.459 105.407 1.00 52.28  ? 47  ALA D O     1 
ATOM   6943 C  CB    . ALA D 2 47  ? 125.175 161.458 105.503 1.00 42.37  ? 47  ALA D CB    1 
ATOM   6944 N  N     . TYR D 2 48  ? 122.917 162.537 103.358 1.00 49.80  ? 48  TYR D N     1 
ATOM   6945 C  CA    . TYR D 2 48  ? 121.496 162.582 103.060 1.00 52.38  ? 48  TYR D CA    1 
ATOM   6946 C  C     . TYR D 2 48  ? 120.891 161.191 103.206 1.00 52.51  ? 48  TYR D C     1 
ATOM   6947 O  O     . TYR D 2 48  ? 121.601 160.200 103.390 1.00 56.85  ? 48  TYR D O     1 
ATOM   6948 C  CB    . TYR D 2 48  ? 121.248 163.130 101.651 1.00 52.91  ? 48  TYR D CB    1 
ATOM   6949 C  CG    . TYR D 2 48  ? 121.719 164.557 101.446 1.00 54.11  ? 48  TYR D CG    1 
ATOM   6950 C  CD1   . TYR D 2 48  ? 123.036 164.837 101.095 1.00 55.55  ? 48  TYR D CD1   1 
ATOM   6951 C  CD2   . TYR D 2 48  ? 120.846 165.625 101.612 1.00 55.76  ? 48  TYR D CD2   1 
ATOM   6952 C  CE1   . TYR D 2 48  ? 123.467 166.138 100.911 1.00 55.48  ? 48  TYR D CE1   1 
ATOM   6953 C  CE2   . TYR D 2 48  ? 121.267 166.930 101.430 1.00 56.09  ? 48  TYR D CE2   1 
ATOM   6954 C  CZ    . TYR D 2 48  ? 122.578 167.179 101.081 1.00 57.34  ? 48  TYR D CZ    1 
ATOM   6955 O  OH    . TYR D 2 48  ? 122.999 168.477 100.899 1.00 59.82  ? 48  TYR D OH    1 
ATOM   6956 N  N     . GLU D 2 49  ? 119.563 161.128 103.138 1.00 59.55  ? 49  GLU D N     1 
ATOM   6957 C  CA    . GLU D 2 49  ? 118.882 159.846 103.250 1.00 60.45  ? 49  GLU D CA    1 
ATOM   6958 C  C     . GLU D 2 49  ? 119.075 159.022 101.983 1.00 63.02  ? 49  GLU D C     1 
ATOM   6959 O  O     . GLU D 2 49  ? 118.944 159.526 100.865 1.00 62.51  ? 49  GLU D O     1 
ATOM   6960 C  CB    . GLU D 2 49  ? 117.391 160.044 103.525 1.00 58.01  ? 49  GLU D CB    1 
ATOM   6961 C  CG    . GLU D 2 49  ? 117.052 160.136 105.001 1.00 62.61  ? 49  GLU D CG    1 
ATOM   6962 C  CD    . GLU D 2 49  ? 116.297 161.398 105.346 1.00 67.36  ? 49  GLU D CD    1 
ATOM   6963 O  OE1   . GLU D 2 49  ? 116.467 161.907 106.474 1.00 68.69  ? 49  GLU D OE1   1 
ATOM   6964 O  OE2   . GLU D 2 49  ? 115.517 161.869 104.493 1.00 67.74  ? 49  GLU D OE2   1 
ATOM   6965 N  N     . GLY D 2 50  ? 119.387 157.740 102.168 1.00 51.86  ? 50  GLY D N     1 
ATOM   6966 C  CA    . GLY D 2 50  ? 119.685 156.854 101.069 1.00 49.44  ? 50  GLY D CA    1 
ATOM   6967 C  C     . GLY D 2 50  ? 121.130 156.857 100.620 1.00 53.59  ? 50  GLY D C     1 
ATOM   6968 O  O     . GLY D 2 50  ? 121.468 156.140 99.671  1.00 57.52  ? 50  GLY D O     1 
ATOM   6969 N  N     . ASP D 2 51  ? 121.990 157.639 101.267 1.00 47.58  ? 51  ASP D N     1 
ATOM   6970 C  CA    . ASP D 2 51  ? 123.399 157.668 100.904 1.00 42.70  ? 51  ASP D CA    1 
ATOM   6971 C  C     . ASP D 2 51  ? 124.117 156.457 101.481 1.00 38.67  ? 51  ASP D C     1 
ATOM   6972 O  O     . ASP D 2 51  ? 123.993 156.157 102.672 1.00 39.41  ? 51  ASP D O     1 
ATOM   6973 C  CB    . ASP D 2 51  ? 124.052 158.954 101.412 1.00 43.76  ? 51  ASP D CB    1 
ATOM   6974 C  CG    . ASP D 2 51  ? 124.013 160.073 100.394 1.00 48.87  ? 51  ASP D CG    1 
ATOM   6975 O  OD1   . ASP D 2 51  ? 123.574 159.828 99.251  1.00 51.96  ? 51  ASP D OD1   1 
ATOM   6976 O  OD2   . ASP D 2 51  ? 124.426 161.199 100.734 1.00 50.69  ? 51  ASP D OD2   1 
ATOM   6977 N  N     . VAL D 2 52  ? 124.870 155.760 100.641 1.00 39.62  ? 52  VAL D N     1 
ATOM   6978 C  CA    . VAL D 2 52  ? 125.732 154.670 101.076 1.00 39.02  ? 52  VAL D CA    1 
ATOM   6979 C  C     . VAL D 2 52  ? 127.161 155.168 100.908 1.00 34.49  ? 52  VAL D C     1 
ATOM   6980 O  O     . VAL D 2 52  ? 127.656 155.303 99.784  1.00 37.60  ? 52  VAL D O     1 
ATOM   6981 C  CB    . VAL D 2 52  ? 125.478 153.380 100.289 1.00 38.42  ? 52  VAL D CB    1 
ATOM   6982 C  CG1   . VAL D 2 52  ? 126.224 152.224 100.923 1.00 35.77  ? 52  VAL D CG1   1 
ATOM   6983 C  CG2   . VAL D 2 52  ? 123.991 153.084 100.228 1.00 30.29  ? 52  VAL D CG2   1 
ATOM   6984 N  N     . ILE D 2 53  ? 127.827 155.445 102.023 1.00 30.72  ? 53  ILE D N     1 
ATOM   6985 C  CA    . ILE D 2 53  ? 129.104 156.149 102.031 1.00 29.65  ? 53  ILE D CA    1 
ATOM   6986 C  C     . ILE D 2 53  ? 130.200 155.188 102.464 1.00 32.42  ? 53  ILE D C     1 
ATOM   6987 O  O     . ILE D 2 53  ? 130.112 154.573 103.534 1.00 32.94  ? 53  ILE D O     1 
ATOM   6988 C  CB    . ILE D 2 53  ? 129.056 157.385 102.946 1.00 35.70  ? 53  ILE D CB    1 
ATOM   6989 C  CG1   . ILE D 2 53  ? 127.919 158.310 102.513 1.00 35.80  ? 53  ILE D CG1   1 
ATOM   6990 C  CG2   . ILE D 2 53  ? 130.381 158.127 102.918 1.00 33.49  ? 53  ILE D CG2   1 
ATOM   6991 C  CD1   . ILE D 2 53  ? 127.543 159.333 103.540 1.00 34.37  ? 53  ILE D CD1   1 
ATOM   6992 N  N     . GLY D 2 54  ? 131.232 155.064 101.634 1.00 38.07  ? 54  GLY D N     1 
ATOM   6993 C  CA    . GLY D 2 54  ? 132.378 154.229 101.941 1.00 27.26  ? 54  GLY D CA    1 
ATOM   6994 C  C     . GLY D 2 54  ? 133.513 155.060 102.509 1.00 28.17  ? 54  GLY D C     1 
ATOM   6995 O  O     . GLY D 2 54  ? 133.910 156.072 101.929 1.00 35.30  ? 54  GLY D O     1 
ATOM   6996 N  N     . LEU D 2 55  ? 134.027 154.618 103.653 1.00 33.69  ? 55  LEU D N     1 
ATOM   6997 C  CA    . LEU D 2 55  ? 135.148 155.268 104.318 1.00 31.42  ? 55  LEU D CA    1 
ATOM   6998 C  C     . LEU D 2 55  ? 136.422 154.506 103.985 1.00 30.20  ? 55  LEU D C     1 
ATOM   6999 O  O     . LEU D 2 55  ? 136.624 153.386 104.468 1.00 31.37  ? 55  LEU D O     1 
ATOM   7000 C  CB    . LEU D 2 55  ? 134.932 155.324 105.832 1.00 28.61  ? 55  LEU D CB    1 
ATOM   7001 C  CG    . LEU D 2 55  ? 134.399 156.623 106.444 1.00 35.58  ? 55  LEU D CG    1 
ATOM   7002 C  CD1   . LEU D 2 55  ? 133.073 157.043 105.825 1.00 34.84  ? 55  LEU D CD1   1 
ATOM   7003 C  CD2   . LEU D 2 55  ? 134.267 156.497 107.951 1.00 33.43  ? 55  LEU D CD2   1 
ATOM   7004 N  N     . VAL D 2 56  ? 137.280 155.111 103.164 1.00 27.94  ? 56  VAL D N     1 
ATOM   7005 C  CA    . VAL D 2 56  ? 138.501 154.470 102.698 1.00 28.09  ? 56  VAL D CA    1 
ATOM   7006 C  C     . VAL D 2 56  ? 139.704 155.220 103.253 1.00 28.70  ? 56  VAL D C     1 
ATOM   7007 O  O     . VAL D 2 56  ? 139.608 156.368 103.692 1.00 36.19  ? 56  VAL D O     1 
ATOM   7008 C  CB    . VAL D 2 56  ? 138.575 154.397 101.156 1.00 29.05  ? 56  VAL D CB    1 
ATOM   7009 C  CG1   . VAL D 2 56  ? 137.396 153.616 100.602 1.00 26.32  ? 56  VAL D CG1   1 
ATOM   7010 C  CG2   . VAL D 2 56  ? 138.636 155.790 100.551 1.00 28.04  ? 56  VAL D CG2   1 
ATOM   7011 N  N     . GLY D 2 57  ? 140.843 154.545 103.237 1.00 29.14  ? 57  GLY D N     1 
ATOM   7012 C  CA    . GLY D 2 57  ? 142.079 155.131 103.713 1.00 19.28  ? 57  GLY D CA    1 
ATOM   7013 C  C     . GLY D 2 57  ? 143.002 154.070 104.260 1.00 22.61  ? 57  GLY D C     1 
ATOM   7014 O  O     . GLY D 2 57  ? 142.620 152.922 104.472 1.00 40.40  ? 57  GLY D O     1 
ATOM   7015 N  N     . ILE D 2 58  ? 144.243 154.487 104.499 1.00 30.28  ? 58  ILE D N     1 
ATOM   7016 C  CA    . ILE D 2 58  ? 145.290 153.601 104.999 1.00 28.18  ? 58  ILE D CA    1 
ATOM   7017 C  C     . ILE D 2 58  ? 145.093 153.361 106.489 1.00 27.19  ? 58  ILE D C     1 
ATOM   7018 O  O     . ILE D 2 58  ? 144.215 153.967 107.113 1.00 38.04  ? 58  ILE D O     1 
ATOM   7019 C  CB    . ILE D 2 58  ? 146.690 154.170 104.702 1.00 31.16  ? 58  ILE D CB    1 
ATOM   7020 C  CG1   . ILE D 2 58  ? 146.904 155.495 105.436 1.00 32.89  ? 58  ILE D CG1   1 
ATOM   7021 C  CG2   . ILE D 2 58  ? 146.881 154.348 103.206 1.00 23.49  ? 58  ILE D CG2   1 
ATOM   7022 C  CD1   . ILE D 2 58  ? 148.357 155.880 105.593 1.00 27.56  ? 58  ILE D CD1   1 
ATOM   7023 N  N     . ASN D 2 59  ? 145.872 152.434 107.050 1.00 24.13  ? 59  ASN D N     1 
ATOM   7024 C  CA    . ASN D 2 59  ? 145.772 152.089 108.465 1.00 28.47  ? 59  ASN D CA    1 
ATOM   7025 C  C     . ASN D 2 59  ? 146.114 153.281 109.353 1.00 33.36  ? 59  ASN D C     1 
ATOM   7026 O  O     . ASN D 2 59  ? 147.086 154.000 109.105 1.00 41.66  ? 59  ASN D O     1 
ATOM   7027 C  CB    . ASN D 2 59  ? 146.706 150.921 108.783 1.00 26.96  ? 59  ASN D CB    1 
ATOM   7028 C  CG    . ASN D 2 59  ? 146.223 149.611 108.199 1.00 27.03  ? 59  ASN D CG    1 
ATOM   7029 O  OD1   . ASN D 2 59  ? 147.010 148.708 107.930 1.00 34.74  ? 59  ASN D OD1   1 
ATOM   7030 N  ND2   . ASN D 2 59  ? 144.917 149.501 108.006 1.00 33.95  ? 59  ASN D ND2   1 
ATOM   7031 N  N     . GLY D 2 60  ? 145.301 153.489 110.385 1.00 25.60  ? 60  GLY D N     1 
ATOM   7032 C  CA    . GLY D 2 60  ? 145.477 154.605 111.288 1.00 18.00  ? 60  GLY D CA    1 
ATOM   7033 C  C     . GLY D 2 60  ? 145.026 155.947 110.757 1.00 31.15  ? 60  GLY D C     1 
ATOM   7034 O  O     . GLY D 2 60  ? 145.468 156.975 111.278 1.00 40.87  ? 60  GLY D O     1 
ATOM   7035 N  N     . SER D 2 61  ? 144.169 155.972 109.735 1.00 25.81  ? 61  SER D N     1 
ATOM   7036 C  CA    . SER D 2 61  ? 143.734 157.243 109.163 1.00 21.48  ? 61  SER D CA    1 
ATOM   7037 C  C     . SER D 2 61  ? 142.727 157.949 110.060 1.00 30.50  ? 61  SER D C     1 
ATOM   7038 O  O     . SER D 2 61  ? 142.729 159.181 110.151 1.00 40.51  ? 61  SER D O     1 
ATOM   7039 C  CB    . SER D 2 61  ? 143.136 157.023 107.776 1.00 27.05  ? 61  SER D CB    1 
ATOM   7040 O  OG    . SER D 2 61  ? 144.129 156.625 106.853 1.00 34.42  ? 61  SER D OG    1 
ATOM   7041 N  N     . GLY D 2 62  ? 141.852 157.196 110.717 1.00 19.60  ? 62  GLY D N     1 
ATOM   7042 C  CA    . GLY D 2 62  ? 140.857 157.794 111.583 1.00 17.84  ? 62  GLY D CA    1 
ATOM   7043 C  C     . GLY D 2 62  ? 139.434 157.479 111.180 1.00 20.36  ? 62  GLY D C     1 
ATOM   7044 O  O     . GLY D 2 62  ? 138.501 158.162 111.608 1.00 39.27  ? 62  GLY D O     1 
ATOM   7045 N  N     . LYS D 2 63  ? 139.252 156.452 110.350 1.00 24.80  ? 63  LYS D N     1 
ATOM   7046 C  CA    . LYS D 2 63  ? 137.914 156.114 109.881 1.00 30.13  ? 63  LYS D CA    1 
ATOM   7047 C  C     . LYS D 2 63  ? 137.097 155.371 110.936 1.00 22.53  ? 63  LYS D C     1 
ATOM   7048 O  O     . LYS D 2 63  ? 135.872 155.524 110.976 1.00 31.19  ? 63  LYS D O     1 
ATOM   7049 C  CB    . LYS D 2 63  ? 138.002 155.313 108.579 1.00 29.17  ? 63  LYS D CB    1 
ATOM   7050 C  CG    . LYS D 2 63  ? 138.727 153.993 108.680 1.00 37.81  ? 63  LYS D CG    1 
ATOM   7051 C  CD    . LYS D 2 63  ? 139.038 153.430 107.307 1.00 30.69  ? 63  LYS D CD    1 
ATOM   7052 C  CE    . LYS D 2 63  ? 140.368 153.933 106.810 1.00 31.44  ? 63  LYS D CE    1 
ATOM   7053 N  NZ    . LYS D 2 63  ? 141.439 152.941 107.071 1.00 28.85  ? 63  LYS D NZ    1 
ATOM   7054 N  N     . SER D 2 64  ? 137.743 154.588 111.805 1.00 18.65  ? 64  SER D N     1 
ATOM   7055 C  CA    . SER D 2 64  ? 137.013 153.976 112.911 1.00 18.25  ? 64  SER D CA    1 
ATOM   7056 C  C     . SER D 2 64  ? 136.656 155.010 113.969 1.00 28.20  ? 64  SER D C     1 
ATOM   7057 O  O     . SER D 2 64  ? 135.609 154.903 114.612 1.00 38.31  ? 64  SER D O     1 
ATOM   7058 C  CB    . SER D 2 64  ? 137.826 152.839 113.527 1.00 23.08  ? 64  SER D CB    1 
ATOM   7059 O  OG    . SER D 2 64  ? 137.996 151.780 112.604 1.00 38.54  ? 64  SER D OG    1 
ATOM   7060 N  N     . THR D 2 65  ? 137.512 156.021 114.151 1.00 23.81  ? 65  THR D N     1 
ATOM   7061 C  CA    . THR D 2 65  ? 137.193 157.129 115.048 1.00 28.66  ? 65  THR D CA    1 
ATOM   7062 C  C     . THR D 2 65  ? 135.988 157.915 114.543 1.00 27.88  ? 65  THR D C     1 
ATOM   7063 O  O     . THR D 2 65  ? 135.078 158.240 115.318 1.00 38.80  ? 65  THR D O     1 
ATOM   7064 C  CB    . THR D 2 65  ? 138.414 158.042 115.192 1.00 31.83  ? 65  THR D CB    1 
ATOM   7065 O  OG1   . THR D 2 65  ? 139.520 157.283 115.693 1.00 35.04  ? 65  THR D OG1   1 
ATOM   7066 C  CG2   . THR D 2 65  ? 138.131 159.193 116.142 1.00 27.90  ? 65  THR D CG2   1 
ATOM   7067 N  N     . LEU D 2 66  ? 135.944 158.187 113.235 1.00 27.33  ? 66  LEU D N     1 
ATOM   7068 C  CA    . LEU D 2 66  ? 134.802 158.877 112.644 1.00 24.30  ? 66  LEU D CA    1 
ATOM   7069 C  C     . LEU D 2 66  ? 133.545 158.017 112.695 1.00 31.98  ? 66  LEU D C     1 
ATOM   7070 O  O     . LEU D 2 66  ? 132.448 158.529 112.943 1.00 39.33  ? 66  LEU D O     1 
ATOM   7071 C  CB    . LEU D 2 66  ? 135.128 159.281 111.207 1.00 28.26  ? 66  LEU D CB    1 
ATOM   7072 C  CG    . LEU D 2 66  ? 134.111 160.159 110.475 1.00 30.93  ? 66  LEU D CG    1 
ATOM   7073 C  CD1   . LEU D 2 66  ? 133.918 161.479 111.201 1.00 29.66  ? 66  LEU D CD1   1 
ATOM   7074 C  CD2   . LEU D 2 66  ? 134.555 160.397 109.044 1.00 24.37  ? 66  LEU D CD2   1 
ATOM   7075 N  N     . SER D 2 67  ? 133.688 156.703 112.493 1.00 34.40  ? 67  SER D N     1 
ATOM   7076 C  CA    . SER D 2 67  ? 132.535 155.811 112.548 1.00 23.90  ? 67  SER D CA    1 
ATOM   7077 C  C     . SER D 2 67  ? 131.991 155.673 113.969 1.00 27.71  ? 67  SER D C     1 
ATOM   7078 O  O     . SER D 2 67  ? 130.777 155.567 114.162 1.00 37.65  ? 67  SER D O     1 
ATOM   7079 C  CB    . SER D 2 67  ? 132.903 154.443 111.975 1.00 28.60  ? 67  SER D CB    1 
ATOM   7080 O  OG    . SER D 2 67  ? 133.342 153.558 112.988 1.00 38.18  ? 67  SER D OG    1 
ATOM   7081 N  N     . ASN D 2 68  ? 132.870 155.681 114.976 1.00 28.88  ? 68  ASN D N     1 
ATOM   7082 C  CA    . ASN D 2 68  ? 132.409 155.629 116.360 1.00 23.96  ? 68  ASN D CA    1 
ATOM   7083 C  C     . ASN D 2 68  ? 131.807 156.959 116.794 1.00 29.39  ? 68  ASN D C     1 
ATOM   7084 O  O     . ASN D 2 68  ? 130.913 156.993 117.646 1.00 41.62  ? 68  ASN D O     1 
ATOM   7085 C  CB    . ASN D 2 68  ? 133.559 155.238 117.289 1.00 32.08  ? 68  ASN D CB    1 
ATOM   7086 C  CG    . ASN D 2 68  ? 134.013 153.808 117.087 1.00 34.89  ? 68  ASN D CG    1 
ATOM   7087 O  OD1   . ASN D 2 68  ? 133.253 152.962 116.622 1.00 39.13  ? 68  ASN D OD1   1 
ATOM   7088 N  ND2   . ASN D 2 68  ? 135.262 153.534 117.439 1.00 39.21  ? 68  ASN D ND2   1 
ATOM   7089 N  N     . ILE D 2 69  ? 132.302 158.065 116.234 1.00 34.75  ? 69  ILE D N     1 
ATOM   7090 C  CA    . ILE D 2 69  ? 131.719 159.373 116.517 1.00 34.76  ? 69  ILE D CA    1 
ATOM   7091 C  C     . ILE D 2 69  ? 130.326 159.482 115.900 1.00 32.97  ? 69  ILE D C     1 
ATOM   7092 O  O     . ILE D 2 69  ? 129.393 160.004 116.526 1.00 43.91  ? 69  ILE D O     1 
ATOM   7093 C  CB    . ILE D 2 69  ? 132.682 160.478 116.031 1.00 35.05  ? 69  ILE D CB    1 
ATOM   7094 C  CG1   . ILE D 2 69  ? 133.710 160.788 117.120 1.00 29.79  ? 69  ILE D CG1   1 
ATOM   7095 C  CG2   . ILE D 2 69  ? 131.958 161.750 115.619 1.00 36.24  ? 69  ILE D CG2   1 
ATOM   7096 C  CD1   . ILE D 2 69  ? 134.910 161.545 116.627 1.00 32.28  ? 69  ILE D CD1   1 
ATOM   7097 N  N     . ILE D 2 70  ? 130.159 158.963 114.678 1.00 33.68  ? 70  ILE D N     1 
ATOM   7098 C  CA    . ILE D 2 70  ? 128.845 158.919 114.035 1.00 33.75  ? 70  ILE D CA    1 
ATOM   7099 C  C     . ILE D 2 70  ? 127.903 157.990 114.798 1.00 40.82  ? 70  ILE D C     1 
ATOM   7100 O  O     . ILE D 2 70  ? 126.742 158.333 115.055 1.00 43.85  ? 70  ILE D O     1 
ATOM   7101 C  CB    . ILE D 2 70  ? 128.998 158.498 112.558 1.00 38.46  ? 70  ILE D CB    1 
ATOM   7102 C  CG1   . ILE D 2 70  ? 129.575 159.647 111.731 1.00 38.83  ? 70  ILE D CG1   1 
ATOM   7103 C  CG2   . ILE D 2 70  ? 127.673 158.045 111.958 1.00 32.91  ? 70  ILE D CG2   1 
ATOM   7104 C  CD1   . ILE D 2 70  ? 130.269 159.195 110.464 1.00 31.31  ? 70  ILE D CD1   1 
ATOM   7105 N  N     . GLY D 2 71  ? 128.400 156.826 115.217 1.00 40.95  ? 71  GLY D N     1 
ATOM   7106 C  CA    . GLY D 2 71  ? 127.586 155.861 115.934 1.00 36.58  ? 71  GLY D CA    1 
ATOM   7107 C  C     . GLY D 2 71  ? 127.257 156.239 117.363 1.00 44.28  ? 71  GLY D C     1 
ATOM   7108 O  O     . GLY D 2 71  ? 126.402 155.588 117.972 1.00 53.53  ? 71  GLY D O     1 
ATOM   7109 N  N     . GLY D 2 72  ? 127.881 157.269 117.937 1.00 41.23  ? 72  GLY D N     1 
ATOM   7110 C  CA    . GLY D 2 72  ? 127.585 157.760 119.299 1.00 40.12  ? 72  GLY D CA    1 
ATOM   7111 C  C     . GLY D 2 72  ? 128.438 157.180 120.417 1.00 39.93  ? 72  GLY D C     1 
ATOM   7112 O  O     . GLY D 2 72  ? 128.296 157.655 121.524 1.00 47.77  ? 72  GLY D O     1 
ATOM   7113 N  N     . SER D 2 73  ? 129.245 156.163 120.174 1.00 31.52  ? 73  SER D N     1 
ATOM   7114 C  CA    . SER D 2 73  ? 130.161 155.537 121.160 1.00 32.30  ? 73  SER D CA    1 
ATOM   7115 C  C     . SER D 2 73  ? 131.241 156.518 121.632 1.00 39.41  ? 73  SER D C     1 
ATOM   7116 O  O     . SER D 2 73  ? 131.688 156.348 122.762 1.00 40.99  ? 73  SER D O     1 
ATOM   7117 C  CB    . SER D 2 73  ? 130.732 154.262 120.635 1.00 40.30  ? 73  SER D CB    1 
ATOM   7118 O  OG    . SER D 2 73  ? 130.286 153.998 119.315 1.00 45.58  ? 73  SER D OG    1 
ATOM   7119 N  N     . LEU D 2 74  ? 131.729 157.378 120.742 1.00 36.07  ? 74  LEU D N     1 
ATOM   7120 C  CA    . LEU D 2 74  ? 132.846 158.296 121.024 1.00 26.26  ? 74  LEU D CA    1 
ATOM   7121 C  C     . LEU D 2 74  ? 132.399 159.744 120.882 1.00 33.22  ? 74  LEU D C     1 
ATOM   7122 O  O     . LEU D 2 74  ? 131.581 160.040 120.007 1.00 41.25  ? 74  LEU D O     1 
ATOM   7123 C  CB    . LEU D 2 74  ? 134.020 157.929 120.119 1.00 36.08  ? 74  LEU D CB    1 
ATOM   7124 C  CG    . LEU D 2 74  ? 135.351 158.641 120.340 1.00 36.21  ? 74  LEU D CG    1 
ATOM   7125 C  CD1   . LEU D 2 74  ? 136.027 158.030 121.548 1.00 37.39  ? 74  LEU D CD1   1 
ATOM   7126 C  CD2   . LEU D 2 74  ? 136.160 158.383 119.086 1.00 30.77  ? 74  LEU D CD2   1 
ATOM   7127 N  N     . SER D 2 75  ? 132.790 160.566 121.838 1.00 37.66  ? 75  SER D N     1 
ATOM   7128 C  CA    . SER D 2 75  ? 132.476 162.003 121.816 1.00 36.50  ? 75  SER D CA    1 
ATOM   7129 C  C     . SER D 2 75  ? 133.540 162.806 121.061 1.00 38.94  ? 75  SER D C     1 
ATOM   7130 O  O     . SER D 2 75  ? 134.724 162.532 121.228 1.00 40.37  ? 75  SER D O     1 
ATOM   7131 C  CB    . SER D 2 75  ? 132.287 162.508 123.224 1.00 37.05  ? 75  SER D CB    1 
ATOM   7132 O  OG    . SER D 2 75  ? 131.407 163.620 123.251 1.00 46.97  ? 75  SER D OG    1 
ATOM   7133 N  N     . PRO D 2 76  ? 133.160 163.762 120.200 1.00 36.43  ? 76  PRO D N     1 
ATOM   7134 C  CA    . PRO D 2 76  ? 134.153 164.666 119.579 1.00 32.74  ? 76  PRO D CA    1 
ATOM   7135 C  C     . PRO D 2 76  ? 134.834 165.556 120.611 1.00 35.96  ? 76  PRO D C     1 
ATOM   7136 O  O     . PRO D 2 76  ? 134.193 165.925 121.607 1.00 46.76  ? 76  PRO D O     1 
ATOM   7137 C  CB    . PRO D 2 76  ? 133.291 165.517 118.667 1.00 37.69  ? 76  PRO D CB    1 
ATOM   7138 C  CG    . PRO D 2 76  ? 131.977 164.806 118.483 1.00 35.56  ? 76  PRO D CG    1 
ATOM   7139 C  CD    . PRO D 2 76  ? 131.772 164.043 119.732 1.00 29.66  ? 76  PRO D CD    1 
ATOM   7140 N  N     . THR D 2 77  ? 136.130 165.808 120.500 1.00 34.83  ? 77  THR D N     1 
ATOM   7141 C  CA    . THR D 2 77  ? 136.776 166.829 121.344 1.00 40.29  ? 77  THR D CA    1 
ATOM   7142 C  C     . THR D 2 77  ? 136.188 168.183 120.986 1.00 41.77  ? 77  THR D C     1 
ATOM   7143 O  O     . THR D 2 77  ? 135.883 168.946 121.903 1.00 46.80  ? 77  THR D O     1 
ATOM   7144 C  CB    . THR D 2 77  ? 138.300 166.773 121.209 1.00 40.16  ? 77  THR D CB    1 
ATOM   7145 O  OG1   . THR D 2 77  ? 138.717 165.557 121.809 1.00 35.96  ? 77  THR D OG1   1 
ATOM   7146 C  CG2   . THR D 2 77  ? 139.008 167.907 121.922 1.00 42.90  ? 77  THR D CG2   1 
ATOM   7147 N  N     . VAL D 2 78  ? 136.001 168.467 119.706 1.00 41.81  ? 78  VAL D N     1 
ATOM   7148 C  CA    . VAL D 2 78  ? 135.449 169.756 119.208 1.00 41.22  ? 78  VAL D CA    1 
ATOM   7149 C  C     . VAL D 2 78  ? 134.489 169.399 118.068 1.00 42.36  ? 78  VAL D C     1 
ATOM   7150 O  O     . VAL D 2 78  ? 134.664 168.343 117.499 1.00 41.74  ? 78  VAL D O     1 
ATOM   7151 C  CB    . VAL D 2 78  ? 136.455 170.838 118.751 1.00 43.85  ? 78  VAL D CB    1 
ATOM   7152 C  CG1   . VAL D 2 78  ? 135.864 172.240 118.769 1.00 42.72  ? 78  VAL D CG1   1 
ATOM   7153 C  CG2   . VAL D 2 78  ? 137.765 170.799 119.521 1.00 46.82  ? 78  VAL D CG2   1 
ATOM   7154 N  N     . GLY D 2 79  ? 133.518 170.257 117.786 1.00 49.96  ? 79  GLY D N     1 
ATOM   7155 C  CA    . GLY D 2 79  ? 132.520 170.082 116.728 1.00 45.50  ? 79  GLY D CA    1 
ATOM   7156 C  C     . GLY D 2 79  ? 131.311 169.326 117.180 1.00 46.90  ? 79  GLY D C     1 
ATOM   7157 O  O     . GLY D 2 79  ? 131.316 168.832 118.303 1.00 52.85  ? 79  GLY D O     1 
ATOM   7158 N  N     . LYS D 2 80  ? 130.324 169.209 116.302 1.00 46.62  ? 80  LYS D N     1 
ATOM   7159 C  CA    . LYS D 2 80  ? 129.058 168.515 116.623 1.00 45.51  ? 80  LYS D CA    1 
ATOM   7160 C  C     . LYS D 2 80  ? 128.643 167.552 115.528 1.00 49.21  ? 80  LYS D C     1 
ATOM   7161 O  O     . LYS D 2 80  ? 128.993 167.793 114.367 1.00 55.32  ? 80  LYS D O     1 
ATOM   7162 C  CB    . LYS D 2 80  ? 127.932 169.545 116.682 1.00 50.62  ? 80  LYS D CB    1 
ATOM   7163 C  CG    . LYS D 2 80  ? 127.094 169.520 117.946 1.00 54.12  ? 80  LYS D CG    1 
ATOM   7164 C  CD    . LYS D 2 80  ? 125.630 169.181 117.693 1.00 52.79  ? 80  LYS D CD    1 
ATOM   7165 C  CE    . LYS D 2 80  ? 125.141 168.057 118.544 1.00 53.82  ? 80  LYS D CE    1 
ATOM   7166 N  NZ    . LYS D 2 80  ? 123.932 167.454 117.979 1.00 51.43  ? 80  LYS D NZ    1 
ATOM   7167 N  N     . VAL D 2 81  ? 128.013 166.463 115.911 1.00 49.03  ? 81  VAL D N     1 
ATOM   7168 C  CA    . VAL D 2 81  ? 127.391 165.528 114.947 1.00 47.59  ? 81  VAL D CA    1 
ATOM   7169 C  C     . VAL D 2 81  ? 125.884 165.644 115.190 1.00 48.16  ? 81  VAL D C     1 
ATOM   7170 O  O     . VAL D 2 81  ? 125.465 165.454 116.320 1.00 54.88  ? 81  VAL D O     1 
ATOM   7171 C  CB    . VAL D 2 81  ? 127.882 164.076 115.112 1.00 50.84  ? 81  VAL D CB    1 
ATOM   7172 C  CG1   . VAL D 2 81  ? 127.167 163.109 114.179 1.00 45.57  ? 81  VAL D CG1   1 
ATOM   7173 C  CG2   . VAL D 2 81  ? 129.384 163.974 114.917 1.00 47.72  ? 81  VAL D CG2   1 
ATOM   7174 N  N     . ASP D 2 82  ? 125.104 165.926 114.153 1.00 51.02  ? 82  ASP D N     1 
ATOM   7175 C  CA    . ASP D 2 82  ? 123.627 165.947 114.247 1.00 49.26  ? 82  ASP D CA    1 
ATOM   7176 C  C     . ASP D 2 82  ? 123.096 164.773 113.445 1.00 47.17  ? 82  ASP D C     1 
ATOM   7177 O  O     . ASP D 2 82  ? 123.350 164.716 112.248 1.00 51.02  ? 82  ASP D O     1 
ATOM   7178 C  CB    . ASP D 2 82  ? 123.035 167.151 113.556 1.00 50.26  ? 82  ASP D CB    1 
ATOM   7179 C  CG    . ASP D 2 82  ? 123.216 168.496 114.234 1.00 55.61  ? 82  ASP D CG    1 
ATOM   7180 O  OD1   . ASP D 2 82  ? 123.238 169.504 113.504 1.00 56.96  ? 82  ASP D OD1   1 
ATOM   7181 O  OD2   . ASP D 2 82  ? 123.328 168.525 115.472 1.00 57.33  ? 82  ASP D OD2   1 
ATOM   7182 N  N     . ARG D 2 83  ? 122.336 163.905 114.083 1.00 49.48  ? 83  ARG D N     1 
ATOM   7183 C  CA    . ARG D 2 83  ? 121.810 162.695 113.417 1.00 47.92  ? 83  ARG D CA    1 
ATOM   7184 C  C     . ARG D 2 83  ? 120.291 162.796 113.421 1.00 48.43  ? 83  ARG D C     1 
ATOM   7185 O  O     . ARG D 2 83  ? 119.747 163.133 114.470 1.00 53.50  ? 83  ARG D O     1 
ATOM   7186 C  CB    . ARG D 2 83  ? 122.307 161.469 114.189 1.00 45.77  ? 83  ARG D CB    1 
ATOM   7187 C  CG    . ARG D 2 83  ? 123.773 161.349 114.557 1.00 49.32  ? 83  ARG D CG    1 
ATOM   7188 C  CD    . ARG D 2 83  ? 123.905 160.286 115.627 1.00 45.32  ? 83  ARG D CD    1 
ATOM   7189 N  NE    . ARG D 2 83  ? 125.253 160.203 116.193 1.00 49.20  ? 83  ARG D NE    1 
ATOM   7190 C  CZ    . ARG D 2 83  ? 125.689 160.960 117.183 1.00 50.83  ? 83  ARG D CZ    1 
ATOM   7191 N  NH1   . ARG D 2 83  ? 124.839 161.709 117.851 1.00 52.36  ? 83  ARG D NH1   1 
ATOM   7192 N  NH2   . ARG D 2 83  ? 126.965 160.966 117.505 1.00 53.34  ? 83  ARG D NH2   1 
ATOM   7193 N  N     . ASN D 2 84  ? 119.651 162.642 112.278 1.00 53.73  ? 84  ASN D N     1 
ATOM   7194 C  CA    . ASN D 2 84  ? 118.177 162.575 112.276 1.00 54.18  ? 84  ASN D CA    1 
ATOM   7195 C  C     . ASN D 2 84  ? 117.886 161.096 112.136 1.00 57.37  ? 84  ASN D C     1 
ATOM   7196 O  O     . ASN D 2 84  ? 117.978 160.573 111.013 1.00 60.01  ? 84  ASN D O     1 
ATOM   7197 C  CB    . ASN D 2 84  ? 117.591 163.378 111.127 1.00 57.39  ? 84  ASN D CB    1 
ATOM   7198 C  CG    . ASN D 2 84  ? 116.083 163.354 111.126 1.00 62.84  ? 84  ASN D CG    1 
ATOM   7199 O  OD1   . ASN D 2 84  ? 115.456 163.745 112.115 1.00 61.80  ? 84  ASN D OD1   1 
ATOM   7200 N  ND2   . ASN D 2 84  ? 115.486 162.891 110.037 1.00 61.82  ? 84  ASN D ND2   1 
ATOM   7201 N  N     . GLY D 2 85  ? 117.453 160.482 113.214 1.00 54.47  ? 85  GLY D N     1 
ATOM   7202 C  CA    . GLY D 2 85  ? 117.205 159.048 113.176 1.00 56.21  ? 85  GLY D CA    1 
ATOM   7203 C  C     . GLY D 2 85  ? 118.028 158.226 114.107 1.00 55.78  ? 85  GLY D C     1 
ATOM   7204 O  O     . GLY D 2 85  ? 118.972 158.776 114.685 1.00 55.22  ? 85  GLY D O     1 
ATOM   7205 N  N     . GLU D 2 86  ? 117.611 156.980 114.294 1.00 52.95  ? 86  GLU D N     1 
ATOM   7206 C  CA    . GLU D 2 86  ? 118.345 156.003 115.113 1.00 53.43  ? 86  GLU D CA    1 
ATOM   7207 C  C     . GLU D 2 86  ? 119.610 155.525 114.410 1.00 54.21  ? 86  GLU D C     1 
ATOM   7208 O  O     . GLU D 2 86  ? 119.601 155.480 113.192 1.00 53.99  ? 86  GLU D O     1 
ATOM   7209 C  CB    . GLU D 2 86  ? 117.379 154.848 115.357 1.00 54.09  ? 86  GLU D CB    1 
ATOM   7210 C  CG    . GLU D 2 86  ? 115.966 155.313 115.690 1.00 57.42  ? 86  GLU D CG    1 
ATOM   7211 C  CD    . GLU D 2 86  ? 115.694 155.528 117.169 1.00 61.81  ? 86  GLU D CD    1 
ATOM   7212 O  OE1   . GLU D 2 86  ? 116.550 156.113 117.865 1.00 58.72  ? 86  GLU D OE1   1 
ATOM   7213 O  OE2   . GLU D 2 86  ? 114.612 155.107 117.628 1.00 60.52  ? 86  GLU D OE2   1 
ATOM   7214 N  N     . VAL D 2 87  ? 120.623 155.156 115.179 1.00 46.68  ? 87  VAL D N     1 
ATOM   7215 C  CA    . VAL D 2 87  ? 121.901 154.659 114.619 1.00 42.78  ? 87  VAL D CA    1 
ATOM   7216 C  C     . VAL D 2 87  ? 122.111 153.232 115.140 1.00 41.33  ? 87  VAL D C     1 
ATOM   7217 O  O     . VAL D 2 87  ? 121.907 153.011 116.321 1.00 44.35  ? 87  VAL D O     1 
ATOM   7218 C  CB    . VAL D 2 87  ? 123.109 155.579 114.901 1.00 39.11  ? 87  VAL D CB    1 
ATOM   7219 C  CG1   . VAL D 2 87  ? 124.372 155.066 114.229 1.00 40.11  ? 87  VAL D CG1   1 
ATOM   7220 C  CG2   . VAL D 2 87  ? 122.839 157.008 114.463 1.00 40.34  ? 87  VAL D CG2   1 
ATOM   7221 N  N     . SER D 2 88  ? 122.443 152.306 114.259 1.00 36.70  ? 88  SER D N     1 
ATOM   7222 C  CA    . SER D 2 88  ? 122.794 150.933 114.670 1.00 35.14  ? 88  SER D CA    1 
ATOM   7223 C  C     . SER D 2 88  ? 124.153 150.613 114.063 1.00 38.23  ? 88  SER D C     1 
ATOM   7224 O  O     . SER D 2 88  ? 124.455 151.134 113.013 1.00 37.57  ? 88  SER D O     1 
ATOM   7225 C  CB    . SER D 2 88  ? 121.784 149.915 114.298 1.00 39.10  ? 88  SER D CB    1 
ATOM   7226 O  OG    . SER D 2 88  ? 120.810 149.759 115.319 1.00 49.57  ? 88  SER D OG    1 
ATOM   7227 N  N     . VAL D 2 89  ? 124.945 149.833 114.767 1.00 83.56  ? 89  VAL D N     1 
ATOM   7228 C  CA    . VAL D 2 89  ? 126.302 149.463 114.322 1.00 83.69  ? 89  VAL D CA    1 
ATOM   7229 C  C     . VAL D 2 89  ? 126.298 147.944 114.145 1.00 87.24  ? 89  VAL D C     1 
ATOM   7230 O  O     . VAL D 2 89  ? 125.898 147.249 115.052 1.00 88.73  ? 89  VAL D O     1 
ATOM   7231 C  CB    . VAL D 2 89  ? 127.342 149.937 115.357 1.00 81.13  ? 89  VAL D CB    1 
ATOM   7232 C  CG1   . VAL D 2 89  ? 128.755 149.558 114.945 1.00 81.75  ? 89  VAL D CG1   1 
ATOM   7233 C  CG2   . VAL D 2 89  ? 127.243 151.433 115.615 1.00 81.26  ? 89  VAL D CG2   1 
ATOM   7234 N  N     . ILE D 2 90  ? 126.755 147.473 113.004 1.00 90.21  ? 90  ILE D N     1 
ATOM   7235 C  CA    . ILE D 2 90  ? 126.874 146.004 112.895 1.00 90.06  ? 90  ILE D CA    1 
ATOM   7236 C  C     . ILE D 2 90  ? 128.285 145.610 113.344 1.00 92.56  ? 90  ILE D C     1 
ATOM   7237 O  O     . ILE D 2 90  ? 129.223 145.796 112.567 1.00 88.00  ? 90  ILE D O     1 
ATOM   7238 C  CB    . ILE D 2 90  ? 126.459 145.469 111.507 1.00 86.97  ? 90  ILE D CB    1 
ATOM   7239 C  CG1   . ILE D 2 90  ? 124.950 145.554 111.331 1.00 87.57  ? 90  ILE D CG1   1 
ATOM   7240 C  CG2   . ILE D 2 90  ? 126.960 144.046 111.271 1.00 91.32  ? 90  ILE D CG2   1 
ATOM   7241 C  CD1   . ILE D 2 90  ? 124.477 145.365 109.906 1.00 90.81  ? 90  ILE D CD1   1 
ATOM   7242 N  N     . ALA D 2 91  ? 128.403 145.177 114.603 1.00 107.82 ? 91  ALA D N     1 
ATOM   7243 C  CA    . ALA D 2 91  ? 129.647 144.587 115.128 1.00 106.39 ? 91  ALA D CA    1 
ATOM   7244 C  C     . ALA D 2 91  ? 129.176 143.241 115.668 1.00 109.92 ? 91  ALA D C     1 
ATOM   7245 O  O     . ALA D 2 91  ? 128.549 143.279 116.748 1.00 112.90 ? 91  ALA D O     1 
ATOM   7246 C  CB    . ALA D 2 91  ? 130.149 145.470 116.221 1.00 100.00 ? 91  ALA D CB    1 
ATOM   7247 N  N     . ILE D 2 92  ? 129.567 142.112 115.066 1.00 103.77 ? 92  ILE D N     1 
ATOM   7248 C  CA    . ILE D 2 92  ? 128.979 140.768 115.396 1.00 105.91 ? 92  ILE D CA    1 
ATOM   7249 C  C     . ILE D 2 92  ? 129.254 140.285 116.838 1.00 102.19 ? 92  ILE D C     1 
ATOM   7250 O  O     . ILE D 2 92  ? 128.330 139.734 117.455 1.00 103.81 ? 92  ILE D O     1 
ATOM   7251 C  CB    . ILE D 2 92  ? 129.334 139.737 114.293 1.00 103.74 ? 92  ILE D CB    1 
ATOM   7252 C  CG1   . ILE D 2 92  ? 130.756 139.209 114.382 1.00 98.05  ? 92  ILE D CG1   1 
ATOM   7253 C  CG2   . ILE D 2 92  ? 129.039 140.319 112.909 1.00 102.88 ? 92  ILE D CG2   1 
ATOM   7254 C  CD1   . ILE D 2 92  ? 131.209 138.496 113.123 1.00 95.59  ? 92  ILE D CD1   1 
ATOM   7255 N  N     . SER D 2 93  ? 130.443 140.507 117.372 1.00 99.53  ? 93  SER D N     1 
ATOM   7256 C  CA    . SER D 2 93  ? 130.824 139.925 118.682 1.00 104.19 ? 93  SER D CA    1 
ATOM   7257 C  C     . SER D 2 93  ? 130.551 140.726 119.962 1.00 105.59 ? 93  SER D C     1 
ATOM   7258 O  O     . SER D 2 93  ? 130.691 140.103 121.028 1.00 105.35 ? 93  SER D O     1 
ATOM   7259 C  CB    . SER D 2 93  ? 132.287 139.651 118.590 1.00 107.85 ? 93  SER D CB    1 
ATOM   7260 O  OG    . SER D 2 93  ? 132.839 140.187 117.394 1.00 111.19 ? 93  SER D OG    1 
ATOM   7261 N  N     . ALA D 2 94  ? 130.022 141.945 119.916 1.00 105.70 ? 94  ALA D N     1 
ATOM   7262 C  CA    . ALA D 2 94  ? 129.986 142.829 121.132 1.00 107.12 ? 94  ALA D CA    1 
ATOM   7263 C  C     . ALA D 2 94  ? 129.194 142.224 122.307 1.00 108.37 ? 94  ALA D C     1 
ATOM   7264 O  O     . ALA D 2 94  ? 129.726 142.257 123.417 1.00 108.76 ? 94  ALA D O     1 
ATOM   7265 C  CB    . ALA D 2 94  ? 129.494 144.219 120.774 1.00 104.27 ? 94  ALA D CB    1 
ATOM   7266 N  N     . GLY D 2 95  ? 128.052 141.594 122.077 1.00 103.24 ? 95  GLY D N     1 
ATOM   7267 C  CA    . GLY D 2 95  ? 127.347 140.892 123.173 1.00 99.77  ? 95  GLY D CA    1 
ATOM   7268 C  C     . GLY D 2 95  ? 127.652 139.396 123.298 1.00 100.49 ? 95  GLY D C     1 
ATOM   7269 O  O     . GLY D 2 95  ? 126.914 138.772 124.084 1.00 95.56  ? 95  GLY D O     1 
ATOM   7270 N  N     . LEU D 2 96  ? 128.591 138.791 122.527 1.00 94.46  ? 96  LEU D N     1 
ATOM   7271 C  CA    . LEU D 2 96  ? 128.736 137.290 122.557 1.00 89.27  ? 96  LEU D CA    1 
ATOM   7272 C  C     . LEU D 2 96  ? 129.619 136.787 123.703 1.00 87.82  ? 96  LEU D C     1 
ATOM   7273 O  O     . LEU D 2 96  ? 130.801 137.112 123.719 1.00 89.31  ? 96  LEU D O     1 
ATOM   7274 C  CB    . LEU D 2 96  ? 129.122 136.647 121.225 1.00 84.56  ? 96  LEU D CB    1 
ATOM   7275 C  CG    . LEU D 2 96  ? 127.993 135.949 120.463 1.00 89.18  ? 96  LEU D CG    1 
ATOM   7276 C  CD1   . LEU D 2 96  ? 126.932 136.943 120.048 1.00 86.30  ? 96  LEU D CD1   1 
ATOM   7277 C  CD2   . LEU D 2 96  ? 128.494 135.185 119.258 1.00 88.22  ? 96  LEU D CD2   1 
ATOM   7278 N  N     . SER D 2 97  ? 129.090 135.874 124.504 1.00 72.27  ? 97  SER D N     1 
ATOM   7279 C  CA    . SER D 2 97  ? 129.762 135.285 125.673 1.00 71.22  ? 97  SER D CA    1 
ATOM   7280 C  C     . SER D 2 97  ? 130.030 133.819 125.353 1.00 68.45  ? 97  SER D C     1 
ATOM   7281 O  O     . SER D 2 97  ? 129.099 133.161 124.937 1.00 73.11  ? 97  SER D O     1 
ATOM   7282 C  CB    . SER D 2 97  ? 128.889 135.432 126.881 1.00 69.07  ? 97  SER D CB    1 
ATOM   7283 O  OG    . SER D 2 97  ? 129.478 134.818 128.016 1.00 71.32  ? 97  SER D OG    1 
ATOM   7284 N  N     . GLY D 2 98  ? 131.255 133.352 125.541 1.00 66.64  ? 98  GLY D N     1 
ATOM   7285 C  CA    . GLY D 2 98  ? 131.604 131.945 125.357 1.00 66.99  ? 98  GLY D CA    1 
ATOM   7286 C  C     . GLY D 2 98  ? 130.852 131.077 126.326 1.00 73.22  ? 98  GLY D C     1 
ATOM   7287 O  O     . GLY D 2 98  ? 130.540 129.964 125.971 1.00 75.06  ? 98  GLY D O     1 
ATOM   7288 N  N     . GLN D 2 99  ? 130.675 131.528 127.553 1.00 34.58  ? 99  GLN D N     1 
ATOM   7289 C  CA    . GLN D 2 99  ? 129.977 130.783 128.627 1.00 30.62  ? 99  GLN D CA    1 
ATOM   7290 C  C     . GLN D 2 99  ? 128.506 130.544 128.282 1.00 33.35  ? 99  GLN D C     1 
ATOM   7291 O  O     . GLN D 2 99  ? 128.010 129.483 128.610 1.00 40.41  ? 99  GLN D O     1 
ATOM   7292 C  CB    . GLN D 2 99  ? 130.231 131.542 129.931 1.00 30.41  ? 99  GLN D CB    1 
ATOM   7293 C  CG    . GLN D 2 99  ? 131.704 131.741 130.253 1.00 32.19  ? 99  GLN D CG    1 
ATOM   7294 C  CD    . GLN D 2 99  ? 132.145 133.182 130.143 1.00 40.18  ? 99  GLN D CD    1 
ATOM   7295 O  OE1   . GLN D 2 99  ? 131.603 133.977 129.366 1.00 43.00  ? 99  GLN D OE1   1 
ATOM   7296 N  NE2   . GLN D 2 99  ? 133.149 133.538 130.928 1.00 43.24  ? 99  GLN D NE2   1 
ATOM   7297 N  N     . LEU D 2 100 ? 127.830 131.522 127.700 1.00 29.78  ? 100 LEU D N     1 
ATOM   7298 C  CA    . LEU D 2 100 ? 126.418 131.368 127.298 1.00 28.15  ? 100 LEU D CA    1 
ATOM   7299 C  C     . LEU D 2 100 ? 126.268 130.476 126.071 1.00 26.23  ? 100 LEU D C     1 
ATOM   7300 O  O     . LEU D 2 100 ? 127.180 130.443 125.256 1.00 33.73  ? 100 LEU D O     1 
ATOM   7301 C  CB    . LEU D 2 100 ? 125.694 132.714 127.189 1.00 28.22  ? 100 LEU D CB    1 
ATOM   7302 C  CG    . LEU D 2 100 ? 125.666 133.579 128.449 1.00 29.94  ? 100 LEU D CG    1 
ATOM   7303 C  CD1   . LEU D 2 100 ? 124.930 134.857 128.149 1.00 26.89  ? 100 LEU D CD1   1 
ATOM   7304 C  CD2   . LEU D 2 100 ? 125.070 132.858 129.642 1.00 25.54  ? 100 LEU D CD2   1 
ATOM   7305 N  N     . THR D 2 101 ? 125.175 129.746 125.996 1.00 23.07  ? 101 THR D N     1 
ATOM   7306 C  CA    . THR D 2 101 ? 124.818 128.954 124.817 1.00 24.06  ? 101 THR D CA    1 
ATOM   7307 C  C     . THR D 2 101 ? 124.326 129.875 123.723 1.00 30.77  ? 101 THR D C     1 
ATOM   7308 O  O     . THR D 2 101 ? 124.110 131.034 123.993 1.00 38.71  ? 101 THR D O     1 
ATOM   7309 C  CB    . THR D 2 101 ? 123.807 127.864 125.174 1.00 26.01  ? 101 THR D CB    1 
ATOM   7310 O  OG1   . THR D 2 101 ? 122.495 128.409 125.159 1.00 33.89  ? 101 THR D OG1   1 
ATOM   7311 C  CG2   . THR D 2 101 ? 124.107 127.214 126.509 1.00 22.04  ? 101 THR D CG2   1 
ATOM   7312 N  N     . GLY D 2 102 ? 124.261 129.400 122.492 1.00 28.92  ? 102 GLY D N     1 
ATOM   7313 C  CA    . GLY D 2 102 ? 123.861 130.264 121.386 1.00 25.38  ? 102 GLY D CA    1 
ATOM   7314 C  C     . GLY D 2 102 ? 122.477 130.801 121.569 1.00 26.27  ? 102 GLY D C     1 
ATOM   7315 O  O     . GLY D 2 102 ? 122.292 131.955 121.198 1.00 34.89  ? 102 GLY D O     1 
ATOM   7316 N  N     . ILE D 2 103 ? 121.532 130.028 122.064 1.00 28.84  ? 103 ILE D N     1 
ATOM   7317 C  CA    . ILE D 2 103 ? 120.147 130.470 122.374 1.00 29.61  ? 103 ILE D CA    1 
ATOM   7318 C  C     . ILE D 2 103 ? 120.166 131.555 123.455 1.00 31.68  ? 103 ILE D C     1 
ATOM   7319 O  O     . ILE D 2 103 ? 119.441 132.540 123.297 1.00 35.04  ? 103 ILE D O     1 
ATOM   7320 C  CB    . ILE D 2 103 ? 119.345 129.228 122.820 1.00 33.44  ? 103 ILE D CB    1 
ATOM   7321 C  CG1   . ILE D 2 103 ? 119.006 128.323 121.655 1.00 27.18  ? 103 ILE D CG1   1 
ATOM   7322 C  CG2   . ILE D 2 103 ? 118.088 129.601 123.602 1.00 40.36  ? 103 ILE D CG2   1 
ATOM   7323 C  CD1   . ILE D 2 103 ? 117.534 128.313 121.303 1.00 37.42  ? 103 ILE D CD1   1 
ATOM   7324 N  N     . GLU D 2 104 ? 120.962 131.399 124.498 1.00 29.17  ? 104 GLU D N     1 
ATOM   7325 C  CA    . GLU D 2 104 ? 121.153 132.408 125.562 1.00 25.08  ? 104 GLU D CA    1 
ATOM   7326 C  C     . GLU D 2 104 ? 121.827 133.684 125.057 1.00 29.00  ? 104 GLU D C     1 
ATOM   7327 O  O     . GLU D 2 104 ? 121.377 134.740 125.457 1.00 44.30  ? 104 GLU D O     1 
ATOM   7328 C  CB    . GLU D 2 104 ? 121.905 131.749 126.715 1.00 34.07  ? 104 GLU D CB    1 
ATOM   7329 C  CG    . GLU D 2 104 ? 121.145 130.610 127.379 1.00 30.55  ? 104 GLU D CG    1 
ATOM   7330 C  CD    . GLU D 2 104 ? 122.039 129.913 128.382 1.00 37.23  ? 104 GLU D CD    1 
ATOM   7331 O  OE1   . GLU D 2 104 ? 123.236 130.229 128.415 1.00 37.21  ? 104 GLU D OE1   1 
ATOM   7332 O  OE2   . GLU D 2 104 ? 121.551 129.053 129.132 1.00 42.28  ? 104 GLU D OE2   1 
ATOM   7333 N  N     . ASN D 2 105 ? 122.824 133.587 124.182 1.00 31.85  ? 105 ASN D N     1 
ATOM   7334 C  CA    . ASN D 2 105 ? 123.507 134.769 123.599 1.00 26.54  ? 105 ASN D CA    1 
ATOM   7335 C  C     . ASN D 2 105 ? 122.520 135.609 122.798 1.00 23.65  ? 105 ASN D C     1 
ATOM   7336 O  O     . ASN D 2 105 ? 122.712 136.808 122.782 1.00 32.80  ? 105 ASN D O     1 
ATOM   7337 C  CB    . ASN D 2 105 ? 124.789 134.422 122.841 1.00 27.08  ? 105 ASN D CB    1 
ATOM   7338 C  CG    . ASN D 2 105 ? 126.002 134.419 123.724 1.00 27.11  ? 105 ASN D CG    1 
ATOM   7339 O  OD1   . ASN D 2 105 ? 126.415 135.474 124.197 1.00 40.18  ? 105 ASN D OD1   1 
ATOM   7340 N  ND2   . ASN D 2 105 ? 126.572 133.254 123.959 1.00 30.01  ? 105 ASN D ND2   1 
ATOM   7341 N  N     . ILE D 2 106 ? 121.599 134.984 122.076 1.00 25.78  ? 106 ILE D N     1 
ATOM   7342 C  CA    . ILE D 2 106 ? 120.644 135.746 121.232 1.00 27.61  ? 106 ILE D CA    1 
ATOM   7343 C  C     . ILE D 2 106 ? 119.798 136.645 122.122 1.00 28.90  ? 106 ILE D C     1 
ATOM   7344 O  O     . ILE D 2 106 ? 119.764 137.820 121.842 1.00 36.67  ? 106 ILE D O     1 
ATOM   7345 C  CB    . ILE D 2 106 ? 119.749 134.796 120.393 1.00 29.44  ? 106 ILE D CB    1 
ATOM   7346 C  CG1   . ILE D 2 106 ? 120.540 133.936 119.417 1.00 32.44  ? 106 ILE D CG1   1 
ATOM   7347 C  CG2   . ILE D 2 106 ? 118.627 135.555 119.687 1.00 28.06  ? 106 ILE D CG2   1 
ATOM   7348 C  CD1   . ILE D 2 106 ? 119.799 132.703 118.938 1.00 29.28  ? 106 ILE D CD1   1 
ATOM   7349 N  N     . GLU D 2 107 ? 119.279 136.121 123.225 1.00 37.87  ? 107 GLU D N     1 
ATOM   7350 C  CA    . GLU D 2 107 ? 118.510 136.924 124.198 1.00 31.48  ? 107 GLU D CA    1 
ATOM   7351 C  C     . GLU D 2 107 ? 119.339 137.987 124.913 1.00 29.70  ? 107 GLU D C     1 
ATOM   7352 O  O     . GLU D 2 107 ? 118.863 139.090 124.990 1.00 32.35  ? 107 GLU D O     1 
ATOM   7353 C  CB    . GLU D 2 107 ? 117.837 136.008 125.213 1.00 32.04  ? 107 GLU D CB    1 
ATOM   7354 C  CG    . GLU D 2 107 ? 116.801 136.790 126.013 1.00 32.96  ? 107 GLU D CG    1 
ATOM   7355 C  CD    . GLU D 2 107 ? 116.259 136.164 127.273 1.00 44.08  ? 107 GLU D CD    1 
ATOM   7356 O  OE1   . GLU D 2 107 ? 116.732 135.083 127.638 1.00 48.16  ? 107 GLU D OE1   1 
ATOM   7357 O  OE2   . GLU D 2 107 ? 115.346 136.760 127.871 1.00 46.20  ? 107 GLU D OE2   1 
ATOM   7358 N  N     . PHE D 2 108 ? 120.531 137.658 125.357 1.00 30.16  ? 108 PHE D N     1 
ATOM   7359 C  CA    . PHE D 2 108 ? 121.420 138.604 126.032 1.00 22.97  ? 108 PHE D CA    1 
ATOM   7360 C  C     . PHE D 2 108 ? 121.874 139.718 125.122 1.00 32.61  ? 108 PHE D C     1 
ATOM   7361 O  O     . PHE D 2 108 ? 121.856 140.863 125.562 1.00 34.32  ? 108 PHE D O     1 
ATOM   7362 C  CB    . PHE D 2 108 ? 122.589 137.731 126.465 1.00 24.16  ? 108 PHE D CB    1 
ATOM   7363 C  CG    . PHE D 2 108 ? 123.724 138.430 127.193 1.00 32.56  ? 108 PHE D CG    1 
ATOM   7364 C  CD1   . PHE D 2 108 ? 123.536 138.972 128.453 1.00 33.42  ? 108 PHE D CD1   1 
ATOM   7365 C  CD2   . PHE D 2 108 ? 124.976 138.541 126.609 1.00 33.84  ? 108 PHE D CD2   1 
ATOM   7366 C  CE1   . PHE D 2 108 ? 124.572 139.610 129.110 1.00 34.82  ? 108 PHE D CE1   1 
ATOM   7367 C  CE2   . PHE D 2 108 ? 126.009 139.181 127.270 1.00 34.12  ? 108 PHE D CE2   1 
ATOM   7368 C  CZ    . PHE D 2 108 ? 125.802 139.717 128.516 1.00 34.09  ? 108 PHE D CZ    1 
ATOM   7369 N  N     . LYS D 2 109 ? 122.285 139.398 123.903 1.00 39.12  ? 109 LYS D N     1 
ATOM   7370 C  CA    . LYS D 2 109 ? 122.724 140.431 122.943 1.00 34.47  ? 109 LYS D CA    1 
ATOM   7371 C  C     . LYS D 2 109 ? 121.539 141.299 122.540 1.00 33.51  ? 109 LYS D C     1 
ATOM   7372 O  O     . LYS D 2 109 ? 121.724 142.487 122.527 1.00 36.53  ? 109 LYS D O     1 
ATOM   7373 C  CB    . LYS D 2 109 ? 123.494 139.832 121.762 1.00 34.85  ? 109 LYS D CB    1 
ATOM   7374 C  CG    . LYS D 2 109 ? 124.231 140.800 120.860 1.00 36.29  ? 109 LYS D CG    1 
ATOM   7375 C  CD    . LYS D 2 109 ? 124.762 140.149 119.591 1.00 47.37  ? 109 LYS D CD    1 
ATOM   7376 C  CE    . LYS D 2 109 ? 125.454 141.102 118.671 1.00 43.41  ? 109 LYS D CE    1 
ATOM   7377 N  NZ    . LYS D 2 109 ? 126.293 142.041 119.418 1.00 45.19  ? 109 LYS D NZ    1 
ATOM   7378 N  N     . MET D 2 110 ? 120.386 140.713 122.272 1.00 35.83  ? 110 MET D N     1 
ATOM   7379 C  CA    . MET D 2 110 ? 119.144 141.399 121.868 1.00 38.58  ? 110 MET D CA    1 
ATOM   7380 C  C     . MET D 2 110 ? 118.647 142.302 123.000 1.00 37.99  ? 110 MET D C     1 
ATOM   7381 O  O     . MET D 2 110 ? 118.077 143.327 122.673 1.00 44.26  ? 110 MET D O     1 
ATOM   7382 C  CB    . MET D 2 110 ? 118.116 140.385 121.365 1.00 36.92  ? 110 MET D CB    1 
ATOM   7383 C  CG    . MET D 2 110 ? 118.283 140.042 119.914 1.00 35.88  ? 110 MET D CG    1 
ATOM   7384 S  SD    . MET D 2 110 ? 116.890 139.022 119.418 1.00 56.53  ? 110 MET D SD    1 
ATOM   7385 C  CE    . MET D 2 110 ? 115.929 140.289 118.588 1.00 40.74  ? 110 MET D CE    1 
ATOM   7386 N  N     . LEU D 2 111 ? 118.741 141.888 124.251 1.00 41.50  ? 111 LEU D N     1 
ATOM   7387 C  CA    . LEU D 2 111 ? 118.395 142.711 125.433 1.00 31.26  ? 111 LEU D CA    1 
ATOM   7388 C  C     . LEU D 2 111 ? 119.335 143.903 125.495 1.00 34.65  ? 111 LEU D C     1 
ATOM   7389 O  O     . LEU D 2 111 ? 118.864 144.984 125.831 1.00 42.95  ? 111 LEU D O     1 
ATOM   7390 C  CB    . LEU D 2 111 ? 118.434 141.906 126.730 1.00 33.56  ? 111 LEU D CB    1 
ATOM   7391 C  CG    . LEU D 2 111 ? 117.280 140.939 127.003 1.00 32.85  ? 111 LEU D CG    1 
ATOM   7392 C  CD1   . LEU D 2 111 ? 117.633 140.035 128.164 1.00 37.97  ? 111 LEU D CD1   1 
ATOM   7393 C  CD2   . LEU D 2 111 ? 115.954 141.624 127.233 1.00 35.49  ? 111 LEU D CD2   1 
ATOM   7394 N  N     . CYS D 2 112 ? 120.606 143.692 125.194 1.00 41.00  ? 112 CYS D N     1 
ATOM   7395 C  CA    . CYS D 2 112 ? 121.629 144.753 125.227 1.00 34.90  ? 112 CYS D CA    1 
ATOM   7396 C  C     . CYS D 2 112 ? 121.475 145.653 123.997 1.00 43.26  ? 112 CYS D C     1 
ATOM   7397 O  O     . CYS D 2 112 ? 121.894 146.799 124.094 1.00 50.42  ? 112 CYS D O     1 
ATOM   7398 C  CB    . CYS D 2 112 ? 123.021 144.184 125.465 1.00 42.80  ? 112 CYS D CB    1 
ATOM   7399 S  SG    . CYS D 2 112 ? 123.240 143.273 127.013 1.00 49.19  ? 112 CYS D SG    1 
ATOM   7400 N  N     . MET D 2 113 ? 120.943 145.162 122.865 1.00 45.14  ? 113 MET D N     1 
ATOM   7401 C  CA    . MET D 2 113 ? 120.620 146.134 121.819 1.00 44.93  ? 113 MET D CA    1 
ATOM   7402 C  C     . MET D 2 113 ? 119.358 146.936 122.109 1.00 48.68  ? 113 MET D C     1 
ATOM   7403 O  O     . MET D 2 113 ? 119.140 147.960 121.455 1.00 59.73  ? 113 MET D O     1 
ATOM   7404 C  CB    . MET D 2 113 ? 120.462 145.470 120.447 1.00 46.26  ? 113 MET D CB    1 
ATOM   7405 C  CG    . MET D 2 113 ? 121.491 144.427 120.098 1.00 44.26  ? 113 MET D CG    1 
ATOM   7406 S  SD    . MET D 2 113 ? 120.962 143.360 118.750 1.00 55.89  ? 113 MET D SD    1 
ATOM   7407 C  CE    . MET D 2 113 ? 122.445 143.331 117.764 1.00 46.78  ? 113 MET D CE    1 
ATOM   7408 N  N     . GLY D 2 114 ? 118.524 146.505 123.048 1.00 38.18  ? 114 GLY D N     1 
ATOM   7409 C  CA    . GLY D 2 114 ? 117.337 147.252 123.397 1.00 38.52  ? 114 GLY D CA    1 
ATOM   7410 C  C     . GLY D 2 114 ? 116.025 146.671 122.925 1.00 44.78  ? 114 GLY D C     1 
ATOM   7411 O  O     . GLY D 2 114 ? 115.013 147.377 122.959 1.00 48.07  ? 114 GLY D O     1 
ATOM   7412 N  N     . PHE D 2 115 ? 116.008 145.420 122.476 1.00 47.91  ? 115 PHE D N     1 
ATOM   7413 C  CA    . PHE D 2 115 ? 114.760 144.783 122.089 1.00 47.44  ? 115 PHE D CA    1 
ATOM   7414 C  C     . PHE D 2 115 ? 113.946 144.415 123.326 1.00 47.06  ? 115 PHE D C     1 
ATOM   7415 O  O     . PHE D 2 115 ? 114.486 144.217 124.417 1.00 49.04  ? 115 PHE D O     1 
ATOM   7416 C  CB    . PHE D 2 115 ? 115.030 143.531 121.254 1.00 47.30  ? 115 PHE D CB    1 
ATOM   7417 C  CG    . PHE D 2 115 ? 115.561 143.819 119.880 1.00 48.24  ? 115 PHE D CG    1 
ATOM   7418 C  CD1   . PHE D 2 115 ? 116.924 143.941 119.659 1.00 47.67  ? 115 PHE D CD1   1 
ATOM   7419 C  CD2   . PHE D 2 115 ? 114.695 143.962 118.807 1.00 48.33  ? 115 PHE D CD2   1 
ATOM   7420 C  CE1   . PHE D 2 115 ? 117.415 144.205 118.394 1.00 46.77  ? 115 PHE D CE1   1 
ATOM   7421 C  CE2   . PHE D 2 115 ? 115.179 144.225 117.539 1.00 50.26  ? 115 PHE D CE2   1 
ATOM   7422 C  CZ    . PHE D 2 115 ? 116.540 144.345 117.333 1.00 47.01  ? 115 PHE D CZ    1 
ATOM   7423 N  N     . LYS D 2 116 ? 112.632 144.334 123.147 1.00 52.97  ? 116 LYS D N     1 
ATOM   7424 C  CA    . LYS D 2 116 ? 111.749 143.955 124.237 1.00 52.85  ? 116 LYS D CA    1 
ATOM   7425 C  C     . LYS D 2 116 ? 111.575 142.440 124.277 1.00 54.82  ? 116 LYS D C     1 
ATOM   7426 O  O     . LYS D 2 116 ? 112.025 141.714 123.388 1.00 63.94  ? 116 LYS D O     1 
ATOM   7427 C  CB    . LYS D 2 116 ? 110.400 144.657 124.104 1.00 55.20  ? 116 LYS D CB    1 
ATOM   7428 C  CG    . LYS D 2 116 ? 110.505 146.171 124.028 1.00 55.76  ? 116 LYS D CG    1 
ATOM   7429 C  CD    . LYS D 2 116 ? 111.232 146.728 125.241 1.00 56.20  ? 116 LYS D CD    1 
ATOM   7430 C  CE    . LYS D 2 116 ? 112.071 147.939 124.875 1.00 56.04  ? 116 LYS D CE    1 
ATOM   7431 N  NZ    . LYS D 2 116 ? 112.772 148.507 126.059 1.00 56.51  ? 116 LYS D NZ    1 
ATOM   7432 N  N     . ARG D 2 117 ? 110.913 141.970 125.339 1.00 50.48  ? 117 ARG D N     1 
ATOM   7433 C  CA    . ARG D 2 117 ? 110.767 140.535 125.586 1.00 51.56  ? 117 ARG D CA    1 
ATOM   7434 C  C     . ARG D 2 117 ? 109.926 139.859 124.508 1.00 54.04  ? 117 ARG D C     1 
ATOM   7435 O  O     . ARG D 2 117 ? 110.276 138.776 124.016 1.00 54.22  ? 117 ARG D O     1 
ATOM   7436 C  CB    . ARG D 2 117 ? 110.145 140.319 126.965 1.00 48.51  ? 117 ARG D CB    1 
ATOM   7437 C  CG    . ARG D 2 117 ? 110.259 138.908 127.501 1.00 52.94  ? 117 ARG D CG    1 
ATOM   7438 C  CD    . ARG D 2 117 ? 109.386 138.719 128.732 1.00 53.20  ? 117 ARG D CD    1 
ATOM   7439 N  NE    . ARG D 2 117 ? 109.177 139.967 129.456 1.00 54.96  ? 117 ARG D NE    1 
ATOM   7440 C  CZ    . ARG D 2 117 ? 108.581 140.058 130.638 1.00 57.84  ? 117 ARG D CZ    1 
ATOM   7441 N  NH1   . ARG D 2 117 ? 108.151 138.983 131.278 1.00 56.18  ? 117 ARG D NH1   1 
ATOM   7442 N  NH2   . ARG D 2 117 ? 108.416 141.256 131.191 1.00 51.30  ? 117 ARG D NH2   1 
ATOM   7443 N  N     . LYS D 2 118 ? 108.814 140.494 124.126 1.00 58.32  ? 118 LYS D N     1 
ATOM   7444 C  CA    . LYS D 2 118 ? 107.937 139.934 123.101 1.00 54.55  ? 118 LYS D CA    1 
ATOM   7445 C  C     . LYS D 2 118 ? 108.612 139.928 121.736 1.00 55.58  ? 118 LYS D C     1 
ATOM   7446 O  O     . LYS D 2 118 ? 108.428 138.989 120.956 1.00 55.37  ? 118 LYS D O     1 
ATOM   7447 C  CB    . LYS D 2 118 ? 106.618 140.712 123.042 1.00 54.87  ? 118 LYS D CB    1 
ATOM   7448 C  CG    . LYS D 2 118 ? 105.462 140.153 123.889 1.00 59.18  ? 118 LYS D CG    1 
ATOM   7449 C  CD    . LYS D 2 118 ? 105.799 139.960 125.362 1.00 58.98  ? 118 LYS D CD    1 
ATOM   7450 C  CE    . LYS D 2 118 ? 104.536 139.811 126.197 1.00 57.96  ? 118 LYS D CE    1 
ATOM   7451 N  NZ    . LYS D 2 118 ? 103.744 141.073 126.231 1.00 55.18  ? 118 LYS D NZ    1 
ATOM   7452 N  N     . GLU D 2 119 ? 109.416 140.955 121.447 1.00 55.92  ? 119 GLU D N     1 
ATOM   7453 C  CA    . GLU D 2 119 ? 110.153 141.002 120.186 1.00 55.83  ? 119 GLU D CA    1 
ATOM   7454 C  C     . GLU D 2 119 ? 111.204 139.899 120.109 1.00 58.08  ? 119 GLU D C     1 
ATOM   7455 O  O     . GLU D 2 119 ? 111.339 139.238 119.072 1.00 54.48  ? 119 GLU D O     1 
ATOM   7456 C  CB    . GLU D 2 119 ? 110.798 142.375 120.013 1.00 52.49  ? 119 GLU D CB    1 
ATOM   7457 C  CG    . GLU D 2 119 ? 109.820 143.474 119.635 1.00 57.84  ? 119 GLU D CG    1 
ATOM   7458 C  CD    . GLU D 2 119 ? 110.217 144.828 120.186 1.00 61.61  ? 119 GLU D CD    1 
ATOM   7459 O  OE1   . GLU D 2 119 ? 109.401 145.438 120.908 1.00 63.05  ? 119 GLU D OE1   1 
ATOM   7460 O  OE2   . GLU D 2 119 ? 111.344 145.282 119.900 1.00 61.33  ? 119 GLU D OE2   1 
ATOM   7461 N  N     . ILE D 2 120 ? 111.948 139.684 121.202 1.00 53.31  ? 120 ILE D N     1 
ATOM   7462 C  CA    . ILE D 2 120 ? 112.976 138.643 121.242 1.00 46.83  ? 120 ILE D CA    1 
ATOM   7463 C  C     . ILE D 2 120 ? 112.343 137.264 121.103 1.00 47.14  ? 120 ILE D C     1 
ATOM   7464 O  O     . ILE D 2 120 ? 112.815 136.419 120.329 1.00 53.44  ? 120 ILE D O     1 
ATOM   7465 C  CB    . ILE D 2 120 ? 113.804 138.762 122.537 1.00 48.10  ? 120 ILE D CB    1 
ATOM   7466 C  CG1   . ILE D 2 120 ? 114.658 140.026 122.509 1.00 47.24  ? 120 ILE D CG1   1 
ATOM   7467 C  CG2   . ILE D 2 120 ? 114.702 137.549 122.739 1.00 47.89  ? 120 ILE D CG2   1 
ATOM   7468 C  CD1   . ILE D 2 120 ? 115.357 140.316 123.810 1.00 44.06  ? 120 ILE D CD1   1 
ATOM   7469 N  N     . LYS D 2 121 ? 111.232 137.036 121.817 1.00 49.32  ? 121 LYS D N     1 
ATOM   7470 C  CA    . LYS D 2 121 ? 110.509 135.772 121.693 1.00 49.86  ? 121 LYS D CA    1 
ATOM   7471 C  C     . LYS D 2 121 ? 109.900 135.592 120.307 1.00 50.51  ? 121 LYS D C     1 
ATOM   7472 O  O     . LYS D 2 121 ? 109.743 134.457 119.843 1.00 52.02  ? 121 LYS D O     1 
ATOM   7473 C  CB    . LYS D 2 121 ? 109.415 135.686 122.757 1.00 50.81  ? 121 LYS D CB    1 
ATOM   7474 C  CG    . LYS D 2 121 ? 109.066 134.266 123.163 1.00 53.13  ? 121 LYS D CG    1 
ATOM   7475 C  CD    . LYS D 2 121 ? 107.586 133.985 122.969 1.00 53.43  ? 121 LYS D CD    1 
ATOM   7476 C  CE    . LYS D 2 121 ? 107.192 132.655 123.590 1.00 54.12  ? 121 LYS D CE    1 
ATOM   7477 N  NZ    . LYS D 2 121 ? 105.973 132.082 122.952 1.00 53.60  ? 121 LYS D NZ    1 
ATOM   7478 N  N     . ALA D 2 122 ? 109.551 136.691 119.633 1.00 53.19  ? 122 ALA D N     1 
ATOM   7479 C  CA    . ALA D 2 122 ? 109.005 136.586 118.286 1.00 52.32  ? 122 ALA D CA    1 
ATOM   7480 C  C     . ALA D 2 122 ? 110.076 136.212 117.269 1.00 51.99  ? 122 ALA D C     1 
ATOM   7481 O  O     . ALA D 2 122 ? 109.854 135.329 116.433 1.00 54.93  ? 122 ALA D O     1 
ATOM   7482 C  CB    . ALA D 2 122 ? 108.326 137.899 117.892 1.00 50.35  ? 122 ALA D CB    1 
ATOM   7483 N  N     . MET D 2 123 ? 111.241 136.859 117.314 1.00 55.21  ? 123 MET D N     1 
ATOM   7484 C  CA    . MET D 2 123 ? 112.189 136.655 116.219 1.00 54.86  ? 123 MET D CA    1 
ATOM   7485 C  C     . MET D 2 123 ? 113.414 135.824 116.585 1.00 52.41  ? 123 MET D C     1 
ATOM   7486 O  O     . MET D 2 123 ? 114.369 135.805 115.808 1.00 58.33  ? 123 MET D O     1 
ATOM   7487 C  CB    . MET D 2 123 ? 112.644 137.990 115.617 1.00 55.90  ? 123 MET D CB    1 
ATOM   7488 C  CG    . MET D 2 123 ? 113.302 138.932 116.570 1.00 52.70  ? 123 MET D CG    1 
ATOM   7489 S  SD    . MET D 2 123 ? 112.720 140.635 116.439 1.00 73.20  ? 123 MET D SD    1 
ATOM   7490 C  CE    . MET D 2 123 ? 113.461 141.143 114.890 1.00 57.83  ? 123 MET D CE    1 
ATOM   7491 N  N     . THR D 2 124 ? 113.422 135.142 117.732 1.00 43.99  ? 124 THR D N     1 
ATOM   7492 C  CA    . THR D 2 124 ? 114.419 134.093 117.962 1.00 44.92  ? 124 THR D CA    1 
ATOM   7493 C  C     . THR D 2 124 ? 114.428 132.957 116.922 1.00 46.62  ? 124 THR D C     1 
ATOM   7494 O  O     . THR D 2 124 ? 115.536 132.580 116.487 1.00 45.38  ? 124 THR D O     1 
ATOM   7495 C  CB    . THR D 2 124 ? 114.255 133.552 119.390 1.00 45.43  ? 124 THR D CB    1 
ATOM   7496 O  OG1   . THR D 2 124 ? 114.280 134.643 120.316 1.00 52.19  ? 124 THR D OG1   1 
ATOM   7497 C  CG2   . THR D 2 124 ? 115.374 132.590 119.749 1.00 41.68  ? 124 THR D CG2   1 
ATOM   7498 N  N     . PRO D 2 125 ? 113.288 132.353 116.491 1.00 55.25  ? 125 PRO D N     1 
ATOM   7499 C  CA    . PRO D 2 125 ? 113.410 131.183 115.588 1.00 49.28  ? 125 PRO D CA    1 
ATOM   7500 C  C     . PRO D 2 125 ? 113.974 131.469 114.202 1.00 46.86  ? 125 PRO D C     1 
ATOM   7501 O  O     . PRO D 2 125 ? 114.689 130.617 113.664 1.00 49.59  ? 125 PRO D O     1 
ATOM   7502 C  CB    . PRO D 2 125 ? 111.971 130.651 115.503 1.00 53.03  ? 125 PRO D CB    1 
ATOM   7503 C  CG    . PRO D 2 125 ? 111.305 131.172 116.693 1.00 46.30  ? 125 PRO D CG    1 
ATOM   7504 C  CD    . PRO D 2 125 ? 111.863 132.529 116.855 1.00 49.09  ? 125 PRO D CD    1 
ATOM   7505 N  N     . LYS D 2 126 ? 113.700 132.630 113.602 1.00 43.50  ? 126 LYS D N     1 
ATOM   7506 C  CA    . LYS D 2 126 ? 114.324 132.908 112.311 1.00 45.21  ? 126 LYS D CA    1 
ATOM   7507 C  C     . LYS D 2 126 ? 115.789 133.304 112.457 1.00 45.82  ? 126 LYS D C     1 
ATOM   7508 O  O     . LYS D 2 126 ? 116.566 133.133 111.514 1.00 49.10  ? 126 LYS D O     1 
ATOM   7509 C  CB    . LYS D 2 126 ? 113.539 133.951 111.512 1.00 49.07  ? 126 LYS D CB    1 
ATOM   7510 C  CG    . LYS D 2 126 ? 112.055 133.647 111.368 1.00 52.34  ? 126 LYS D CG    1 
ATOM   7511 C  CD    . LYS D 2 126 ? 111.163 134.838 111.617 1.00 53.42  ? 126 LYS D CD    1 
ATOM   7512 C  CE    . LYS D 2 126 ? 111.138 135.220 113.065 1.00 54.91  ? 126 LYS D CE    1 
ATOM   7513 N  NZ    . LYS D 2 126 ? 110.103 134.464 113.827 1.00 50.23  ? 126 LYS D NZ    1 
ATOM   7514 N  N     . ILE D 2 127 ? 116.203 133.782 113.635 1.00 42.42  ? 127 ILE D N     1 
ATOM   7515 C  CA    . ILE D 2 127 ? 117.636 133.944 113.892 1.00 37.40  ? 127 ILE D CA    1 
ATOM   7516 C  C     . ILE D 2 127 ? 118.322 132.582 113.956 1.00 37.11  ? 127 ILE D C     1 
ATOM   7517 O  O     . ILE D 2 127 ? 119.407 132.387 113.385 1.00 43.57  ? 127 ILE D O     1 
ATOM   7518 C  CB    . ILE D 2 127 ? 117.871 134.773 115.173 1.00 36.99  ? 127 ILE D CB    1 
ATOM   7519 C  CG1   . ILE D 2 127 ? 117.470 136.229 114.950 1.00 35.68  ? 127 ILE D CG1   1 
ATOM   7520 C  CG2   . ILE D 2 127 ? 119.326 134.724 115.619 1.00 32.19  ? 127 ILE D CG2   1 
ATOM   7521 C  CD1   . ILE D 2 127 ? 117.509 137.066 116.204 1.00 35.11  ? 127 ILE D CD1   1 
ATOM   7522 N  N     . ILE D 2 128 ? 117.679 131.613 114.621 1.00 37.73  ? 128 ILE D N     1 
ATOM   7523 C  CA    . ILE D 2 128 ? 118.199 130.244 114.670 1.00 36.79  ? 128 ILE D CA    1 
ATOM   7524 C  C     . ILE D 2 128 ? 118.246 129.627 113.274 1.00 40.08  ? 128 ILE D C     1 
ATOM   7525 O  O     . ILE D 2 128 ? 119.221 128.957 112.906 1.00 44.95  ? 128 ILE D O     1 
ATOM   7526 C  CB    . ILE D 2 128 ? 117.351 129.395 115.639 1.00 38.44  ? 128 ILE D CB    1 
ATOM   7527 C  CG1   . ILE D 2 128 ? 117.452 129.940 117.059 1.00 37.78  ? 128 ILE D CG1   1 
ATOM   7528 C  CG2   . ILE D 2 128 ? 117.776 127.933 115.627 1.00 36.85  ? 128 ILE D CG2   1 
ATOM   7529 C  CD1   . ILE D 2 128 ? 116.342 129.454 117.946 1.00 39.17  ? 128 ILE D CD1   1 
ATOM   7530 N  N     . GLU D 2 129 ? 117.208 129.868 112.468 1.00 42.03  ? 129 GLU D N     1 
ATOM   7531 C  CA    . GLU D 2 129 ? 117.155 129.327 111.111 1.00 43.01  ? 129 GLU D CA    1 
ATOM   7532 C  C     . GLU D 2 129 ? 118.197 129.986 110.210 1.00 47.47  ? 129 GLU D C     1 
ATOM   7533 O  O     . GLU D 2 129 ? 118.779 129.326 109.341 1.00 52.62  ? 129 GLU D O     1 
ATOM   7534 C  CB    . GLU D 2 129 ? 115.712 129.460 110.578 1.00 43.21  ? 129 GLU D CB    1 
ATOM   7535 C  CG    . GLU D 2 129 ? 115.379 129.411 109.049 1.00 49.83  ? 129 GLU D CG    1 
ATOM   7536 C  CD    . GLU D 2 129 ? 115.804 130.632 108.226 1.00 56.90  ? 129 GLU D CD    1 
ATOM   7537 O  OE1   . GLU D 2 129 ? 116.487 130.448 107.195 1.00 53.26  ? 129 GLU D OE1   1 
ATOM   7538 O  OE2   . GLU D 2 129 ? 115.455 131.766 108.614 1.00 54.13  ? 129 GLU D OE2   1 
ATOM   7539 N  N     . PHE D 2 130 ? 118.438 131.287 110.395 1.00 45.13  ? 130 PHE D N     1 
ATOM   7540 C  CA    . PHE D 2 130 ? 119.422 131.990 109.581 1.00 41.86  ? 130 PHE D CA    1 
ATOM   7541 C  C     . PHE D 2 130 ? 120.842 131.582 109.947 1.00 39.29  ? 130 PHE D C     1 
ATOM   7542 O  O     . PHE D 2 130 ? 121.715 131.523 109.075 1.00 45.73  ? 130 PHE D O     1 
ATOM   7543 C  CB    . PHE D 2 130 ? 119.240 133.500 109.739 1.00 38.97  ? 130 PHE D CB    1 
ATOM   7544 C  CG    . PHE D 2 130 ? 119.960 134.314 108.701 1.00 40.98  ? 130 PHE D CG    1 
ATOM   7545 C  CD1   . PHE D 2 130 ? 119.368 134.576 107.475 1.00 43.04  ? 130 PHE D CD1   1 
ATOM   7546 C  CD2   . PHE D 2 130 ? 121.224 134.827 108.954 1.00 37.47  ? 130 PHE D CD2   1 
ATOM   7547 C  CE1   . PHE D 2 130 ? 120.026 135.329 106.520 1.00 43.24  ? 130 PHE D CE1   1 
ATOM   7548 C  CE2   . PHE D 2 130 ? 121.887 135.579 108.003 1.00 42.28  ? 130 PHE D CE2   1 
ATOM   7549 C  CZ    . PHE D 2 130 ? 121.286 135.829 106.784 1.00 40.79  ? 130 PHE D CZ    1 
ATOM   7550 N  N     . SER D 2 131 ? 121.097 131.309 111.230 1.00 42.12  ? 131 SER D N     1 
ATOM   7551 C  CA    . SER D 2 131 ? 122.448 130.971 111.669 1.00 35.63  ? 131 SER D CA    1 
ATOM   7552 C  C     . SER D 2 131 ? 122.910 129.607 111.168 1.00 43.25  ? 131 SER D C     1 
ATOM   7553 O  O     . SER D 2 131 ? 124.120 129.409 111.014 1.00 47.86  ? 131 SER D O     1 
ATOM   7554 C  CB    . SER D 2 131 ? 122.528 131.024 113.194 1.00 33.39  ? 131 SER D CB    1 
ATOM   7555 O  OG    . SER D 2 131 ? 122.008 129.842 113.773 1.00 47.53  ? 131 SER D OG    1 
ATOM   7556 N  N     . GLU D 2 132 ? 121.971 128.683 110.916 1.00 48.41  ? 132 GLU D N     1 
ATOM   7557 C  CA    . GLU D 2 132 ? 122.226 127.326 110.409 1.00 47.13  ? 132 GLU D CA    1 
ATOM   7558 C  C     . GLU D 2 132 ? 123.185 126.539 111.300 1.00 41.64  ? 132 GLU D C     1 
ATOM   7559 O  O     . GLU D 2 132 ? 124.004 125.760 110.810 1.00 49.24  ? 132 GLU D O     1 
ATOM   7560 C  CB    . GLU D 2 132 ? 122.747 127.344 108.966 1.00 45.43  ? 132 GLU D CB    1 
ATOM   7561 C  CG    . GLU D 2 132 ? 121.926 128.184 108.011 1.00 48.60  ? 132 GLU D CG    1 
ATOM   7562 C  CD    . GLU D 2 132 ? 122.561 128.282 106.639 1.00 54.47  ? 132 GLU D CD    1 
ATOM   7563 O  OE1   . GLU D 2 132 ? 123.805 128.348 106.564 1.00 57.41  ? 132 GLU D OE1   1 
ATOM   7564 O  OE2   . GLU D 2 132 ? 121.817 128.295 105.637 1.00 55.33  ? 132 GLU D OE2   1 
ATOM   7565 N  N     . LEU D 2 133 ? 123.092 126.736 112.614 1.00 37.78  ? 133 LEU D N     1 
ATOM   7566 C  CA    . LEU D 2 133 ? 124.003 126.071 113.534 1.00 33.76  ? 133 LEU D CA    1 
ATOM   7567 C  C     . LEU D 2 133 ? 123.549 124.664 113.892 1.00 43.71  ? 133 LEU D C     1 
ATOM   7568 O  O     . LEU D 2 133 ? 124.380 123.847 114.303 1.00 45.34  ? 133 LEU D O     1 
ATOM   7569 C  CB    . LEU D 2 133 ? 124.170 126.909 114.802 1.00 37.60  ? 133 LEU D CB    1 
ATOM   7570 C  CG    . LEU D 2 133 ? 124.915 128.226 114.574 1.00 41.62  ? 133 LEU D CG    1 
ATOM   7571 C  CD1   . LEU D 2 133 ? 124.937 129.077 115.827 1.00 34.97  ? 133 LEU D CD1   1 
ATOM   7572 C  CD2   . LEU D 2 133 ? 126.325 127.958 114.083 1.00 39.59  ? 133 LEU D CD2   1 
ATOM   7573 N  N     . GLY D 2 134 ? 122.263 124.367 113.743 1.00 41.54  ? 134 GLY D N     1 
ATOM   7574 C  CA    . GLY D 2 134 ? 121.792 123.009 113.960 1.00 36.43  ? 134 GLY D CA    1 
ATOM   7575 C  C     . GLY D 2 134 ? 121.725 122.668 115.433 1.00 41.65  ? 134 GLY D C     1 
ATOM   7576 O  O     . GLY D 2 134 ? 121.054 123.340 116.223 1.00 43.80  ? 134 GLY D O     1 
ATOM   7577 N  N     . GLU D 2 135 ? 122.434 121.605 115.810 1.00 49.16  ? 135 GLU D N     1 
ATOM   7578 C  CA    . GLU D 2 135 ? 122.392 121.109 117.179 1.00 41.80  ? 135 GLU D CA    1 
ATOM   7579 C  C     . GLU D 2 135 ? 123.265 121.942 118.112 1.00 41.81  ? 135 GLU D C     1 
ATOM   7580 O  O     . GLU D 2 135 ? 123.081 121.892 119.333 1.00 45.85  ? 135 GLU D O     1 
ATOM   7581 C  CB    . GLU D 2 135 ? 122.818 119.638 117.186 1.00 45.61  ? 135 GLU D CB    1 
ATOM   7582 C  CG    . GLU D 2 135 ? 122.487 118.865 118.447 1.00 46.13  ? 135 GLU D CG    1 
ATOM   7583 C  CD    . GLU D 2 135 ? 121.959 117.481 118.143 1.00 54.30  ? 135 GLU D CD    1 
ATOM   7584 O  OE1   . GLU D 2 135 ? 121.828 117.139 116.949 1.00 52.64  ? 135 GLU D OE1   1 
ATOM   7585 O  OE2   . GLU D 2 135 ? 121.641 116.748 119.096 1.00 55.07  ? 135 GLU D OE2   1 
ATOM   7586 N  N     . PHE D 2 136 ? 124.179 122.742 117.564 1.00 30.64  ? 136 PHE D N     1 
ATOM   7587 C  CA    . PHE D 2 136 ? 125.109 123.515 118.376 1.00 28.31  ? 136 PHE D CA    1 
ATOM   7588 C  C     . PHE D 2 136 ? 124.505 124.793 118.944 1.00 29.00  ? 136 PHE D C     1 
ATOM   7589 O  O     . PHE D 2 136 ? 125.194 125.499 119.684 1.00 30.76  ? 136 PHE D O     1 
ATOM   7590 C  CB    . PHE D 2 136 ? 126.360 123.852 117.562 1.00 34.27  ? 136 PHE D CB    1 
ATOM   7591 C  CG    . PHE D 2 136 ? 127.461 122.839 117.701 1.00 37.00  ? 136 PHE D CG    1 
ATOM   7592 C  CD1   . PHE D 2 136 ? 128.394 122.948 118.720 1.00 30.71  ? 136 PHE D CD1   1 
ATOM   7593 C  CD2   . PHE D 2 136 ? 127.554 121.770 116.823 1.00 33.32  ? 136 PHE D CD2   1 
ATOM   7594 C  CE1   . PHE D 2 136 ? 129.407 122.014 118.857 1.00 26.46  ? 136 PHE D CE1   1 
ATOM   7595 C  CE2   . PHE D 2 136 ? 128.563 120.831 116.955 1.00 25.67  ? 136 PHE D CE2   1 
ATOM   7596 C  CZ    . PHE D 2 136 ? 129.490 120.955 117.974 1.00 28.67  ? 136 PHE D CZ    1 
ATOM   7597 N  N     . ILE D 2 137 ? 123.243 125.106 118.632 1.00 29.66  ? 137 ILE D N     1 
ATOM   7598 C  CA    . ILE D 2 137 ? 122.600 126.283 119.209 1.00 27.37  ? 137 ILE D CA    1 
ATOM   7599 C  C     . ILE D 2 137 ? 122.295 126.088 120.696 1.00 28.28  ? 137 ILE D C     1 
ATOM   7600 O  O     . ILE D 2 137 ? 122.117 127.070 121.424 1.00 33.18  ? 137 ILE D O     1 
ATOM   7601 C  CB    . ILE D 2 137 ? 121.334 126.648 118.388 1.00 32.03  ? 137 ILE D CB    1 
ATOM   7602 C  CG1   . ILE D 2 137 ? 120.936 128.116 118.586 1.00 32.50  ? 137 ILE D CG1   1 
ATOM   7603 C  CG2   . ILE D 2 137 ? 120.169 125.729 118.706 1.00 25.51  ? 137 ILE D CG2   1 
ATOM   7604 C  CD1   . ILE D 2 137 ? 121.995 129.105 118.171 1.00 30.62  ? 137 ILE D CD1   1 
ATOM   7605 N  N     . TYR D 2 138 ? 122.265 124.844 121.175 1.00 35.88  ? 138 TYR D N     1 
ATOM   7606 C  CA    . TYR D 2 138 ? 122.128 124.559 122.597 1.00 29.88  ? 138 TYR D CA    1 
ATOM   7607 C  C     . TYR D 2 138 ? 123.470 124.328 123.277 1.00 33.73  ? 138 TYR D C     1 
ATOM   7608 O  O     . TYR D 2 138 ? 123.502 124.004 124.467 1.00 43.20  ? 138 TYR D O     1 
ATOM   7609 C  CB    . TYR D 2 138 ? 121.221 123.345 122.826 1.00 35.82  ? 138 TYR D CB    1 
ATOM   7610 C  CG    . TYR D 2 138 ? 119.933 123.347 122.032 1.00 37.44  ? 138 TYR D CG    1 
ATOM   7611 C  CD1   . TYR D 2 138 ? 119.852 122.723 120.791 1.00 33.52  ? 138 TYR D CD1   1 
ATOM   7612 C  CD2   . TYR D 2 138 ? 118.805 124.002 122.513 1.00 36.71  ? 138 TYR D CD2   1 
ATOM   7613 C  CE1   . TYR D 2 138 ? 118.675 122.727 120.066 1.00 39.63  ? 138 TYR D CE1   1 
ATOM   7614 C  CE2   . TYR D 2 138 ? 117.627 124.017 121.794 1.00 35.13  ? 138 TYR D CE2   1 
ATOM   7615 C  CZ    . TYR D 2 138 ? 117.568 123.380 120.572 1.00 42.65  ? 138 TYR D CZ    1 
ATOM   7616 O  OH    . TYR D 2 138 ? 116.397 123.393 119.852 1.00 45.74  ? 138 TYR D OH    1 
ATOM   7617 N  N     . GLN D 2 139 ? 124.573 124.490 122.554 1.00 32.16  ? 139 GLN D N     1 
ATOM   7618 C  CA    . GLN D 2 139 ? 125.925 124.310 123.052 1.00 21.74  ? 139 GLN D CA    1 
ATOM   7619 C  C     . GLN D 2 139 ? 126.562 125.663 123.365 1.00 25.43  ? 139 GLN D C     1 
ATOM   7620 O  O     . GLN D 2 139 ? 126.177 126.675 122.773 1.00 34.84  ? 139 GLN D O     1 
ATOM   7621 C  CB    . GLN D 2 139 ? 126.781 123.557 122.026 1.00 25.77  ? 139 GLN D CB    1 
ATOM   7622 C  CG    . GLN D 2 139 ? 126.508 122.066 121.986 1.00 29.87  ? 139 GLN D CG    1 
ATOM   7623 C  CD    . GLN D 2 139 ? 126.623 121.421 123.354 1.00 32.69  ? 139 GLN D CD    1 
ATOM   7624 O  OE1   . GLN D 2 139 ? 127.698 121.394 123.949 1.00 36.23  ? 139 GLN D OE1   1 
ATOM   7625 N  NE2   . GLN D 2 139 ? 125.513 120.902 123.861 1.00 29.24  ? 139 GLN D NE2   1 
ATOM   7626 N  N     . PRO D 2 140 ? 127.511 125.718 124.306 1.00 29.85  ? 140 PRO D N     1 
ATOM   7627 C  CA    . PRO D 2 140 ? 128.180 126.991 124.613 1.00 27.40  ? 140 PRO D CA    1 
ATOM   7628 C  C     . PRO D 2 140 ? 128.998 127.523 123.442 1.00 31.86  ? 140 PRO D C     1 
ATOM   7629 O  O     . PRO D 2 140 ? 129.495 126.769 122.607 1.00 31.67  ? 140 PRO D O     1 
ATOM   7630 C  CB    . PRO D 2 140 ? 129.075 126.643 125.807 1.00 23.23  ? 140 PRO D CB    1 
ATOM   7631 C  CG    . PRO D 2 140 ? 128.428 125.475 126.434 1.00 26.74  ? 140 PRO D CG    1 
ATOM   7632 C  CD    . PRO D 2 140 ? 127.815 124.689 125.319 1.00 30.29  ? 140 PRO D CD    1 
ATOM   7633 N  N     . VAL D 2 141 ? 129.124 128.851 123.401 1.00 30.07  ? 141 VAL D N     1 
ATOM   7634 C  CA    . VAL D 2 141 ? 129.720 129.548 122.264 1.00 31.25  ? 141 VAL D CA    1 
ATOM   7635 C  C     . VAL D 2 141 ? 131.238 129.359 122.239 1.00 29.65  ? 141 VAL D C     1 
ATOM   7636 O  O     . VAL D 2 141 ? 131.858 129.372 121.167 1.00 32.39  ? 141 VAL D O     1 
ATOM   7637 C  CB    . VAL D 2 141 ? 129.254 131.026 122.320 1.00 30.44  ? 141 VAL D CB    1 
ATOM   7638 C  CG1   . VAL D 2 141 ? 130.200 132.012 121.645 1.00 32.29  ? 141 VAL D CG1   1 
ATOM   7639 C  CG2   . VAL D 2 141 ? 127.867 131.139 121.709 1.00 19.81  ? 141 VAL D CG2   1 
ATOM   7640 N  N     . LYS D 2 142 ? 131.846 129.073 123.396 1.00 34.12  ? 142 LYS D N     1 
ATOM   7641 C  CA    . LYS D 2 142 ? 133.279 128.787 123.438 1.00 27.47  ? 142 LYS D CA    1 
ATOM   7642 C  C     . LYS D 2 142 ? 133.626 127.459 122.768 1.00 36.49  ? 142 LYS D C     1 
ATOM   7643 O  O     . LYS D 2 142 ? 134.791 127.223 122.431 1.00 45.51  ? 142 LYS D O     1 
ATOM   7644 C  CB    . LYS D 2 142 ? 133.773 128.785 124.883 1.00 30.01  ? 142 LYS D CB    1 
ATOM   7645 C  CG    . LYS D 2 142 ? 133.075 127.772 125.767 1.00 33.18  ? 142 LYS D CG    1 
ATOM   7646 C  CD    . LYS D 2 142 ? 133.919 127.410 126.971 1.00 35.14  ? 142 LYS D CD    1 
ATOM   7647 C  CE    . LYS D 2 142 ? 133.047 126.947 128.121 1.00 40.18  ? 142 LYS D CE    1 
ATOM   7648 N  NZ    . LYS D 2 142 ? 132.979 125.465 128.224 1.00 41.41  ? 142 LYS D NZ    1 
ATOM   7649 N  N     . LYS D 2 143 ? 132.640 126.587 122.564 1.00 30.87  ? 143 LYS D N     1 
ATOM   7650 C  CA    . LYS D 2 143 ? 132.835 125.342 121.833 1.00 20.68  ? 143 LYS D CA    1 
ATOM   7651 C  C     . LYS D 2 143 ? 132.618 125.495 120.333 1.00 24.48  ? 143 LYS D C     1 
ATOM   7652 O  O     . LYS D 2 143 ? 132.689 124.498 119.611 1.00 30.68  ? 143 LYS D O     1 
ATOM   7653 C  CB    . LYS D 2 143 ? 131.897 124.263 122.378 1.00 31.80  ? 143 LYS D CB    1 
ATOM   7654 C  CG    . LYS D 2 143 ? 132.196 123.856 123.803 1.00 31.25  ? 143 LYS D CG    1 
ATOM   7655 C  CD    . LYS D 2 143 ? 131.109 122.960 124.369 1.00 30.08  ? 143 LYS D CD    1 
ATOM   7656 C  CE    . LYS D 2 143 ? 131.434 122.518 125.788 1.00 36.41  ? 143 LYS D CE    1 
ATOM   7657 N  NZ    . LYS D 2 143 ? 132.837 122.825 126.184 1.00 37.64  ? 143 LYS D NZ    1 
ATOM   7658 N  N     . TYR D 2 144 ? 132.348 126.704 119.853 1.00 34.77  ? 144 TYR D N     1 
ATOM   7659 C  CA    . TYR D 2 144 ? 132.080 126.912 118.438 1.00 24.36  ? 144 TYR D CA    1 
ATOM   7660 C  C     . TYR D 2 144 ? 133.386 127.026 117.661 1.00 31.22  ? 144 TYR D C     1 
ATOM   7661 O  O     . TYR D 2 144 ? 134.463 127.243 118.222 1.00 36.57  ? 144 TYR D O     1 
ATOM   7662 C  CB    . TYR D 2 144 ? 131.268 128.191 118.202 1.00 18.56  ? 144 TYR D CB    1 
ATOM   7663 C  CG    . TYR D 2 144 ? 129.787 128.155 118.538 1.00 26.67  ? 144 TYR D CG    1 
ATOM   7664 C  CD1   . TYR D 2 144 ? 129.243 127.158 119.342 1.00 24.24  ? 144 TYR D CD1   1 
ATOM   7665 C  CD2   . TYR D 2 144 ? 128.934 129.137 118.050 1.00 24.20  ? 144 TYR D CD2   1 
ATOM   7666 C  CE1   . TYR D 2 144 ? 127.901 127.143 119.648 1.00 17.77  ? 144 TYR D CE1   1 
ATOM   7667 C  CE2   . TYR D 2 144 ? 127.587 129.129 118.348 1.00 18.99  ? 144 TYR D CE2   1 
ATOM   7668 C  CZ    . TYR D 2 144 ? 127.076 128.128 119.145 1.00 28.86  ? 144 TYR D CZ    1 
ATOM   7669 O  OH    . TYR D 2 144 ? 125.735 128.115 119.444 1.00 33.37  ? 144 TYR D OH    1 
ATOM   7670 N  N     . SER D 2 145 ? 133.276 126.879 116.347 1.00 28.39  ? 145 SER D N     1 
ATOM   7671 C  CA    . SER D 2 145 ? 134.330 127.324 115.456 1.00 24.68  ? 145 SER D CA    1 
ATOM   7672 C  C     . SER D 2 145 ? 134.207 128.832 115.240 1.00 27.78  ? 145 SER D C     1 
ATOM   7673 O  O     . SER D 2 145 ? 133.224 129.460 115.638 1.00 35.68  ? 145 SER D O     1 
ATOM   7674 C  CB    . SER D 2 145 ? 134.266 126.561 114.134 1.00 24.97  ? 145 SER D CB    1 
ATOM   7675 O  OG    . SER D 2 145 ? 133.544 127.279 113.153 1.00 35.16  ? 145 SER D OG    1 
ATOM   7676 N  N     . SER D 2 146 ? 135.236 129.419 114.619 1.00 29.70  ? 146 SER D N     1 
ATOM   7677 C  CA    . SER D 2 146 ? 135.243 130.862 114.385 1.00 18.46  ? 146 SER D CA    1 
ATOM   7678 C  C     . SER D 2 146 ? 134.169 131.273 113.384 1.00 29.15  ? 146 SER D C     1 
ATOM   7679 O  O     . SER D 2 146 ? 133.517 132.313 113.555 1.00 38.36  ? 146 SER D O     1 
ATOM   7680 C  CB    . SER D 2 146 ? 136.621 131.311 113.904 1.00 27.54  ? 146 SER D CB    1 
ATOM   7681 O  OG    . SER D 2 146 ? 137.651 130.645 114.612 1.00 40.72  ? 146 SER D OG    1 
ATOM   7682 N  N     . GLY D 2 147 ? 133.970 130.463 112.343 1.00 23.70  ? 147 GLY D N     1 
ATOM   7683 C  CA    . GLY D 2 147 ? 132.915 130.744 111.384 1.00 15.16  ? 147 GLY D CA    1 
ATOM   7684 C  C     . GLY D 2 147 ? 131.527 130.608 111.977 1.00 22.28  ? 147 GLY D C     1 
ATOM   7685 O  O     . GLY D 2 147 ? 130.627 131.378 111.641 1.00 32.71  ? 147 GLY D O     1 
ATOM   7686 N  N     . MET D 2 148 ? 131.311 129.636 112.911 1.00 27.11  ? 148 MET D N     1 
ATOM   7687 C  CA    . MET D 2 148 ? 130.019 129.460 113.572 1.00 24.46  ? 148 MET D CA    1 
ATOM   7688 C  C     . MET D 2 148 ? 129.695 130.634 114.490 1.00 28.67  ? 148 MET D C     1 
ATOM   7689 O  O     . MET D 2 148 ? 128.554 131.117 114.521 1.00 33.14  ? 148 MET D O     1 
ATOM   7690 C  CB    . MET D 2 148 ? 130.018 128.148 114.357 1.00 21.77  ? 148 MET D CB    1 
ATOM   7691 C  CG    . MET D 2 148 ? 130.021 126.905 113.485 1.00 29.66  ? 148 MET D CG    1 
ATOM   7692 S  SD    . MET D 2 148 ? 130.526 125.420 114.369 1.00 35.90  ? 148 MET D SD    1 
ATOM   7693 C  CE    . MET D 2 148 ? 129.143 125.191 115.479 1.00 25.11  ? 148 MET D CE    1 
ATOM   7694 N  N     . ARG D 2 149 ? 130.699 131.110 115.236 1.00 26.60  ? 149 ARG D N     1 
ATOM   7695 C  CA    . ARG D 2 149 ? 130.538 132.286 116.085 1.00 22.90  ? 149 ARG D CA    1 
ATOM   7696 C  C     . ARG D 2 149 ? 130.239 133.529 115.255 1.00 27.38  ? 149 ARG D C     1 
ATOM   7697 O  O     . ARG D 2 149 ? 129.390 134.352 115.628 1.00 40.55  ? 149 ARG D O     1 
ATOM   7698 C  CB    . ARG D 2 149 ? 131.805 132.494 116.913 1.00 19.00  ? 149 ARG D CB    1 
ATOM   7699 C  CG    . ARG D 2 149 ? 131.561 132.860 118.355 1.00 33.34  ? 149 ARG D CG    1 
ATOM   7700 C  CD    . ARG D 2 149 ? 132.864 133.047 119.113 1.00 39.49  ? 149 ARG D CD    1 
ATOM   7701 N  NE    . ARG D 2 149 ? 133.958 132.264 118.548 1.00 40.79  ? 149 ARG D NE    1 
ATOM   7702 C  CZ    . ARG D 2 149 ? 134.337 131.072 118.990 1.00 38.66  ? 149 ARG D CZ    1 
ATOM   7703 N  NH1   . ARG D 2 149 ? 133.719 130.478 119.997 1.00 35.75  ? 149 ARG D NH1   1 
ATOM   7704 N  NH2   . ARG D 2 149 ? 135.361 130.458 118.405 1.00 38.44  ? 149 ARG D NH2   1 
ATOM   7705 N  N     . ALA D 2 150 ? 130.924 133.668 114.116 1.00 26.58  ? 150 ALA D N     1 
ATOM   7706 C  CA    . ALA D 2 150 ? 130.682 134.791 113.218 1.00 20.67  ? 150 ALA D CA    1 
ATOM   7707 C  C     . ALA D 2 150 ? 129.277 134.744 112.622 1.00 24.04  ? 150 ALA D C     1 
ATOM   7708 O  O     . ALA D 2 150 ? 128.612 135.780 112.507 1.00 31.14  ? 150 ALA D O     1 
ATOM   7709 C  CB    . ALA D 2 150 ? 131.739 134.799 112.117 1.00 23.20  ? 150 ALA D CB    1 
ATOM   7710 N  N     . LYS D 2 151 ? 128.812 133.545 112.252 1.00 29.33  ? 151 LYS D N     1 
ATOM   7711 C  CA    . LYS D 2 151 ? 127.464 133.380 111.712 1.00 25.04  ? 151 LYS D CA    1 
ATOM   7712 C  C     . LYS D 2 151 ? 126.398 133.720 112.744 1.00 28.27  ? 151 LYS D C     1 
ATOM   7713 O  O     . LYS D 2 151 ? 125.412 134.395 112.423 1.00 31.92  ? 151 LYS D O     1 
ATOM   7714 C  CB    . LYS D 2 151 ? 127.273 131.947 111.211 1.00 28.34  ? 151 LYS D CB    1 
ATOM   7715 C  CG    . LYS D 2 151 ? 127.910 131.649 109.866 1.00 32.21  ? 151 LYS D CG    1 
ATOM   7716 C  CD    . LYS D 2 151 ? 127.511 130.275 109.350 1.00 31.86  ? 151 LYS D CD    1 
ATOM   7717 C  CE    . LYS D 2 151 ? 127.804 129.185 110.364 1.00 31.34  ? 151 LYS D CE    1 
ATOM   7718 N  NZ    . LYS D 2 151 ? 127.207 127.881 109.967 1.00 39.20  ? 151 LYS D NZ    1 
ATOM   7719 N  N     . LEU D 2 152 ? 126.584 133.268 113.992 1.00 31.88  ? 152 LEU D N     1 
ATOM   7720 C  CA    . LEU D 2 152 ? 125.623 133.579 115.048 1.00 25.36  ? 152 LEU D CA    1 
ATOM   7721 C  C     . LEU D 2 152 ? 125.598 135.072 115.364 1.00 28.75  ? 152 LEU D C     1 
ATOM   7722 O  O     . LEU D 2 152 ? 124.518 135.665 115.509 1.00 36.34  ? 152 LEU D O     1 
ATOM   7723 C  CB    . LEU D 2 152 ? 125.937 132.770 116.307 1.00 25.26  ? 152 LEU D CB    1 
ATOM   7724 C  CG    . LEU D 2 152 ? 124.997 133.007 117.494 1.00 27.23  ? 152 LEU D CG    1 
ATOM   7725 C  CD1   . LEU D 2 152 ? 123.579 132.587 117.147 1.00 21.69  ? 152 LEU D CD1   1 
ATOM   7726 C  CD2   . LEU D 2 152 ? 125.484 132.282 118.733 1.00 30.63  ? 152 LEU D CD2   1 
ATOM   7727 N  N     . GLY D 2 153 ? 126.778 135.699 115.449 1.00 28.07  ? 153 GLY D N     1 
ATOM   7728 C  CA    . GLY D 2 153 ? 126.838 137.129 115.711 1.00 24.40  ? 153 GLY D CA    1 
ATOM   7729 C  C     . GLY D 2 153 ? 126.230 137.963 114.601 1.00 27.64  ? 153 GLY D C     1 
ATOM   7730 O  O     . GLY D 2 153 ? 125.527 138.942 114.864 1.00 37.07  ? 153 GLY D O     1 
ATOM   7731 N  N     . PHE D 2 154 ? 126.461 137.567 113.345 1.00 31.63  ? 154 PHE D N     1 
ATOM   7732 C  CA    . PHE D 2 154 ? 125.843 138.257 112.218 1.00 23.67  ? 154 PHE D CA    1 
ATOM   7733 C  C     . PHE D 2 154 ? 124.332 138.064 112.202 1.00 30.59  ? 154 PHE D C     1 
ATOM   7734 O  O     . PHE D 2 154 ? 123.592 138.996 111.868 1.00 38.75  ? 154 PHE D O     1 
ATOM   7735 C  CB    . PHE D 2 154 ? 126.458 137.774 110.904 1.00 31.63  ? 154 PHE D CB    1 
ATOM   7736 C  CG    . PHE D 2 154 ? 126.175 138.673 109.735 1.00 32.72  ? 154 PHE D CG    1 
ATOM   7737 C  CD1   . PHE D 2 154 ? 127.025 139.725 109.433 1.00 34.23  ? 154 PHE D CD1   1 
ATOM   7738 C  CD2   . PHE D 2 154 ? 125.060 138.467 108.935 1.00 30.72  ? 154 PHE D CD2   1 
ATOM   7739 C  CE1   . PHE D 2 154 ? 126.767 140.556 108.360 1.00 34.44  ? 154 PHE D CE1   1 
ATOM   7740 C  CE2   . PHE D 2 154 ? 124.793 139.297 107.866 1.00 30.90  ? 154 PHE D CE2   1 
ATOM   7741 C  CZ    . PHE D 2 154 ? 125.651 140.339 107.575 1.00 34.33  ? 154 PHE D CZ    1 
ATOM   7742 N  N     . SER D 2 155 ? 123.857 136.861 112.548 1.00 34.69  ? 155 SER D N     1 
ATOM   7743 C  CA    . SER D 2 155 ? 122.421 136.594 112.550 1.00 29.26  ? 155 SER D CA    1 
ATOM   7744 C  C     . SER D 2 155 ? 121.703 137.401 113.622 1.00 38.08  ? 155 SER D C     1 
ATOM   7745 O  O     . SER D 2 155 ? 120.574 137.857 113.408 1.00 37.72  ? 155 SER D O     1 
ATOM   7746 C  CB    . SER D 2 155 ? 122.165 135.100 112.742 1.00 31.20  ? 155 SER D CB    1 
ATOM   7747 O  OG    . SER D 2 155 ? 123.020 134.331 111.916 1.00 40.94  ? 155 SER D OG    1 
ATOM   7748 N  N     . ILE D 2 156 ? 122.334 137.588 114.785 1.00 29.89  ? 156 ILE D N     1 
ATOM   7749 C  CA    . ILE D 2 156 ? 121.740 138.473 115.786 1.00 30.07  ? 156 ILE D CA    1 
ATOM   7750 C  C     . ILE D 2 156 ? 121.824 139.932 115.340 1.00 31.78  ? 156 ILE D C     1 
ATOM   7751 O  O     . ILE D 2 156 ? 120.851 140.685 115.463 1.00 38.79  ? 156 ILE D O     1 
ATOM   7752 C  CB    . ILE D 2 156 ? 122.388 138.265 117.168 1.00 37.85  ? 156 ILE D CB    1 
ATOM   7753 C  CG1   . ILE D 2 156 ? 122.300 136.802 117.592 1.00 28.83  ? 156 ILE D CG1   1 
ATOM   7754 C  CG2   . ILE D 2 156 ? 121.689 139.113 118.215 1.00 31.33  ? 156 ILE D CG2   1 
ATOM   7755 C  CD1   . ILE D 2 156 ? 123.302 136.425 118.658 1.00 19.74  ? 156 ILE D CD1   1 
ATOM   7756 N  N     . ASN D 2 157 ? 122.970 140.346 114.785 1.00 38.11  ? 157 ASN D N     1 
ATOM   7757 C  CA    . ASN D 2 157 ? 123.195 141.755 114.479 1.00 35.68  ? 157 ASN D CA    1 
ATOM   7758 C  C     . ASN D 2 157 ? 122.381 142.251 113.288 1.00 38.76  ? 157 ASN D C     1 
ATOM   7759 O  O     . ASN D 2 157 ? 122.112 143.453 113.193 1.00 48.40  ? 157 ASN D O     1 
ATOM   7760 C  CB    . ASN D 2 157 ? 124.683 142.000 114.221 1.00 36.43  ? 157 ASN D CB    1 
ATOM   7761 C  CG    . ASN D 2 157 ? 125.254 143.088 115.099 1.00 45.43  ? 157 ASN D CG    1 
ATOM   7762 O  OD1   . ASN D 2 157 ? 126.352 142.954 115.640 1.00 45.95  ? 157 ASN D OD1   1 
ATOM   7763 N  ND2   . ASN D 2 157 ? 124.511 144.175 115.251 1.00 48.68  ? 157 ASN D ND2   1 
ATOM   7764 N  N     . ILE D 2 158 ? 121.975 141.357 112.383 1.00 38.18  ? 158 ILE D N     1 
ATOM   7765 C  CA    . ILE D 2 158 ? 121.295 141.782 111.160 1.00 40.22  ? 158 ILE D CA    1 
ATOM   7766 C  C     . ILE D 2 158 ? 119.825 142.111 111.374 1.00 40.83  ? 158 ILE D C     1 
ATOM   7767 O  O     . ILE D 2 158 ? 119.179 142.639 110.458 1.00 45.30  ? 158 ILE D O     1 
ATOM   7768 C  CB    . ILE D 2 158 ? 121.508 140.692 110.088 1.00 40.65  ? 158 ILE D CB    1 
ATOM   7769 C  CG1   . ILE D 2 158 ? 121.643 141.319 108.698 1.00 41.81  ? 158 ILE D CG1   1 
ATOM   7770 C  CG2   . ILE D 2 158 ? 120.413 139.624 110.134 1.00 39.55  ? 158 ILE D CG2   1 
ATOM   7771 C  CD1   . ILE D 2 158 ? 122.759 142.329 108.594 1.00 39.85  ? 158 ILE D CD1   1 
ATOM   7772 N  N     . THR D 2 159 ? 119.283 141.863 112.565 1.00 40.22  ? 159 THR D N     1 
ATOM   7773 C  CA    . THR D 2 159 ? 117.859 142.041 112.828 1.00 40.61  ? 159 THR D CA    1 
ATOM   7774 C  C     . THR D 2 159 ? 117.491 143.456 113.266 1.00 42.40  ? 159 THR D C     1 
ATOM   7775 O  O     . THR D 2 159 ? 116.317 143.701 113.563 1.00 43.74  ? 159 THR D O     1 
ATOM   7776 C  CB    . THR D 2 159 ? 117.393 141.042 113.890 1.00 42.61  ? 159 THR D CB    1 
ATOM   7777 O  OG1   . THR D 2 159 ? 118.234 141.140 115.047 1.00 44.41  ? 159 THR D OG1   1 
ATOM   7778 C  CG2   . THR D 2 159 ? 117.459 139.628 113.345 1.00 41.78  ? 159 THR D CG2   1 
ATOM   7779 N  N     . VAL D 2 160 ? 118.447 144.387 113.316 1.00 44.74  ? 160 VAL D N     1 
ATOM   7780 C  CA    . VAL D 2 160 ? 118.125 145.757 113.710 1.00 43.89  ? 160 VAL D CA    1 
ATOM   7781 C  C     . VAL D 2 160 ? 117.410 146.477 112.568 1.00 49.81  ? 160 VAL D C     1 
ATOM   7782 O  O     . VAL D 2 160 ? 117.493 146.097 111.396 1.00 53.10  ? 160 VAL D O     1 
ATOM   7783 C  CB    . VAL D 2 160 ? 119.391 146.515 114.136 1.00 46.87  ? 160 VAL D CB    1 
ATOM   7784 C  CG1   . VAL D 2 160 ? 119.960 145.921 115.412 1.00 48.91  ? 160 VAL D CG1   1 
ATOM   7785 C  CG2   . VAL D 2 160 ? 120.428 146.491 113.020 1.00 47.68  ? 160 VAL D CG2   1 
ATOM   7786 N  N     . ASN D 2 161 ? 116.676 147.531 112.927 1.00 53.98  ? 161 ASN D N     1 
ATOM   7787 C  CA    . ASN D 2 161 ? 115.964 148.366 111.955 1.00 48.22  ? 161 ASN D CA    1 
ATOM   7788 C  C     . ASN D 2 161 ? 116.209 149.838 112.269 1.00 49.88  ? 161 ASN D C     1 
ATOM   7789 O  O     . ASN D 2 161 ? 115.338 150.528 112.811 1.00 52.40  ? 161 ASN D O     1 
ATOM   7790 C  CB    . ASN D 2 161 ? 114.470 148.040 111.956 1.00 48.76  ? 161 ASN D CB    1 
ATOM   7791 C  CG    . ASN D 2 161 ? 113.748 148.611 110.755 1.00 51.97  ? 161 ASN D CG    1 
ATOM   7792 O  OD1   . ASN D 2 161 ? 114.283 148.627 109.646 1.00 57.45  ? 161 ASN D OD1   1 
ATOM   7793 N  ND2   . ASN D 2 161 ? 112.525 149.077 110.966 1.00 53.11  ? 161 ASN D ND2   1 
ATOM   7794 N  N     . PRO D 2 162 ? 117.388 150.356 111.935 1.00 52.44  ? 162 PRO D N     1 
ATOM   7795 C  CA    . PRO D 2 162 ? 117.712 151.745 112.256 1.00 47.94  ? 162 PRO D CA    1 
ATOM   7796 C  C     . PRO D 2 162 ? 117.310 152.706 111.141 1.00 46.52  ? 162 PRO D C     1 
ATOM   7797 O  O     . PRO D 2 162 ? 116.698 152.329 110.141 1.00 52.05  ? 162 PRO D O     1 
ATOM   7798 C  CB    . PRO D 2 162 ? 119.235 151.706 112.407 1.00 44.45  ? 162 PRO D CB    1 
ATOM   7799 C  CG    . PRO D 2 162 ? 119.662 150.650 111.418 1.00 45.09  ? 162 PRO D CG    1 
ATOM   7800 C  CD    . PRO D 2 162 ? 118.489 149.714 111.193 1.00 43.13  ? 162 PRO D CD    1 
ATOM   7801 N  N     . ASP D 2 163 ? 117.660 153.975 111.347 1.00 42.20  ? 163 ASP D N     1 
ATOM   7802 C  CA    . ASP D 2 163 ? 117.608 154.940 110.255 1.00 45.93  ? 163 ASP D CA    1 
ATOM   7803 C  C     . ASP D 2 163 ? 118.988 155.140 109.644 1.00 42.45  ? 163 ASP D C     1 
ATOM   7804 O  O     . ASP D 2 163 ? 119.113 155.340 108.431 1.00 42.72  ? 163 ASP D O     1 
ATOM   7805 C  CB    . ASP D 2 163 ? 117.045 156.273 110.747 1.00 47.59  ? 163 ASP D CB    1 
ATOM   7806 C  CG    . ASP D 2 163 ? 115.566 156.199 111.063 1.00 53.59  ? 163 ASP D CG    1 
ATOM   7807 O  OD1   . ASP D 2 163 ? 114.769 155.968 110.130 1.00 51.22  ? 163 ASP D OD1   1 
ATOM   7808 O  OD2   . ASP D 2 163 ? 115.200 156.374 112.243 1.00 51.24  ? 163 ASP D OD2   1 
ATOM   7809 N  N     . ILE D 2 164 ? 120.028 155.088 110.471 1.00 37.98  ? 164 ILE D N     1 
ATOM   7810 C  CA    . ILE D 2 164 ? 121.414 155.184 110.034 1.00 38.56  ? 164 ILE D CA    1 
ATOM   7811 C  C     . ILE D 2 164 ? 122.116 153.896 110.440 1.00 33.89  ? 164 ILE D C     1 
ATOM   7812 O  O     . ILE D 2 164 ? 122.026 153.477 111.598 1.00 35.04  ? 164 ILE D O     1 
ATOM   7813 C  CB    . ILE D 2 164 ? 122.118 156.415 110.640 1.00 42.73  ? 164 ILE D CB    1 
ATOM   7814 C  CG1   . ILE D 2 164 ? 121.375 157.698 110.261 1.00 39.48  ? 164 ILE D CG1   1 
ATOM   7815 C  CG2   . ILE D 2 164 ? 123.568 156.490 110.182 1.00 38.15  ? 164 ILE D CG2   1 
ATOM   7816 C  CD1   . ILE D 2 164 ? 121.261 158.691 111.391 1.00 38.19  ? 164 ILE D CD1   1 
ATOM   7817 N  N     . LEU D 2 165 ? 122.797 153.267 109.489 1.00 34.22  ? 165 LEU D N     1 
ATOM   7818 C  CA    . LEU D 2 165 ? 123.500 152.015 109.728 1.00 31.56  ? 165 LEU D CA    1 
ATOM   7819 C  C     . LEU D 2 165 ? 124.997 152.226 109.565 1.00 30.75  ? 165 LEU D C     1 
ATOM   7820 O  O     . LEU D 2 165 ? 125.441 152.912 108.641 1.00 33.11  ? 165 LEU D O     1 
ATOM   7821 C  CB    . LEU D 2 165 ? 123.015 150.923 108.772 1.00 37.04  ? 165 LEU D CB    1 
ATOM   7822 C  CG    . LEU D 2 165 ? 123.492 149.499 109.055 1.00 34.06  ? 165 LEU D CG    1 
ATOM   7823 C  CD1   . LEU D 2 165 ? 123.014 149.031 110.419 1.00 28.89  ? 165 LEU D CD1   1 
ATOM   7824 C  CD2   . LEU D 2 165 ? 123.018 148.555 107.967 1.00 33.48  ? 165 LEU D CD2   1 
ATOM   7825 N  N     . VAL D 2 166 ? 125.773 151.648 110.478 1.00 31.72  ? 166 VAL D N     1 
ATOM   7826 C  CA    . VAL D 2 166 ? 127.230 151.688 110.425 1.00 32.25  ? 166 VAL D CA    1 
ATOM   7827 C  C     . VAL D 2 166 ? 127.732 150.254 110.349 1.00 34.77  ? 166 VAL D C     1 
ATOM   7828 O  O     . VAL D 2 166 ? 127.423 149.440 111.225 1.00 37.06  ? 166 VAL D O     1 
ATOM   7829 C  CB    . VAL D 2 166 ? 127.837 152.413 111.640 1.00 36.38  ? 166 VAL D CB    1 
ATOM   7830 C  CG1   . VAL D 2 166 ? 129.353 152.398 111.564 1.00 36.24  ? 166 VAL D CG1   1 
ATOM   7831 C  CG2   . VAL D 2 166 ? 127.321 153.843 111.724 1.00 28.00  ? 166 VAL D CG2   1 
ATOM   7832 N  N     . ILE D 2 167 ? 128.499 149.946 109.305 1.00 40.58  ? 167 ILE D N     1 
ATOM   7833 C  CA    . ILE D 2 167 ? 129.057 148.617 109.083 1.00 38.61  ? 167 ILE D CA    1 
ATOM   7834 C  C     . ILE D 2 167 ? 130.574 148.732 109.052 1.00 41.63  ? 167 ILE D C     1 
ATOM   7835 O  O     . ILE D 2 167 ? 131.125 149.579 108.341 1.00 44.46  ? 167 ILE D O     1 
ATOM   7836 C  CB    . ILE D 2 167 ? 128.527 147.986 107.776 1.00 39.43  ? 167 ILE D CB    1 
ATOM   7837 C  CG1   . ILE D 2 167 ? 126.998 147.945 107.777 1.00 37.77  ? 167 ILE D CG1   1 
ATOM   7838 C  CG2   . ILE D 2 167 ? 129.090 146.591 107.578 1.00 40.69  ? 167 ILE D CG2   1 
ATOM   7839 C  CD1   . ILE D 2 167 ? 126.398 147.669 106.420 1.00 40.52  ? 167 ILE D CD1   1 
ATOM   7840 N  N     . ASP D 2 168 ? 131.249 147.884 109.828 1.00 58.27  ? 168 ASP D N     1 
ATOM   7841 C  CA    . ASP D 2 168 ? 132.703 147.917 109.958 1.00 53.56  ? 168 ASP D CA    1 
ATOM   7842 C  C     . ASP D 2 168 ? 133.296 146.604 109.459 1.00 56.56  ? 168 ASP D C     1 
ATOM   7843 O  O     . ASP D 2 168 ? 133.064 145.545 110.056 1.00 54.04  ? 168 ASP D O     1 
ATOM   7844 C  CB    . ASP D 2 168 ? 133.109 148.181 111.406 1.00 49.17  ? 168 ASP D CB    1 
ATOM   7845 C  CG    . ASP D 2 168 ? 134.284 149.135 111.518 1.00 60.19  ? 168 ASP D CG    1 
ATOM   7846 O  OD1   . ASP D 2 168 ? 134.199 150.097 112.310 1.00 62.27  ? 168 ASP D OD1   1 
ATOM   7847 O  OD2   . ASP D 2 168 ? 135.296 148.924 110.819 1.00 60.60  ? 168 ASP D OD2   1 
ATOM   7848 N  N     . GLU D 2 169 ? 134.038 146.677 108.351 1.00 60.27  ? 169 GLU D N     1 
ATOM   7849 C  CA    . GLU D 2 169 ? 134.988 145.688 107.838 1.00 60.26  ? 169 GLU D CA    1 
ATOM   7850 C  C     . GLU D 2 169 ? 134.367 144.380 107.359 1.00 63.30  ? 169 GLU D C     1 
ATOM   7851 O  O     . GLU D 2 169 ? 135.120 143.475 106.978 1.00 66.23  ? 169 GLU D O     1 
ATOM   7852 C  CB    . GLU D 2 169 ? 136.083 145.352 108.861 1.00 63.41  ? 169 GLU D CB    1 
ATOM   7853 C  CG    . GLU D 2 169 ? 136.973 146.530 109.230 1.00 60.45  ? 169 GLU D CG    1 
ATOM   7854 C  CD    . GLU D 2 169 ? 138.127 146.727 108.266 1.00 62.57  ? 169 GLU D CD    1 
ATOM   7855 O  OE1   . GLU D 2 169 ? 138.366 145.835 107.426 1.00 60.88  ? 169 GLU D OE1   1 
ATOM   7856 O  OE2   . GLU D 2 169 ? 138.796 147.779 108.351 1.00 64.12  ? 169 GLU D OE2   1 
ATOM   7857 N  N     . ALA D 2 170 ? 133.041 144.242 107.338 1.00 60.38  ? 170 ALA D N     1 
ATOM   7858 C  CA    . ALA D 2 170 ? 132.446 142.962 106.955 1.00 59.24  ? 170 ALA D CA    1 
ATOM   7859 C  C     . ALA D 2 170 ? 131.049 143.186 106.396 1.00 60.78  ? 170 ALA D C     1 
ATOM   7860 O  O     . ALA D 2 170 ? 130.111 143.425 107.160 1.00 62.40  ? 170 ALA D O     1 
ATOM   7861 C  CB    . ALA D 2 170 ? 132.405 142.013 108.147 1.00 56.58  ? 170 ALA D CB    1 
ATOM   7862 N  N     . LEU D 2 171 ? 130.909 143.095 105.071 1.00 46.25  ? 171 LEU D N     1 
ATOM   7863 C  CA    . LEU D 2 171 ? 129.579 142.941 104.493 1.00 43.27  ? 171 LEU D CA    1 
ATOM   7864 C  C     . LEU D 2 171 ? 129.058 141.527 104.696 1.00 49.96  ? 171 LEU D C     1 
ATOM   7865 O  O     . LEU D 2 171 ? 127.867 141.330 104.962 1.00 53.88  ? 171 LEU D O     1 
ATOM   7866 C  CB    . LEU D 2 171 ? 129.591 143.271 102.999 1.00 44.98  ? 171 LEU D CB    1 
ATOM   7867 C  CG    . LEU D 2 171 ? 129.488 144.729 102.550 1.00 45.46  ? 171 LEU D CG    1 
ATOM   7868 C  CD1   . LEU D 2 171 ? 129.032 144.824 101.102 1.00 45.03  ? 171 LEU D CD1   1 
ATOM   7869 C  CD2   . LEU D 2 171 ? 128.605 145.556 103.469 1.00 44.43  ? 171 LEU D CD2   1 
ATOM   7870 N  N     . SER D 2 172 ? 129.934 140.537 104.569 1.00 52.64  ? 172 SER D N     1 
ATOM   7871 C  CA    . SER D 2 172 ? 129.572 139.134 104.662 1.00 47.56  ? 172 SER D CA    1 
ATOM   7872 C  C     . SER D 2 172 ? 130.387 138.455 105.751 1.00 48.37  ? 172 SER D C     1 
ATOM   7873 O  O     . SER D 2 172 ? 131.318 139.030 106.321 1.00 53.00  ? 172 SER D O     1 
ATOM   7874 C  CB    . SER D 2 172 ? 129.784 138.420 103.323 1.00 46.67  ? 172 SER D CB    1 
ATOM   7875 O  OG    . SER D 2 172 ? 131.140 138.058 103.143 1.00 55.83  ? 172 SER D OG    1 
ATOM   7876 N  N     . VAL D 2 173 ? 130.024 137.201 106.026 1.00 45.49  ? 173 VAL D N     1 
ATOM   7877 C  CA    . VAL D 2 173 ? 130.632 136.426 107.098 1.00 43.71  ? 173 VAL D CA    1 
ATOM   7878 C  C     . VAL D 2 173 ? 130.430 134.949 106.775 1.00 45.70  ? 173 VAL D C     1 
ATOM   7879 O  O     . VAL D 2 173 ? 129.491 134.569 106.072 1.00 48.83  ? 173 VAL D O     1 
ATOM   7880 C  CB    . VAL D 2 173 ? 130.039 136.842 108.475 1.00 42.12  ? 173 VAL D CB    1 
ATOM   7881 C  CG1   . VAL D 2 173 ? 129.111 135.783 109.083 1.00 36.33  ? 173 VAL D CG1   1 
ATOM   7882 C  CG2   . VAL D 2 173 ? 131.143 137.252 109.429 1.00 42.11  ? 173 VAL D CG2   1 
ATOM   7883 N  N     . GLY D 2 174 ? 131.358 134.118 107.246 1.00 44.94  ? 174 GLY D N     1 
ATOM   7884 C  CA    . GLY D 2 174 ? 131.258 132.690 107.032 1.00 40.90  ? 174 GLY D CA    1 
ATOM   7885 C  C     . GLY D 2 174 ? 131.987 132.226 105.784 1.00 44.05  ? 174 GLY D C     1 
ATOM   7886 O  O     . GLY D 2 174 ? 132.873 132.896 105.248 1.00 46.49  ? 174 GLY D O     1 
ATOM   7887 N  N     . ASP D 2 175 ? 131.594 131.043 105.317 1.00 41.98  ? 175 ASP D N     1 
ATOM   7888 C  CA    . ASP D 2 175 ? 132.186 130.457 104.122 1.00 41.02  ? 175 ASP D CA    1 
ATOM   7889 C  C     . ASP D 2 175 ? 131.475 130.984 102.871 1.00 44.28  ? 175 ASP D C     1 
ATOM   7890 O  O     . ASP D 2 175 ? 130.698 131.941 102.925 1.00 48.64  ? 175 ASP D O     1 
ATOM   7891 C  CB    . ASP D 2 175 ? 132.222 128.927 104.254 1.00 40.33  ? 175 ASP D CB    1 
ATOM   7892 C  CG    . ASP D 2 175 ? 130.834 128.265 104.387 1.00 48.00  ? 175 ASP D CG    1 
ATOM   7893 O  OD1   . ASP D 2 175 ? 129.821 128.696 103.801 1.00 54.89  ? 175 ASP D OD1   1 
ATOM   7894 O  OD2   . ASP D 2 175 ? 130.766 127.254 105.114 1.00 46.69  ? 175 ASP D OD2   1 
ATOM   7895 N  N     . GLN D 2 176 ? 131.746 130.356 101.724 1.00 47.74  ? 176 GLN D N     1 
ATOM   7896 C  CA    . GLN D 2 176 ? 131.175 130.816 100.461 1.00 46.36  ? 176 GLN D CA    1 
ATOM   7897 C  C     . GLN D 2 176 ? 129.679 130.541 100.377 1.00 49.94  ? 176 GLN D C     1 
ATOM   7898 O  O     . GLN D 2 176 ? 128.951 131.286 99.713  1.00 51.94  ? 176 GLN D O     1 
ATOM   7899 C  CB    . GLN D 2 176 ? 131.901 130.159 99.289  1.00 48.14  ? 176 GLN D CB    1 
ATOM   7900 C  CG    . GLN D 2 176 ? 133.235 130.800 98.949  1.00 48.76  ? 176 GLN D CG    1 
ATOM   7901 C  CD    . GLN D 2 176 ? 134.404 130.131 99.645  1.00 51.00  ? 176 GLN D CD    1 
ATOM   7902 O  OE1   . GLN D 2 176 ? 134.232 129.415 100.631 1.00 54.54  ? 176 GLN D OE1   1 
ATOM   7903 N  NE2   . GLN D 2 176 ? 135.607 130.366 99.135  1.00 52.73  ? 176 GLN D NE2   1 
ATOM   7904 N  N     . THR D 2 177 ? 129.201 129.493 101.046 1.00 51.95  ? 177 THR D N     1 
ATOM   7905 C  CA    . THR D 2 177 ? 127.786 129.152 101.028 1.00 49.26  ? 177 THR D CA    1 
ATOM   7906 C  C     . THR D 2 177 ? 126.941 130.063 101.909 1.00 50.76  ? 177 THR D C     1 
ATOM   7907 O  O     . THR D 2 177 ? 125.715 130.071 101.765 1.00 57.96  ? 177 THR D O     1 
ATOM   7908 C  CB    . THR D 2 177 ? 127.592 127.699 101.465 1.00 53.29  ? 177 THR D CB    1 
ATOM   7909 O  OG1   . THR D 2 177 ? 127.694 127.608 102.890 1.00 50.30  ? 177 THR D OG1   1 
ATOM   7910 C  CG2   . THR D 2 177 ? 128.651 126.810 100.833 1.00 50.84  ? 177 THR D CG2   1 
ATOM   7911 N  N     . PHE D 2 178 ? 127.560 130.828 102.811 1.00 43.26  ? 178 PHE D N     1 
ATOM   7912 C  CA    . PHE D 2 178 ? 126.842 131.711 103.718 1.00 40.60  ? 178 PHE D CA    1 
ATOM   7913 C  C     . PHE D 2 178 ? 126.911 133.181 103.332 1.00 45.01  ? 178 PHE D C     1 
ATOM   7914 O  O     . PHE D 2 178 ? 126.063 133.958 103.779 1.00 48.36  ? 178 PHE D O     1 
ATOM   7915 C  CB    . PHE D 2 178 ? 127.382 131.551 105.147 1.00 41.11  ? 178 PHE D CB    1 
ATOM   7916 C  CG    . PHE D 2 178 ? 126.432 132.014 106.213 1.00 46.16  ? 178 PHE D CG    1 
ATOM   7917 C  CD1   . PHE D 2 178 ? 125.358 131.226 106.588 1.00 45.71  ? 178 PHE D CD1   1 
ATOM   7918 C  CD2   . PHE D 2 178 ? 126.616 133.235 106.845 1.00 41.56  ? 178 PHE D CD2   1 
ATOM   7919 C  CE1   . PHE D 2 178 ? 124.484 131.645 107.568 1.00 45.54  ? 178 PHE D CE1   1 
ATOM   7920 C  CE2   . PHE D 2 178 ? 125.741 133.666 107.824 1.00 44.40  ? 178 PHE D CE2   1 
ATOM   7921 C  CZ    . PHE D 2 178 ? 124.675 132.866 108.189 1.00 44.22  ? 178 PHE D CZ    1 
ATOM   7922 N  N     . ALA D 2 179 ? 127.884 133.575 102.506 1.00 51.42  ? 179 ALA D N     1 
ATOM   7923 C  CA    . ALA D 2 179 ? 128.138 134.990 102.246 1.00 49.35  ? 179 ALA D CA    1 
ATOM   7924 C  C     . ALA D 2 179 ? 127.049 135.630 101.394 1.00 47.16  ? 179 ALA D C     1 
ATOM   7925 O  O     . ALA D 2 179 ? 126.814 136.842 101.499 1.00 54.04  ? 179 ALA D O     1 
ATOM   7926 C  CB    . ALA D 2 179 ? 129.499 135.153 101.573 1.00 48.60  ? 179 ALA D CB    1 
ATOM   7927 N  N     . GLN D 2 180 ? 126.377 134.840 100.552 1.00 44.01  ? 180 GLN D N     1 
ATOM   7928 C  CA    . GLN D 2 180 ? 125.352 135.392 99.669  1.00 49.39  ? 180 GLN D CA    1 
ATOM   7929 C  C     . GLN D 2 180 ? 124.115 135.826 100.448 1.00 50.09  ? 180 GLN D C     1 
ATOM   7930 O  O     . GLN D 2 180 ? 123.479 136.822 100.093 1.00 53.35  ? 180 GLN D O     1 
ATOM   7931 C  CB    . GLN D 2 180 ? 124.984 134.375 98.590  1.00 51.25  ? 180 GLN D CB    1 
ATOM   7932 C  CG    . GLN D 2 180 ? 124.210 134.968 97.423  1.00 53.67  ? 180 GLN D CG    1 
ATOM   7933 C  CD    . GLN D 2 180 ? 124.919 136.155 96.795  1.00 55.41  ? 180 GLN D CD    1 
ATOM   7934 O  OE1   . GLN D 2 180 ? 126.079 136.058 96.394  1.00 54.76  ? 180 GLN D OE1   1 
ATOM   7935 N  NE2   . GLN D 2 180 ? 124.224 137.283 96.711  1.00 48.83  ? 180 GLN D NE2   1 
ATOM   7936 N  N     . LYS D 2 181 ? 123.767 135.100 101.517 1.00 49.19  ? 181 LYS D N     1 
ATOM   7937 C  CA    . LYS D 2 181 ? 122.651 135.510 102.368 1.00 45.31  ? 181 LYS D CA    1 
ATOM   7938 C  C     . LYS D 2 181 ? 122.952 136.819 103.086 1.00 46.39  ? 181 LYS D C     1 
ATOM   7939 O  O     . LYS D 2 181 ? 122.069 137.677 103.233 1.00 54.13  ? 181 LYS D O     1 
ATOM   7940 C  CB    . LYS D 2 181 ? 122.335 134.413 103.384 1.00 50.89  ? 181 LYS D CB    1 
ATOM   7941 C  CG    . LYS D 2 181 ? 122.293 133.008 102.808 1.00 49.63  ? 181 LYS D CG    1 
ATOM   7942 C  CD    . LYS D 2 181 ? 122.239 131.949 103.907 1.00 54.85  ? 181 LYS D CD    1 
ATOM   7943 C  CE    . LYS D 2 181 ? 121.175 132.260 104.952 1.00 51.11  ? 181 LYS D CE    1 
ATOM   7944 N  NZ    . LYS D 2 181 ? 120.990 131.144 105.917 1.00 46.41  ? 181 LYS D NZ    1 
ATOM   7945 N  N     . CYS D 2 182 ? 124.199 136.987 103.535 1.00 45.80  ? 182 CYS D N     1 
ATOM   7946 C  CA    . CYS D 2 182 ? 124.622 138.239 104.151 1.00 43.62  ? 182 CYS D CA    1 
ATOM   7947 C  C     . CYS D 2 182 ? 124.578 139.393 103.157 1.00 46.09  ? 182 CYS D C     1 
ATOM   7948 O  O     . CYS D 2 182 ? 124.139 140.499 103.501 1.00 50.88  ? 182 CYS D O     1 
ATOM   7949 C  CB    . CYS D 2 182 ? 126.028 138.083 104.724 1.00 44.57  ? 182 CYS D CB    1 
ATOM   7950 S  SG    . CYS D 2 182 ? 126.240 136.676 105.829 1.00 52.84  ? 182 CYS D SG    1 
ATOM   7951 N  N     . LEU D 2 183 ? 125.026 139.149 101.917 1.00 45.58  ? 183 LEU D N     1 
ATOM   7952 C  CA    . LEU D 2 183 ? 124.942 140.171 100.874 1.00 44.98  ? 183 LEU D CA    1 
ATOM   7953 C  C     . LEU D 2 183 ? 123.497 140.538 100.554 1.00 45.46  ? 183 LEU D C     1 
ATOM   7954 O  O     . LEU D 2 183 ? 123.187 141.715 100.349 1.00 54.86  ? 183 LEU D O     1 
ATOM   7955 C  CB    . LEU D 2 183 ? 125.663 139.711 99.606  1.00 51.14  ? 183 LEU D CB    1 
ATOM   7956 C  CG    . LEU D 2 183 ? 127.117 140.121 99.349  1.00 46.93  ? 183 LEU D CG    1 
ATOM   7957 C  CD1   . LEU D 2 183 ? 127.967 140.113 100.599 1.00 48.07  ? 183 LEU D CD1   1 
ATOM   7958 C  CD2   . LEU D 2 183 ? 127.731 139.225 98.284  1.00 51.07  ? 183 LEU D CD2   1 
ATOM   7959 N  N     . ASP D 2 184 ? 122.602 139.544 100.522 1.00 46.94  ? 184 ASP D N     1 
ATOM   7960 C  CA    . ASP D 2 184 ? 121.185 139.819 100.285 1.00 51.04  ? 184 ASP D CA    1 
ATOM   7961 C  C     . ASP D 2 184 ? 120.570 140.632 101.416 1.00 49.67  ? 184 ASP D C     1 
ATOM   7962 O  O     . ASP D 2 184 ? 119.768 141.536 101.167 1.00 50.66  ? 184 ASP D O     1 
ATOM   7963 C  CB    . ASP D 2 184 ? 120.414 138.515 100.083 1.00 53.36  ? 184 ASP D CB    1 
ATOM   7964 C  CG    . ASP D 2 184 ? 120.831 137.780 98.827  1.00 57.76  ? 184 ASP D CG    1 
ATOM   7965 O  OD1   . ASP D 2 184 ? 121.573 138.366 98.013  1.00 56.35  ? 184 ASP D OD1   1 
ATOM   7966 O  OD2   . ASP D 2 184 ? 120.418 136.615 98.654  1.00 60.51  ? 184 ASP D OD2   1 
ATOM   7967 N  N     . LYS D 2 185 ? 120.946 140.341 102.665 1.00 45.30  ? 185 LYS D N     1 
ATOM   7968 C  CA    . LYS D 2 185 ? 120.403 141.096 103.794 1.00 48.24  ? 185 LYS D CA    1 
ATOM   7969 C  C     . LYS D 2 185 ? 120.915 142.537 103.813 1.00 54.46  ? 185 LYS D C     1 
ATOM   7970 O  O     . LYS D 2 185 ? 120.147 143.474 104.077 1.00 54.90  ? 185 LYS D O     1 
ATOM   7971 C  CB    . LYS D 2 185 ? 120.732 140.381 105.102 1.00 49.33  ? 185 LYS D CB    1 
ATOM   7972 C  CG    . LYS D 2 185 ? 119.510 140.060 105.942 1.00 50.81  ? 185 LYS D CG    1 
ATOM   7973 C  CD    . LYS D 2 185 ? 118.932 138.705 105.577 1.00 50.15  ? 185 LYS D CD    1 
ATOM   7974 C  CE    . LYS D 2 185 ? 117.671 138.413 106.372 1.00 53.00  ? 185 LYS D CE    1 
ATOM   7975 N  NZ    . LYS D 2 185 ? 117.073 137.100 106.005 1.00 55.63  ? 185 LYS D NZ    1 
ATOM   7976 N  N     . ILE D 2 186 ? 122.203 142.735 103.515 1.00 51.86  ? 186 ILE D N     1 
ATOM   7977 C  CA    . ILE D 2 186 ? 122.762 144.086 103.472 1.00 46.60  ? 186 ILE D CA    1 
ATOM   7978 C  C     . ILE D 2 186 ? 122.187 144.874 102.293 1.00 46.49  ? 186 ILE D C     1 
ATOM   7979 O  O     . ILE D 2 186 ? 121.893 146.073 102.406 1.00 52.26  ? 186 ILE D O     1 
ATOM   7980 C  CB    . ILE D 2 186 ? 124.302 144.011 103.440 1.00 51.81  ? 186 ILE D CB    1 
ATOM   7981 C  CG1   . ILE D 2 186 ? 124.833 143.433 104.756 1.00 47.23  ? 186 ILE D CG1   1 
ATOM   7982 C  CG2   . ILE D 2 186 ? 124.924 145.368 103.203 1.00 48.89  ? 186 ILE D CG2   1 
ATOM   7983 C  CD1   . ILE D 2 186 ? 124.617 144.323 105.960 1.00 48.36  ? 186 ILE D CD1   1 
ATOM   7984 N  N     . TYR D 2 187 ? 121.969 144.209 101.155 1.00 47.66  ? 187 TYR D N     1 
ATOM   7985 C  CA    . TYR D 2 187 ? 121.333 144.870 100.022 1.00 50.52  ? 187 TYR D CA    1 
ATOM   7986 C  C     . TYR D 2 187 ? 119.865 145.179 100.288 1.00 53.01  ? 187 TYR D C     1 
ATOM   7987 O  O     . TYR D 2 187 ? 119.351 146.173 99.765  1.00 51.44  ? 187 TYR D O     1 
ATOM   7988 C  CB    . TYR D 2 187 ? 121.477 144.017 98.757  1.00 55.45  ? 187 TYR D CB    1 
ATOM   7989 C  CG    . TYR D 2 187 ? 122.816 144.122 98.037  1.00 55.06  ? 187 TYR D CG    1 
ATOM   7990 C  CD1   . TYR D 2 187 ? 122.889 143.952 96.661  1.00 57.00  ? 187 TYR D CD1   1 
ATOM   7991 C  CD2   . TYR D 2 187 ? 123.996 144.398 98.724  1.00 55.65  ? 187 TYR D CD2   1 
ATOM   7992 C  CE1   . TYR D 2 187 ? 124.096 144.044 95.989  1.00 58.05  ? 187 TYR D CE1   1 
ATOM   7993 C  CE2   . TYR D 2 187 ? 125.205 144.492 98.064  1.00 55.64  ? 187 TYR D CE2   1 
ATOM   7994 C  CZ    . TYR D 2 187 ? 125.248 144.317 96.697  1.00 61.95  ? 187 TYR D CZ    1 
ATOM   7995 O  OH    . TYR D 2 187 ? 126.449 144.411 96.036  1.00 63.07  ? 187 TYR D OH    1 
ATOM   7996 N  N     . GLU D 2 188 ? 119.188 144.354 101.093 1.00 56.59  ? 188 GLU D N     1 
ATOM   7997 C  CA    . GLU D 2 188 ? 117.840 144.686 101.543 1.00 53.12  ? 188 GLU D CA    1 
ATOM   7998 C  C     . GLU D 2 188 ? 117.846 145.910 102.447 1.00 54.00  ? 188 GLU D C     1 
ATOM   7999 O  O     . GLU D 2 188 ? 116.911 146.714 102.410 1.00 53.08  ? 188 GLU D O     1 
ATOM   8000 C  CB    . GLU D 2 188 ? 117.209 143.496 102.265 1.00 52.43  ? 188 GLU D CB    1 
ATOM   8001 C  CG    . GLU D 2 188 ? 116.606 142.451 101.346 1.00 55.97  ? 188 GLU D CG    1 
ATOM   8002 C  CD    . GLU D 2 188 ? 116.602 141.069 101.967 1.00 59.90  ? 188 GLU D CD    1 
ATOM   8003 O  OE1   . GLU D 2 188 ? 116.586 140.075 101.211 1.00 59.36  ? 188 GLU D OE1   1 
ATOM   8004 O  OE2   . GLU D 2 188 ? 116.610 140.976 103.212 1.00 56.88  ? 188 GLU D OE2   1 
ATOM   8005 N  N     . PHE D 2 189 ? 118.876 146.049 103.289 1.00 52.61  ? 189 PHE D N     1 
ATOM   8006 C  CA    . PHE D 2 189 ? 119.050 147.281 104.063 1.00 47.44  ? 189 PHE D CA    1 
ATOM   8007 C  C     . PHE D 2 189 ? 119.244 148.486 103.148 1.00 51.88  ? 189 PHE D C     1 
ATOM   8008 O  O     . PHE D 2 189 ? 118.736 149.578 103.426 1.00 49.43  ? 189 PHE D O     1 
ATOM   8009 C  CB    . PHE D 2 189 ? 120.244 147.162 105.009 1.00 46.02  ? 189 PHE D CB    1 
ATOM   8010 C  CG    . PHE D 2 189 ? 119.909 146.593 106.349 1.00 47.95  ? 189 PHE D CG    1 
ATOM   8011 C  CD1   . PHE D 2 189 ? 118.872 147.119 107.101 1.00 49.61  ? 189 PHE D CD1   1 
ATOM   8012 C  CD2   . PHE D 2 189 ? 120.649 145.545 106.869 1.00 49.82  ? 189 PHE D CD2   1 
ATOM   8013 C  CE1   . PHE D 2 189 ? 118.570 146.597 108.341 1.00 52.99  ? 189 PHE D CE1   1 
ATOM   8014 C  CE2   . PHE D 2 189 ? 120.353 145.021 108.107 1.00 51.11  ? 189 PHE D CE2   1 
ATOM   8015 C  CZ    . PHE D 2 189 ? 119.314 145.546 108.843 1.00 52.74  ? 189 PHE D CZ    1 
ATOM   8016 N  N     . LYS D 2 190 ? 119.996 148.302 102.062 1.00 56.30  ? 190 LYS D N     1 
ATOM   8017 C  CA    . LYS D 2 190 ? 120.197 149.378 101.095 1.00 48.10  ? 190 LYS D CA    1 
ATOM   8018 C  C     . LYS D 2 190 ? 118.912 149.718 100.342 1.00 51.94  ? 190 LYS D C     1 
ATOM   8019 O  O     . LYS D 2 190 ? 118.716 150.870 99.938  1.00 53.57  ? 190 LYS D O     1 
ATOM   8020 C  CB    . LYS D 2 190 ? 121.304 148.991 100.111 1.00 50.24  ? 190 LYS D CB    1 
ATOM   8021 C  CG    . LYS D 2 190 ? 121.841 150.143 99.280  1.00 48.40  ? 190 LYS D CG    1 
ATOM   8022 C  CD    . LYS D 2 190 ? 122.832 149.670 98.234  1.00 49.93  ? 190 LYS D CD    1 
ATOM   8023 C  CE    . LYS D 2 190 ? 123.206 150.799 97.288  1.00 50.20  ? 190 LYS D CE    1 
ATOM   8024 N  NZ    . LYS D 2 190 ? 124.043 150.324 96.154  1.00 49.04  ? 190 LYS D NZ    1 
ATOM   8025 N  N     . GLU D 2 191 ? 118.023 148.741 100.155 1.00 63.05  ? 191 GLU D N     1 
ATOM   8026 C  CA    . GLU D 2 191 ? 116.827 148.944 99.343  1.00 60.58  ? 191 GLU D CA    1 
ATOM   8027 C  C     . GLU D 2 191 ? 115.748 149.778 100.026 1.00 61.22  ? 191 GLU D C     1 
ATOM   8028 O  O     . GLU D 2 191 ? 114.926 150.380 99.328  1.00 62.76  ? 191 GLU D O     1 
ATOM   8029 C  CB    . GLU D 2 191 ? 116.239 147.595 98.926  1.00 61.21  ? 191 GLU D CB    1 
ATOM   8030 C  CG    . GLU D 2 191 ? 116.676 147.129 97.546  1.00 63.27  ? 191 GLU D CG    1 
ATOM   8031 C  CD    . GLU D 2 191 ? 117.177 145.698 97.536  1.00 68.24  ? 191 GLU D CD    1 
ATOM   8032 O  OE1   . GLU D 2 191 ? 118.102 145.396 96.752  1.00 64.46  ? 191 GLU D OE1   1 
ATOM   8033 O  OE2   . GLU D 2 191 ? 116.649 144.875 98.313  1.00 66.47  ? 191 GLU D OE2   1 
ATOM   8034 N  N     . GLN D 2 192 ? 115.718 149.836 101.358 1.00 56.22  ? 192 GLN D N     1 
ATOM   8035 C  CA    . GLN D 2 192 ? 114.712 150.642 102.047 1.00 57.77  ? 192 GLN D CA    1 
ATOM   8036 C  C     . GLN D 2 192 ? 115.170 152.068 102.332 1.00 60.11  ? 192 GLN D C     1 
ATOM   8037 O  O     . GLN D 2 192 ? 114.612 152.690 103.247 1.00 59.69  ? 192 GLN D O     1 
ATOM   8038 C  CB    . GLN D 2 192 ? 114.276 149.974 103.355 1.00 56.43  ? 192 GLN D CB    1 
ATOM   8039 C  CG    . GLN D 2 192 ? 114.385 148.471 103.357 1.00 57.41  ? 192 GLN D CG    1 
ATOM   8040 C  CD    . GLN D 2 192 ? 114.378 147.878 104.751 1.00 59.09  ? 192 GLN D CD    1 
ATOM   8041 O  OE1   . GLN D 2 192 ? 114.403 148.600 105.746 1.00 59.83  ? 192 GLN D OE1   1 
ATOM   8042 N  NE2   . GLN D 2 192 ? 114.352 146.553 104.829 1.00 58.54  ? 192 GLN D NE2   1 
ATOM   8043 N  N     . ASN D 2 193 ? 116.160 152.569 101.580 1.00 58.95  ? 193 ASN D N     1 
ATOM   8044 C  CA    . ASN D 2 193 ? 116.592 153.974 101.589 1.00 58.18  ? 193 ASN D CA    1 
ATOM   8045 C  C     . ASN D 2 193 ? 117.092 154.416 102.966 1.00 58.10  ? 193 ASN D C     1 
ATOM   8046 O  O     . ASN D 2 193 ? 116.562 155.346 103.578 1.00 59.30  ? 193 ASN D O     1 
ATOM   8047 C  CB    . ASN D 2 193 ? 115.475 154.895 101.083 1.00 61.07  ? 193 ASN D CB    1 
ATOM   8048 C  CG    . ASN D 2 193 ? 116.001 156.192 100.512 1.00 64.91  ? 193 ASN D CG    1 
ATOM   8049 O  OD1   . ASN D 2 193 ? 116.624 156.209 99.452  1.00 66.68  ? 193 ASN D OD1   1 
ATOM   8050 N  ND2   . ASN D 2 193 ? 115.744 157.292 101.210 1.00 63.32  ? 193 ASN D ND2   1 
ATOM   8051 N  N     . LYS D 2 194 ? 118.129 153.740 103.450 1.00 51.32  ? 194 LYS D N     1 
ATOM   8052 C  CA    . LYS D 2 194 ? 118.761 154.067 104.719 1.00 48.00  ? 194 LYS D CA    1 
ATOM   8053 C  C     . LYS D 2 194 ? 120.152 154.632 104.474 1.00 50.91  ? 194 LYS D C     1 
ATOM   8054 O  O     . LYS D 2 194 ? 120.824 154.258 103.508 1.00 53.34  ? 194 LYS D O     1 
ATOM   8055 C  CB    . LYS D 2 194 ? 118.857 152.836 105.626 1.00 47.71  ? 194 LYS D CB    1 
ATOM   8056 C  CG    . LYS D 2 194 ? 117.537 152.141 105.885 1.00 52.59  ? 194 LYS D CG    1 
ATOM   8057 C  CD    . LYS D 2 194 ? 117.755 150.787 106.540 1.00 54.66  ? 194 LYS D CD    1 
ATOM   8058 C  CE    . LYS D 2 194 ? 116.603 150.408 107.460 1.00 51.29  ? 194 LYS D CE    1 
ATOM   8059 N  NZ    . LYS D 2 194 ? 115.479 151.384 107.427 1.00 47.51  ? 194 LYS D NZ    1 
ATOM   8060 N  N     . THR D 2 195 ? 120.578 155.539 105.350 1.00 43.60  ? 195 THR D N     1 
ATOM   8061 C  CA    . THR D 2 195 ? 121.936 156.062 105.290 1.00 42.20  ? 195 THR D CA    1 
ATOM   8062 C  C     . THR D 2 195 ? 122.899 155.035 105.871 1.00 37.26  ? 195 THR D C     1 
ATOM   8063 O  O     . THR D 2 195 ? 122.821 154.703 107.056 1.00 36.90  ? 195 THR D O     1 
ATOM   8064 C  CB    . THR D 2 195 ? 122.036 157.381 106.049 1.00 45.27  ? 195 THR D CB    1 
ATOM   8065 O  OG1   . THR D 2 195 ? 120.900 158.198 105.746 1.00 48.86  ? 195 THR D OG1   1 
ATOM   8066 C  CG2   . THR D 2 195 ? 123.305 158.124 105.663 1.00 39.21  ? 195 THR D CG2   1 
ATOM   8067 N  N     . ILE D 2 196 ? 123.804 154.525 105.040 1.00 37.13  ? 196 ILE D N     1 
ATOM   8068 C  CA    . ILE D 2 196 ? 124.723 153.464 105.433 1.00 38.85  ? 196 ILE D CA    1 
ATOM   8069 C  C     . ILE D 2 196 ? 126.146 153.996 105.354 1.00 33.72  ? 196 ILE D C     1 
ATOM   8070 O  O     . ILE D 2 196 ? 126.548 154.562 104.332 1.00 34.57  ? 196 ILE D O     1 
ATOM   8071 C  CB    . ILE D 2 196 ? 124.556 152.212 104.553 1.00 33.55  ? 196 ILE D CB    1 
ATOM   8072 C  CG1   . ILE D 2 196 ? 123.098 151.752 104.546 1.00 33.77  ? 196 ILE D CG1   1 
ATOM   8073 C  CG2   . ILE D 2 196 ? 125.452 151.085 105.040 1.00 29.69  ? 196 ILE D CG2   1 
ATOM   8074 C  CD1   . ILE D 2 196 ? 122.799 150.708 103.504 1.00 33.49  ? 196 ILE D CD1   1 
ATOM   8075 N  N     . PHE D 2 197 ? 126.898 153.826 106.437 1.00 27.98  ? 197 PHE D N     1 
ATOM   8076 C  CA    . PHE D 2 197 ? 128.321 154.131 106.476 1.00 31.01  ? 197 PHE D CA    1 
ATOM   8077 C  C     . PHE D 2 197 ? 129.102 152.826 106.470 1.00 33.53  ? 197 PHE D C     1 
ATOM   8078 O  O     . PHE D 2 197 ? 128.911 151.980 107.349 1.00 30.31  ? 197 PHE D O     1 
ATOM   8079 C  CB    . PHE D 2 197 ? 128.672 154.960 107.713 1.00 27.94  ? 197 PHE D CB    1 
ATOM   8080 C  CG    . PHE D 2 197 ? 128.277 156.402 107.607 1.00 30.79  ? 197 PHE D CG    1 
ATOM   8081 C  CD1   . PHE D 2 197 ? 129.127 157.327 107.020 1.00 31.12  ? 197 PHE D CD1   1 
ATOM   8082 C  CD2   . PHE D 2 197 ? 127.051 156.835 108.090 1.00 28.69  ? 197 PHE D CD2   1 
ATOM   8083 C  CE1   . PHE D 2 197 ? 128.765 158.658 106.921 1.00 32.84  ? 197 PHE D CE1   1 
ATOM   8084 C  CE2   . PHE D 2 197 ? 126.681 158.164 107.992 1.00 29.92  ? 197 PHE D CE2   1 
ATOM   8085 C  CZ    . PHE D 2 197 ? 127.539 159.077 107.406 1.00 32.58  ? 197 PHE D CZ    1 
ATOM   8086 N  N     . PHE D 2 198 ? 129.974 152.664 105.480 1.00 36.13  ? 198 PHE D N     1 
ATOM   8087 C  CA    . PHE D 2 198 ? 130.735 151.435 105.291 1.00 28.65  ? 198 PHE D CA    1 
ATOM   8088 C  C     . PHE D 2 198 ? 132.217 151.739 105.460 1.00 30.15  ? 198 PHE D C     1 
ATOM   8089 O  O     . PHE D 2 198 ? 132.747 152.641 104.804 1.00 37.97  ? 198 PHE D O     1 
ATOM   8090 C  CB    . PHE D 2 198 ? 130.455 150.827 103.915 1.00 32.69  ? 198 PHE D CB    1 
ATOM   8091 C  CG    . PHE D 2 198 ? 131.044 149.461 103.724 1.00 37.62  ? 198 PHE D CG    1 
ATOM   8092 C  CD1   . PHE D 2 198 ? 131.106 148.564 104.780 1.00 34.15  ? 198 PHE D CD1   1 
ATOM   8093 C  CD2   . PHE D 2 198 ? 131.536 149.072 102.488 1.00 34.39  ? 198 PHE D CD2   1 
ATOM   8094 C  CE1   . PHE D 2 198 ? 131.649 147.308 104.608 1.00 32.87  ? 198 PHE D CE1   1 
ATOM   8095 C  CE2   . PHE D 2 198 ? 132.078 147.815 102.309 1.00 32.51  ? 198 PHE D CE2   1 
ATOM   8096 C  CZ    . PHE D 2 198 ? 132.135 146.935 103.373 1.00 34.92  ? 198 PHE D CZ    1 
ATOM   8097 N  N     . VAL D 2 199 ? 132.876 150.984 106.331 1.00 28.43  ? 199 VAL D N     1 
ATOM   8098 C  CA    . VAL D 2 199 ? 134.296 151.144 106.620 1.00 41.34  ? 199 VAL D CA    1 
ATOM   8099 C  C     . VAL D 2 199 ? 134.986 149.837 106.260 1.00 40.89  ? 199 VAL D C     1 
ATOM   8100 O  O     . VAL D 2 199 ? 134.782 148.824 106.937 1.00 47.25  ? 199 VAL D O     1 
ATOM   8101 C  CB    . VAL D 2 199 ? 134.532 151.493 108.099 1.00 41.07  ? 199 VAL D CB    1 
ATOM   8102 C  CG1   . VAL D 2 199 ? 136.011 151.515 108.415 1.00 36.16  ? 199 VAL D CG1   1 
ATOM   8103 C  CG2   . VAL D 2 199 ? 133.877 152.812 108.454 1.00 40.55  ? 199 VAL D CG2   1 
ATOM   8104 N  N     . SER D 2 200 ? 135.806 149.852 105.210 1.00 38.70  ? 200 SER D N     1 
ATOM   8105 C  CA    . SER D 2 200 ? 136.469 148.631 104.767 1.00 42.93  ? 200 SER D CA    1 
ATOM   8106 C  C     . SER D 2 200 ? 137.690 148.967 103.924 1.00 43.22  ? 200 SER D C     1 
ATOM   8107 O  O     . SER D 2 200 ? 137.873 150.099 103.472 1.00 41.25  ? 200 SER D O     1 
ATOM   8108 C  CB    . SER D 2 200 ? 135.521 147.733 103.970 1.00 43.21  ? 200 SER D CB    1 
ATOM   8109 O  OG    . SER D 2 200 ? 135.851 147.726 102.593 1.00 49.35  ? 200 SER D OG    1 
ATOM   8110 N  N     . HIS D 2 201 ? 138.526 147.947 103.724 1.00 42.40  ? 201 HIS D N     1 
ATOM   8111 C  CA    . HIS D 2 201 ? 139.619 147.988 102.767 1.00 39.31  ? 201 HIS D CA    1 
ATOM   8112 C  C     . HIS D 2 201 ? 139.318 147.215 101.493 1.00 42.13  ? 201 HIS D C     1 
ATOM   8113 O  O     . HIS D 2 201 ? 140.041 147.378 100.505 1.00 47.37  ? 201 HIS D O     1 
ATOM   8114 C  CB    . HIS D 2 201 ? 140.901 147.425 103.394 1.00 36.75  ? 201 HIS D CB    1 
ATOM   8115 C  CG    . HIS D 2 201 ? 141.478 148.286 104.471 1.00 40.85  ? 201 HIS D CG    1 
ATOM   8116 N  ND1   . HIS D 2 201 ? 142.273 149.378 104.205 1.00 44.62  ? 201 HIS D ND1   1 
ATOM   8117 C  CD2   . HIS D 2 201 ? 141.380 148.211 105.818 1.00 39.37  ? 201 HIS D CD2   1 
ATOM   8118 C  CE1   . HIS D 2 201 ? 142.638 149.940 105.342 1.00 33.00  ? 201 HIS D CE1   1 
ATOM   8119 N  NE2   . HIS D 2 201 ? 142.111 149.251 106.335 1.00 36.12  ? 201 HIS D NE2   1 
ATOM   8120 N  N     . ASN D 2 202 ? 138.286 146.375 101.495 1.00 47.65  ? 202 ASN D N     1 
ATOM   8121 C  CA    . ASN D 2 202 ? 137.898 145.595 100.322 1.00 40.94  ? 202 ASN D CA    1 
ATOM   8122 C  C     . ASN D 2 202 ? 137.251 146.531 99.313  1.00 40.40  ? 202 ASN D C     1 
ATOM   8123 O  O     . ASN D 2 202 ? 136.075 146.880 99.435  1.00 48.73  ? 202 ASN D O     1 
ATOM   8124 C  CB    . ASN D 2 202 ? 136.948 144.472 100.724 1.00 44.02  ? 202 ASN D CB    1 
ATOM   8125 C  CG    . ASN D 2 202 ? 136.907 143.346 99.709  1.00 51.01  ? 202 ASN D CG    1 
ATOM   8126 O  OD1   . ASN D 2 202 ? 137.472 143.452 98.620  1.00 48.95  ? 202 ASN D OD1   1 
ATOM   8127 N  ND2   . ASN D 2 202 ? 136.232 142.261 100.062 1.00 49.30  ? 202 ASN D ND2   1 
ATOM   8128 N  N     . LEU D 2 203 ? 138.020 146.935 98.303  1.00 37.06  ? 203 LEU D N     1 
ATOM   8129 C  CA    . LEU D 2 203 ? 137.545 147.942 97.362  1.00 41.63  ? 203 LEU D CA    1 
ATOM   8130 C  C     . LEU D 2 203 ? 136.526 147.384 96.376  1.00 46.61  ? 203 LEU D C     1 
ATOM   8131 O  O     . LEU D 2 203 ? 135.763 148.157 95.788  1.00 45.83  ? 203 LEU D O     1 
ATOM   8132 C  CB    . LEU D 2 203 ? 138.730 148.555 96.614  1.00 45.21  ? 203 LEU D CB    1 
ATOM   8133 C  CG    . LEU D 2 203 ? 139.718 149.400 97.430  1.00 47.31  ? 203 LEU D CG    1 
ATOM   8134 C  CD1   . LEU D 2 203 ? 140.531 150.297 96.517  1.00 47.56  ? 203 LEU D CD1   1 
ATOM   8135 C  CD2   . LEU D 2 203 ? 139.022 150.227 98.508  1.00 37.55  ? 203 LEU D CD2   1 
ATOM   8136 N  N     . GLY D 2 204 ? 136.501 146.064 96.177  1.00 49.82  ? 204 GLY D N     1 
ATOM   8137 C  CA    . GLY D 2 204 ? 135.472 145.469 95.337  1.00 43.57  ? 204 GLY D CA    1 
ATOM   8138 C  C     . GLY D 2 204 ? 134.083 145.573 95.940  1.00 45.99  ? 204 GLY D C     1 
ATOM   8139 O  O     . GLY D 2 204 ? 133.124 145.935 95.250  1.00 48.92  ? 204 GLY D O     1 
ATOM   8140 N  N     . GLN D 2 205 ? 133.961 145.276 97.238  1.00 45.49  ? 205 GLN D N     1 
ATOM   8141 C  CA    . GLN D 2 205 ? 132.681 145.418 97.928  1.00 45.86  ? 205 GLN D CA    1 
ATOM   8142 C  C     . GLN D 2 205 ? 132.280 146.881 98.044  1.00 47.79  ? 205 GLN D C     1 
ATOM   8143 O  O     . GLN D 2 205 ? 131.091 147.214 97.984  1.00 53.65  ? 205 GLN D O     1 
ATOM   8144 C  CB    . GLN D 2 205 ? 132.754 144.775 99.313  1.00 42.59  ? 205 GLN D CB    1 
ATOM   8145 C  CG    . GLN D 2 205 ? 132.755 143.259 99.303  1.00 49.90  ? 205 GLN D CG    1 
ATOM   8146 C  CD    . GLN D 2 205 ? 132.658 142.665 100.694 1.00 51.88  ? 205 GLN D CD    1 
ATOM   8147 O  OE1   . GLN D 2 205 ? 132.881 143.350 101.692 1.00 49.61  ? 205 GLN D OE1   1 
ATOM   8148 N  NE2   . GLN D 2 205 ? 132.324 141.383 100.767 1.00 52.61  ? 205 GLN D NE2   1 
ATOM   8149 N  N     . VAL D 2 206 ? 133.266 147.764 98.214  1.00 43.95  ? 206 VAL D N     1 
ATOM   8150 C  CA    . VAL D 2 206 ? 133.015 149.202 98.272  1.00 37.67  ? 206 VAL D CA    1 
ATOM   8151 C  C     . VAL D 2 206 ? 132.487 149.708 96.932  1.00 41.78  ? 206 VAL D C     1 
ATOM   8152 O  O     . VAL D 2 206 ? 131.516 150.475 96.880  1.00 42.94  ? 206 VAL D O     1 
ATOM   8153 C  CB    . VAL D 2 206 ? 134.303 149.931 98.707  1.00 41.06  ? 206 VAL D CB    1 
ATOM   8154 C  CG1   . VAL D 2 206 ? 134.257 151.400 98.362  1.00 40.84  ? 206 VAL D CG1   1 
ATOM   8155 C  CG2   . VAL D 2 206 ? 134.536 149.745 100.197 1.00 42.06  ? 206 VAL D CG2   1 
ATOM   8156 N  N     . ARG D 2 207 ? 133.094 149.258 95.829  1.00 47.97  ? 207 ARG D N     1 
ATOM   8157 C  CA    . ARG D 2 207 ? 132.656 149.684 94.501  1.00 48.21  ? 207 ARG D CA    1 
ATOM   8158 C  C     . ARG D 2 207 ? 131.281 149.120 94.158  1.00 47.80  ? 207 ARG D C     1 
ATOM   8159 O  O     . ARG D 2 207 ? 130.435 149.826 93.598  1.00 50.25  ? 207 ARG D O     1 
ATOM   8160 C  CB    . ARG D 2 207 ? 133.688 149.263 93.454  1.00 48.07  ? 207 ARG D CB    1 
ATOM   8161 C  CG    . ARG D 2 207 ? 133.291 149.564 92.018  1.00 48.10  ? 207 ARG D CG    1 
ATOM   8162 C  CD    . ARG D 2 207 ? 134.461 149.390 91.069  1.00 50.88  ? 207 ARG D CD    1 
ATOM   8163 N  NE    . ARG D 2 207 ? 135.152 150.647 90.812  1.00 51.71  ? 207 ARG D NE    1 
ATOM   8164 C  CZ    . ARG D 2 207 ? 136.391 150.913 91.202  1.00 54.56  ? 207 ARG D CZ    1 
ATOM   8165 N  NH1   . ARG D 2 207 ? 137.107 150.031 91.881  1.00 49.38  ? 207 ARG D NH1   1 
ATOM   8166 N  NH2   . ARG D 2 207 ? 136.926 152.094 90.902  1.00 51.87  ? 207 ARG D NH2   1 
ATOM   8167 N  N     . GLN D 2 208 ? 131.029 147.858 94.503  1.00 50.40  ? 208 GLN D N     1 
ATOM   8168 C  CA    . GLN D 2 208 ? 129.751 147.238 94.186  1.00 50.69  ? 208 GLN D CA    1 
ATOM   8169 C  C     . GLN D 2 208 ? 128.636 147.606 95.159  1.00 49.70  ? 208 GLN D C     1 
ATOM   8170 O  O     . GLN D 2 208 ? 127.466 147.345 94.860  1.00 49.54  ? 208 GLN D O     1 
ATOM   8171 C  CB    . GLN D 2 208 ? 129.917 145.713 94.113  1.00 48.71  ? 208 GLN D CB    1 
ATOM   8172 C  CG    . GLN D 2 208 ? 129.641 144.960 95.404  1.00 54.10  ? 208 GLN D CG    1 
ATOM   8173 C  CD    . GLN D 2 208 ? 130.507 143.723 95.553  1.00 59.16  ? 208 GLN D CD    1 
ATOM   8174 O  OE1   . GLN D 2 208 ? 131.218 143.333 94.626  1.00 55.45  ? 208 GLN D OE1   1 
ATOM   8175 N  NE2   . GLN D 2 208 ? 130.443 143.092 96.720  1.00 57.05  ? 208 GLN D NE2   1 
ATOM   8176 N  N     . PHE D 2 209 ? 128.953 148.233 96.290  1.00 49.81  ? 209 PHE D N     1 
ATOM   8177 C  CA    . PHE D 2 209 ? 127.953 148.547 97.305  1.00 45.56  ? 209 PHE D CA    1 
ATOM   8178 C  C     . PHE D 2 209 ? 127.718 150.037 97.499  1.00 49.53  ? 209 PHE D C     1 
ATOM   8179 O  O     . PHE D 2 209 ? 126.564 150.471 97.538  1.00 48.52  ? 209 PHE D O     1 
ATOM   8180 C  CB    . PHE D 2 209 ? 128.362 147.911 98.645  1.00 45.62  ? 209 PHE D CB    1 
ATOM   8181 C  CG    . PHE D 2 209 ? 127.398 148.171 99.770  1.00 49.46  ? 209 PHE D CG    1 
ATOM   8182 C  CD1   . PHE D 2 209 ? 126.037 147.947 99.610  1.00 50.10  ? 209 PHE D CD1   1 
ATOM   8183 C  CD2   . PHE D 2 209 ? 127.858 148.625 100.996 1.00 48.43  ? 209 PHE D CD2   1 
ATOM   8184 C  CE1   . PHE D 2 209 ? 125.154 148.184 100.650 1.00 48.49  ? 209 PHE D CE1   1 
ATOM   8185 C  CE2   . PHE D 2 209 ? 126.982 148.858 102.040 1.00 47.16  ? 209 PHE D CE2   1 
ATOM   8186 C  CZ    . PHE D 2 209 ? 125.629 148.644 101.864 1.00 46.93  ? 209 PHE D CZ    1 
ATOM   8187 N  N     . CYS D 2 210 ? 128.772 150.838 97.620  1.00 47.64  ? 210 CYS D N     1 
ATOM   8188 C  CA    . CYS D 2 210 ? 128.632 152.228 98.031  1.00 44.55  ? 210 CYS D CA    1 
ATOM   8189 C  C     . CYS D 2 210 ? 128.306 153.134 96.850  1.00 42.05  ? 210 CYS D C     1 
ATOM   8190 O  O     . CYS D 2 210 ? 128.543 152.791 95.689  1.00 46.97  ? 210 CYS D O     1 
ATOM   8191 C  CB    . CYS D 2 210 ? 129.909 152.713 98.718  1.00 39.06  ? 210 CYS D CB    1 
ATOM   8192 S  SG    . CYS D 2 210 ? 130.386 151.727 100.155 1.00 53.00  ? 210 CYS D SG    1 
ATOM   8193 N  N     . THR D 2 211 ? 127.741 154.301 97.168  1.00 38.29  ? 211 THR D N     1 
ATOM   8194 C  CA    . THR D 2 211 ? 127.456 155.331 96.180  1.00 37.75  ? 211 THR D CA    1 
ATOM   8195 C  C     . THR D 2 211 ? 128.282 156.594 96.367  1.00 39.63  ? 211 THR D C     1 
ATOM   8196 O  O     . THR D 2 211 ? 128.391 157.385 95.427  1.00 38.95  ? 211 THR D O     1 
ATOM   8197 C  CB    . THR D 2 211 ? 125.967 155.711 96.207  1.00 40.79  ? 211 THR D CB    1 
ATOM   8198 O  OG1   . THR D 2 211 ? 125.604 156.152 97.521  1.00 43.59  ? 211 THR D OG1   1 
ATOM   8199 C  CG2   . THR D 2 211 ? 125.106 154.519 95.824  1.00 42.10  ? 211 THR D CG2   1 
ATOM   8200 N  N     . LYS D 2 212 ? 128.852 156.803 97.552  1.00 43.41  ? 212 LYS D N     1 
ATOM   8201 C  CA    . LYS D 2 212 ? 129.717 157.940 97.823  1.00 35.71  ? 212 LYS D CA    1 
ATOM   8202 C  C     . LYS D 2 212 ? 130.944 157.454 98.578  1.00 36.72  ? 212 LYS D C     1 
ATOM   8203 O  O     . LYS D 2 212 ? 130.908 156.434 99.269  1.00 41.26  ? 212 LYS D O     1 
ATOM   8204 C  CB    . LYS D 2 212 ? 128.992 159.027 98.625  1.00 36.13  ? 212 LYS D CB    1 
ATOM   8205 C  CG    . LYS D 2 212 ? 128.147 159.957 97.776  1.00 37.51  ? 212 LYS D CG    1 
ATOM   8206 C  CD    . LYS D 2 212 ? 127.266 160.834 98.640  1.00 42.47  ? 212 LYS D CD    1 
ATOM   8207 C  CE    . LYS D 2 212 ? 127.062 162.200 98.011  1.00 44.40  ? 212 LYS D CE    1 
ATOM   8208 N  NZ    . LYS D 2 212 ? 126.538 163.188 98.994  1.00 46.88  ? 212 LYS D NZ    1 
ATOM   8209 N  N     . ILE D 2 213 ? 132.044 158.190 98.432  1.00 37.15  ? 213 ILE D N     1 
ATOM   8210 C  CA    . ILE D 2 213 ? 133.321 157.828 99.037  1.00 38.40  ? 213 ILE D CA    1 
ATOM   8211 C  C     . ILE D 2 213 ? 133.806 158.987 99.893  1.00 36.70  ? 213 ILE D C     1 
ATOM   8212 O  O     . ILE D 2 213 ? 133.854 160.130 99.426  1.00 39.94  ? 213 ILE D O     1 
ATOM   8213 C  CB    . ILE D 2 213 ? 134.376 157.461 97.972  1.00 40.41  ? 213 ILE D CB    1 
ATOM   8214 C  CG1   . ILE D 2 213 ? 133.928 156.240 97.175  1.00 35.25  ? 213 ILE D CG1   1 
ATOM   8215 C  CG2   . ILE D 2 213 ? 135.724 157.171 98.611  1.00 34.98  ? 213 ILE D CG2   1 
ATOM   8216 C  CD1   . ILE D 2 213 ? 133.694 155.031 98.025  1.00 37.60  ? 213 ILE D CD1   1 
ATOM   8217 N  N     . ALA D 2 214 ? 134.154 158.695 101.143 1.00 36.34  ? 214 ALA D N     1 
ATOM   8218 C  CA    . ALA D 2 214 ? 134.839 159.634 102.021 1.00 32.22  ? 214 ALA D CA    1 
ATOM   8219 C  C     . ALA D 2 214 ? 136.256 159.127 102.257 1.00 32.43  ? 214 ALA D C     1 
ATOM   8220 O  O     . ALA D 2 214 ? 136.455 158.154 102.992 1.00 33.51  ? 214 ALA D O     1 
ATOM   8221 C  CB    . ALA D 2 214 ? 134.094 159.797 103.345 1.00 29.52  ? 214 ALA D CB    1 
ATOM   8222 N  N     . TRP D 2 215 ? 137.231 159.781 101.633 1.00 32.68  ? 215 TRP D N     1 
ATOM   8223 C  CA    . TRP D 2 215 ? 138.639 159.411 101.741 1.00 29.22  ? 215 TRP D CA    1 
ATOM   8224 C  C     . TRP D 2 215 ? 139.228 160.145 102.940 1.00 31.29  ? 215 TRP D C     1 
ATOM   8225 O  O     . TRP D 2 215 ? 139.192 161.378 103.002 1.00 32.67  ? 215 TRP D O     1 
ATOM   8226 C  CB    . TRP D 2 215 ? 139.377 159.746 100.442 1.00 32.23  ? 215 TRP D CB    1 
ATOM   8227 C  CG    . TRP D 2 215 ? 140.848 159.374 100.377 1.00 33.55  ? 215 TRP D CG    1 
ATOM   8228 C  CD1   . TRP D 2 215 ? 141.562 158.621 101.271 1.00 30.28  ? 215 TRP D CD1   1 
ATOM   8229 C  CD2   . TRP D 2 215 ? 141.767 159.734 99.341  1.00 30.10  ? 215 TRP D CD2   1 
ATOM   8230 N  NE1   . TRP D 2 215 ? 142.865 158.510 100.862 1.00 32.01  ? 215 TRP D NE1   1 
ATOM   8231 C  CE2   . TRP D 2 215 ? 143.018 159.181 99.678  1.00 36.51  ? 215 TRP D CE2   1 
ATOM   8232 C  CE3   . TRP D 2 215 ? 141.655 160.475 98.161  1.00 33.29  ? 215 TRP D CE3   1 
ATOM   8233 C  CZ2   . TRP D 2 215 ? 144.147 159.343 98.877  1.00 33.62  ? 215 TRP D CZ2   1 
ATOM   8234 C  CZ3   . TRP D 2 215 ? 142.776 160.637 97.368  1.00 32.60  ? 215 TRP D CZ3   1 
ATOM   8235 C  CH2   . TRP D 2 215 ? 144.005 160.074 97.730  1.00 32.31  ? 215 TRP D CH2   1 
ATOM   8236 N  N     . ILE D 2 216 ? 139.777 159.381 103.882 1.00 27.21  ? 216 ILE D N     1 
ATOM   8237 C  CA    . ILE D 2 216 ? 140.408 159.921 105.081 1.00 31.62  ? 216 ILE D CA    1 
ATOM   8238 C  C     . ILE D 2 216 ? 141.908 159.694 104.979 1.00 31.65  ? 216 ILE D C     1 
ATOM   8239 O  O     . ILE D 2 216 ? 142.359 158.563 104.762 1.00 38.11  ? 216 ILE D O     1 
ATOM   8240 C  CB    . ILE D 2 216 ? 139.839 159.271 106.355 1.00 34.77  ? 216 ILE D CB    1 
ATOM   8241 C  CG1   . ILE D 2 216 ? 138.312 159.176 106.277 1.00 39.91  ? 216 ILE D CG1   1 
ATOM   8242 C  CG2   . ILE D 2 216 ? 140.275 160.042 107.592 1.00 27.09  ? 216 ILE D CG2   1 
ATOM   8243 C  CD1   . ILE D 2 216 ? 137.603 160.515 106.312 1.00 34.26  ? 216 ILE D CD1   1 
ATOM   8244 N  N     . GLU D 2 217 ? 142.682 160.765 105.136 1.00 35.58  ? 217 GLU D N     1 
ATOM   8245 C  CA    . GLU D 2 217 ? 144.138 160.692 105.042 1.00 37.99  ? 217 GLU D CA    1 
ATOM   8246 C  C     . GLU D 2 217 ? 144.737 161.516 106.173 1.00 38.92  ? 217 GLU D C     1 
ATOM   8247 O  O     . GLU D 2 217 ? 144.637 162.747 106.164 1.00 45.38  ? 217 GLU D O     1 
ATOM   8248 C  CB    . GLU D 2 217 ? 144.630 161.193 103.682 1.00 36.65  ? 217 GLU D CB    1 
ATOM   8249 C  CG    . GLU D 2 217 ? 146.140 161.342 103.577 1.00 37.67  ? 217 GLU D CG    1 
ATOM   8250 C  CD    . GLU D 2 217 ? 146.670 160.968 102.207 1.00 49.45  ? 217 GLU D CD    1 
ATOM   8251 O  OE1   . GLU D 2 217 ? 146.525 159.793 101.809 1.00 49.29  ? 217 GLU D OE1   1 
ATOM   8252 O  OE2   . GLU D 2 217 ? 147.231 161.850 101.526 1.00 49.97  ? 217 GLU D OE2   1 
ATOM   8253 N  N     . GLY D 2 218 ? 145.358 160.838 107.133 1.00 35.91  ? 218 GLY D N     1 
ATOM   8254 C  CA    . GLY D 2 218 ? 146.053 161.505 108.224 1.00 31.47  ? 218 GLY D CA    1 
ATOM   8255 C  C     . GLY D 2 218 ? 145.155 162.279 109.164 1.00 38.23  ? 218 GLY D C     1 
ATOM   8256 O  O     . GLY D 2 218 ? 145.543 163.349 109.648 1.00 44.42  ? 218 GLY D O     1 
ATOM   8257 N  N     . GLY D 2 219 ? 143.961 161.761 109.437 1.00 39.72  ? 219 GLY D N     1 
ATOM   8258 C  CA    . GLY D 2 219 ? 143.021 162.451 110.295 1.00 29.03  ? 219 GLY D CA    1 
ATOM   8259 C  C     . GLY D 2 219 ? 142.188 163.510 109.618 1.00 33.08  ? 219 GLY D C     1 
ATOM   8260 O  O     . GLY D 2 219 ? 141.367 164.147 110.284 1.00 38.01  ? 219 GLY D O     1 
ATOM   8261 N  N     . LYS D 2 220 ? 142.358 163.710 108.316 1.00 35.05  ? 220 LYS D N     1 
ATOM   8262 C  CA    . LYS D 2 220 ? 141.649 164.742 107.578 1.00 34.58  ? 220 LYS D CA    1 
ATOM   8263 C  C     . LYS D 2 220 ? 140.842 164.115 106.452 1.00 34.04  ? 220 LYS D C     1 
ATOM   8264 O  O     . LYS D 2 220 ? 141.185 163.054 105.927 1.00 40.66  ? 220 LYS D O     1 
ATOM   8265 C  CB    . LYS D 2 220 ? 142.620 165.781 107.001 1.00 34.56  ? 220 LYS D CB    1 
ATOM   8266 C  CG    . LYS D 2 220 ? 143.123 166.791 108.012 1.00 39.36  ? 220 LYS D CG    1 
ATOM   8267 C  CD    . LYS D 2 220 ? 144.636 166.866 107.998 1.00 40.54  ? 220 LYS D CD    1 
ATOM   8268 C  CE    . LYS D 2 220 ? 145.113 168.307 107.988 1.00 43.67  ? 220 LYS D CE    1 
ATOM   8269 N  NZ    . LYS D 2 220 ? 146.591 168.403 108.140 1.00 46.32  ? 220 LYS D NZ    1 
ATOM   8270 N  N     . LEU D 2 221 ? 139.759 164.788 106.083 1.00 34.35  ? 221 LEU D N     1 
ATOM   8271 C  CA    . LEU D 2 221 ? 138.955 164.377 104.938 1.00 36.93  ? 221 LEU D CA    1 
ATOM   8272 C  C     . LEU D 2 221 ? 139.676 164.836 103.679 1.00 33.79  ? 221 LEU D C     1 
ATOM   8273 O  O     . LEU D 2 221 ? 139.675 166.021 103.344 1.00 39.41  ? 221 LEU D O     1 
ATOM   8274 C  CB    . LEU D 2 221 ? 137.550 164.957 105.026 1.00 38.60  ? 221 LEU D CB    1 
ATOM   8275 C  CG    . LEU D 2 221 ? 136.606 164.632 103.870 1.00 35.58  ? 221 LEU D CG    1 
ATOM   8276 C  CD1   . LEU D 2 221 ? 136.229 163.161 103.880 1.00 32.46  ? 221 LEU D CD1   1 
ATOM   8277 C  CD2   . LEU D 2 221 ? 135.368 165.509 103.937 1.00 36.23  ? 221 LEU D CD2   1 
ATOM   8278 N  N     . LYS D 2 222 ? 140.317 163.891 102.987 1.00 39.04  ? 222 LYS D N     1 
ATOM   8279 C  CA    . LYS D 2 222 ? 141.054 164.232 101.775 1.00 38.81  ? 222 LYS D CA    1 
ATOM   8280 C  C     . LYS D 2 222 ? 140.109 164.553 100.625 1.00 40.34  ? 222 LYS D C     1 
ATOM   8281 O  O     . LYS D 2 222 ? 140.310 165.539 99.907  1.00 47.05  ? 222 LYS D O     1 
ATOM   8282 C  CB    . LYS D 2 222 ? 141.995 163.089 101.397 1.00 36.50  ? 222 LYS D CB    1 
ATOM   8283 C  CG    . LYS D 2 222 ? 142.898 163.397 100.218 1.00 40.44  ? 222 LYS D CG    1 
ATOM   8284 C  CD    . LYS D 2 222 ? 144.356 163.392 100.625 1.00 41.61  ? 222 LYS D CD    1 
ATOM   8285 C  CE    . LYS D 2 222 ? 145.222 164.051 99.569  1.00 44.80  ? 222 LYS D CE    1 
ATOM   8286 N  NZ    . LYS D 2 222 ? 144.862 163.598 98.200  1.00 48.76  ? 222 LYS D NZ    1 
ATOM   8287 N  N     . ASP D 2 223 ? 139.072 163.740 100.440 1.00 39.07  ? 223 ASP D N     1 
ATOM   8288 C  CA    . ASP D 2 223 ? 138.097 163.979 99.388  1.00 38.51  ? 223 ASP D CA    1 
ATOM   8289 C  C     . ASP D 2 223 ? 136.776 163.343 99.787  1.00 38.91  ? 223 ASP D C     1 
ATOM   8290 O  O     . ASP D 2 223 ? 136.738 162.331 100.491 1.00 43.09  ? 223 ASP D O     1 
ATOM   8291 C  CB    . ASP D 2 223 ? 138.573 163.430 98.040  1.00 37.15  ? 223 ASP D CB    1 
ATOM   8292 C  CG    . ASP D 2 223 ? 137.888 164.100 96.868  1.00 45.89  ? 223 ASP D CG    1 
ATOM   8293 O  OD1   . ASP D 2 223 ? 137.128 165.065 97.092  1.00 50.23  ? 223 ASP D OD1   1 
ATOM   8294 O  OD2   . ASP D 2 223 ? 138.106 163.660 95.722  1.00 48.46  ? 223 ASP D OD2   1 
ATOM   8295 N  N     . TYR D 2 224 ? 135.690 163.958 99.326  1.00 39.03  ? 224 TYR D N     1 
ATOM   8296 C  CA    . TYR D 2 224 ? 134.349 163.447 99.573  1.00 37.78  ? 224 TYR D CA    1 
ATOM   8297 C  C     . TYR D 2 224 ? 133.497 163.748 98.351  1.00 42.77  ? 224 TYR D C     1 
ATOM   8298 O  O     . TYR D 2 224 ? 133.472 164.889 97.882  1.00 47.22  ? 224 TYR D O     1 
ATOM   8299 C  CB    . TYR D 2 224 ? 133.742 164.072 100.833 1.00 38.90  ? 224 TYR D CB    1 
ATOM   8300 C  CG    . TYR D 2 224 ? 132.313 163.666 101.107 1.00 44.18  ? 224 TYR D CG    1 
ATOM   8301 C  CD1   . TYR D 2 224 ? 131.974 162.333 101.311 1.00 46.04  ? 224 TYR D CD1   1 
ATOM   8302 C  CD2   . TYR D 2 224 ? 131.302 164.618 101.171 1.00 44.83  ? 224 TYR D CD2   1 
ATOM   8303 C  CE1   . TYR D 2 224 ? 130.667 161.959 101.564 1.00 38.20  ? 224 TYR D CE1   1 
ATOM   8304 C  CE2   . TYR D 2 224 ? 129.993 164.253 101.424 1.00 43.83  ? 224 TYR D CE2   1 
ATOM   8305 C  CZ    . TYR D 2 224 ? 129.683 162.923 101.619 1.00 43.84  ? 224 TYR D CZ    1 
ATOM   8306 O  OH    . TYR D 2 224 ? 128.382 162.558 101.871 1.00 48.80  ? 224 TYR D OH    1 
ATOM   8307 N  N     . GLY D 2 225 ? 132.813 162.732 97.839  1.00 41.54  ? 225 GLY D N     1 
ATOM   8308 C  CA    . GLY D 2 225 ? 132.009 162.902 96.643  1.00 42.94  ? 225 GLY D CA    1 
ATOM   8309 C  C     . GLY D 2 225 ? 131.519 161.560 96.139  1.00 45.21  ? 225 GLY D C     1 
ATOM   8310 O  O     . GLY D 2 225 ? 131.471 160.586 96.888  1.00 45.66  ? 225 GLY D O     1 
ATOM   8311 N  N     . GLU D 2 226 ? 131.164 161.530 94.854  1.00 48.29  ? 226 GLU D N     1 
ATOM   8312 C  CA    . GLU D 2 226 ? 130.627 160.320 94.242  1.00 49.68  ? 226 GLU D CA    1 
ATOM   8313 C  C     . GLU D 2 226 ? 131.705 159.248 94.120  1.00 51.30  ? 226 GLU D C     1 
ATOM   8314 O  O     . GLU D 2 226 ? 132.904 159.536 94.163  1.00 54.80  ? 226 GLU D O     1 
ATOM   8315 C  CB    . GLU D 2 226 ? 130.043 160.633 92.865  1.00 50.28  ? 226 GLU D CB    1 
ATOM   8316 C  CG    . GLU D 2 226 ? 129.074 161.801 92.849  1.00 51.99  ? 226 GLU D CG    1 
ATOM   8317 C  CD    . GLU D 2 226 ? 127.794 161.511 93.606  1.00 55.96  ? 226 GLU D CD    1 
ATOM   8318 O  OE1   . GLU D 2 226 ? 127.316 160.360 93.550  1.00 58.28  ? 226 GLU D OE1   1 
ATOM   8319 O  OE2   . GLU D 2 226 ? 127.265 162.436 94.258  1.00 57.47  ? 226 GLU D OE2   1 
ATOM   8320 N  N     . LEU D 2 227 ? 131.256 157.997 93.978  1.00 49.60  ? 227 LEU D N     1 
ATOM   8321 C  CA    . LEU D 2 227 ? 132.171 156.856 93.970  1.00 46.54  ? 227 LEU D CA    1 
ATOM   8322 C  C     . LEU D 2 227 ? 133.069 156.868 92.738  1.00 45.97  ? 227 LEU D C     1 
ATOM   8323 O  O     . LEU D 2 227 ? 134.287 156.671 92.843  1.00 50.96  ? 227 LEU D O     1 
ATOM   8324 C  CB    . LEU D 2 227 ? 131.375 155.553 94.049  1.00 46.22  ? 227 LEU D CB    1 
ATOM   8325 C  CG    . LEU D 2 227 ? 132.157 154.239 93.988  1.00 48.15  ? 227 LEU D CG    1 
ATOM   8326 C  CD1   . LEU D 2 227 ? 131.827 153.372 95.186  1.00 44.99  ? 227 LEU D CD1   1 
ATOM   8327 C  CD2   . LEU D 2 227 ? 131.856 153.498 92.698  1.00 49.50  ? 227 LEU D CD2   1 
ATOM   8328 N  N     . ASP D 2 228 ? 132.491 157.144 91.567  1.00 50.50  ? 228 ASP D N     1 
ATOM   8329 C  CA    . ASP D 2 228 ? 133.247 157.197 90.320  1.00 54.36  ? 228 ASP D CA    1 
ATOM   8330 C  C     . ASP D 2 228 ? 134.168 158.407 90.233  1.00 57.43  ? 228 ASP D C     1 
ATOM   8331 O  O     . ASP D 2 228 ? 135.033 158.442 89.352  1.00 57.96  ? 228 ASP D O     1 
ATOM   8332 C  CB    . ASP D 2 228 ? 132.289 157.199 89.130  1.00 54.35  ? 228 ASP D CB    1 
ATOM   8333 C  CG    . ASP D 2 228 ? 131.722 155.824 88.836  1.00 59.42  ? 228 ASP D CG    1 
ATOM   8334 O  OD1   . ASP D 2 228 ? 130.489 155.711 88.677  1.00 57.09  ? 228 ASP D OD1   1 
ATOM   8335 O  OD2   . ASP D 2 228 ? 132.511 154.860 88.762  1.00 60.18  ? 228 ASP D OD2   1 
ATOM   8336 N  N     . ASP D 2 229 ? 134.002 159.392 91.114  1.00 59.30  ? 229 ASP D N     1 
ATOM   8337 C  CA    . ASP D 2 229 ? 134.839 160.582 91.144  1.00 56.24  ? 229 ASP D CA    1 
ATOM   8338 C  C     . ASP D 2 229 ? 135.998 160.398 92.124  1.00 56.81  ? 229 ASP D C     1 
ATOM   8339 O  O     . ASP D 2 229 ? 137.132 160.776 91.821  1.00 60.95  ? 229 ASP D O     1 
ATOM   8340 C  CB    . ASP D 2 229 ? 133.960 161.794 91.506  1.00 56.56  ? 229 ASP D CB    1 
ATOM   8341 C  CG    . ASP D 2 229 ? 134.743 162.996 92.043  1.00 62.82  ? 229 ASP D CG    1 
ATOM   8342 O  OD1   . ASP D 2 229 ? 134.185 163.697 92.913  1.00 67.09  ? 229 ASP D OD1   1 
ATOM   8343 O  OD2   . ASP D 2 229 ? 135.832 163.334 91.526  1.00 61.39  ? 229 ASP D OD2   1 
ATOM   8344 N  N     . VAL D 2 230 ? 135.738 159.798 93.284  1.00 48.15  ? 230 VAL D N     1 
ATOM   8345 C  CA    . VAL D 2 230 ? 136.724 159.772 94.362  1.00 51.35  ? 230 VAL D CA    1 
ATOM   8346 C  C     . VAL D 2 230 ? 137.481 158.447 94.417  1.00 50.35  ? 230 VAL D C     1 
ATOM   8347 O  O     . VAL D 2 230 ? 138.695 158.442 94.644  1.00 56.89  ? 230 VAL D O     1 
ATOM   8348 C  CB    . VAL D 2 230 ? 136.028 160.094 95.703  1.00 44.60  ? 230 VAL D CB    1 
ATOM   8349 C  CG1   . VAL D 2 230 ? 137.038 160.203 96.834  1.00 45.62  ? 230 VAL D CG1   1 
ATOM   8350 C  CG2   . VAL D 2 230 ? 135.260 161.393 95.586  1.00 41.38  ? 230 VAL D CG2   1 
ATOM   8351 N  N     . LEU D 2 231 ? 136.792 157.318 94.227  1.00 45.09  ? 231 LEU D N     1 
ATOM   8352 C  CA    . LEU D 2 231 ? 137.446 156.011 94.312  1.00 44.36  ? 231 LEU D CA    1 
ATOM   8353 C  C     . LEU D 2 231 ? 138.555 155.760 93.278  1.00 47.31  ? 231 LEU D C     1 
ATOM   8354 O  O     . LEU D 2 231 ? 139.551 155.112 93.654  1.00 44.73  ? 231 LEU D O     1 
ATOM   8355 C  CB    . LEU D 2 231 ? 136.387 154.897 94.264  1.00 47.86  ? 231 LEU D CB    1 
ATOM   8356 C  CG    . LEU D 2 231 ? 136.834 153.502 94.709  1.00 48.13  ? 231 LEU D CG    1 
ATOM   8357 C  CD1   . LEU D 2 231 ? 137.325 153.523 96.149  1.00 46.87  ? 231 LEU D CD1   1 
ATOM   8358 C  CD2   . LEU D 2 231 ? 135.723 152.480 94.526  1.00 40.87  ? 231 LEU D CD2   1 
ATOM   8359 N  N     . PRO D 2 232 ? 138.459 156.183 91.997  1.00 49.85  ? 232 PRO D N     1 
ATOM   8360 C  CA    . PRO D 2 232 ? 139.654 156.090 91.134  1.00 50.82  ? 232 PRO D CA    1 
ATOM   8361 C  C     . PRO D 2 232 ? 140.858 156.885 91.619  1.00 47.84  ? 232 PRO D C     1 
ATOM   8362 O  O     . PRO D 2 232 ? 141.991 156.455 91.387  1.00 51.15  ? 232 PRO D O     1 
ATOM   8363 C  CB    . PRO D 2 232 ? 139.143 156.609 89.785  1.00 52.44  ? 232 PRO D CB    1 
ATOM   8364 C  CG    . PRO D 2 232 ? 137.746 156.214 89.769  1.00 53.21  ? 232 PRO D CG    1 
ATOM   8365 C  CD    . PRO D 2 232 ? 137.266 156.456 91.163  1.00 49.03  ? 232 PRO D CD    1 
ATOM   8366 N  N     . LYS D 2 233 ? 140.658 158.015 92.301  1.00 44.05  ? 233 LYS D N     1 
ATOM   8367 C  CA    . LYS D 2 233 ? 141.805 158.770 92.806  1.00 47.50  ? 233 LYS D CA    1 
ATOM   8368 C  C     . LYS D 2 233 ? 142.455 158.078 94.000  1.00 46.43  ? 233 LYS D C     1 
ATOM   8369 O  O     . LYS D 2 233 ? 143.685 158.102 94.137  1.00 46.73  ? 233 LYS D O     1 
ATOM   8370 C  CB    . LYS D 2 233 ? 141.386 160.197 93.152  1.00 46.60  ? 233 LYS D CB    1 
ATOM   8371 C  CG    . LYS D 2 233 ? 140.391 160.780 92.168  1.00 47.40  ? 233 LYS D CG    1 
ATOM   8372 C  CD    . LYS D 2 233 ? 140.607 162.269 91.956  1.00 47.89  ? 233 LYS D CD    1 
ATOM   8373 C  CE    . LYS D 2 233 ? 140.183 163.071 93.170  1.00 50.26  ? 233 LYS D CE    1 
ATOM   8374 N  NZ    . LYS D 2 233 ? 138.962 162.506 93.801  1.00 51.61  ? 233 LYS D NZ    1 
ATOM   8375 N  N     . TYR D 2 234 ? 141.657 157.439 94.861  1.00 38.47  ? 234 TYR D N     1 
ATOM   8376 C  CA    . TYR D 2 234 ? 142.227 156.637 95.941  1.00 37.66  ? 234 TYR D CA    1 
ATOM   8377 C  C     . TYR D 2 234 ? 142.949 155.410 95.397  1.00 41.24  ? 234 TYR D C     1 
ATOM   8378 O  O     . TYR D 2 234 ? 144.003 155.021 95.919  1.00 38.94  ? 234 TYR D O     1 
ATOM   8379 C  CB    . TYR D 2 234 ? 141.141 156.220 96.932  1.00 34.15  ? 234 TYR D CB    1 
ATOM   8380 C  CG    . TYR D 2 234 ? 141.660 155.376 98.074  1.00 40.96  ? 234 TYR D CG    1 
ATOM   8381 C  CD1   . TYR D 2 234 ? 142.678 155.838 98.898  1.00 36.99  ? 234 TYR D CD1   1 
ATOM   8382 C  CD2   . TYR D 2 234 ? 141.140 154.111 98.324  1.00 37.98  ? 234 TYR D CD2   1 
ATOM   8383 C  CE1   . TYR D 2 234 ? 143.161 155.071 99.942  1.00 30.52  ? 234 TYR D CE1   1 
ATOM   8384 C  CE2   . TYR D 2 234 ? 141.615 153.334 99.365  1.00 34.97  ? 234 TYR D CE2   1 
ATOM   8385 C  CZ    . TYR D 2 234 ? 142.625 153.821 100.171 1.00 34.30  ? 234 TYR D CZ    1 
ATOM   8386 O  OH    . TYR D 2 234 ? 143.102 153.054 101.207 1.00 40.86  ? 234 TYR D OH    1 
ATOM   8387 N  N     . GLU D 2 235 ? 142.402 154.795 94.343  1.00 50.98  ? 235 GLU D N     1 
ATOM   8388 C  CA    . GLU D 2 235 ? 143.086 153.680 93.693  1.00 48.12  ? 235 GLU D CA    1 
ATOM   8389 C  C     . GLU D 2 235 ? 144.388 154.129 93.038  1.00 49.80  ? 235 GLU D C     1 
ATOM   8390 O  O     . GLU D 2 235 ? 145.390 153.407 93.078  1.00 53.87  ? 235 GLU D O     1 
ATOM   8391 C  CB    . GLU D 2 235 ? 142.162 153.029 92.664  1.00 51.59  ? 235 GLU D CB    1 
ATOM   8392 C  CG    . GLU D 2 235 ? 141.366 151.857 93.206  1.00 49.46  ? 235 GLU D CG    1 
ATOM   8393 C  CD    . GLU D 2 235 ? 140.033 151.678 92.507  1.00 55.86  ? 235 GLU D CD    1 
ATOM   8394 O  OE1   . GLU D 2 235 ? 139.800 152.348 91.480  1.00 55.94  ? 235 GLU D OE1   1 
ATOM   8395 O  OE2   . GLU D 2 235 ? 139.217 150.864 92.986  1.00 56.48  ? 235 GLU D OE2   1 
ATOM   8396 N  N     . ALA D 2 236 ? 144.390 155.324 92.437  1.00 49.77  ? 236 ALA D N     1 
ATOM   8397 C  CA    . ALA D 2 236 ? 145.605 155.873 91.840  1.00 49.11  ? 236 ALA D CA    1 
ATOM   8398 C  C     . ALA D 2 236 ? 146.660 156.169 92.898  1.00 49.00  ? 236 ALA D C     1 
ATOM   8399 O  O     . ALA D 2 236 ? 147.852 155.934 92.670  1.00 53.46  ? 236 ALA D O     1 
ATOM   8400 C  CB    . ALA D 2 236 ? 145.274 157.135 91.046  1.00 47.30  ? 236 ALA D CB    1 
ATOM   8401 N  N     . PHE D 2 237 ? 146.238 156.674 94.063  1.00 51.31  ? 237 PHE D N     1 
ATOM   8402 C  CA    . PHE D 2 237 ? 147.161 156.857 95.181  1.00 45.88  ? 237 PHE D CA    1 
ATOM   8403 C  C     . PHE D 2 237 ? 147.723 155.522 95.658  1.00 42.51  ? 237 PHE D C     1 
ATOM   8404 O  O     . PHE D 2 237 ? 148.913 155.424 95.988  1.00 50.00  ? 237 PHE D O     1 
ATOM   8405 C  CB    . PHE D 2 237 ? 146.460 157.586 96.332  1.00 44.98  ? 237 PHE D CB    1 
ATOM   8406 C  CG    . PHE D 2 237 ? 147.101 157.363 97.679  1.00 45.94  ? 237 PHE D CG    1 
ATOM   8407 C  CD1   . PHE D 2 237 ? 148.302 157.979 97.997  1.00 46.89  ? 237 PHE D CD1   1 
ATOM   8408 C  CD2   . PHE D 2 237 ? 146.501 156.543 98.626  1.00 51.19  ? 237 PHE D CD2   1 
ATOM   8409 C  CE1   . PHE D 2 237 ? 148.898 157.775 99.230  1.00 45.73  ? 237 PHE D CE1   1 
ATOM   8410 C  CE2   . PHE D 2 237 ? 147.095 156.334 99.857  1.00 48.63  ? 237 PHE D CE2   1 
ATOM   8411 C  CZ    . PHE D 2 237 ? 148.293 156.953 100.159 1.00 47.09  ? 237 PHE D CZ    1 
ATOM   8412 N  N     . LEU D 2 238 ? 146.874 154.489 95.708  1.00 48.33  ? 238 LEU D N     1 
ATOM   8413 C  CA    . LEU D 2 238 ? 147.318 153.173 96.158  1.00 48.95  ? 238 LEU D CA    1 
ATOM   8414 C  C     . LEU D 2 238 ? 148.344 152.564 95.208  1.00 50.21  ? 238 LEU D C     1 
ATOM   8415 O  O     . LEU D 2 238 ? 149.345 152.000 95.657  1.00 50.40  ? 238 LEU D O     1 
ATOM   8416 C  CB    . LEU D 2 238 ? 146.121 152.238 96.320  1.00 52.84  ? 238 LEU D CB    1 
ATOM   8417 C  CG    . LEU D 2 238 ? 145.346 152.348 97.636  1.00 48.97  ? 238 LEU D CG    1 
ATOM   8418 C  CD1   . LEU D 2 238 ? 144.301 151.249 97.729  1.00 48.90  ? 238 LEU D CD1   1 
ATOM   8419 C  CD2   . LEU D 2 238 ? 146.283 152.300 98.834  1.00 45.59  ? 238 LEU D CD2   1 
ATOM   8420 N  N     . ASN D 2 239 ? 148.122 152.676 93.893  1.00 55.89  ? 239 ASN D N     1 
ATOM   8421 C  CA    . ASN D 2 239 ? 149.116 152.154 92.953  1.00 56.85  ? 239 ASN D CA    1 
ATOM   8422 C  C     . ASN D 2 239 ? 150.350 153.047 92.884  1.00 57.91  ? 239 ASN D C     1 
ATOM   8423 O  O     . ASN D 2 239 ? 151.443 152.574 92.549  1.00 64.80  ? 239 ASN D O     1 
ATOM   8424 C  CB    . ASN D 2 239 ? 148.531 151.959 91.547  1.00 58.81  ? 239 ASN D CB    1 
ATOM   8425 C  CG    . ASN D 2 239 ? 147.107 151.423 91.549  1.00 64.09  ? 239 ASN D CG    1 
ATOM   8426 O  OD1   . ASN D 2 239 ? 146.285 151.838 90.731  1.00 65.44  ? 239 ASN D OD1   1 
ATOM   8427 N  ND2   . ASN D 2 239 ? 146.831 150.446 92.409  1.00 59.21  ? 239 ASN D ND2   1 
ATOM   8428 N  N     . ASP D 2 240 ? 150.202 154.339 93.185  1.00 60.28  ? 240 ASP D N     1 
ATOM   8429 C  CA    . ASP D 2 240 ? 151.359 155.225 93.204  1.00 57.38  ? 240 ASP D CA    1 
ATOM   8430 C  C     . ASP D 2 240 ? 152.239 154.961 94.419  1.00 61.24  ? 240 ASP D C     1 
ATOM   8431 O  O     . ASP D 2 240 ? 153.446 155.223 94.382  1.00 65.95  ? 240 ASP D O     1 
ATOM   8432 C  CB    . ASP D 2 240 ? 150.900 156.683 93.182  1.00 58.81  ? 240 ASP D CB    1 
ATOM   8433 C  CG    . ASP D 2 240 ? 150.828 157.252 91.780  1.00 67.37  ? 240 ASP D CG    1 
ATOM   8434 O  OD1   . ASP D 2 240 ? 150.859 158.492 91.640  1.00 67.17  ? 240 ASP D OD1   1 
ATOM   8435 O  OD2   . ASP D 2 240 ? 150.739 156.461 90.817  1.00 69.71  ? 240 ASP D OD2   1 
ATOM   8436 N  N     . PHE D 2 241 ? 151.652 154.453 95.506  1.00 58.11  ? 241 PHE D N     1 
ATOM   8437 C  CA    . PHE D 2 241 ? 152.426 154.228 96.723  1.00 54.05  ? 241 PHE D CA    1 
ATOM   8438 C  C     . PHE D 2 241 ? 153.370 153.036 96.588  1.00 56.96  ? 241 PHE D C     1 
ATOM   8439 O  O     . PHE D 2 241 ? 154.475 153.048 97.143  1.00 62.37  ? 241 PHE D O     1 
ATOM   8440 C  CB    . PHE D 2 241 ? 151.492 154.035 97.916  1.00 56.72  ? 241 PHE D CB    1 
ATOM   8441 C  CG    . PHE D 2 241 ? 152.171 154.195 99.242  1.00 56.11  ? 241 PHE D CG    1 
ATOM   8442 C  CD1   . PHE D 2 241 ? 152.436 155.456 99.749  1.00 56.97  ? 241 PHE D CD1   1 
ATOM   8443 C  CD2   . PHE D 2 241 ? 152.565 153.086 99.974  1.00 58.74  ? 241 PHE D CD2   1 
ATOM   8444 C  CE1   . PHE D 2 241 ? 153.067 155.607 100.969 1.00 57.18  ? 241 PHE D CE1   1 
ATOM   8445 C  CE2   . PHE D 2 241 ? 153.194 153.231 101.195 1.00 57.72  ? 241 PHE D CE2   1 
ATOM   8446 C  CZ    . PHE D 2 241 ? 153.445 154.495 101.693 1.00 59.72  ? 241 PHE D CZ    1 
ATOM   8447 N  N     . LYS D 2 242 ? 152.955 151.991 95.865  1.00 57.05  ? 242 LYS D N     1 
ATOM   8448 C  CA    . LYS D 2 242 ? 153.808 150.810 95.733  1.00 59.23  ? 242 LYS D CA    1 
ATOM   8449 C  C     . LYS D 2 242 ? 154.981 151.029 94.791  1.00 61.32  ? 242 LYS D C     1 
ATOM   8450 O  O     . LYS D 2 242 ? 155.948 150.263 94.848  1.00 65.07  ? 242 LYS D O     1 
ATOM   8451 C  CB    . LYS D 2 242 ? 153.008 149.599 95.243  1.00 61.29  ? 242 LYS D CB    1 
ATOM   8452 C  CG    . LYS D 2 242 ? 151.534 149.630 95.569  1.00 64.39  ? 242 LYS D CG    1 
ATOM   8453 C  CD    . LYS D 2 242 ? 151.255 149.299 97.025  1.00 61.04  ? 242 LYS D CD    1 
ATOM   8454 C  CE    . LYS D 2 242 ? 149.822 148.829 97.206  1.00 61.24  ? 242 LYS D CE    1 
ATOM   8455 N  NZ    . LYS D 2 242 ? 149.403 147.901 96.121  1.00 61.59  ? 242 LYS D NZ    1 
ATOM   8456 N  N     . LYS D 2 243 ? 154.925 152.043 93.931  1.00 65.16  ? 243 LYS D N     1 
ATOM   8457 C  CA    . LYS D 2 243 ? 155.992 152.325 92.985  1.00 66.57  ? 243 LYS D CA    1 
ATOM   8458 C  C     . LYS D 2 243 ? 157.063 153.242 93.557  1.00 67.39  ? 243 LYS D C     1 
ATOM   8459 O  O     . LYS D 2 243 ? 158.014 153.578 92.846  1.00 71.15  ? 243 LYS D O     1 
ATOM   8460 C  CB    . LYS D 2 243 ? 155.412 152.931 91.703  1.00 66.62  ? 243 LYS D CB    1 
ATOM   8461 C  CG    . LYS D 2 243 ? 154.986 151.890 90.682  1.00 68.13  ? 243 LYS D CG    1 
ATOM   8462 C  CD    . LYS D 2 243 ? 153.713 152.291 89.956  1.00 69.35  ? 243 LYS D CD    1 
ATOM   8463 C  CE    . LYS D 2 243 ? 154.010 153.210 88.784  1.00 70.31  ? 243 LYS D CE    1 
ATOM   8464 N  NZ    . LYS D 2 243 ? 152.915 154.192 88.554  1.00 70.37  ? 243 LYS D NZ    1 
ATOM   8465 N  N     . LYS D 2 244 ? 156.932 153.655 94.812  1.00 63.51  ? 244 LYS D N     1 
ATOM   8466 C  CA    . LYS D 2 244 ? 157.959 154.440 95.478  1.00 64.58  ? 244 LYS D CA    1 
ATOM   8467 C  C     . LYS D 2 244 ? 158.977 153.524 96.149  1.00 65.52  ? 244 LYS D C     1 
ATOM   8468 O  O     . LYS D 2 244 ? 158.733 152.337 96.370  1.00 65.93  ? 244 LYS D O     1 
ATOM   8469 C  CB    . LYS D 2 244 ? 157.344 155.374 96.521  1.00 63.79  ? 244 LYS D CB    1 
ATOM   8470 C  CG    . LYS D 2 244 ? 156.178 156.202 96.030  1.00 64.55  ? 244 LYS D CG    1 
ATOM   8471 C  CD    . LYS D 2 244 ? 155.371 156.739 97.199  1.00 64.93  ? 244 LYS D CD    1 
ATOM   8472 C  CE    . LYS D 2 244 ? 155.401 158.254 97.245  1.00 66.64  ? 244 LYS D CE    1 
ATOM   8473 N  NZ    . LYS D 2 244 ? 154.264 158.802 98.032  1.00 67.64  ? 244 LYS D NZ    1 
ATOM   8474 N  N     . SER D 2 245 ? 160.130 154.099 96.475  1.00 66.98  ? 245 SER D N     1 
ATOM   8475 C  CA    . SER D 2 245 ? 161.131 153.385 97.249  1.00 66.64  ? 245 SER D CA    1 
ATOM   8476 C  C     . SER D 2 245 ? 160.738 153.366 98.726  1.00 67.49  ? 245 SER D C     1 
ATOM   8477 O  O     . SER D 2 245 ? 159.768 154.002 99.146  1.00 71.05  ? 245 SER D O     1 
ATOM   8478 C  CB    . SER D 2 245 ? 162.507 154.025 97.065  1.00 66.87  ? 245 SER D CB    1 
ATOM   8479 O  OG    . SER D 2 245 ? 162.480 155.401 97.398  1.00 68.29  ? 245 SER D OG    1 
ATOM   8480 N  N     . LYS D 2 246 ? 161.507 152.613 99.517  1.00 68.42  ? 246 LYS D N     1 
ATOM   8481 C  CA    . LYS D 2 246 ? 161.232 152.513 100.949 1.00 67.24  ? 246 LYS D CA    1 
ATOM   8482 C  C     . LYS D 2 246 ? 161.505 153.833 101.659 1.00 65.81  ? 246 LYS D C     1 
ATOM   8483 O  O     . LYS D 2 246 ? 160.804 154.190 102.615 1.00 67.78  ? 246 LYS D O     1 
ATOM   8484 C  CB    . LYS D 2 246 ? 162.065 151.390 101.565 1.00 69.32  ? 246 LYS D CB    1 
ATOM   8485 C  CG    . LYS D 2 246 ? 161.505 149.996 101.330 1.00 68.97  ? 246 LYS D CG    1 
ATOM   8486 C  CD    . LYS D 2 246 ? 161.538 149.168 102.605 1.00 70.27  ? 246 LYS D CD    1 
ATOM   8487 C  CE    . LYS D 2 246 ? 161.033 147.753 102.362 1.00 71.71  ? 246 LYS D CE    1 
ATOM   8488 N  NZ    . LYS D 2 246 ? 159.563 147.640 102.568 1.00 69.99  ? 246 LYS D NZ    1 
ATOM   8489 N  N     . ALA D 2 247 ? 162.521 154.571 101.202 1.00 65.58  ? 247 ALA D N     1 
ATOM   8490 C  CA    . ALA D 2 247 ? 162.812 155.884 101.767 1.00 67.00  ? 247 ALA D CA    1 
ATOM   8491 C  C     . ALA D 2 247 ? 161.700 156.878 101.460 1.00 67.98  ? 247 ALA D C     1 
ATOM   8492 O  O     . ALA D 2 247 ? 161.344 157.700 102.311 1.00 69.40  ? 247 ALA D O     1 
ATOM   8493 C  CB    . ALA D 2 247 ? 164.152 156.398 101.240 1.00 68.02  ? 247 ALA D CB    1 
ATOM   8494 N  N     . GLU D 2 248 ? 161.131 156.809 100.253 1.00 65.63  ? 248 GLU D N     1 
ATOM   8495 C  CA    . GLU D 2 248 ? 160.033 157.700 99.885  1.00 66.90  ? 248 GLU D CA    1 
ATOM   8496 C  C     . GLU D 2 248 ? 158.766 157.384 100.676 1.00 67.78  ? 248 GLU D C     1 
ATOM   8497 O  O     . GLU D 2 248 ? 158.043 158.299 101.089 1.00 67.15  ? 248 GLU D O     1 
ATOM   8498 C  CB    . GLU D 2 248 ? 159.765 157.605 98.385  1.00 65.91  ? 248 GLU D CB    1 
ATOM   8499 C  CG    . GLU D 2 248 ? 160.515 158.629 97.556  1.00 68.61  ? 248 GLU D CG    1 
ATOM   8500 C  CD    . GLU D 2 248 ? 160.461 158.326 96.072  1.00 70.95  ? 248 GLU D CD    1 
ATOM   8501 O  OE1   . GLU D 2 248 ? 160.459 159.281 95.267  1.00 69.29  ? 248 GLU D OE1   1 
ATOM   8502 O  OE2   . GLU D 2 248 ? 160.421 157.131 95.712  1.00 71.24  ? 248 GLU D OE2   1 
ATOM   8503 N  N     . GLN D 2 249 ? 158.488 156.096 100.900 1.00 60.14  ? 249 GLN D N     1 
ATOM   8504 C  CA    . GLN D 2 249 ? 157.335 155.706 101.708 1.00 60.24  ? 249 GLN D CA    1 
ATOM   8505 C  C     . GLN D 2 249 ? 157.515 156.114 103.166 1.00 59.15  ? 249 GLN D C     1 
ATOM   8506 O  O     . GLN D 2 249 ? 156.557 156.554 103.817 1.00 60.51  ? 249 GLN D O     1 
ATOM   8507 C  CB    . GLN D 2 249 ? 157.106 154.200 101.597 1.00 61.73  ? 249 GLN D CB    1 
ATOM   8508 C  CG    . GLN D 2 249 ? 156.677 153.743 100.215 1.00 59.34  ? 249 GLN D CG    1 
ATOM   8509 C  CD    . GLN D 2 249 ? 156.512 152.242 100.129 1.00 59.34  ? 249 GLN D CD    1 
ATOM   8510 O  OE1   . GLN D 2 249 ? 156.602 151.538 101.133 1.00 61.26  ? 249 GLN D OE1   1 
ATOM   8511 N  NE2   . GLN D 2 249 ? 156.271 151.742 98.924  1.00 61.93  ? 249 GLN D NE2   1 
ATOM   8512 N  N     . LYS D 2 250 ? 158.738 155.983 103.689 1.00 62.73  ? 250 LYS D N     1 
ATOM   8513 C  CA    . LYS D 2 250 ? 159.019 156.438 105.049 1.00 62.90  ? 250 LYS D CA    1 
ATOM   8514 C  C     . LYS D 2 250 ? 158.906 157.954 105.163 1.00 62.23  ? 250 LYS D C     1 
ATOM   8515 O  O     . LYS D 2 250 ? 158.425 158.469 106.177 1.00 63.17  ? 250 LYS D O     1 
ATOM   8516 C  CB    . LYS D 2 250 ? 160.407 155.971 105.483 1.00 64.54  ? 250 LYS D CB    1 
ATOM   8517 C  CG    . LYS D 2 250 ? 160.525 155.700 106.970 1.00 63.78  ? 250 LYS D CG    1 
ATOM   8518 C  CD    . LYS D 2 250 ? 161.890 156.105 107.496 1.00 67.97  ? 250 LYS D CD    1 
ATOM   8519 C  CE    . LYS D 2 250 ? 161.883 156.222 109.010 1.00 66.13  ? 250 LYS D CE    1 
ATOM   8520 N  NZ    . LYS D 2 250 ? 161.340 154.998 109.659 1.00 63.96  ? 250 LYS D NZ    1 
ATOM   8521 N  N     . GLU D 2 251 ? 159.336 158.680 104.125 1.00 63.71  ? 251 GLU D N     1 
ATOM   8522 C  CA    . GLU D 2 251 ? 159.204 160.134 104.109 1.00 62.61  ? 251 GLU D CA    1 
ATOM   8523 C  C     . GLU D 2 251 ? 157.739 160.555 104.063 1.00 62.51  ? 251 GLU D C     1 
ATOM   8524 O  O     . GLU D 2 251 ? 157.344 161.514 104.735 1.00 66.60  ? 251 GLU D O     1 
ATOM   8525 C  CB    . GLU D 2 251 ? 159.967 160.707 102.913 1.00 63.77  ? 251 GLU D CB    1 
ATOM   8526 C  CG    . GLU D 2 251 ? 160.200 162.215 102.929 1.00 66.20  ? 251 GLU D CG    1 
ATOM   8527 C  CD    . GLU D 2 251 ? 160.429 162.778 104.322 1.00 71.58  ? 251 GLU D CD    1 
ATOM   8528 O  OE1   . GLU D 2 251 ? 159.501 163.395 104.886 1.00 71.12  ? 251 GLU D OE1   1 
ATOM   8529 O  OE2   . GLU D 2 251 ? 161.546 162.607 104.854 1.00 67.75  ? 251 GLU D OE2   1 
ATOM   8530 N  N     . PHE D 2 252 ? 156.918 159.837 103.288 1.00 61.30  ? 252 PHE D N     1 
ATOM   8531 C  CA    . PHE D 2 252 ? 155.484 160.122 103.246 1.00 57.86  ? 252 PHE D CA    1 
ATOM   8532 C  C     . PHE D 2 252 ? 154.820 159.849 104.590 1.00 56.33  ? 252 PHE D C     1 
ATOM   8533 O  O     . PHE D 2 252 ? 153.985 160.640 105.046 1.00 61.15  ? 252 PHE D O     1 
ATOM   8534 C  CB    . PHE D 2 252 ? 154.810 159.300 102.144 1.00 58.37  ? 252 PHE D CB    1 
ATOM   8535 C  CG    . PHE D 2 252 ? 153.324 159.531 102.033 1.00 60.44  ? 252 PHE D CG    1 
ATOM   8536 C  CD1   . PHE D 2 252 ? 152.833 160.648 101.376 1.00 62.65  ? 252 PHE D CD1   1 
ATOM   8537 C  CD2   . PHE D 2 252 ? 152.417 158.631 102.583 1.00 60.25  ? 252 PHE D CD2   1 
ATOM   8538 C  CE1   . PHE D 2 252 ? 151.470 160.868 101.272 1.00 62.15  ? 252 PHE D CE1   1 
ATOM   8539 C  CE2   . PHE D 2 252 ? 151.056 158.846 102.484 1.00 58.81  ? 252 PHE D CE2   1 
ATOM   8540 C  CZ    . PHE D 2 252 ? 150.581 159.965 101.826 1.00 58.74  ? 252 PHE D CZ    1 
ATOM   8541 N  N     . ARG D 2 253 ? 155.179 158.734 105.237 1.00 58.77  ? 253 ARG D N     1 
ATOM   8542 C  CA    . ARG D 2 253 ? 154.615 158.414 106.546 1.00 56.83  ? 253 ARG D CA    1 
ATOM   8543 C  C     . ARG D 2 253 ? 155.047 159.423 107.606 1.00 59.41  ? 253 ARG D C     1 
ATOM   8544 O  O     . ARG D 2 253 ? 154.243 159.822 108.457 1.00 61.06  ? 253 ARG D O     1 
ATOM   8545 C  CB    . ARG D 2 253 ? 155.017 156.999 106.957 1.00 57.80  ? 253 ARG D CB    1 
ATOM   8546 C  CG    . ARG D 2 253 ? 153.904 155.977 106.816 1.00 59.53  ? 253 ARG D CG    1 
ATOM   8547 C  CD    . ARG D 2 253 ? 154.381 154.579 107.169 1.00 61.25  ? 253 ARG D CD    1 
ATOM   8548 N  NE    . ARG D 2 253 ? 154.940 153.878 106.020 1.00 61.15  ? 253 ARG D NE    1 
ATOM   8549 C  CZ    . ARG D 2 253 ? 156.225 153.583 105.875 1.00 63.98  ? 253 ARG D CZ    1 
ATOM   8550 N  NH1   . ARG D 2 253 ? 157.120 153.924 106.786 1.00 61.26  ? 253 ARG D NH1   1 
ATOM   8551 N  NH2   . ARG D 2 253 ? 156.621 152.926 104.789 1.00 63.72  ? 253 ARG D NH2   1 
ATOM   8552 N  N     . ASN D 2 254 ? 156.308 159.864 107.554 1.00 64.54  ? 254 ASN D N     1 
ATOM   8553 C  CA    . ASN D 2 254 ? 156.800 160.852 108.509 1.00 62.52  ? 254 ASN D CA    1 
ATOM   8554 C  C     . ASN D 2 254 ? 156.156 162.214 108.288 1.00 58.44  ? 254 ASN D C     1 
ATOM   8555 O  O     . ASN D 2 254 ? 155.843 162.918 109.254 1.00 63.43  ? 254 ASN D O     1 
ATOM   8556 C  CB    . ASN D 2 254 ? 158.322 160.955 108.414 1.00 61.86  ? 254 ASN D CB    1 
ATOM   8557 C  CG    . ASN D 2 254 ? 159.023 159.843 109.159 1.00 63.58  ? 254 ASN D CG    1 
ATOM   8558 O  OD1   . ASN D 2 254 ? 158.433 159.195 110.021 1.00 61.81  ? 254 ASN D OD1   1 
ATOM   8559 N  ND2   . ASN D 2 254 ? 160.287 159.609 108.825 1.00 65.34  ? 254 ASN D ND2   1 
ATOM   8560 N  N     . LYS D 2 255 ? 155.937 162.600 107.028 1.00 56.98  ? 255 LYS D N     1 
ATOM   8561 C  CA    . LYS D 2 255 ? 155.282 163.873 106.741 1.00 58.45  ? 255 LYS D CA    1 
ATOM   8562 C  C     . LYS D 2 255 ? 153.809 163.819 107.132 1.00 59.92  ? 255 LYS D C     1 
ATOM   8563 O  O     . LYS D 2 255 ? 153.232 164.834 107.536 1.00 63.90  ? 255 LYS D O     1 
ATOM   8564 C  CB    . LYS D 2 255 ? 155.494 164.224 105.258 1.00 59.64  ? 255 LYS D CB    1 
ATOM   8565 C  CG    . LYS D 2 255 ? 154.972 165.579 104.698 1.00 59.56  ? 255 LYS D CG    1 
ATOM   8566 C  CD    . LYS D 2 255 ? 153.492 165.639 104.307 1.00 63.67  ? 255 LYS D CD    1 
ATOM   8567 C  CE    . LYS D 2 255 ? 153.074 164.398 103.537 1.00 63.39  ? 255 LYS D CE    1 
ATOM   8568 N  NZ    . LYS D 2 255 ? 151.594 164.242 103.508 1.00 63.28  ? 255 LYS D NZ    1 
ATOM   8569 N  N     . LEU D 2 256 ? 153.181 162.645 107.004 1.00 56.66  ? 256 LEU D N     1 
ATOM   8570 C  CA    . LEU D 2 256 ? 151.808 162.486 107.470 1.00 55.29  ? 256 LEU D CA    1 
ATOM   8571 C  C     . LEU D 2 256 ? 151.722 162.573 108.990 1.00 52.46  ? 256 LEU D C     1 
ATOM   8572 O  O     . LEU D 2 256 ? 150.806 163.200 109.532 1.00 58.06  ? 256 LEU D O     1 
ATOM   8573 C  CB    . LEU D 2 256 ? 151.242 161.153 106.977 1.00 54.93  ? 256 LEU D CB    1 
ATOM   8574 C  CG    . LEU D 2 256 ? 149.789 161.152 106.502 1.00 54.27  ? 256 LEU D CG    1 
ATOM   8575 C  CD1   . LEU D 2 256 ? 149.598 162.166 105.393 1.00 53.76  ? 256 LEU D CD1   1 
ATOM   8576 C  CD2   . LEU D 2 256 ? 149.383 159.767 106.035 1.00 55.33  ? 256 LEU D CD2   1 
ATOM   8577 N  N     . ASP D 2 257 ? 152.672 161.954 109.694 1.00 56.80  ? 257 ASP D N     1 
ATOM   8578 C  CA    . ASP D 2 257 ? 152.630 161.927 111.150 1.00 54.85  ? 257 ASP D CA    1 
ATOM   8579 C  C     . ASP D 2 257 ? 153.161 163.202 111.793 1.00 55.54  ? 257 ASP D C     1 
ATOM   8580 O  O     . ASP D 2 257 ? 152.943 163.407 112.991 1.00 58.71  ? 257 ASP D O     1 
ATOM   8581 C  CB    . ASP D 2 257 ? 153.419 160.724 111.670 1.00 53.61  ? 257 ASP D CB    1 
ATOM   8582 C  CG    . ASP D 2 257 ? 152.525 159.636 112.227 1.00 61.83  ? 257 ASP D CG    1 
ATOM   8583 O  OD1   . ASP D 2 257 ? 151.290 159.831 112.247 1.00 59.83  ? 257 ASP D OD1   1 
ATOM   8584 O  OD2   . ASP D 2 257 ? 153.054 158.585 112.645 1.00 62.78  ? 257 ASP D OD2   1 
ATOM   8585 N  N     . GLU D 2 258 ? 153.865 164.047 111.034 1.00 61.80  ? 258 GLU D N     1 
ATOM   8586 C  CA    . GLU D 2 258 ? 154.400 165.287 111.591 1.00 62.14  ? 258 GLU D CA    1 
ATOM   8587 C  C     . GLU D 2 258 ? 153.290 166.273 111.939 1.00 63.12  ? 258 GLU D C     1 
ATOM   8588 O  O     . GLU D 2 258 ? 153.307 166.879 113.017 1.00 65.49  ? 258 GLU D O     1 
ATOM   8589 C  CB    . GLU D 2 258 ? 155.388 165.906 110.601 1.00 61.98  ? 258 GLU D CB    1 
ATOM   8590 C  CG    . GLU D 2 258 ? 155.769 167.345 110.884 1.00 63.96  ? 258 GLU D CG    1 
ATOM   8591 C  CD    . GLU D 2 258 ? 156.990 167.782 110.101 1.00 68.86  ? 258 GLU D CD    1 
ATOM   8592 O  OE1   . GLU D 2 258 ? 157.110 167.391 108.921 1.00 68.29  ? 258 GLU D OE1   1 
ATOM   8593 O  OE2   . GLU D 2 258 ? 157.829 168.515 110.665 1.00 68.94  ? 258 GLU D OE2   1 
ATOM   8594 N  N     . SER D 2 259 ? 152.310 166.435 111.050 1.00 54.53  ? 259 SER D N     1 
ATOM   8595 C  CA    . SER D 2 259 ? 151.200 167.346 111.292 1.00 51.96  ? 259 SER D CA    1 
ATOM   8596 C  C     . SER D 2 259 ? 150.217 166.831 112.335 1.00 49.23  ? 259 SER D C     1 
ATOM   8597 O  O     . SER D 2 259 ? 149.503 167.639 112.939 1.00 54.60  ? 259 SER D O     1 
ATOM   8598 C  CB    . SER D 2 259 ? 150.457 167.626 109.985 1.00 50.88  ? 259 SER D CB    1 
ATOM   8599 O  OG    . SER D 2 259 ? 149.845 166.449 109.484 1.00 53.76  ? 259 SER D OG    1 
ATOM   8600 N  N     . ARG D 2 260 ? 150.164 165.521 112.567 1.00 39.01  ? 260 ARG D N     1 
ATOM   8601 C  CA    . ARG D 2 260 ? 149.214 164.950 113.513 1.00 32.04  ? 260 ARG D CA    1 
ATOM   8602 C  C     . ARG D 2 260 ? 149.666 165.067 114.960 1.00 34.36  ? 260 ARG D C     1 
ATOM   8603 O  O     . ARG D 2 260 ? 148.858 164.854 115.869 1.00 36.60  ? 260 ARG D O     1 
ATOM   8604 C  CB    . ARG D 2 260 ? 148.963 163.477 113.183 1.00 32.47  ? 260 ARG D CB    1 
ATOM   8605 C  CG    . ARG D 2 260 ? 147.743 163.226 112.321 1.00 29.13  ? 260 ARG D CG    1 
ATOM   8606 C  CD    . ARG D 2 260 ? 147.616 161.753 111.997 1.00 33.93  ? 260 ARG D CD    1 
ATOM   8607 N  NE    . ARG D 2 260 ? 146.335 161.206 112.423 1.00 33.57  ? 260 ARG D NE    1 
ATOM   8608 C  CZ    . ARG D 2 260 ? 145.861 160.031 112.036 1.00 27.18  ? 260 ARG D CZ    1 
ATOM   8609 N  NH1   . ARG D 2 260 ? 146.540 159.248 111.216 1.00 29.43  ? 260 ARG D NH1   1 
ATOM   8610 N  NH2   . ARG D 2 260 ? 144.676 159.630 112.486 1.00 33.29  ? 260 ARG D NH2   1 
ATOM   8611 N  N     . PHE D 2 261 ? 150.932 165.398 115.199 1.00 44.74  ? 261 PHE D N     1 
ATOM   8612 C  CA    . PHE D 2 261 ? 151.472 165.535 116.546 1.00 37.76  ? 261 PHE D CA    1 
ATOM   8613 C  C     . PHE D 2 261 ? 151.817 166.995 116.806 1.00 42.02  ? 261 PHE D C     1 
ATOM   8614 O  O     . PHE D 2 261 ? 152.396 167.664 115.943 1.00 46.68  ? 261 PHE D O     1 
ATOM   8615 C  CB    . PHE D 2 261 ? 152.708 164.657 116.734 1.00 37.49  ? 261 PHE D CB    1 
ATOM   8616 C  CG    . PHE D 2 261 ? 152.397 163.209 116.988 1.00 36.38  ? 261 PHE D CG    1 
ATOM   8617 C  CD1   . PHE D 2 261 ? 152.345 162.301 115.941 1.00 40.10  ? 261 PHE D CD1   1 
ATOM   8618 C  CD2   . PHE D 2 261 ? 152.164 162.754 118.277 1.00 39.14  ? 261 PHE D CD2   1 
ATOM   8619 C  CE1   . PHE D 2 261 ? 152.062 160.966 116.174 1.00 39.95  ? 261 PHE D CE1   1 
ATOM   8620 C  CE2   . PHE D 2 261 ? 151.882 161.422 118.517 1.00 35.54  ? 261 PHE D CE2   1 
ATOM   8621 C  CZ    . PHE D 2 261 ? 151.832 160.527 117.464 1.00 35.65  ? 261 PHE D CZ    1 
ATOM   8622 N  N     . VAL D 2 262 ? 151.460 167.486 117.994 1.00 45.09  ? 262 VAL D N     1 
ATOM   8623 C  CA    . VAL D 2 262 ? 151.642 168.885 118.355 1.00 48.23  ? 262 VAL D CA    1 
ATOM   8624 C  C     . VAL D 2 262 ? 151.720 168.979 119.877 1.00 47.18  ? 262 VAL D C     1 
ATOM   8625 O  O     . VAL D 2 262 ? 151.070 168.228 120.608 1.00 46.74  ? 262 VAL D O     1 
ATOM   8626 C  CB    . VAL D 2 262 ? 150.501 169.769 117.772 1.00 47.64  ? 262 VAL D CB    1 
ATOM   8627 C  CG1   . VAL D 2 262 ? 149.137 169.277 118.221 1.00 45.53  ? 262 VAL D CG1   1 
ATOM   8628 C  CG2   . VAL D 2 262 ? 150.690 171.264 118.061 1.00 47.32  ? 262 VAL D CG2   1 
ATOM   8629 N  N     . ILE D 2 263 ? 152.576 169.881 120.356 1.00 55.13  ? 263 ILE D N     1 
ATOM   8630 C  CA    . ILE D 2 263 ? 152.692 170.187 121.777 1.00 54.78  ? 263 ILE D CA    1 
ATOM   8631 C  C     . ILE D 2 263 ? 151.743 171.337 122.087 1.00 54.75  ? 263 ILE D C     1 
ATOM   8632 O  O     . ILE D 2 263 ? 151.906 172.446 121.561 1.00 56.80  ? 263 ILE D O     1 
ATOM   8633 C  CB    . ILE D 2 263 ? 154.135 170.545 122.165 1.00 53.21  ? 263 ILE D CB    1 
ATOM   8634 C  CG1   . ILE D 2 263 ? 155.067 169.347 121.928 1.00 50.28  ? 263 ILE D CG1   1 
ATOM   8635 C  CG2   . ILE D 2 263 ? 154.191 171.065 123.602 1.00 52.99  ? 263 ILE D CG2   1 
ATOM   8636 C  CD1   . ILE D 2 263 ? 155.138 168.355 123.075 1.00 54.82  ? 263 ILE D CD1   1 
ATOM   8637 N  N     . LYS D 2 264 ? 150.752 171.074 122.933 1.00 56.14  ? 264 LYS D N     1 
ATOM   8638 C  CA    . LYS D 2 264 ? 149.810 172.104 123.354 1.00 55.40  ? 264 LYS D CA    1 
ATOM   8639 C  C     . LYS D 2 264 ? 149.272 171.808 124.749 1.00 57.35  ? 264 LYS D C     1 
ATOM   8640 O  O     . LYS D 2 264 ? 148.697 172.681 125.400 1.00 58.22  ? 264 LYS D O     1 
ATOM   8641 C  CB    . LYS D 2 264 ? 148.650 172.228 122.364 1.00 55.69  ? 264 LYS D CB    1 
ATOM   8642 C  CG    . LYS D 2 264 ? 148.206 170.919 121.744 1.00 56.31  ? 264 LYS D CG    1 
ATOM   8643 C  CD    . LYS D 2 264 ? 146.921 171.085 120.949 1.00 55.36  ? 264 LYS D CD    1 
ATOM   8644 C  CE    . LYS D 2 264 ? 145.797 171.626 121.818 1.00 55.08  ? 264 LYS D CE    1 
ATOM   8645 N  NZ    . LYS D 2 264 ? 144.546 171.830 121.039 1.00 59.02  ? 264 LYS D NZ    1 
ATOM   8646 O  OXT   . LYS D 2 264 ? 149.403 170.692 125.252 1.00 58.15  ? 264 LYS D OXT   1 
HETATM 8647 C  C1    . AV0 E 3 .   ? 141.082 111.170 134.453 1.00 63.36  ? 301 AV0 A C1    1 
HETATM 8648 O  O1    . AV0 E 3 .   ? 139.887 111.835 134.734 1.00 64.29  ? 301 AV0 A O1    1 
HETATM 8649 C  C2    . AV0 E 3 .   ? 141.058 109.807 135.131 1.00 61.86  ? 301 AV0 A C2    1 
HETATM 8650 O  O2    . AV0 E 3 .   ? 141.041 109.933 136.550 1.00 64.28  ? 301 AV0 A O2    1 
HETATM 8651 C  C3    . AV0 E 3 .   ? 142.274 109.021 134.736 1.00 62.03  ? 301 AV0 A C3    1 
HETATM 8652 O  O3    . AV0 E 3 .   ? 142.218 107.732 135.341 1.00 64.48  ? 301 AV0 A O3    1 
HETATM 8653 C  C4    . AV0 E 3 .   ? 142.318 108.919 133.225 1.00 64.28  ? 301 AV0 A C4    1 
HETATM 8654 O  O4    . AV0 E 3 .   ? 143.459 108.143 132.836 1.00 61.73  ? 301 AV0 A O4    1 
HETATM 8655 C  C5    . AV0 E 3 .   ? 142.336 110.309 132.604 1.00 64.08  ? 301 AV0 A C5    1 
HETATM 8656 O  O5    . AV0 E 3 .   ? 141.178 111.038 133.047 1.00 64.12  ? 301 AV0 A O5    1 
HETATM 8657 C  C6    . AV0 E 3 .   ? 142.265 110.282 131.099 1.00 63.96  ? 301 AV0 A C6    1 
HETATM 8658 O  O6    . AV0 E 3 .   ? 143.534 109.994 130.528 1.00 65.04  ? 301 AV0 A O6    1 
HETATM 8659 C  CAA   . AV0 E 3 .   ? 132.752 119.548 143.391 1.00 57.36  ? 301 AV0 A CAA   1 
HETATM 8660 C  CAB   . AV0 E 3 .   ? 144.423 116.285 145.148 1.00 59.95  ? 301 AV0 A CAB   1 
HETATM 8661 O  OAI   . AV0 E 3 .   ? 141.114 104.787 134.519 1.00 69.86  ? 301 AV0 A OAI   1 
HETATM 8662 O  OAJ   . AV0 E 3 .   ? 139.627 113.941 124.069 1.00 63.02  ? 301 AV0 A OAJ   1 
HETATM 8663 O  OAL   . AV0 E 3 .   ? 136.878 116.160 129.629 1.00 63.98  ? 301 AV0 A OAL   1 
HETATM 8664 O  OAN   . AV0 E 3 .   ? 137.679 110.768 129.768 1.00 64.20  ? 301 AV0 A OAN   1 
HETATM 8665 O  OAP   . AV0 E 3 .   ? 138.077 111.037 132.578 1.00 67.92  ? 301 AV0 A OAP   1 
HETATM 8666 O  OAQ   . AV0 E 3 .   ? 141.095 104.308 129.938 1.00 63.21  ? 301 AV0 A OAQ   1 
HETATM 8667 O  OAR   . AV0 E 3 .   ? 135.322 111.974 124.646 1.00 61.24  ? 301 AV0 A OAR   1 
HETATM 8668 O  OAS   . AV0 E 3 .   ? 143.470 105.560 129.000 1.00 67.13  ? 301 AV0 A OAS   1 
HETATM 8669 O  OAT   . AV0 E 3 .   ? 135.685 115.244 126.187 1.00 63.06  ? 301 AV0 A OAT   1 
HETATM 8670 O  OAU   . AV0 E 3 .   ? 144.660 107.519 130.704 1.00 66.75  ? 301 AV0 A OAU   1 
HETATM 8671 O  OAV   . AV0 E 3 .   ? 135.881 111.862 127.560 1.00 64.36  ? 301 AV0 A OAV   1 
HETATM 8672 C  CAW   . AV0 E 3 .   ? 132.471 118.907 142.059 1.00 57.23  ? 301 AV0 A CAW   1 
HETATM 8673 C  CAX   . AV0 E 3 .   ? 144.179 114.936 144.518 1.00 60.05  ? 301 AV0 A CAX   1 
HETATM 8674 C  CAY   . AV0 E 3 .   ? 132.367 117.414 142.117 1.00 62.76  ? 301 AV0 A CAY   1 
HETATM 8675 C  CAZ   . AV0 E 3 .   ? 143.360 114.947 143.252 1.00 63.63  ? 301 AV0 A CAZ   1 
HETATM 8676 C  CBA   . AV0 E 3 .   ? 132.425 116.714 140.787 1.00 62.04  ? 301 AV0 A CBA   1 
HETATM 8677 C  CBB   . AV0 E 3 .   ? 143.670 113.784 142.336 1.00 61.90  ? 301 AV0 A CBB   1 
HETATM 8678 C  CBC   . AV0 E 3 .   ? 133.817 116.521 140.266 1.00 58.25  ? 301 AV0 A CBC   1 
HETATM 8679 C  CBD   . AV0 E 3 .   ? 142.696 113.590 141.202 1.00 63.66  ? 301 AV0 A CBD   1 
HETATM 8680 C  CBE   . AV0 E 3 .   ? 133.961 115.406 139.270 1.00 60.30  ? 301 AV0 A CBE   1 
HETATM 8681 C  CBF   . AV0 E 3 .   ? 142.589 114.758 140.253 1.00 62.94  ? 301 AV0 A CBF   1 
HETATM 8682 C  CBG   . AV0 E 3 .   ? 135.124 115.594 138.343 1.00 60.43  ? 301 AV0 A CBG   1 
HETATM 8683 C  CBH   . AV0 E 3 .   ? 141.177 115.238 140.021 1.00 61.55  ? 301 AV0 A CBH   1 
HETATM 8684 C  CBI   . AV0 E 3 .   ? 135.845 114.333 137.953 1.00 61.34  ? 301 AV0 A CBI   1 
HETATM 8685 C  CBJ   . AV0 E 3 .   ? 140.359 114.354 139.114 1.00 60.57  ? 301 AV0 A CBJ   1 
HETATM 8686 C  CBK   . AV0 E 3 .   ? 136.576 114.451 136.644 1.00 63.31  ? 301 AV0 A CBK   1 
HETATM 8687 C  CBL   . AV0 E 3 .   ? 140.713 114.470 137.653 1.00 62.89  ? 301 AV0 A CBL   1 
HETATM 8688 C  CBM   . AV0 E 3 .   ? 141.823 104.388 133.342 1.00 65.52  ? 301 AV0 A CBM   1 
HETATM 8689 C  CBN   . AV0 E 3 .   ? 138.289 114.262 124.447 1.00 61.49  ? 301 AV0 A CBN   1 
HETATM 8690 C  CBP   . AV0 E 3 .   ? 138.206 115.705 129.420 1.00 61.69  ? 301 AV0 A CBP   1 
HETATM 8691 C  CBQ   . AV0 E 3 .   ? 137.577 113.359 136.379 1.00 62.58  ? 301 AV0 A CBQ   1 
HETATM 8692 C  CBR   . AV0 E 3 .   ? 139.571 114.904 136.763 1.00 64.03  ? 301 AV0 A CBR   1 
HETATM 8693 C  CBS   . AV0 E 3 .   ? 139.939 112.647 135.917 1.00 61.06  ? 301 AV0 A CBS   1 
HETATM 8694 C  CBT   . AV0 E 3 .   ? 138.860 114.339 134.427 1.00 62.56  ? 301 AV0 A CBT   1 
HETATM 8695 O  OBV   . AV0 E 3 .   ? 137.915 113.627 133.607 1.00 62.94  ? 301 AV0 A OBV   1 
HETATM 8696 O  OBX   . AV0 E 3 .   ? 137.973 114.517 131.486 1.00 65.38  ? 301 AV0 A OBX   1 
HETATM 8697 O  OBY   . AV0 E 3 .   ? 141.801 106.580 132.421 1.00 66.63  ? 301 AV0 A OBY   1 
HETATM 8698 O  OBZ   . AV0 E 3 .   ? 138.053 112.483 125.986 1.00 63.65  ? 301 AV0 A OBZ   1 
HETATM 8699 O  OCB   . AV0 E 3 .   ? 138.531 112.984 128.205 1.00 67.34  ? 301 AV0 A OCB   1 
HETATM 8700 C  CCC   . AV0 E 3 .   ? 141.427 105.218 132.141 1.00 66.00  ? 301 AV0 A CCC   1 
HETATM 8701 C  CCD   . AV0 E 3 .   ? 137.512 113.006 124.772 1.00 63.87  ? 301 AV0 A CCD   1 
HETATM 8702 C  CCF   . AV0 E 3 .   ? 138.504 114.414 130.151 1.00 63.99  ? 301 AV0 A CCF   1 
HETATM 8703 C  CCH   . AV0 E 3 .   ? 138.260 111.937 130.333 1.00 61.71  ? 301 AV0 A CCH   1 
HETATM 8704 C  CCJ   . AV0 E 3 .   ? 138.359 113.425 132.295 1.00 62.13  ? 301 AV0 A CCJ   1 
HETATM 8705 C  CCL   . AV0 E 3 .   ? 137.758 112.143 131.742 1.00 63.30  ? 301 AV0 A CCL   1 
HETATM 8706 C  CCM   . AV0 E 3 .   ? 138.958 113.813 135.859 1.00 62.47  ? 301 AV0 A CCM   1 
HETATM 8707 C  CCN   . AV0 E 3 .   ? 142.093 104.774 130.843 1.00 65.60  ? 301 AV0 A CCN   1 
HETATM 8708 C  CCO   . AV0 E 3 .   ? 135.989 113.208 124.886 1.00 62.96  ? 301 AV0 A CCO   1 
HETATM 8709 C  CCQ   . AV0 E 3 .   ? 137.937 113.164 129.496 1.00 62.18  ? 301 AV0 A CCQ   1 
HETATM 8710 C  CCR   . AV0 E 3 .   ? 143.212 106.794 132.519 1.00 64.72  ? 301 AV0 A CCR   1 
HETATM 8711 C  CCS   . AV0 E 3 .   ? 137.756 113.308 127.081 1.00 63.61  ? 301 AV0 A CCS   1 
HETATM 8712 C  CCT   . AV0 E 3 .   ? 142.858 105.937 130.234 1.00 65.68  ? 301 AV0 A CCT   1 
HETATM 8713 C  CCU   . AV0 E 3 .   ? 135.536 113.825 126.204 1.00 63.13  ? 301 AV0 A CCU   1 
HETATM 8714 C  CCV   . AV0 E 3 .   ? 143.903 106.426 131.213 1.00 65.13  ? 301 AV0 A CCV   1 
HETATM 8715 C  CCW   . AV0 E 3 .   ? 136.269 113.224 127.382 1.00 65.15  ? 301 AV0 A CCW   1 
HETATM 8716 C  C1    . AV0 F 3 .   ? 141.478 139.070 176.650 1.00 69.86  ? 302 AV0 A C1    1 
HETATM 8717 O  O1    . AV0 F 3 .   ? 140.184 139.465 176.325 1.00 69.26  ? 302 AV0 A O1    1 
HETATM 8718 C  C2    . AV0 F 3 .   ? 141.961 139.816 177.883 1.00 68.39  ? 302 AV0 A C2    1 
HETATM 8719 O  O2    . AV0 F 3 .   ? 142.666 140.990 177.492 1.00 69.05  ? 302 AV0 A O2    1 
HETATM 8720 C  C3    . AV0 F 3 .   ? 142.850 138.915 178.678 1.00 66.81  ? 302 AV0 A C3    1 
HETATM 8721 O  O3    . AV0 F 3 .   ? 143.470 139.636 179.736 1.00 68.13  ? 302 AV0 A O3    1 
HETATM 8722 C  C4    . AV0 F 3 .   ? 142.014 137.775 179.219 1.00 69.70  ? 302 AV0 A C4    1 
HETATM 8723 O  O4    . AV0 F 3 .   ? 142.941 136.825 179.761 1.00 72.18  ? 302 AV0 A O4    1 
HETATM 8724 C  C5    . AV0 F 3 .   ? 141.253 137.085 178.093 1.00 69.04  ? 302 AV0 A C5    1 
HETATM 8725 O  O5    . AV0 F 3 .   ? 141.529 137.659 176.787 1.00 70.31  ? 302 AV0 A O5    1 
HETATM 8726 C  C6    . AV0 F 3 .   ? 139.763 136.959 178.284 1.00 66.27  ? 302 AV0 A C6    1 
HETATM 8727 O  O6    . AV0 F 3 .   ? 139.442 136.177 179.431 1.00 71.27  ? 302 AV0 A O6    1 
HETATM 8728 C  CAA   . AV0 F 3 .   ? 136.725 146.662 165.776 1.00 61.30  ? 302 AV0 A CAA   1 
HETATM 8729 C  CAB   . AV0 F 3 .   ? 141.429 131.409 165.731 1.00 60.87  ? 302 AV0 A CAB   1 
HETATM 8730 O  OAI   . AV0 F 3 .   ? 142.240 138.915 183.586 1.00 70.59  ? 302 AV0 A OAI   1 
HETATM 8731 O  OAJ   . AV0 F 3 .   ? 136.770 142.951 183.860 1.00 71.54  ? 302 AV0 A OAJ   1 
HETATM 8732 O  OAL   . AV0 F 3 .   ? 138.352 139.215 180.160 1.00 72.81  ? 302 AV0 A OAL   1 
HETATM 8733 O  OAN   . AV0 F 3 .   ? 134.124 137.837 179.069 1.00 69.10  ? 302 AV0 A OAN   1 
HETATM 8734 O  OAP   . AV0 F 3 .   ? 135.225 136.991 176.732 1.00 68.50  ? 302 AV0 A OAP   1 
HETATM 8735 O  OAQ   . AV0 F 3 .   ? 140.541 134.803 184.207 1.00 69.08  ? 302 AV0 A OAQ   1 
HETATM 8736 O  OAR   . AV0 F 3 .   ? 133.631 140.556 185.238 1.00 68.64  ? 302 AV0 A OAR   1 
HETATM 8737 O  OAS   . AV0 F 3 .   ? 141.442 133.034 182.209 1.00 67.77  ? 302 AV0 A OAS   1 
HETATM 8738 O  OAT   . AV0 F 3 .   ? 132.405 138.755 183.072 1.00 71.85  ? 302 AV0 A OAT   1 
HETATM 8739 O  OAU   . AV0 F 3 .   ? 142.156 134.414 179.679 1.00 69.21  ? 302 AV0 A OAU   1 
HETATM 8740 O  OAV   . AV0 F 3 .   ? 132.691 141.687 181.105 1.00 64.75  ? 302 AV0 A OAV   1 
HETATM 8741 C  CAW   . AV0 F 3 .   ? 137.149 146.344 167.181 1.00 61.90  ? 302 AV0 A CAW   1 
HETATM 8742 C  CAX   . AV0 F 3 .   ? 140.659 131.646 166.996 1.00 60.60  ? 302 AV0 A CAX   1 
HETATM 8743 C  CAY   . AV0 F 3 .   ? 136.141 145.519 167.921 1.00 62.12  ? 302 AV0 A CAY   1 
HETATM 8744 C  CAZ   . AV0 F 3 .   ? 141.520 132.100 168.133 1.00 60.48  ? 302 AV0 A CAZ   1 
HETATM 8745 C  CBA   . AV0 F 3 .   ? 136.699 144.461 168.830 1.00 58.67  ? 302 AV0 A CBA   1 
HETATM 8746 C  CBB   . AV0 F 3 .   ? 141.145 133.409 168.766 1.00 58.80  ? 302 AV0 A CBB   1 
HETATM 8747 C  CBC   . AV0 F 3 .   ? 135.743 144.042 169.904 1.00 62.48  ? 302 AV0 A CBC   1 
HETATM 8748 C  CBD   . AV0 F 3 .   ? 142.333 134.182 169.229 1.00 61.01  ? 302 AV0 A CBD   1 
HETATM 8749 C  CBE   . AV0 F 3 .   ? 135.810 142.591 170.264 1.00 63.36  ? 302 AV0 A CBE   1 
HETATM 8750 C  CBF   . AV0 F 3 .   ? 142.277 134.643 170.646 1.00 64.63  ? 302 AV0 A CBF   1 
HETATM 8751 C  CBG   . AV0 F 3 .   ? 136.764 142.278 171.377 1.00 64.41  ? 302 AV0 A CBG   1 
HETATM 8752 C  CBH   . AV0 F 3 .   ? 141.931 136.092 170.819 1.00 62.60  ? 302 AV0 A CBH   1 
HETATM 8753 C  CBI   . AV0 F 3 .   ? 136.865 140.817 171.701 1.00 61.57  ? 302 AV0 A CBI   1 
HETATM 8754 C  CBJ   . AV0 F 3 .   ? 140.759 136.314 171.730 1.00 62.92  ? 302 AV0 A CBJ   1 
HETATM 8755 C  CBK   . AV0 F 3 .   ? 137.547 140.539 173.002 1.00 64.71  ? 302 AV0 A CBK   1 
HETATM 8756 C  CBL   . AV0 F 3 .   ? 140.673 137.685 172.331 1.00 65.22  ? 302 AV0 A CBL   1 
HETATM 8757 C  CBM   . AV0 F 3 .   ? 142.464 137.513 183.738 1.00 66.52  ? 302 AV0 A CBM   1 
HETATM 8758 C  CBN   . AV0 F 3 .   ? 136.025 141.830 184.331 1.00 68.82  ? 302 AV0 A CBN   1 
HETATM 8759 C  CBP   . AV0 F 3 .   ? 138.302 140.067 179.018 1.00 69.06  ? 302 AV0 A CBP   1 
HETATM 8760 C  CBQ   . AV0 F 3 .   ? 138.807 139.740 172.868 1.00 62.81  ? 302 AV0 A CBQ   1 
HETATM 8761 C  CBR   . AV0 F 3 .   ? 140.059 137.684 173.700 1.00 65.98  ? 302 AV0 A CBR   1 
HETATM 8762 C  CBS   . AV0 F 3 .   ? 140.031 139.880 174.958 1.00 64.83  ? 302 AV0 A CBS   1 
HETATM 8763 C  CBT   . AV0 F 3 .   ? 137.887 138.404 174.670 1.00 67.05  ? 302 AV0 A CBT   1 
HETATM 8764 O  OBV   . AV0 F 3 .   ? 137.798 138.467 176.103 1.00 67.49  ? 302 AV0 A OBV   1 
HETATM 8765 O  OBX   . AV0 F 3 .   ? 136.784 140.264 177.148 1.00 70.26  ? 302 AV0 A OBX   1 
HETATM 8766 O  OBY   . AV0 F 3 .   ? 141.562 136.974 181.618 1.00 68.96  ? 302 AV0 A OBY   1 
HETATM 8767 O  OBZ   . AV0 F 3 .   ? 135.405 141.263 182.109 1.00 70.49  ? 302 AV0 A OBZ   1 
HETATM 8768 O  OCB   . AV0 F 3 .   ? 134.938 140.496 179.980 1.00 70.15  ? 302 AV0 A OCB   1 
HETATM 8769 C  CCC   . AV0 F 3 .   ? 141.406 136.708 183.022 1.00 69.69  ? 302 AV0 A CCC   1 
HETATM 8770 C  CCD   . AV0 F 3 .   ? 134.861 141.514 183.423 1.00 67.59  ? 302 AV0 A CCD   1 
HETATM 8771 C  CCF   . AV0 F 3 .   ? 136.882 140.359 178.600 1.00 69.20  ? 302 AV0 A CCF   1 
HETATM 8772 C  CCH   . AV0 F 3 .   ? 134.975 138.742 178.374 1.00 67.27  ? 302 AV0 A CCH   1 
HETATM 8773 C  CCJ   . AV0 F 3 .   ? 136.588 138.985 176.560 1.00 69.73  ? 302 AV0 A CCJ   1 
HETATM 8774 C  CCL   . AV0 F 3 .   ? 135.910 137.989 177.486 1.00 68.25  ? 302 AV0 A CCL   1 
HETATM 8775 C  CCM   . AV0 F 3 .   ? 139.213 138.911 174.100 1.00 60.73  ? 302 AV0 A CCM   1 
HETATM 8776 C  CCN   . AV0 F 3 .   ? 141.533 135.208 183.271 1.00 69.43  ? 302 AV0 A CCN   1 
HETATM 8777 C  CCO   . AV0 F 3 .   ? 134.049 140.317 183.895 1.00 67.64  ? 302 AV0 A CCO   1 
HETATM 8778 C  CCQ   . AV0 F 3 .   ? 135.809 139.560 179.337 1.00 69.42  ? 302 AV0 A CCQ   1 
HETATM 8779 C  CCR   . AV0 F 3 .   ? 142.697 136.337 181.054 1.00 68.59  ? 302 AV0 A CCR   1 
HETATM 8780 C  CCS   . AV0 F 3 .   ? 134.683 140.305 181.344 1.00 69.16  ? 302 AV0 A CCS   1 
HETATM 8781 C  CCT   . AV0 F 3 .   ? 141.381 134.439 181.968 1.00 68.55  ? 302 AV0 A CCT   1 
HETATM 8782 C  CCU   . AV0 F 3 .   ? 132.838 140.112 183.000 1.00 69.92  ? 302 AV0 A CCU   1 
HETATM 8783 C  CCV   . AV0 F 3 .   ? 142.480 134.831 181.000 1.00 68.80  ? 302 AV0 A CCV   1 
HETATM 8784 C  CCW   . AV0 F 3 .   ? 133.183 140.428 181.561 1.00 67.89  ? 302 AV0 A CCW   1 
HETATM 8785 P  PG    . AGS G 4 .   ? 135.645 127.094 110.535 1.00 32.67  ? 301 AGS B PG    1 
HETATM 8786 S  S1G   . AGS G 4 .   ? 136.272 127.477 108.737 1.00 49.56  ? 301 AGS B S1G   1 
HETATM 8787 O  O2G   . AGS G 4 .   ? 136.701 127.569 111.572 1.00 30.84  ? 301 AGS B O2G   1 
HETATM 8788 O  O3G   . AGS G 4 .   ? 134.312 127.847 110.792 1.00 29.59  ? 301 AGS B O3G   1 
HETATM 8789 P  PB    . AGS G 4 .   ? 136.421 124.595 111.345 1.00 18.22  ? 301 AGS B PB    1 
HETATM 8790 O  O1B   . AGS G 4 .   ? 137.716 125.275 111.510 1.00 26.43  ? 301 AGS B O1B   1 
HETATM 8791 O  O2B   . AGS G 4 .   ? 136.528 123.370 110.437 1.00 27.96  ? 301 AGS B O2B   1 
HETATM 8792 O  O3B   . AGS G 4 .   ? 135.392 125.561 110.645 1.00 40.27  ? 301 AGS B O3B   1 
HETATM 8793 P  PA    . AGS G 4 .   ? 136.686 123.628 113.954 1.00 16.96  ? 301 AGS B PA    1 
HETATM 8794 O  O1A   . AGS G 4 .   ? 137.872 122.876 113.522 1.00 33.03  ? 301 AGS B O1A   1 
HETATM 8795 O  O2A   . AGS G 4 .   ? 137.017 124.878 114.768 1.00 27.86  ? 301 AGS B O2A   1 
HETATM 8796 O  O3A   . AGS G 4 .   ? 135.809 124.102 112.724 1.00 27.59  ? 301 AGS B O3A   1 
HETATM 8797 O  "O5'" . AGS G 4 .   ? 135.743 122.656 114.767 1.00 26.51  ? 301 AGS B "O5'" 1 
HETATM 8798 C  "C5'" . AGS G 4 .   ? 134.897 121.694 114.108 1.00 22.30  ? 301 AGS B "C5'" 1 
HETATM 8799 C  "C4'" . AGS G 4 .   ? 133.723 121.353 114.990 1.00 21.61  ? 301 AGS B "C4'" 1 
HETATM 8800 O  "O4'" . AGS G 4 .   ? 134.184 121.058 116.328 1.00 37.98  ? 301 AGS B "O4'" 1 
HETATM 8801 C  "C3'" . AGS G 4 .   ? 132.660 122.448 115.120 1.00 18.57  ? 301 AGS B "C3'" 1 
HETATM 8802 O  "O3'" . AGS G 4 .   ? 131.359 121.912 114.910 1.00 28.88  ? 301 AGS B "O3'" 1 
HETATM 8803 C  "C2'" . AGS G 4 .   ? 132.845 122.959 116.552 1.00 14.40  ? 301 AGS B "C2'" 1 
HETATM 8804 O  "O2'" . AGS G 4 .   ? 131.620 123.406 117.119 1.00 33.08  ? 301 AGS B "O2'" 1 
HETATM 8805 C  "C1'" . AGS G 4 .   ? 133.340 121.702 117.257 1.00 26.55  ? 301 AGS B "C1'" 1 
HETATM 8806 N  N9    . AGS G 4 .   ? 134.095 121.953 118.479 1.00 19.88  ? 301 AGS B N9    1 
HETATM 8807 C  C8    . AGS G 4 .   ? 135.267 122.651 118.605 1.00 21.71  ? 301 AGS B C8    1 
HETATM 8808 N  N7    . AGS G 4 .   ? 135.720 122.717 119.833 1.00 28.47  ? 301 AGS B N7    1 
HETATM 8809 C  C5    . AGS G 4 .   ? 134.780 122.011 120.568 1.00 23.13  ? 301 AGS B C5    1 
HETATM 8810 C  C6    . AGS G 4 .   ? 134.678 121.711 121.941 1.00 23.14  ? 301 AGS B C6    1 
HETATM 8811 N  N6    . AGS G 4 .   ? 135.570 122.099 122.854 1.00 28.57  ? 301 AGS B N6    1 
HETATM 8812 N  N1    . AGS G 4 .   ? 133.612 120.984 122.347 1.00 22.74  ? 301 AGS B N1    1 
HETATM 8813 C  C2    . AGS G 4 .   ? 132.715 120.593 121.437 1.00 27.19  ? 301 AGS B C2    1 
HETATM 8814 N  N3    . AGS G 4 .   ? 132.707 120.816 120.121 1.00 25.96  ? 301 AGS B N3    1 
HETATM 8815 C  C4    . AGS G 4 .   ? 133.773 121.535 119.747 1.00 22.38  ? 301 AGS B C4    1 
HETATM 8816 MG MG    . MG  H 5 .   ? 138.339 128.158 112.300 1.00 37.60  ? 302 MG  B MG    1 
HETATM 8817 C  C1    . AV0 I 3 .   ? 136.943 166.883 134.474 1.00 63.36  ? 301 AV0 C C1    1 
HETATM 8818 O  O1    . AV0 I 3 .   ? 138.138 166.218 134.754 1.00 64.29  ? 301 AV0 C O1    1 
HETATM 8819 C  C2    . AV0 I 3 .   ? 136.966 168.246 135.153 1.00 61.86  ? 301 AV0 C C2    1 
HETATM 8820 O  O2    . AV0 I 3 .   ? 136.984 168.119 136.571 1.00 64.28  ? 301 AV0 C O2    1 
HETATM 8821 C  C3    . AV0 I 3 .   ? 135.749 169.031 134.759 1.00 62.03  ? 301 AV0 C C3    1 
HETATM 8822 O  O3    . AV0 I 3 .   ? 135.805 170.320 135.364 1.00 64.48  ? 301 AV0 C O3    1 
HETATM 8823 C  C4    . AV0 I 3 .   ? 135.705 169.134 133.248 1.00 64.28  ? 301 AV0 C C4    1 
HETATM 8824 O  O4    . AV0 I 3 .   ? 134.563 169.910 132.859 1.00 61.73  ? 301 AV0 C O4    1 
HETATM 8825 C  C5    . AV0 I 3 .   ? 135.687 167.744 132.626 1.00 64.08  ? 301 AV0 C C5    1 
HETATM 8826 O  O5    . AV0 I 3 .   ? 136.845 167.015 133.068 1.00 64.12  ? 301 AV0 C O5    1 
HETATM 8827 C  C6    . AV0 I 3 .   ? 135.758 167.772 131.121 1.00 63.96  ? 301 AV0 C C6    1 
HETATM 8828 O  O6    . AV0 I 3 .   ? 134.489 168.060 130.551 1.00 65.04  ? 301 AV0 C O6    1 
HETATM 8829 C  CAA   . AV0 I 3 .   ? 145.278 158.504 143.405 1.00 57.36  ? 301 AV0 C CAA   1 
HETATM 8830 C  CAB   . AV0 I 3 .   ? 133.606 161.761 145.167 1.00 59.95  ? 301 AV0 C CAB   1 
HETATM 8831 O  OAI   . AV0 I 3 .   ? 136.908 173.266 134.543 1.00 69.86  ? 301 AV0 C OAI   1 
HETATM 8832 O  OAJ   . AV0 I 3 .   ? 138.396 164.117 124.089 1.00 63.02  ? 301 AV0 C OAJ   1 
HETATM 8833 O  OAL   . AV0 I 3 .   ? 141.147 161.897 129.647 1.00 63.98  ? 301 AV0 C OAL   1 
HETATM 8834 O  OAN   . AV0 I 3 .   ? 140.344 167.288 129.789 1.00 64.20  ? 301 AV0 C OAN   1 
HETATM 8835 O  OAP   . AV0 I 3 .   ? 139.947 167.018 132.598 1.00 67.92  ? 301 AV0 C OAP   1 
HETATM 8836 O  OAQ   . AV0 I 3 .   ? 136.925 173.747 129.963 1.00 63.21  ? 301 AV0 C OAQ   1 
HETATM 8837 O  OAR   . AV0 I 3 .   ? 142.700 166.086 124.666 1.00 61.24  ? 301 AV0 C OAR   1 
HETATM 8838 O  OAS   . AV0 I 3 .   ? 134.551 172.494 129.025 1.00 67.13  ? 301 AV0 C OAS   1 
HETATM 8839 O  OAT   . AV0 I 3 .   ? 142.339 162.815 126.205 1.00 63.06  ? 301 AV0 C OAT   1 
HETATM 8840 O  OAU   . AV0 I 3 .   ? 133.362 170.534 130.728 1.00 66.75  ? 301 AV0 C OAU   1 
HETATM 8841 O  OAV   . AV0 I 3 .   ? 142.142 166.196 127.580 1.00 64.36  ? 301 AV0 C OAV   1 
HETATM 8842 C  CAW   . AV0 I 3 .   ? 145.558 159.146 142.074 1.00 57.23  ? 301 AV0 C CAW   1 
HETATM 8843 C  CAX   . AV0 I 3 .   ? 133.849 163.111 144.539 1.00 60.05  ? 301 AV0 C CAX   1 
HETATM 8844 C  CAY   . AV0 I 3 .   ? 145.662 160.638 142.133 1.00 62.76  ? 301 AV0 C CAY   1 
HETATM 8845 C  CAZ   . AV0 I 3 .   ? 134.668 163.101 143.272 1.00 63.63  ? 301 AV0 C CAZ   1 
HETATM 8846 C  CBA   . AV0 I 3 .   ? 145.603 161.339 140.803 1.00 62.04  ? 301 AV0 C CBA   1 
HETATM 8847 C  CBB   . AV0 I 3 .   ? 134.357 164.264 142.356 1.00 61.90  ? 301 AV0 C CBB   1 
HETATM 8848 C  CBC   . AV0 I 3 .   ? 144.211 161.532 140.283 1.00 58.25  ? 301 AV0 C CBC   1 
HETATM 8849 C  CBD   . AV0 I 3 .   ? 135.331 164.459 141.222 1.00 63.66  ? 301 AV0 C CBD   1 
HETATM 8850 C  CBE   . AV0 I 3 .   ? 144.066 162.647 139.287 1.00 60.30  ? 301 AV0 C CBE   1 
HETATM 8851 C  CBF   . AV0 I 3 .   ? 135.439 163.292 140.273 1.00 62.94  ? 301 AV0 C CBF   1 
HETATM 8852 C  CBG   . AV0 I 3 .   ? 142.902 162.459 138.360 1.00 60.43  ? 301 AV0 C CBG   1 
HETATM 8853 C  CBH   . AV0 I 3 .   ? 136.851 162.812 140.040 1.00 61.55  ? 301 AV0 C CBH   1 
HETATM 8854 C  CBI   . AV0 I 3 .   ? 142.181 163.720 137.971 1.00 61.34  ? 301 AV0 C CBI   1 
HETATM 8855 C  CBJ   . AV0 I 3 .   ? 137.667 163.697 139.134 1.00 60.57  ? 301 AV0 C CBJ   1 
HETATM 8856 C  CBK   . AV0 I 3 .   ? 141.450 163.602 136.662 1.00 63.31  ? 301 AV0 C CBK   1 
HETATM 8857 C  CBL   . AV0 I 3 .   ? 137.313 163.581 137.673 1.00 62.89  ? 301 AV0 C CBL   1 
HETATM 8858 C  CBM   . AV0 I 3 .   ? 136.199 173.665 133.367 1.00 65.52  ? 301 AV0 C CBM   1 
HETATM 8859 C  CBN   . AV0 I 3 .   ? 139.734 163.797 124.466 1.00 61.49  ? 301 AV0 C CBN   1 
HETATM 8860 C  CBP   . AV0 I 3 .   ? 139.819 162.352 129.438 1.00 61.69  ? 301 AV0 C CBP   1 
HETATM 8861 C  CBQ   . AV0 I 3 .   ? 140.448 164.694 136.398 1.00 62.58  ? 301 AV0 C CBQ   1 
HETATM 8862 C  CBR   . AV0 I 3 .   ? 138.456 163.149 136.782 1.00 64.03  ? 301 AV0 C CBR   1 
HETATM 8863 C  CBS   . AV0 I 3 .   ? 138.086 165.406 135.937 1.00 61.06  ? 301 AV0 C CBS   1 
HETATM 8864 C  CBT   . AV0 I 3 .   ? 139.165 163.715 134.446 1.00 62.56  ? 301 AV0 C CBT   1 
HETATM 8865 O  OBV   . AV0 I 3 .   ? 140.110 164.427 133.626 1.00 62.94  ? 301 AV0 C OBV   1 
HETATM 8866 O  OBX   . AV0 I 3 .   ? 140.052 163.538 131.505 1.00 65.38  ? 301 AV0 C OBX   1 
HETATM 8867 O  OBY   . AV0 I 3 .   ? 136.221 171.474 132.445 1.00 66.63  ? 301 AV0 C OBY   1 
HETATM 8868 O  OBZ   . AV0 I 3 .   ? 139.969 165.575 126.005 1.00 63.65  ? 301 AV0 C OBZ   1 
HETATM 8869 O  OCB   . AV0 I 3 .   ? 139.492 165.073 128.225 1.00 67.34  ? 301 AV0 C OCB   1 
HETATM 8870 C  CCC   . AV0 I 3 .   ? 136.594 172.836 132.165 1.00 66.00  ? 301 AV0 C CCC   1 
HETATM 8871 C  CCD   . AV0 I 3 .   ? 140.511 165.053 124.792 1.00 63.87  ? 301 AV0 C CCD   1 
HETATM 8872 C  CCF   . AV0 I 3 .   ? 139.520 163.642 130.170 1.00 63.99  ? 301 AV0 C CCF   1 
HETATM 8873 C  CCH   . AV0 I 3 .   ? 139.764 166.119 130.353 1.00 61.71  ? 301 AV0 C CCH   1 
HETATM 8874 C  CCJ   . AV0 I 3 .   ? 139.666 164.630 132.315 1.00 62.13  ? 301 AV0 C CCJ   1 
HETATM 8875 C  CCL   . AV0 I 3 .   ? 140.266 165.912 131.761 1.00 63.30  ? 301 AV0 C CCL   1 
HETATM 8876 C  CCM   . AV0 I 3 .   ? 139.068 164.240 135.878 1.00 62.47  ? 301 AV0 C CCM   1 
HETATM 8877 C  CCN   . AV0 I 3 .   ? 135.928 173.280 130.868 1.00 65.60  ? 301 AV0 C CCN   1 
HETATM 8878 C  CCO   . AV0 I 3 .   ? 142.034 164.852 124.905 1.00 62.96  ? 301 AV0 C CCO   1 
HETATM 8879 C  CCQ   . AV0 I 3 .   ? 140.086 164.893 129.515 1.00 62.18  ? 301 AV0 C CCQ   1 
HETATM 8880 C  CCR   . AV0 I 3 .   ? 134.810 171.259 132.543 1.00 64.72  ? 301 AV0 C CCR   1 
HETATM 8881 C  CCS   . AV0 I 3 .   ? 140.268 164.749 127.100 1.00 63.61  ? 301 AV0 C CCS   1 
HETATM 8882 C  CCT   . AV0 I 3 .   ? 135.163 172.117 130.258 1.00 65.68  ? 301 AV0 C CCT   1 
HETATM 8883 C  CCU   . AV0 I 3 .   ? 142.487 164.234 126.223 1.00 63.13  ? 301 AV0 C CCU   1 
HETATM 8884 C  CCV   . AV0 I 3 .   ? 134.119 171.627 131.238 1.00 65.13  ? 301 AV0 C CCV   1 
HETATM 8885 C  CCW   . AV0 I 3 .   ? 141.754 164.834 127.401 1.00 65.15  ? 301 AV0 C CCW   1 
HETATM 8886 P  PG    . AGS J 4 .   ? 142.442 150.965 110.479 1.00 32.67  ? 301 AGS D PG    1 
HETATM 8887 S  S1G   . AGS J 4 .   ? 141.813 150.586 108.681 1.00 49.56  ? 301 AGS D S1G   1 
HETATM 8888 O  O2G   . AGS J 4 .   ? 141.389 150.486 111.516 1.00 30.84  ? 301 AGS D O2G   1 
HETATM 8889 O  O3G   . AGS J 4 .   ? 143.777 150.214 110.732 1.00 29.59  ? 301 AGS D O3G   1 
HETATM 8890 P  PB    . AGS J 4 .   ? 141.664 153.461 111.296 1.00 18.22  ? 301 AGS D PB    1 
HETATM 8891 O  O1B   . AGS J 4 .   ? 140.370 152.779 111.461 1.00 26.43  ? 301 AGS D O1B   1 
HETATM 8892 O  O2B   . AGS J 4 .   ? 141.553 154.688 110.391 1.00 27.96  ? 301 AGS D O2B   1 
HETATM 8893 O  O3B   . AGS J 4 .   ? 142.693 152.499 110.592 1.00 40.27  ? 301 AGS D O3B   1 
HETATM 8894 P  PA    . AGS J 4 .   ? 141.401 154.422 113.907 1.00 16.96  ? 301 AGS D PA    1 
HETATM 8895 O  O1A   . AGS J 4 .   ? 140.213 155.173 113.479 1.00 33.03  ? 301 AGS D O1A   1 
HETATM 8896 O  O2A   . AGS J 4 .   ? 141.073 153.170 114.719 1.00 27.86  ? 301 AGS D O2A   1 
HETATM 8897 O  O3A   . AGS J 4 .   ? 142.277 153.952 112.675 1.00 27.59  ? 301 AGS D O3A   1 
HETATM 8898 O  "O5'" . AGS J 4 .   ? 142.344 155.394 114.721 1.00 26.51  ? 301 AGS D "O5'" 1 
HETATM 8899 C  "C5'" . AGS J 4 .   ? 143.187 156.358 114.063 1.00 22.30  ? 301 AGS D "C5'" 1 
HETATM 8900 C  "C4'" . AGS J 4 .   ? 144.362 156.699 114.944 1.00 21.61  ? 301 AGS D "C4'" 1 
HETATM 8901 O  "O4'" . AGS J 4 .   ? 143.903 156.990 116.284 1.00 37.98  ? 301 AGS D "O4'" 1 
HETATM 8902 C  "C3'" . AGS J 4 .   ? 145.427 155.606 115.070 1.00 18.57  ? 301 AGS D "C3'" 1 
HETATM 8903 O  "O3'" . AGS J 4 .   ? 146.727 156.144 114.859 1.00 28.88  ? 301 AGS D "O3'" 1 
HETATM 8904 C  "C2'" . AGS J 4 .   ? 145.245 155.091 116.501 1.00 14.40  ? 301 AGS D "C2'" 1 
HETATM 8905 O  "O2'" . AGS J 4 .   ? 146.471 154.645 117.065 1.00 33.08  ? 301 AGS D "O2'" 1 
HETATM 8906 C  "C1'" . AGS J 4 .   ? 144.749 156.346 117.210 1.00 26.55  ? 301 AGS D "C1'" 1 
HETATM 8907 N  N9    . AGS J 4 .   ? 143.996 156.091 118.432 1.00 19.88  ? 301 AGS D N9    1 
HETATM 8908 C  C8    . AGS J 4 .   ? 142.825 155.391 118.558 1.00 21.71  ? 301 AGS D C8    1 
HETATM 8909 N  N7    . AGS J 4 .   ? 142.374 155.321 119.787 1.00 28.47  ? 301 AGS D N7    1 
HETATM 8910 C  C5    . AGS J 4 .   ? 143.314 156.027 120.522 1.00 23.13  ? 301 AGS D C5    1 
HETATM 8911 C  C6    . AGS J 4 .   ? 143.418 156.324 121.896 1.00 23.14  ? 301 AGS D C6    1 
HETATM 8912 N  N6    . AGS J 4 .   ? 142.528 155.932 122.809 1.00 28.57  ? 301 AGS D N6    1 
HETATM 8913 N  N1    . AGS J 4 .   ? 144.483 157.052 122.302 1.00 22.74  ? 301 AGS D N1    1 
HETATM 8914 C  C2    . AGS J 4 .   ? 145.378 157.446 121.391 1.00 27.19  ? 301 AGS D C2    1 
HETATM 8915 N  N3    . AGS J 4 .   ? 145.385 157.226 120.075 1.00 25.96  ? 301 AGS D N3    1 
HETATM 8916 C  C4    . AGS J 4 .   ? 144.319 156.506 119.701 1.00 22.38  ? 301 AGS D C4    1 
HETATM 8917 MG MG    . MG  K 5 .   ? 139.753 149.893 112.245 1.00 37.60  ? 302 MG  D MG    1 
HETATM 8918 O  O     . HOH L 6 .   ? 137.536 127.224 114.976 1.00 50.00  ? 401 HOH B O     1 
HETATM 8919 O  O     . HOH L 6 .   ? 139.891 127.332 109.972 1.00 50.00  ? 402 HOH B O     1 
HETATM 8920 O  O     . HOH L 6 .   ? 134.738 131.315 108.245 1.00 45.03  ? 403 HOH B O     1 
HETATM 8921 O  O     . HOH L 6 .   ? 140.140 130.244 112.477 1.00 50.00  ? 404 HOH B O     1 
HETATM 8922 O  O     . HOH M 6 .   ? 140.558 150.822 114.922 1.00 50.00  ? 401 HOH D O     1 
HETATM 8923 O  O     . HOH M 6 .   ? 138.196 150.722 109.922 1.00 50.00  ? 402 HOH D O     1 
HETATM 8924 O  O     . HOH M 6 .   ? 143.352 146.751 108.178 1.00 45.03  ? 403 HOH D O     1 
HETATM 8925 O  O     . HOH M 6 .   ? 137.955 147.804 112.420 1.00 50.00  ? 404 HOH D O     1 
# 
