data_9OB5
# 
_entry.id   9OB5 
# 
_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   9OB5         pdb_00009ob5 10.2210/pdb9ob5/pdb 
WWPDB D_1000295128 ?            ?                   
# 
_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       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9OB5 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mholliday@relaytx.com MICHAEL HOLLIDAY ? 'principal investigator/group leader' 0000-0002-1112-9892 
3 jpbaird@alumni.iu.edu Jason   Baird    ? 'principal investigator/group leader' 0009-0006-0823-7565 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Baird, J.'      1 0000-0002-1112-9892 
'Holliday, M.H.' 2 0009-0006-0823-7565 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Nanoscale direct-to-biology optimization of Cdk2 inhibitors' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Douthwaite, J.L.' 1  ? 
primary 'Houde, D.J.'      2  ? 
primary 'Pardo, E.'        3  ? 
primary 'Moran, M.S.'      4  ? 
primary 'Baird, J.'        5  ? 
primary 'Meyer, S.R.'      6  ? 
primary 'Mahjour, B.'      7  ? 
primary 'Zhao, Q.'         8  ? 
primary 'Larrow, J.F.'     9  ? 
primary 'Juang, Y.'        10 ? 
primary 'Han, C.K.'        11 ? 
primary 'Kelley, B.'       12 ? 
primary 'Dunstan, D.R.'    13 ? 
primary 'Holliday, M.J.'   14 ? 
primary 'Billings, K.J.'   15 ? 
primary 'Mader, M.M.'      16 ? 
primary 'Taylor, A.M.'     17 ? 
primary 'Sexton, J.Z.'     18 ? 
primary 'Boezio, A.A.'     19 ? 
primary 'Cernak, T.'       20 ? 
# 
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 'Cyclin-dependent kinase 2'                                                                             
34412.895 1  2.7.11.22 ? ? ? 
2 polymer     man 'G1/S-specific cyclin-E1'                                                                               
33053.500 1  ?         ? ? ? 
3 non-polymer syn '(1R,3R)-3-{3-[3-(pyridin-3-yl)propanamido]-1H-pyrazol-5-yl}cyclopentyl (1-methylcyclopropyl)carbamate' 397.471 
1  ?         ? ? ? 
4 water       nat water                                                                                                   18.015 
37 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cell division protein kinase 2,p33 protein kinase' 
# 
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 yes 
;SHMMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY
LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR
TY(TPO)HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSM
PDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
;SHMMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY
LVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVR
TYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK
PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
A ? 
2 'polypeptide(L)' no no  
;GSIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFF
DRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVY
MQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVP
FAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
;GSIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFF
DRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVY
MQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVP
FAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 '(1R,3R)-3-{3-[3-(pyridin-3-yl)propanamido]-1H-pyrazol-5-yl}cyclopentyl (1-methylcyclopropyl)carbamate' A1CAG 
4 water                                                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   HIS n 
1 3   MET n 
1 4   MET n 
1 5   GLU n 
1 6   ASN n 
1 7   PHE n 
1 8   GLN n 
1 9   LYS n 
1 10  VAL n 
1 11  GLU n 
1 12  LYS n 
1 13  ILE n 
1 14  GLY n 
1 15  GLU n 
1 16  GLY n 
1 17  THR n 
1 18  TYR n 
1 19  GLY n 
1 20  VAL n 
1 21  VAL n 
1 22  TYR n 
1 23  LYS n 
1 24  ALA n 
1 25  ARG n 
1 26  ASN n 
1 27  LYS n 
1 28  LEU n 
1 29  THR n 
1 30  GLY n 
1 31  GLU n 
1 32  VAL n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  LYS n 
1 37  LYS n 
1 38  ILE n 
1 39  ARG n 
1 40  LEU n 
1 41  ASP n 
1 42  THR n 
1 43  GLU n 
1 44  THR n 
1 45  GLU n 
1 46  GLY n 
1 47  VAL n 
1 48  PRO n 
1 49  SER n 
1 50  THR n 
1 51  ALA n 
1 52  ILE n 
1 53  ARG n 
1 54  GLU n 
1 55  ILE n 
1 56  SER n 
1 57  LEU n 
1 58  LEU n 
1 59  LYS n 
1 60  GLU n 
1 61  LEU n 
1 62  ASN n 
1 63  HIS n 
1 64  PRO n 
1 65  ASN n 
1 66  ILE n 
1 67  VAL n 
1 68  LYS n 
1 69  LEU n 
1 70  LEU n 
1 71  ASP n 
1 72  VAL n 
1 73  ILE n 
1 74  HIS n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  LEU n 
1 80  TYR n 
1 81  LEU n 
1 82  VAL n 
1 83  PHE n 
1 84  GLU n 
1 85  PHE n 
1 86  LEU n 
1 87  HIS n 
1 88  GLN n 
1 89  ASP n 
1 90  LEU n 
1 91  LYS n 
1 92  LYS n 
1 93  PHE n 
1 94  MET n 
1 95  ASP n 
1 96  ALA n 
1 97  SER n 
1 98  ALA n 
1 99  LEU n 
1 100 THR n 
1 101 GLY n 
1 102 ILE n 
1 103 PRO n 
1 104 LEU n 
1 105 PRO n 
1 106 LEU n 
1 107 ILE n 
1 108 LYS n 
1 109 SER n 
1 110 TYR n 
1 111 LEU n 
1 112 PHE n 
1 113 GLN n 
1 114 LEU n 
1 115 LEU n 
1 116 GLN n 
1 117 GLY n 
1 118 LEU n 
1 119 ALA n 
1 120 PHE n 
1 121 CYS n 
1 122 HIS n 
1 123 SER n 
1 124 HIS n 
1 125 ARG n 
1 126 VAL n 
1 127 LEU n 
1 128 HIS n 
1 129 ARG n 
1 130 ASP n 
1 131 LEU n 
1 132 LYS n 
1 133 PRO n 
1 134 GLN n 
1 135 ASN n 
1 136 LEU n 
1 137 LEU n 
1 138 ILE n 
1 139 ASN n 
1 140 THR n 
1 141 GLU n 
1 142 GLY n 
1 143 ALA n 
1 144 ILE n 
1 145 LYS n 
1 146 LEU n 
1 147 ALA n 
1 148 ASP n 
1 149 PHE n 
1 150 GLY n 
1 151 LEU n 
1 152 ALA n 
1 153 ARG n 
1 154 ALA n 
1 155 PHE n 
1 156 GLY n 
1 157 VAL n 
1 158 PRO n 
1 159 VAL n 
1 160 ARG n 
1 161 THR n 
1 162 TYR n 
1 163 TPO n 
1 164 HIS n 
1 165 GLU n 
1 166 VAL n 
1 167 VAL n 
1 168 THR n 
1 169 LEU n 
1 170 TRP n 
1 171 TYR n 
1 172 ARG n 
1 173 ALA n 
1 174 PRO n 
1 175 GLU n 
1 176 ILE n 
1 177 LEU n 
1 178 LEU n 
1 179 GLY n 
1 180 CYS n 
1 181 LYS n 
1 182 TYR n 
1 183 TYR n 
1 184 SER n 
1 185 THR n 
1 186 ALA n 
1 187 VAL n 
1 188 ASP n 
1 189 ILE n 
1 190 TRP n 
1 191 SER n 
1 192 LEU n 
1 193 GLY n 
1 194 CYS n 
1 195 ILE n 
1 196 PHE n 
1 197 ALA n 
1 198 GLU n 
1 199 MET n 
1 200 VAL n 
1 201 THR n 
1 202 ARG n 
1 203 ARG n 
1 204 ALA n 
1 205 LEU n 
1 206 PHE n 
1 207 PRO n 
1 208 GLY n 
1 209 ASP n 
1 210 SER n 
1 211 GLU n 
1 212 ILE n 
1 213 ASP n 
1 214 GLN n 
1 215 LEU n 
1 216 PHE n 
1 217 ARG n 
1 218 ILE n 
1 219 PHE n 
1 220 ARG n 
1 221 THR n 
1 222 LEU n 
1 223 GLY n 
1 224 THR n 
1 225 PRO n 
1 226 ASP n 
1 227 GLU n 
1 228 VAL n 
1 229 VAL n 
1 230 TRP n 
1 231 PRO n 
1 232 GLY n 
1 233 VAL n 
1 234 THR n 
1 235 SER n 
1 236 MET n 
1 237 PRO n 
1 238 ASP n 
1 239 TYR n 
1 240 LYS n 
1 241 PRO n 
1 242 SER n 
1 243 PHE n 
1 244 PRO n 
1 245 LYS n 
1 246 TRP n 
1 247 ALA n 
1 248 ARG n 
1 249 GLN n 
1 250 ASP n 
1 251 PHE n 
1 252 SER n 
1 253 LYS n 
1 254 VAL n 
1 255 VAL n 
1 256 PRO n 
1 257 PRO n 
1 258 LEU n 
1 259 ASP n 
1 260 GLU n 
1 261 ASP n 
1 262 GLY n 
1 263 ARG n 
1 264 SER n 
1 265 LEU n 
1 266 LEU n 
1 267 SER n 
1 268 GLN n 
1 269 MET n 
1 270 LEU n 
1 271 HIS n 
1 272 TYR n 
1 273 ASP n 
1 274 PRO n 
1 275 ASN n 
1 276 LYS n 
1 277 ARG n 
1 278 ILE n 
1 279 SER n 
1 280 ALA n 
1 281 LYS n 
1 282 ALA n 
1 283 ALA n 
1 284 LEU n 
1 285 ALA n 
1 286 HIS n 
1 287 PRO n 
1 288 PHE n 
1 289 PHE n 
1 290 GLN n 
1 291 ASP n 
1 292 VAL n 
1 293 THR n 
1 294 LYS n 
1 295 PRO n 
1 296 VAL n 
1 297 PRO n 
1 298 HIS n 
1 299 LEU n 
1 300 ARG n 
1 301 LEU n 
2 1   GLY n 
2 2   SER n 
2 3   ILE n 
2 4   ILE n 
2 5   ALA n 
2 6   PRO n 
2 7   SER n 
2 8   ARG n 
2 9   GLY n 
2 10  SER n 
2 11  PRO n 
2 12  LEU n 
2 13  PRO n 
2 14  VAL n 
2 15  LEU n 
2 16  SER n 
2 17  TRP n 
2 18  ALA n 
2 19  ASN n 
2 20  ARG n 
2 21  GLU n 
2 22  GLU n 
2 23  VAL n 
2 24  TRP n 
2 25  LYS n 
2 26  ILE n 
2 27  MET n 
2 28  LEU n 
2 29  ASN n 
2 30  LYS n 
2 31  GLU n 
2 32  LYS n 
2 33  THR n 
2 34  TYR n 
2 35  LEU n 
2 36  ARG n 
2 37  ASP n 
2 38  GLN n 
2 39  HIS n 
2 40  PHE n 
2 41  LEU n 
2 42  GLU n 
2 43  GLN n 
2 44  HIS n 
2 45  PRO n 
2 46  LEU n 
2 47  LEU n 
2 48  GLN n 
2 49  PRO n 
2 50  LYS n 
2 51  MET n 
2 52  ARG n 
2 53  ALA n 
2 54  ILE n 
2 55  LEU n 
2 56  LEU n 
2 57  ASP n 
2 58  TRP n 
2 59  LEU n 
2 60  MET n 
2 61  GLU n 
2 62  VAL n 
2 63  CYS n 
2 64  GLU n 
2 65  VAL n 
2 66  TYR n 
2 67  LYS n 
2 68  LEU n 
2 69  HIS n 
2 70  ARG n 
2 71  GLU n 
2 72  THR n 
2 73  PHE n 
2 74  TYR n 
2 75  LEU n 
2 76  ALA n 
2 77  GLN n 
2 78  ASP n 
2 79  PHE n 
2 80  PHE n 
2 81  ASP n 
2 82  ARG n 
2 83  TYR n 
2 84  MET n 
2 85  ALA n 
2 86  THR n 
2 87  GLN n 
2 88  GLU n 
2 89  ASN n 
2 90  VAL n 
2 91  VAL n 
2 92  LYS n 
2 93  THR n 
2 94  LEU n 
2 95  LEU n 
2 96  GLN n 
2 97  LEU n 
2 98  ILE n 
2 99  GLY n 
2 100 ILE n 
2 101 SER n 
2 102 SER n 
2 103 LEU n 
2 104 PHE n 
2 105 ILE n 
2 106 ALA n 
2 107 ALA n 
2 108 LYS n 
2 109 LEU n 
2 110 GLU n 
2 111 GLU n 
2 112 ILE n 
2 113 TYR n 
2 114 PRO n 
2 115 PRO n 
2 116 LYS n 
2 117 LEU n 
2 118 HIS n 
2 119 GLN n 
2 120 PHE n 
2 121 ALA n 
2 122 TYR n 
2 123 VAL n 
2 124 THR n 
2 125 ASP n 
2 126 GLY n 
2 127 ALA n 
2 128 CYS n 
2 129 SER n 
2 130 GLY n 
2 131 ASP n 
2 132 GLU n 
2 133 ILE n 
2 134 LEU n 
2 135 THR n 
2 136 MET n 
2 137 GLU n 
2 138 LEU n 
2 139 MET n 
2 140 ILE n 
2 141 MET n 
2 142 LYS n 
2 143 ALA n 
2 144 LEU n 
2 145 LYS n 
2 146 TRP n 
2 147 ARG n 
2 148 LEU n 
2 149 SER n 
2 150 PRO n 
2 151 LEU n 
2 152 THR n 
2 153 ILE n 
2 154 VAL n 
2 155 SER n 
2 156 TRP n 
2 157 LEU n 
2 158 ASN n 
2 159 VAL n 
2 160 TYR n 
2 161 MET n 
2 162 GLN n 
2 163 VAL n 
2 164 ALA n 
2 165 TYR n 
2 166 LEU n 
2 167 ASN n 
2 168 ASP n 
2 169 LEU n 
2 170 HIS n 
2 171 GLU n 
2 172 VAL n 
2 173 LEU n 
2 174 LEU n 
2 175 PRO n 
2 176 GLN n 
2 177 TYR n 
2 178 PRO n 
2 179 GLN n 
2 180 GLN n 
2 181 ILE n 
2 182 PHE n 
2 183 ILE n 
2 184 GLN n 
2 185 ILE n 
2 186 ALA n 
2 187 GLU n 
2 188 LEU n 
2 189 LEU n 
2 190 ASP n 
2 191 LEU n 
2 192 CYS n 
2 193 VAL n 
2 194 LEU n 
2 195 ASP n 
2 196 VAL n 
2 197 ASP n 
2 198 CYS n 
2 199 LEU n 
2 200 GLU n 
2 201 PHE n 
2 202 PRO n 
2 203 TYR n 
2 204 GLY n 
2 205 ILE n 
2 206 LEU n 
2 207 ALA n 
2 208 ALA n 
2 209 SER n 
2 210 ALA n 
2 211 LEU n 
2 212 TYR n 
2 213 HIS n 
2 214 PHE n 
2 215 SER n 
2 216 SER n 
2 217 SER n 
2 218 GLU n 
2 219 LEU n 
2 220 MET n 
2 221 GLN n 
2 222 LYS n 
2 223 VAL n 
2 224 SER n 
2 225 GLY n 
2 226 TYR n 
2 227 GLN n 
2 228 TRP n 
2 229 CYS n 
2 230 ASP n 
2 231 ILE n 
2 232 GLU n 
2 233 ASN n 
2 234 CYS n 
2 235 VAL n 
2 236 LYS n 
2 237 TRP n 
2 238 MET n 
2 239 VAL n 
2 240 PRO n 
2 241 PHE n 
2 242 ALA n 
2 243 MET n 
2 244 VAL n 
2 245 ILE n 
2 246 ARG n 
2 247 GLU n 
2 248 THR n 
2 249 GLY n 
2 250 SER n 
2 251 SER n 
2 252 LYS n 
2 253 LEU n 
2 254 LYS n 
2 255 HIS n 
2 256 PHE n 
2 257 ARG n 
2 258 GLY n 
2 259 VAL n 
2 260 ALA n 
2 261 ASP n 
2 262 GLU n 
2 263 ASP n 
2 264 ALA n 
2 265 HIS n 
2 266 ASN n 
2 267 ILE n 
2 268 GLN n 
2 269 THR n 
2 270 HIS n 
2 271 ARG n 
2 272 ASP n 
2 273 SER n 
2 274 LEU n 
2 275 ASP n 
2 276 LEU n 
2 277 LEU n 
2 278 ASP n 
2 279 LYS n 
2 280 ALA n 
2 281 ARG n 
2 282 ALA n 
2 283 LYS n 
2 284 LYS n 
2 285 ALA 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' 1 301 human ? 'CDK2, CDKN2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 285 human ? 'CCNE1, CCNE' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1CAG non-polymer         . 
'(1R,3R)-3-{3-[3-(pyridin-3-yl)propanamido]-1H-pyrazol-5-yl}cyclopentyl (1-methylcyclopropyl)carbamate' ?                  
'C21 H27 N5 O3'  397.471 
ALA   'L-peptide linking' y ALANINE ?                  'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ?                  'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                  'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                  'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ?                  'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                  'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                  'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ?                  'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ?                  'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ?                  'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                  'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ?                  'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ?                  'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ?                  'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ?                  'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ?                  'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ?                  'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ?                  'C4 H9 N O3'     119.119 
TPO   'L-peptide linking' n PHOSPHOTHREONINE PHOSPHONOTHREONINE 'C4 H10 N O6 P'  199.099 
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   SER 1   -2  ?   ?   ?   A . n 
A 1 2   HIS 2   -1  ?   ?   ?   A . n 
A 1 3   MET 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   GLU 5   2   2   GLU GLU A . n 
A 1 6   ASN 6   3   3   ASN ASN A . n 
A 1 7   PHE 7   4   4   PHE PHE A . n 
A 1 8   GLN 8   5   5   GLN GLN A . n 
A 1 9   LYS 9   6   6   LYS LYS A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  GLU 11  8   8   GLU GLU A . n 
A 1 12  LYS 12  9   9   LYS LYS A . n 
A 1 13  ILE 13  10  10  ILE ILE A . n 
A 1 14  GLY 14  11  11  GLY GLY A . n 
A 1 15  GLU 15  12  12  GLU GLU A . n 
A 1 16  GLY 16  13  13  GLY GLY A . n 
A 1 17  THR 17  14  14  THR THR A . n 
A 1 18  TYR 18  15  15  TYR TYR A . n 
A 1 19  GLY 19  16  16  GLY GLY A . n 
A 1 20  VAL 20  17  17  VAL VAL A . n 
A 1 21  VAL 21  18  18  VAL VAL A . n 
A 1 22  TYR 22  19  19  TYR TYR A . n 
A 1 23  LYS 23  20  20  LYS LYS A . n 
A 1 24  ALA 24  21  21  ALA ALA A . n 
A 1 25  ARG 25  22  22  ARG ARG A . n 
A 1 26  ASN 26  23  23  ASN ASN A . n 
A 1 27  LYS 27  24  24  LYS LYS A . n 
A 1 28  LEU 28  25  25  LEU LEU A . n 
A 1 29  THR 29  26  26  THR THR A . n 
A 1 30  GLY 30  27  27  GLY GLY A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  VAL 33  30  30  VAL VAL A . n 
A 1 34  ALA 34  31  31  ALA ALA A . n 
A 1 35  LEU 35  32  32  LEU LEU A . n 
A 1 36  LYS 36  33  33  LYS LYS A . n 
A 1 37  LYS 37  34  34  LYS LYS A . n 
A 1 38  ILE 38  35  35  ILE ILE A . n 
A 1 39  ARG 39  36  36  ARG ARG A . n 
A 1 40  LEU 40  37  37  LEU LEU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  THR 42  39  39  THR THR A . n 
A 1 43  GLU 43  40  40  GLU GLU A . n 
A 1 44  THR 44  41  41  THR THR A . n 
A 1 45  GLU 45  42  42  GLU GLU A . n 
A 1 46  GLY 46  43  43  GLY GLY A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  PRO 48  45  45  PRO PRO A . n 
A 1 49  SER 49  46  46  SER SER A . n 
A 1 50  THR 50  47  47  THR THR A . n 
A 1 51  ALA 51  48  48  ALA ALA A . n 
A 1 52  ILE 52  49  49  ILE ILE A . n 
A 1 53  ARG 53  50  50  ARG ARG A . n 
A 1 54  GLU 54  51  51  GLU GLU A . n 
A 1 55  ILE 55  52  52  ILE ILE A . n 
A 1 56  SER 56  53  53  SER SER A . n 
A 1 57  LEU 57  54  54  LEU LEU A . n 
A 1 58  LEU 58  55  55  LEU LEU A . n 
A 1 59  LYS 59  56  56  LYS LYS A . n 
A 1 60  GLU 60  57  57  GLU GLU A . n 
A 1 61  LEU 61  58  58  LEU LEU A . n 
A 1 62  ASN 62  59  59  ASN ASN A . n 
A 1 63  HIS 63  60  60  HIS HIS A . n 
A 1 64  PRO 64  61  61  PRO PRO A . n 
A 1 65  ASN 65  62  62  ASN ASN A . n 
A 1 66  ILE 66  63  63  ILE ILE A . n 
A 1 67  VAL 67  64  64  VAL VAL A . n 
A 1 68  LYS 68  65  65  LYS LYS A . n 
A 1 69  LEU 69  66  66  LEU LEU A . n 
A 1 70  LEU 70  67  67  LEU LEU A . n 
A 1 71  ASP 71  68  68  ASP ASP A . n 
A 1 72  VAL 72  69  69  VAL VAL A . n 
A 1 73  ILE 73  70  70  ILE ILE A . n 
A 1 74  HIS 74  71  71  HIS HIS A . n 
A 1 75  THR 75  72  72  THR THR A . n 
A 1 76  GLU 76  73  73  GLU GLU A . n 
A 1 77  ASN 77  74  74  ASN ASN A . n 
A 1 78  LYS 78  75  75  LYS LYS A . n 
A 1 79  LEU 79  76  76  LEU LEU A . n 
A 1 80  TYR 80  77  77  TYR TYR A . n 
A 1 81  LEU 81  78  78  LEU LEU A . n 
A 1 82  VAL 82  79  79  VAL VAL A . n 
A 1 83  PHE 83  80  80  PHE PHE A . n 
A 1 84  GLU 84  81  81  GLU GLU A . n 
A 1 85  PHE 85  82  82  PHE PHE A . n 
A 1 86  LEU 86  83  83  LEU LEU A . n 
A 1 87  HIS 87  84  84  HIS HIS A . n 
A 1 88  GLN 88  85  85  GLN GLN A . n 
A 1 89  ASP 89  86  86  ASP ASP A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  LYS 91  88  88  LYS LYS A . n 
A 1 92  LYS 92  89  89  LYS LYS A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  MET 94  91  91  MET MET A . n 
A 1 95  ASP 95  92  92  ASP ASP A . n 
A 1 96  ALA 96  93  93  ALA ALA A . n 
A 1 97  SER 97  94  94  SER SER A . n 
A 1 98  ALA 98  95  95  ALA ALA A . n 
A 1 99  LEU 99  96  96  LEU LEU A . n 
A 1 100 THR 100 97  97  THR THR A . n 
A 1 101 GLY 101 98  98  GLY GLY A . n 
A 1 102 ILE 102 99  99  ILE ILE A . n 
A 1 103 PRO 103 100 100 PRO PRO A . n 
A 1 104 LEU 104 101 101 LEU LEU A . n 
A 1 105 PRO 105 102 102 PRO PRO A . n 
A 1 106 LEU 106 103 103 LEU LEU A . n 
A 1 107 ILE 107 104 104 ILE ILE A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 SER 109 106 106 SER SER A . n 
A 1 110 TYR 110 107 107 TYR TYR A . n 
A 1 111 LEU 111 108 108 LEU LEU A . n 
A 1 112 PHE 112 109 109 PHE PHE A . n 
A 1 113 GLN 113 110 110 GLN GLN A . n 
A 1 114 LEU 114 111 111 LEU LEU A . n 
A 1 115 LEU 115 112 112 LEU LEU A . n 
A 1 116 GLN 116 113 113 GLN GLN A . n 
A 1 117 GLY 117 114 114 GLY GLY A . n 
A 1 118 LEU 118 115 115 LEU LEU A . n 
A 1 119 ALA 119 116 116 ALA ALA A . n 
A 1 120 PHE 120 117 117 PHE PHE A . n 
A 1 121 CYS 121 118 118 CYS CYS A . n 
A 1 122 HIS 122 119 119 HIS HIS A . n 
A 1 123 SER 123 120 120 SER SER A . n 
A 1 124 HIS 124 121 121 HIS HIS A . n 
A 1 125 ARG 125 122 122 ARG ARG A . n 
A 1 126 VAL 126 123 123 VAL VAL A . n 
A 1 127 LEU 127 124 124 LEU LEU A . n 
A 1 128 HIS 128 125 125 HIS HIS A . n 
A 1 129 ARG 129 126 126 ARG ARG A . n 
A 1 130 ASP 130 127 127 ASP ASP A . n 
A 1 131 LEU 131 128 128 LEU LEU A . n 
A 1 132 LYS 132 129 129 LYS LYS A . n 
A 1 133 PRO 133 130 130 PRO PRO A . n 
A 1 134 GLN 134 131 131 GLN GLN A . n 
A 1 135 ASN 135 132 132 ASN ASN A . n 
A 1 136 LEU 136 133 133 LEU LEU A . n 
A 1 137 LEU 137 134 134 LEU LEU A . n 
A 1 138 ILE 138 135 135 ILE ILE A . n 
A 1 139 ASN 139 136 136 ASN ASN A . n 
A 1 140 THR 140 137 137 THR THR A . n 
A 1 141 GLU 141 138 138 GLU GLU A . n 
A 1 142 GLY 142 139 139 GLY GLY A . n 
A 1 143 ALA 143 140 140 ALA ALA A . n 
A 1 144 ILE 144 141 141 ILE ILE A . n 
A 1 145 LYS 145 142 142 LYS LYS A . n 
A 1 146 LEU 146 143 143 LEU LEU A . n 
A 1 147 ALA 147 144 144 ALA ALA A . n 
A 1 148 ASP 148 145 145 ASP ASP A . n 
A 1 149 PHE 149 146 146 PHE PHE A . n 
A 1 150 GLY 150 147 147 GLY GLY A . n 
A 1 151 LEU 151 148 148 LEU LEU A . n 
A 1 152 ALA 152 149 149 ALA ALA A . n 
A 1 153 ARG 153 150 150 ARG ARG A . n 
A 1 154 ALA 154 151 151 ALA ALA A . n 
A 1 155 PHE 155 152 152 PHE PHE A . n 
A 1 156 GLY 156 153 153 GLY GLY A . n 
A 1 157 VAL 157 154 154 VAL VAL A . n 
A 1 158 PRO 158 155 155 PRO PRO A . n 
A 1 159 VAL 159 156 156 VAL VAL A . n 
A 1 160 ARG 160 157 157 ARG ARG A . n 
A 1 161 THR 161 158 158 THR THR A . n 
A 1 162 TYR 162 159 159 TYR TYR A . n 
A 1 163 TPO 163 160 160 TPO TPO A . n 
A 1 164 HIS 164 161 161 HIS HIS A . n 
A 1 165 GLU 165 162 162 GLU GLU A . n 
A 1 166 VAL 166 163 163 VAL VAL A . n 
A 1 167 VAL 167 164 164 VAL VAL A . n 
A 1 168 THR 168 165 165 THR THR A . n 
A 1 169 LEU 169 166 166 LEU LEU A . n 
A 1 170 TRP 170 167 167 TRP TRP A . n 
A 1 171 TYR 171 168 168 TYR TYR A . n 
A 1 172 ARG 172 169 169 ARG ARG A . n 
A 1 173 ALA 173 170 170 ALA ALA A . n 
A 1 174 PRO 174 171 171 PRO PRO A . n 
A 1 175 GLU 175 172 172 GLU GLU A . n 
A 1 176 ILE 176 173 173 ILE ILE A . n 
A 1 177 LEU 177 174 174 LEU LEU A . n 
A 1 178 LEU 178 175 175 LEU LEU A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 CYS 180 177 177 CYS CYS A . n 
A 1 181 LYS 181 178 178 LYS LYS A . n 
A 1 182 TYR 182 179 179 TYR TYR A . n 
A 1 183 TYR 183 180 180 TYR TYR A . n 
A 1 184 SER 184 181 181 SER SER A . n 
A 1 185 THR 185 182 182 THR THR A . n 
A 1 186 ALA 186 183 183 ALA ALA A . n 
A 1 187 VAL 187 184 184 VAL VAL A . n 
A 1 188 ASP 188 185 185 ASP ASP A . n 
A 1 189 ILE 189 186 186 ILE ILE A . n 
A 1 190 TRP 190 187 187 TRP TRP A . n 
A 1 191 SER 191 188 188 SER SER A . n 
A 1 192 LEU 192 189 189 LEU LEU A . n 
A 1 193 GLY 193 190 190 GLY GLY A . n 
A 1 194 CYS 194 191 191 CYS CYS A . n 
A 1 195 ILE 195 192 192 ILE ILE A . n 
A 1 196 PHE 196 193 193 PHE PHE A . n 
A 1 197 ALA 197 194 194 ALA ALA A . n 
A 1 198 GLU 198 195 195 GLU GLU A . n 
A 1 199 MET 199 196 196 MET MET A . n 
A 1 200 VAL 200 197 197 VAL VAL A . n 
A 1 201 THR 201 198 198 THR THR A . n 
A 1 202 ARG 202 199 199 ARG ARG A . n 
A 1 203 ARG 203 200 200 ARG ARG A . n 
A 1 204 ALA 204 201 201 ALA ALA A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 PHE 206 203 203 PHE PHE A . n 
A 1 207 PRO 207 204 204 PRO PRO A . n 
A 1 208 GLY 208 205 205 GLY GLY A . n 
A 1 209 ASP 209 206 206 ASP ASP A . n 
A 1 210 SER 210 207 207 SER SER A . n 
A 1 211 GLU 211 208 208 GLU GLU A . n 
A 1 212 ILE 212 209 209 ILE ILE A . n 
A 1 213 ASP 213 210 210 ASP ASP A . n 
A 1 214 GLN 214 211 211 GLN GLN A . n 
A 1 215 LEU 215 212 212 LEU LEU A . n 
A 1 216 PHE 216 213 213 PHE PHE A . n 
A 1 217 ARG 217 214 214 ARG ARG A . n 
A 1 218 ILE 218 215 215 ILE ILE A . n 
A 1 219 PHE 219 216 216 PHE PHE A . n 
A 1 220 ARG 220 217 217 ARG ARG A . n 
A 1 221 THR 221 218 218 THR THR A . n 
A 1 222 LEU 222 219 219 LEU LEU A . n 
A 1 223 GLY 223 220 220 GLY GLY A . n 
A 1 224 THR 224 221 221 THR THR A . n 
A 1 225 PRO 225 222 222 PRO PRO A . n 
A 1 226 ASP 226 223 223 ASP ASP A . n 
A 1 227 GLU 227 224 224 GLU GLU A . n 
A 1 228 VAL 228 225 225 VAL VAL A . n 
A 1 229 VAL 229 226 226 VAL VAL A . n 
A 1 230 TRP 230 227 227 TRP TRP A . n 
A 1 231 PRO 231 228 228 PRO PRO A . n 
A 1 232 GLY 232 229 229 GLY GLY A . n 
A 1 233 VAL 233 230 230 VAL VAL A . n 
A 1 234 THR 234 231 231 THR THR A . n 
A 1 235 SER 235 232 232 SER SER A . n 
A 1 236 MET 236 233 233 MET MET A . n 
A 1 237 PRO 237 234 234 PRO PRO A . n 
A 1 238 ASP 238 235 235 ASP ASP A . n 
A 1 239 TYR 239 236 236 TYR TYR A . n 
A 1 240 LYS 240 237 237 LYS LYS A . n 
A 1 241 PRO 241 238 238 PRO PRO A . n 
A 1 242 SER 242 239 239 SER SER A . n 
A 1 243 PHE 243 240 240 PHE PHE A . n 
A 1 244 PRO 244 241 241 PRO PRO A . n 
A 1 245 LYS 245 242 242 LYS LYS A . n 
A 1 246 TRP 246 243 243 TRP TRP A . n 
A 1 247 ALA 247 244 244 ALA ALA A . n 
A 1 248 ARG 248 245 245 ARG ARG A . n 
A 1 249 GLN 249 246 246 GLN GLN A . n 
A 1 250 ASP 250 247 247 ASP ASP A . n 
A 1 251 PHE 251 248 248 PHE PHE A . n 
A 1 252 SER 252 249 249 SER SER A . n 
A 1 253 LYS 253 250 250 LYS LYS A . n 
A 1 254 VAL 254 251 251 VAL VAL A . n 
A 1 255 VAL 255 252 252 VAL VAL A . n 
A 1 256 PRO 256 253 253 PRO PRO A . n 
A 1 257 PRO 257 254 254 PRO PRO A . n 
A 1 258 LEU 258 255 255 LEU LEU A . n 
A 1 259 ASP 259 256 256 ASP ASP A . n 
A 1 260 GLU 260 257 257 GLU GLU A . n 
A 1 261 ASP 261 258 258 ASP ASP A . n 
A 1 262 GLY 262 259 259 GLY GLY A . n 
A 1 263 ARG 263 260 260 ARG ARG A . n 
A 1 264 SER 264 261 261 SER SER A . n 
A 1 265 LEU 265 262 262 LEU LEU A . n 
A 1 266 LEU 266 263 263 LEU LEU A . n 
A 1 267 SER 267 264 264 SER SER A . n 
A 1 268 GLN 268 265 265 GLN GLN A . n 
A 1 269 MET 269 266 266 MET MET A . n 
A 1 270 LEU 270 267 267 LEU LEU A . n 
A 1 271 HIS 271 268 268 HIS HIS A . n 
A 1 272 TYR 272 269 269 TYR TYR A . n 
A 1 273 ASP 273 270 270 ASP ASP A . n 
A 1 274 PRO 274 271 271 PRO PRO A . n 
A 1 275 ASN 275 272 272 ASN ASN A . n 
A 1 276 LYS 276 273 273 LYS LYS A . n 
A 1 277 ARG 277 274 274 ARG ARG A . n 
A 1 278 ILE 278 275 275 ILE ILE A . n 
A 1 279 SER 279 276 276 SER SER A . n 
A 1 280 ALA 280 277 277 ALA ALA A . n 
A 1 281 LYS 281 278 278 LYS LYS A . n 
A 1 282 ALA 282 279 279 ALA ALA A . n 
A 1 283 ALA 283 280 280 ALA ALA A . n 
A 1 284 LEU 284 281 281 LEU LEU A . n 
A 1 285 ALA 285 282 282 ALA ALA A . n 
A 1 286 HIS 286 283 283 HIS HIS A . n 
A 1 287 PRO 287 284 284 PRO PRO A . n 
A 1 288 PHE 288 285 285 PHE PHE A . n 
A 1 289 PHE 289 286 286 PHE PHE A . n 
A 1 290 GLN 290 287 287 GLN GLN A . n 
A 1 291 ASP 291 288 288 ASP ASP A . n 
A 1 292 VAL 292 289 289 VAL VAL A . n 
A 1 293 THR 293 290 290 THR THR A . n 
A 1 294 LYS 294 291 291 LYS LYS A . n 
A 1 295 PRO 295 292 292 PRO PRO A . n 
A 1 296 VAL 296 293 293 VAL VAL A . n 
A 1 297 PRO 297 294 294 PRO PRO A . n 
A 1 298 HIS 298 295 295 HIS HIS A . n 
A 1 299 LEU 299 296 296 LEU LEU A . n 
A 1 300 ARG 300 297 297 ARG ARG A . n 
A 1 301 LEU 301 298 298 LEU LEU A . n 
B 2 1   GLY 1   94  ?   ?   ?   B . n 
B 2 2   SER 2   95  ?   ?   ?   B . n 
B 2 3   ILE 3   96  ?   ?   ?   B . n 
B 2 4   ILE 4   97  ?   ?   ?   B . n 
B 2 5   ALA 5   98  ?   ?   ?   B . n 
B 2 6   PRO 6   99  ?   ?   ?   B . n 
B 2 7   SER 7   100 ?   ?   ?   B . n 
B 2 8   ARG 8   101 ?   ?   ?   B . n 
B 2 9   GLY 9   102 102 GLY GLY B . n 
B 2 10  SER 10  103 103 SER SER B . n 
B 2 11  PRO 11  104 104 PRO PRO B . n 
B 2 12  LEU 12  105 105 LEU LEU B . n 
B 2 13  PRO 13  106 106 PRO PRO B . n 
B 2 14  VAL 14  107 107 VAL VAL B . n 
B 2 15  LEU 15  108 108 LEU LEU B . n 
B 2 16  SER 16  109 109 SER SER B . n 
B 2 17  TRP 17  110 110 TRP TRP B . n 
B 2 18  ALA 18  111 111 ALA ALA B . n 
B 2 19  ASN 19  112 112 ASN ASN B . n 
B 2 20  ARG 20  113 113 ARG ARG B . n 
B 2 21  GLU 21  114 114 GLU GLU B . n 
B 2 22  GLU 22  115 115 GLU GLU B . n 
B 2 23  VAL 23  116 116 VAL VAL B . n 
B 2 24  TRP 24  117 117 TRP TRP B . n 
B 2 25  LYS 25  118 118 LYS LYS B . n 
B 2 26  ILE 26  119 119 ILE ILE B . n 
B 2 27  MET 27  120 120 MET MET B . n 
B 2 28  LEU 28  121 121 LEU LEU B . n 
B 2 29  ASN 29  122 122 ASN ASN B . n 
B 2 30  LYS 30  123 123 LYS LYS B . n 
B 2 31  GLU 31  124 124 GLU GLU B . n 
B 2 32  LYS 32  125 125 LYS LYS B . n 
B 2 33  THR 33  126 126 THR THR B . n 
B 2 34  TYR 34  127 127 TYR TYR B . n 
B 2 35  LEU 35  128 128 LEU LEU B . n 
B 2 36  ARG 36  129 129 ARG ARG B . n 
B 2 37  ASP 37  130 130 ASP ASP B . n 
B 2 38  GLN 38  131 131 GLN GLN B . n 
B 2 39  HIS 39  132 132 HIS HIS B . n 
B 2 40  PHE 40  133 133 PHE PHE B . n 
B 2 41  LEU 41  134 134 LEU LEU B . n 
B 2 42  GLU 42  135 135 GLU GLU B . n 
B 2 43  GLN 43  136 136 GLN GLN B . n 
B 2 44  HIS 44  137 137 HIS HIS B . n 
B 2 45  PRO 45  138 138 PRO PRO B . n 
B 2 46  LEU 46  139 139 LEU LEU B . n 
B 2 47  LEU 47  140 140 LEU LEU B . n 
B 2 48  GLN 48  141 141 GLN GLN B . n 
B 2 49  PRO 49  142 142 PRO PRO B . n 
B 2 50  LYS 50  143 143 LYS LYS B . n 
B 2 51  MET 51  144 144 MET MET B . n 
B 2 52  ARG 52  145 145 ARG ARG B . n 
B 2 53  ALA 53  146 146 ALA ALA B . n 
B 2 54  ILE 54  147 147 ILE ILE B . n 
B 2 55  LEU 55  148 148 LEU LEU B . n 
B 2 56  LEU 56  149 149 LEU LEU B . n 
B 2 57  ASP 57  150 150 ASP ASP B . n 
B 2 58  TRP 58  151 151 TRP TRP B . n 
B 2 59  LEU 59  152 152 LEU LEU B . n 
B 2 60  MET 60  153 153 MET MET B . n 
B 2 61  GLU 61  154 154 GLU GLU B . n 
B 2 62  VAL 62  155 155 VAL VAL B . n 
B 2 63  CYS 63  156 156 CYS CYS B . n 
B 2 64  GLU 64  157 157 GLU GLU B . n 
B 2 65  VAL 65  158 158 VAL VAL B . n 
B 2 66  TYR 66  159 159 TYR TYR B . n 
B 2 67  LYS 67  160 160 LYS LYS B . n 
B 2 68  LEU 68  161 161 LEU LEU B . n 
B 2 69  HIS 69  162 162 HIS HIS B . n 
B 2 70  ARG 70  163 163 ARG ARG B . n 
B 2 71  GLU 71  164 164 GLU GLU B . n 
B 2 72  THR 72  165 165 THR THR B . n 
B 2 73  PHE 73  166 166 PHE PHE B . n 
B 2 74  TYR 74  167 167 TYR TYR B . n 
B 2 75  LEU 75  168 168 LEU LEU B . n 
B 2 76  ALA 76  169 169 ALA ALA B . n 
B 2 77  GLN 77  170 170 GLN GLN B . n 
B 2 78  ASP 78  171 171 ASP ASP B . n 
B 2 79  PHE 79  172 172 PHE PHE B . n 
B 2 80  PHE 80  173 173 PHE PHE B . n 
B 2 81  ASP 81  174 174 ASP ASP B . n 
B 2 82  ARG 82  175 175 ARG ARG B . n 
B 2 83  TYR 83  176 176 TYR TYR B . n 
B 2 84  MET 84  177 177 MET MET B . n 
B 2 85  ALA 85  178 178 ALA ALA B . n 
B 2 86  THR 86  179 179 THR THR B . n 
B 2 87  GLN 87  180 180 GLN GLN B . n 
B 2 88  GLU 88  181 181 GLU GLU B . n 
B 2 89  ASN 89  182 182 ASN ASN B . n 
B 2 90  VAL 90  183 183 VAL VAL B . n 
B 2 91  VAL 91  184 184 VAL VAL B . n 
B 2 92  LYS 92  185 185 LYS LYS B . n 
B 2 93  THR 93  186 186 THR THR B . n 
B 2 94  LEU 94  187 187 LEU LEU B . n 
B 2 95  LEU 95  188 188 LEU LEU B . n 
B 2 96  GLN 96  189 189 GLN GLN B . n 
B 2 97  LEU 97  190 190 LEU LEU B . n 
B 2 98  ILE 98  191 191 ILE ILE B . n 
B 2 99  GLY 99  192 192 GLY GLY B . n 
B 2 100 ILE 100 193 193 ILE ILE B . n 
B 2 101 SER 101 194 194 SER SER B . n 
B 2 102 SER 102 195 195 SER SER B . n 
B 2 103 LEU 103 196 196 LEU LEU B . n 
B 2 104 PHE 104 197 197 PHE PHE B . n 
B 2 105 ILE 105 198 198 ILE ILE B . n 
B 2 106 ALA 106 199 199 ALA ALA B . n 
B 2 107 ALA 107 200 200 ALA ALA B . n 
B 2 108 LYS 108 201 201 LYS LYS B . n 
B 2 109 LEU 109 202 202 LEU LEU B . n 
B 2 110 GLU 110 203 203 GLU GLU B . n 
B 2 111 GLU 111 204 204 GLU GLU B . n 
B 2 112 ILE 112 205 205 ILE ILE B . n 
B 2 113 TYR 113 206 206 TYR TYR B . n 
B 2 114 PRO 114 207 207 PRO PRO B . n 
B 2 115 PRO 115 208 208 PRO PRO B . n 
B 2 116 LYS 116 209 209 LYS LYS B . n 
B 2 117 LEU 117 210 210 LEU LEU B . n 
B 2 118 HIS 118 211 211 HIS HIS B . n 
B 2 119 GLN 119 212 212 GLN GLN B . n 
B 2 120 PHE 120 213 213 PHE PHE B . n 
B 2 121 ALA 121 214 214 ALA ALA B . n 
B 2 122 TYR 122 215 215 TYR TYR B . n 
B 2 123 VAL 123 216 216 VAL VAL B . n 
B 2 124 THR 124 217 217 THR THR B . n 
B 2 125 ASP 125 218 218 ASP ASP B . n 
B 2 126 GLY 126 219 219 GLY GLY B . n 
B 2 127 ALA 127 220 220 ALA ALA B . n 
B 2 128 CYS 128 221 221 CYS CYS B . n 
B 2 129 SER 129 222 222 SER SER B . n 
B 2 130 GLY 130 223 223 GLY GLY B . n 
B 2 131 ASP 131 224 224 ASP ASP B . n 
B 2 132 GLU 132 225 225 GLU GLU B . n 
B 2 133 ILE 133 226 226 ILE ILE B . n 
B 2 134 LEU 134 227 227 LEU LEU B . n 
B 2 135 THR 135 228 228 THR THR B . n 
B 2 136 MET 136 229 229 MET MET B . n 
B 2 137 GLU 137 230 230 GLU GLU B . n 
B 2 138 LEU 138 231 231 LEU LEU B . n 
B 2 139 MET 139 232 232 MET MET B . n 
B 2 140 ILE 140 233 233 ILE ILE B . n 
B 2 141 MET 141 234 234 MET MET B . n 
B 2 142 LYS 142 235 235 LYS LYS B . n 
B 2 143 ALA 143 236 236 ALA ALA B . n 
B 2 144 LEU 144 237 237 LEU LEU B . n 
B 2 145 LYS 145 238 238 LYS LYS B . n 
B 2 146 TRP 146 239 239 TRP TRP B . n 
B 2 147 ARG 147 240 240 ARG ARG B . n 
B 2 148 LEU 148 241 241 LEU LEU B . n 
B 2 149 SER 149 242 242 SER SER B . n 
B 2 150 PRO 150 243 243 PRO PRO B . n 
B 2 151 LEU 151 244 244 LEU LEU B . n 
B 2 152 THR 152 245 245 THR THR B . n 
B 2 153 ILE 153 246 246 ILE ILE B . n 
B 2 154 VAL 154 247 247 VAL VAL B . n 
B 2 155 SER 155 248 248 SER SER B . n 
B 2 156 TRP 156 249 249 TRP TRP B . n 
B 2 157 LEU 157 250 250 LEU LEU B . n 
B 2 158 ASN 158 251 251 ASN ASN B . n 
B 2 159 VAL 159 252 252 VAL VAL B . n 
B 2 160 TYR 160 253 253 TYR TYR B . n 
B 2 161 MET 161 254 254 MET MET B . n 
B 2 162 GLN 162 255 255 GLN GLN B . n 
B 2 163 VAL 163 256 256 VAL VAL B . n 
B 2 164 ALA 164 257 257 ALA ALA B . n 
B 2 165 TYR 165 258 258 TYR TYR B . n 
B 2 166 LEU 166 259 259 LEU LEU B . n 
B 2 167 ASN 167 260 260 ASN ASN B . n 
B 2 168 ASP 168 261 261 ASP ASP B . n 
B 2 169 LEU 169 262 262 LEU LEU B . n 
B 2 170 HIS 170 263 263 HIS HIS B . n 
B 2 171 GLU 171 264 264 GLU GLU B . n 
B 2 172 VAL 172 265 265 VAL VAL B . n 
B 2 173 LEU 173 266 266 LEU LEU B . n 
B 2 174 LEU 174 267 267 LEU LEU B . n 
B 2 175 PRO 175 268 268 PRO PRO B . n 
B 2 176 GLN 176 269 269 GLN GLN B . n 
B 2 177 TYR 177 270 270 TYR TYR B . n 
B 2 178 PRO 178 271 271 PRO PRO B . n 
B 2 179 GLN 179 272 272 GLN GLN B . n 
B 2 180 GLN 180 273 273 GLN GLN B . n 
B 2 181 ILE 181 274 274 ILE ILE B . n 
B 2 182 PHE 182 275 275 PHE PHE B . n 
B 2 183 ILE 183 276 276 ILE ILE B . n 
B 2 184 GLN 184 277 277 GLN GLN B . n 
B 2 185 ILE 185 278 278 ILE ILE B . n 
B 2 186 ALA 186 279 279 ALA ALA B . n 
B 2 187 GLU 187 280 280 GLU GLU B . n 
B 2 188 LEU 188 281 281 LEU LEU B . n 
B 2 189 LEU 189 282 282 LEU LEU B . n 
B 2 190 ASP 190 283 283 ASP ASP B . n 
B 2 191 LEU 191 284 284 LEU LEU B . n 
B 2 192 CYS 192 285 285 CYS CYS B . n 
B 2 193 VAL 193 286 286 VAL VAL B . n 
B 2 194 LEU 194 287 287 LEU LEU B . n 
B 2 195 ASP 195 288 288 ASP ASP B . n 
B 2 196 VAL 196 289 289 VAL VAL B . n 
B 2 197 ASP 197 290 290 ASP ASP B . n 
B 2 198 CYS 198 291 291 CYS CYS B . n 
B 2 199 LEU 199 292 292 LEU LEU B . n 
B 2 200 GLU 200 293 293 GLU GLU B . n 
B 2 201 PHE 201 294 294 PHE PHE B . n 
B 2 202 PRO 202 295 295 PRO PRO B . n 
B 2 203 TYR 203 296 296 TYR TYR B . n 
B 2 204 GLY 204 297 297 GLY GLY B . n 
B 2 205 ILE 205 298 298 ILE ILE B . n 
B 2 206 LEU 206 299 299 LEU LEU B . n 
B 2 207 ALA 207 300 300 ALA ALA B . n 
B 2 208 ALA 208 301 301 ALA ALA B . n 
B 2 209 SER 209 302 302 SER SER B . n 
B 2 210 ALA 210 303 303 ALA ALA B . n 
B 2 211 LEU 211 304 304 LEU LEU B . n 
B 2 212 TYR 212 305 305 TYR TYR B . n 
B 2 213 HIS 213 306 306 HIS HIS B . n 
B 2 214 PHE 214 307 307 PHE PHE B . n 
B 2 215 SER 215 308 308 SER SER B . n 
B 2 216 SER 216 309 309 SER SER B . n 
B 2 217 SER 217 310 310 SER SER B . n 
B 2 218 GLU 218 311 311 GLU GLU B . n 
B 2 219 LEU 219 312 312 LEU LEU B . n 
B 2 220 MET 220 313 313 MET MET B . n 
B 2 221 GLN 221 314 314 GLN GLN B . n 
B 2 222 LYS 222 315 315 LYS LYS B . n 
B 2 223 VAL 223 316 316 VAL VAL B . n 
B 2 224 SER 224 317 317 SER SER B . n 
B 2 225 GLY 225 318 318 GLY GLY B . n 
B 2 226 TYR 226 319 319 TYR TYR B . n 
B 2 227 GLN 227 320 320 GLN GLN B . n 
B 2 228 TRP 228 321 321 TRP TRP B . n 
B 2 229 CYS 229 322 322 CYS CYS B . n 
B 2 230 ASP 230 323 323 ASP ASP B . n 
B 2 231 ILE 231 324 324 ILE ILE B . n 
B 2 232 GLU 232 325 325 GLU GLU B . n 
B 2 233 ASN 233 326 326 ASN ASN B . n 
B 2 234 CYS 234 327 327 CYS CYS B . n 
B 2 235 VAL 235 328 328 VAL VAL B . n 
B 2 236 LYS 236 329 329 LYS LYS B . n 
B 2 237 TRP 237 330 330 TRP TRP B . n 
B 2 238 MET 238 331 331 MET MET B . n 
B 2 239 VAL 239 332 332 VAL VAL B . n 
B 2 240 PRO 240 333 333 PRO PRO B . n 
B 2 241 PHE 241 334 334 PHE PHE B . n 
B 2 242 ALA 242 335 335 ALA ALA B . n 
B 2 243 MET 243 336 336 MET MET B . n 
B 2 244 VAL 244 337 337 VAL VAL B . n 
B 2 245 ILE 245 338 338 ILE ILE B . n 
B 2 246 ARG 246 339 339 ARG ARG B . n 
B 2 247 GLU 247 340 340 GLU GLU B . n 
B 2 248 THR 248 341 341 THR THR B . n 
B 2 249 GLY 249 342 342 GLY GLY B . n 
B 2 250 SER 250 343 343 SER SER B . n 
B 2 251 SER 251 344 344 SER SER B . n 
B 2 252 LYS 252 345 345 LYS LYS B . n 
B 2 253 LEU 253 346 346 LEU LEU B . n 
B 2 254 LYS 254 347 347 LYS LYS B . n 
B 2 255 HIS 255 348 348 HIS HIS B . n 
B 2 256 PHE 256 349 349 PHE PHE B . n 
B 2 257 ARG 257 350 350 ARG ARG B . n 
B 2 258 GLY 258 351 351 GLY GLY B . n 
B 2 259 VAL 259 352 352 VAL VAL B . n 
B 2 260 ALA 260 353 353 ALA ALA B . n 
B 2 261 ASP 261 354 354 ASP ASP B . n 
B 2 262 GLU 262 355 355 GLU GLU B . n 
B 2 263 ASP 263 356 356 ASP ASP B . n 
B 2 264 ALA 264 357 357 ALA ALA B . n 
B 2 265 HIS 265 358 358 HIS HIS B . n 
B 2 266 ASN 266 359 359 ASN ASN B . n 
B 2 267 ILE 267 360 360 ILE ILE B . n 
B 2 268 GLN 268 361 361 GLN GLN B . n 
B 2 269 THR 269 362 362 THR THR B . n 
B 2 270 HIS 270 363 363 HIS HIS B . n 
B 2 271 ARG 271 364 364 ARG ARG B . n 
B 2 272 ASP 272 365 365 ASP ASP B . n 
B 2 273 SER 273 366 366 SER SER B . n 
B 2 274 LEU 274 367 367 LEU LEU B . n 
B 2 275 ASP 275 368 368 ASP ASP B . n 
B 2 276 LEU 276 369 369 LEU LEU B . n 
B 2 277 LEU 277 370 370 LEU LEU B . n 
B 2 278 ASP 278 371 371 ASP ASP B . n 
B 2 279 LYS 279 372 372 LYS LYS B . n 
B 2 280 ALA 280 373 373 ALA ALA B . n 
B 2 281 ARG 281 374 374 ARG ARG B . n 
B 2 282 ALA 282 375 375 ALA ALA B . n 
B 2 283 LYS 283 376 ?   ?   ?   B . n 
B 2 284 LYS 284 377 ?   ?   ?   B . n 
B 2 285 ALA 285 378 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1CAG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1CAG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 A1CAG 1  301 1  A1CAG LI1 A . 
D 4 HOH   1  401 28 HOH   HOH A . 
D 4 HOH   2  402 2  HOH   HOH A . 
D 4 HOH   3  403 35 HOH   HOH A . 
D 4 HOH   4  404 9  HOH   HOH A . 
D 4 HOH   5  405 26 HOH   HOH A . 
D 4 HOH   6  406 22 HOH   HOH A . 
D 4 HOH   7  407 37 HOH   HOH A . 
D 4 HOH   8  408 21 HOH   HOH A . 
D 4 HOH   9  409 19 HOH   HOH A . 
D 4 HOH   10 410 10 HOH   HOH A . 
D 4 HOH   11 411 34 HOH   HOH A . 
D 4 HOH   12 412 20 HOH   HOH A . 
D 4 HOH   13 413 8  HOH   HOH A . 
D 4 HOH   14 414 25 HOH   HOH A . 
D 4 HOH   15 415 17 HOH   HOH A . 
D 4 HOH   16 416 24 HOH   HOH A . 
D 4 HOH   17 417 5  HOH   HOH A . 
D 4 HOH   18 418 6  HOH   HOH A . 
D 4 HOH   19 419 13 HOH   HOH A . 
D 4 HOH   20 420 36 HOH   HOH A . 
D 4 HOH   21 421 7  HOH   HOH A . 
D 4 HOH   22 422 32 HOH   HOH A . 
D 4 HOH   23 423 1  HOH   HOH A . 
D 4 HOH   24 424 16 HOH   HOH A . 
D 4 HOH   25 425 33 HOH   HOH A . 
D 4 HOH   26 426 14 HOH   HOH A . 
D 4 HOH   27 427 4  HOH   HOH A . 
D 4 HOH   28 428 18 HOH   HOH A . 
D 4 HOH   29 429 31 HOH   HOH A . 
D 4 HOH   30 430 3  HOH   HOH A . 
D 4 HOH   31 431 29 HOH   HOH A . 
D 4 HOH   32 432 27 HOH   HOH A . 
D 4 HOH   33 433 30 HOH   HOH A . 
D 4 HOH   34 434 11 HOH   HOH A . 
E 4 HOH   1  401 23 HOH   HOH B . 
E 4 HOH   2  402 15 HOH   HOH B . 
E 4 HOH   3  403 12 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.2_5419 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           ? 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OB5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.570 
_cell.length_a_esd                 ? 
_cell.length_b                     101.570 
_cell.length_b_esd                 ? 
_cell.length_c                     151.480 
_cell.length_c_esd                 ? 
_cell.volume                       1562738.103 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9OB5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            'P 4abw 2nw' 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_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                   9OB5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.90 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.52 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.115 M Sodium Citrate, 15% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-08-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.11582 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.11582 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          59.38 
_reflns.entry_id                                       9OB5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               151.48 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     46754 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.082 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.1 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3747 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               27.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.362 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               85.29 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9OB5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             84.36 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     46635 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  44636 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.36 
_refine.ls_percent_reflns_R_free                 4.29 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2339 
_refine.ls_R_factor_R_free                       0.2548 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2329 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 34.1672 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3917 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        84.36 
_refine_hist.number_atoms_solvent             37 
_refine_hist.number_atoms_total               4710 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4644 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0015  ? 4843 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.4153  ? 6578 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0373  ? 735  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0037  ? 826  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 12.4352 ? 1786 ? f_dihedral_angle_d ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.15  . . 138 3101 98.69  . . . . 0.4494 . . . . . . . . . . . . . . . 0.4407 
'X-RAY DIFFRACTION' 2.15 2.21  . . 138 3088 98.17  . . . . 0.4328 . . . . . . . . . . . . . . . 0.4961 
'X-RAY DIFFRACTION' 2.21 2.28  . . 140 3114 98.70  . . . . 0.4915 . . . . . . . . . . . . . . . 0.5228 
'X-RAY DIFFRACTION' 2.28 2.35  . . 140 3129 99.00  . . . . 0.3732 . . . . . . . . . . . . . . . 0.4199 
'X-RAY DIFFRACTION' 2.35 2.43  . . 141 3160 99.19  . . . . 0.3583 . . . . . . . . . . . . . . . 0.3705 
'X-RAY DIFFRACTION' 2.43 2.53  . . 141 3127 99.21  . . . . 0.3068 . . . . . . . . . . . . . . . 0.3479 
'X-RAY DIFFRACTION' 2.53 2.65  . . 141 3162 99.49  . . . . 0.2694 . . . . . . . . . . . . . . . 0.3284 
'X-RAY DIFFRACTION' 2.65 2.79  . . 142 3152 99.52  . . . . 0.2698 . . . . . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 2.79 2.96  . . 142 3189 99.58  . . . . 0.2775 . . . . . . . . . . . . . . . 0.2901 
'X-RAY DIFFRACTION' 2.96 3.19  . . 144 3202 99.70  . . . . 0.2750 . . . . . . . . . . . . . . . 0.3398 
'X-RAY DIFFRACTION' 3.19 3.51  . . 145 3221 99.82  . . . . 0.2476 . . . . . . . . . . . . . . . 0.2972 
'X-RAY DIFFRACTION' 3.51 4.02  . . 145 3238 100.00 . . . . 0.2216 . . . . . . . . . . . . . . . 0.2331 
'X-RAY DIFFRACTION' 4.02 5.06  . . 147 3293 100.00 . . . . 0.1804 . . . . . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 5.06 84.36 . . 155 3460 99.92  . . . . 0.1941 . . . . . . . . . . . . . . . 0.1924 
# 
_struct.entry_id                     9OB5 
_struct.title                        'CDK2/CyclinE bound to compound 20 with P-loop in the EE and CC conformations' 
_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        9OB5 
_struct_keywords.text            'CDK/Cyclin, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
# 
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 CDK2_HUMAN  P24941 ? 1 
;MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
1  
2 UNP CCNE1_HUMAN P24864 ? 2 
;IIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDR
YMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQ
VAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFA
MVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKA
;
96 
# 
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 9OB5 A 4 ? 301 ? P24941 1  ? 298 ? 1  298 
2 2 9OB5 B 3 ? 285 ? P24864 96 ? 378 ? 96 378 
# 
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 9OB5 SER A 1 ? UNP P24941 ? ? 'expression tag' -2 1 
1 9OB5 HIS A 2 ? UNP P24941 ? ? 'expression tag' -1 2 
1 9OB5 MET A 3 ? UNP P24941 ? ? 'expression tag' 0  3 
2 9OB5 GLY B 1 ? UNP P24864 ? ? 'expression tag' 94 4 
2 9OB5 SER B 2 ? UNP P24864 ? ? 'expression tag' 95 5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4430  ? 
1 MORE         -20   ? 
1 'SSA (A^2)'  25090 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 41  ? GLU A 43  ? ASP A 38  GLU A 40  5 ? 3  
HELX_P HELX_P2  AA2 PRO A 48  ? LYS A 59  ? PRO A 45  LYS A 56  1 ? 12 
HELX_P HELX_P3  AA3 LEU A 90  ? SER A 97  ? LEU A 87  SER A 94  1 ? 8  
HELX_P HELX_P4  AA4 PRO A 103 ? HIS A 124 ? PRO A 100 HIS A 121 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 132 ? GLN A 134 ? LYS A 129 GLN A 131 5 ? 3  
HELX_P HELX_P6  AA6 THR A 168 ? ARG A 172 ? THR A 165 ARG A 169 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 173 ? LEU A 178 ? ALA A 170 LEU A 175 1 ? 6  
HELX_P HELX_P8  AA8 THR A 185 ? ARG A 202 ? THR A 182 ARG A 199 1 ? 18 
HELX_P HELX_P9  AA9 SER A 210 ? GLY A 223 ? SER A 207 GLY A 220 1 ? 14 
HELX_P HELX_P10 AB1 GLY A 232 ? MET A 236 ? GLY A 229 MET A 233 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 250 ? VAL A 255 ? ASP A 247 VAL A 252 1 ? 6  
HELX_P HELX_P12 AB3 ASP A 259 ? LEU A 270 ? ASP A 256 LEU A 267 1 ? 12 
HELX_P HELX_P13 AB4 SER A 279 ? ALA A 285 ? SER A 276 ALA A 282 1 ? 7  
HELX_P HELX_P14 AB5 HIS A 286 ? GLN A 290 ? HIS A 283 GLN A 287 5 ? 5  
HELX_P HELX_P15 AB6 ASN B 19  ? TYR B 34  ? ASN B 112 TYR B 127 1 ? 16 
HELX_P HELX_P16 AB7 HIS B 39  ? HIS B 44  ? HIS B 132 HIS B 137 5 ? 6  
HELX_P HELX_P17 AB8 GLN B 48  ? TYR B 66  ? GLN B 141 TYR B 159 1 ? 19 
HELX_P HELX_P18 AB9 HIS B 69  ? ALA B 85  ? HIS B 162 ALA B 178 1 ? 17 
HELX_P HELX_P19 AC1 LEU B 94  ? GLU B 111 ? LEU B 187 GLU B 204 1 ? 18 
HELX_P HELX_P20 AC2 LYS B 116 ? VAL B 123 ? LYS B 209 VAL B 216 1 ? 8  
HELX_P HELX_P21 AC3 SER B 129 ? LEU B 144 ? SER B 222 LEU B 237 1 ? 16 
HELX_P HELX_P22 AC4 THR B 152 ? TYR B 165 ? THR B 245 TYR B 258 1 ? 14 
HELX_P HELX_P23 AC5 PRO B 178 ? VAL B 193 ? PRO B 271 VAL B 286 1 ? 16 
HELX_P HELX_P24 AC6 LEU B 194 ? PHE B 201 ? LEU B 287 PHE B 294 5 ? 8  
HELX_P HELX_P25 AC7 PRO B 202 ? PHE B 214 ? PRO B 295 PHE B 307 1 ? 13 
HELX_P HELX_P26 AC8 SER B 216 ? GLY B 225 ? SER B 309 GLY B 318 1 ? 10 
HELX_P HELX_P27 AC9 GLN B 227 ? MET B 238 ? GLN B 320 MET B 331 1 ? 12 
HELX_P HELX_P28 AD1 MET B 238 ? GLY B 249 ? MET B 331 GLY B 342 1 ? 12 
HELX_P HELX_P29 AD2 ALA B 260 ? ILE B 267 ? ALA B 353 ILE B 360 5 ? 8  
HELX_P HELX_P30 AD3 ASP B 272 ? ALA B 280 ? ASP B 365 ALA B 373 1 ? 9  
# 
_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 
covale1 covale both ? A TYR 162 C ? ? ? 1_555 A TPO 163 N ? ? A TYR 159 A TPO 160 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale2 covale both ? A TPO 163 C ? ? ? 1_555 A HIS 164 N ? ? A TPO 160 A HIS 161 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      TPO 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       163 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       TPO 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        160 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                THR 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        TPO 
_pdbx_modification_feature.type                               Phosphorylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          VAL 
_struct_mon_prot_cis.label_seq_id           157 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           VAL 
_struct_mon_prot_cis.auth_seq_id            154 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    158 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     155 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.79 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? 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 PHE A 7   ? GLU A 15  ? PHE A 4   GLU A 12  
AA1 2 VAL A 20  ? ASN A 26  ? VAL A 17  ASN A 23  
AA1 3 VAL A 32  ? ARG A 39  ? VAL A 29  ARG A 36  
AA1 4 LYS A 78  ? GLU A 84  ? LYS A 75  GLU A 81  
AA1 5 LEU A 69  ? THR A 75  ? LEU A 66  THR A 72  
AA2 1 GLN A 88  ? ASP A 89  ? GLN A 85  ASP A 86  
AA2 2 LEU A 136 ? ILE A 138 ? LEU A 133 ILE A 135 
AA2 3 ILE A 144 ? LEU A 146 ? ILE A 141 LEU A 143 
AA3 1 VAL A 126 ? LEU A 127 ? VAL A 123 LEU A 124 
AA3 2 ARG A 153 ? ALA A 154 ? ARG A 150 ALA A 151 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 10  ? N VAL A 7   O LYS A 23  ? O LYS A 20  
AA1 2 3 N TYR A 22  ? N TYR A 19  O LEU A 35  ? O LEU A 32  
AA1 3 4 N ALA A 34  ? N ALA A 31  O PHE A 83  ? O PHE A 80  
AA1 4 5 O TYR A 80  ? O TYR A 77  N ILE A 73  ? N ILE A 70  
AA2 1 2 N GLN A 88  ? N GLN A 85  O ILE A 138 ? O ILE A 135 
AA2 2 3 N LEU A 137 ? N LEU A 134 O LYS A 145 ? O LYS A 142 
AA3 1 2 N LEU A 127 ? N LEU A 124 O ARG A 153 ? O ARG A 150 
# 
_pdbx_entry_details.entry_id                   9OB5 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 2   ? ? -105.14 -169.21 
2  1 ASN A 3   ? ? 63.97   -1.34   
3  1 LEU A 58  ? ? -117.60 63.28   
4  1 ASP A 127 ? ? -156.27 51.62   
5  1 ASP A 145 ? ? 58.28   87.23   
6  1 VAL A 164 ? ? 68.51   138.98  
7  1 SER A 181 ? ? -151.75 -126.25 
8  1 TRP A 227 ? ? -151.60 88.46   
9  1 ASN B 182 ? ? 56.60   86.04   
10 1 TYR B 258 ? ? -109.67 57.92   
11 1 ASN B 260 ? ? -107.78 -165.72 
12 1 GLN B 269 ? ? -163.46 98.42   
13 1 SER B 308 ? ? -151.74 -109.46 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    TPO 
_pdbx_struct_mod_residue.label_seq_id     163 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     TPO 
_pdbx_struct_mod_residue.auth_seq_id      160 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   THR 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+1/4  
3 y+1/2,-x+1/2,z+3/4  
4 x+1/2,-y+1/2,-z+3/4 
5 -x+1/2,y+1/2,-z+1/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-z+1/2        
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         26.3947532559 
_pdbx_refine_tls.origin_y         6.71367627663 
_pdbx_refine_tls.origin_z         -18.429858723 
_pdbx_refine_tls.T[1][1]          0.430576394823 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0332913026682 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0189327501689 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.64222595218 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.00448673234506 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.453425382964 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.10319877035 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.121222557416 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.692503840241 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.50162757807 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.36361207455 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.12641121525 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.201829563345 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.17004671614 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.142046345531 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.121974061715 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0715048019994 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0689889940368 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.515894595508 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.205450383799 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.246436714165 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   D 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    W 
_pdbx_refine_tls_group.end_auth_seq_id     37 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -2  ? A SER 1   
2  1 Y 1 A HIS -1  ? A HIS 2   
3  1 Y 1 A MET 0   ? A MET 3   
4  1 Y 1 B GLY 94  ? B GLY 1   
5  1 Y 1 B SER 95  ? B SER 2   
6  1 Y 1 B ILE 96  ? B ILE 3   
7  1 Y 1 B ILE 97  ? B ILE 4   
8  1 Y 1 B ALA 98  ? B ALA 5   
9  1 Y 1 B PRO 99  ? B PRO 6   
10 1 Y 1 B SER 100 ? B SER 7   
11 1 Y 1 B ARG 101 ? B ARG 8   
12 1 Y 1 B LYS 376 ? B LYS 283 
13 1 Y 1 B LYS 377 ? B LYS 284 
14 1 Y 1 B ALA 378 ? B ALA 285 
# 
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 
A1CAG C11  C N S 1   
A1CAG C12  C N N 2   
A1CAG C13  C Y N 3   
A1CAG C14  C Y N 4   
A1CAG C15  C Y N 5   
A1CAG C17  C N N 6   
A1CAG C18  C N N 7   
A1CAG C19  C N N 8   
A1CAG C20  C Y N 9   
A1CAG C21  C Y N 10  
A1CAG C23  C Y N 11  
A1CAG C24  C Y N 12  
A1CAG C25  C Y N 13  
A1CAG C01  C N N 14  
A1CAG C02  C N N 15  
A1CAG C03  C N N 16  
A1CAG C04  C N N 17  
A1CAG C06  C N N 18  
A1CAG C08  C N R 19  
A1CAG C09  C N N 20  
A1CAG C10  C N N 21  
A1CAG N05  N N N 22  
A1CAG N16  N N N 23  
A1CAG N22  N Y N 24  
A1CAG N27  N Y N 25  
A1CAG N28  N Y N 26  
A1CAG O07  O N N 27  
A1CAG O26  O N N 28  
A1CAG O29  O N N 29  
A1CAG H111 H N N 30  
A1CAG H122 H N N 31  
A1CAG H121 H N N 32  
A1CAG H141 H N N 33  
A1CAG H182 H N N 34  
A1CAG H181 H N N 35  
A1CAG H191 H N N 36  
A1CAG H192 H N N 37  
A1CAG H211 H N N 38  
A1CAG H231 H N N 39  
A1CAG H241 H N N 40  
A1CAG H251 H N N 41  
A1CAG H012 H N N 42  
A1CAG H011 H N N 43  
A1CAG H013 H N N 44  
A1CAG H032 H N N 45  
A1CAG H031 H N N 46  
A1CAG H041 H N N 47  
A1CAG H042 H N N 48  
A1CAG H081 H N N 49  
A1CAG H092 H N N 50  
A1CAG H091 H N N 51  
A1CAG H102 H N N 52  
A1CAG H101 H N N 53  
A1CAG H051 H N N 54  
A1CAG H161 H N N 55  
A1CAG H281 H N N 56  
ALA   N    N N N 57  
ALA   CA   C N S 58  
ALA   C    C N N 59  
ALA   O    O N N 60  
ALA   CB   C N N 61  
ALA   OXT  O N N 62  
ALA   H    H N N 63  
ALA   H2   H N N 64  
ALA   HA   H N N 65  
ALA   HB1  H N N 66  
ALA   HB2  H N N 67  
ALA   HB3  H N N 68  
ALA   HXT  H N N 69  
ARG   N    N N N 70  
ARG   CA   C N S 71  
ARG   C    C N N 72  
ARG   O    O N N 73  
ARG   CB   C N N 74  
ARG   CG   C N N 75  
ARG   CD   C N N 76  
ARG   NE   N N N 77  
ARG   CZ   C N N 78  
ARG   NH1  N N N 79  
ARG   NH2  N N N 80  
ARG   OXT  O N N 81  
ARG   H    H N N 82  
ARG   H2   H N N 83  
ARG   HA   H N N 84  
ARG   HB2  H N N 85  
ARG   HB3  H N N 86  
ARG   HG2  H N N 87  
ARG   HG3  H N N 88  
ARG   HD2  H N N 89  
ARG   HD3  H N N 90  
ARG   HE   H N N 91  
ARG   HH11 H N N 92  
ARG   HH12 H N N 93  
ARG   HH21 H N N 94  
ARG   HH22 H N N 95  
ARG   HXT  H N N 96  
ASN   N    N N N 97  
ASN   CA   C N S 98  
ASN   C    C N N 99  
ASN   O    O N N 100 
ASN   CB   C N N 101 
ASN   CG   C N N 102 
ASN   OD1  O N N 103 
ASN   ND2  N N N 104 
ASN   OXT  O N N 105 
ASN   H    H N N 106 
ASN   H2   H N N 107 
ASN   HA   H N N 108 
ASN   HB2  H N N 109 
ASN   HB3  H N N 110 
ASN   HD21 H N N 111 
ASN   HD22 H N N 112 
ASN   HXT  H N N 113 
ASP   N    N N N 114 
ASP   CA   C N S 115 
ASP   C    C N N 116 
ASP   O    O N N 117 
ASP   CB   C N N 118 
ASP   CG   C N N 119 
ASP   OD1  O N N 120 
ASP   OD2  O N N 121 
ASP   OXT  O N N 122 
ASP   H    H N N 123 
ASP   H2   H N N 124 
ASP   HA   H N N 125 
ASP   HB2  H N N 126 
ASP   HB3  H N N 127 
ASP   HD2  H N N 128 
ASP   HXT  H N N 129 
CYS   N    N N N 130 
CYS   CA   C N R 131 
CYS   C    C N N 132 
CYS   O    O N N 133 
CYS   CB   C N N 134 
CYS   SG   S N N 135 
CYS   OXT  O N N 136 
CYS   H    H N N 137 
CYS   H2   H N N 138 
CYS   HA   H N N 139 
CYS   HB2  H N N 140 
CYS   HB3  H N N 141 
CYS   HG   H N N 142 
CYS   HXT  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
HIS   N    N N N 193 
HIS   CA   C N S 194 
HIS   C    C N N 195 
HIS   O    O N N 196 
HIS   CB   C N N 197 
HIS   CG   C Y N 198 
HIS   ND1  N Y N 199 
HIS   CD2  C Y N 200 
HIS   CE1  C Y N 201 
HIS   NE2  N Y N 202 
HIS   OXT  O N N 203 
HIS   H    H N N 204 
HIS   H2   H N N 205 
HIS   HA   H N N 206 
HIS   HB2  H N N 207 
HIS   HB3  H N N 208 
HIS   HD1  H N N 209 
HIS   HD2  H N N 210 
HIS   HE1  H N N 211 
HIS   HE2  H N N 212 
HIS   HXT  H N N 213 
HOH   O    O N N 214 
HOH   H1   H N N 215 
HOH   H2   H N N 216 
ILE   N    N N N 217 
ILE   CA   C N S 218 
ILE   C    C N N 219 
ILE   O    O N N 220 
ILE   CB   C N S 221 
ILE   CG1  C N N 222 
ILE   CG2  C N N 223 
ILE   CD1  C N N 224 
ILE   OXT  O N N 225 
ILE   H    H N N 226 
ILE   H2   H N N 227 
ILE   HA   H N N 228 
ILE   HB   H N N 229 
ILE   HG12 H N N 230 
ILE   HG13 H N N 231 
ILE   HG21 H N N 232 
ILE   HG22 H N N 233 
ILE   HG23 H N N 234 
ILE   HD11 H N N 235 
ILE   HD12 H N N 236 
ILE   HD13 H N N 237 
ILE   HXT  H N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
THR   N    N N N 360 
THR   CA   C N S 361 
THR   C    C N N 362 
THR   O    O N N 363 
THR   CB   C N R 364 
THR   OG1  O N N 365 
THR   CG2  C N N 366 
THR   OXT  O N N 367 
THR   H    H N N 368 
THR   H2   H N N 369 
THR   HA   H N N 370 
THR   HB   H N N 371 
THR   HG1  H N N 372 
THR   HG21 H N N 373 
THR   HG22 H N N 374 
THR   HG23 H N N 375 
THR   HXT  H N N 376 
TPO   N    N N N 377 
TPO   CA   C N S 378 
TPO   CB   C N R 379 
TPO   CG2  C N N 380 
TPO   OG1  O N N 381 
TPO   P    P N N 382 
TPO   O1P  O N N 383 
TPO   O2P  O N N 384 
TPO   O3P  O N N 385 
TPO   C    C N N 386 
TPO   O    O N N 387 
TPO   OXT  O N N 388 
TPO   H    H N N 389 
TPO   H2   H N N 390 
TPO   HA   H N N 391 
TPO   HB   H N N 392 
TPO   HG21 H N N 393 
TPO   HG22 H N N 394 
TPO   HG23 H N N 395 
TPO   HOP2 H N N 396 
TPO   HOP3 H N N 397 
TPO   HXT  H N N 398 
TRP   N    N N N 399 
TRP   CA   C N S 400 
TRP   C    C N N 401 
TRP   O    O N N 402 
TRP   CB   C N N 403 
TRP   CG   C Y N 404 
TRP   CD1  C Y N 405 
TRP   CD2  C Y N 406 
TRP   NE1  N Y N 407 
TRP   CE2  C Y N 408 
TRP   CE3  C Y N 409 
TRP   CZ2  C Y N 410 
TRP   CZ3  C Y N 411 
TRP   CH2  C Y N 412 
TRP   OXT  O N N 413 
TRP   H    H N N 414 
TRP   H2   H N N 415 
TRP   HA   H N N 416 
TRP   HB2  H N N 417 
TRP   HB3  H N N 418 
TRP   HD1  H N N 419 
TRP   HE1  H N N 420 
TRP   HE3  H N N 421 
TRP   HZ2  H N N 422 
TRP   HZ3  H N N 423 
TRP   HH2  H N N 424 
TRP   HXT  H N N 425 
TYR   N    N N N 426 
TYR   CA   C N S 427 
TYR   C    C N N 428 
TYR   O    O N N 429 
TYR   CB   C N N 430 
TYR   CG   C Y N 431 
TYR   CD1  C Y N 432 
TYR   CD2  C Y N 433 
TYR   CE1  C Y N 434 
TYR   CE2  C Y N 435 
TYR   CZ   C Y N 436 
TYR   OH   O N N 437 
TYR   OXT  O N N 438 
TYR   H    H N N 439 
TYR   H2   H N N 440 
TYR   HA   H N N 441 
TYR   HB2  H N N 442 
TYR   HB3  H N N 443 
TYR   HD1  H N N 444 
TYR   HD2  H N N 445 
TYR   HE1  H N N 446 
TYR   HE2  H N N 447 
TYR   HH   H N N 448 
TYR   HXT  H N N 449 
VAL   N    N N N 450 
VAL   CA   C N S 451 
VAL   C    C N N 452 
VAL   O    O N N 453 
VAL   CB   C N N 454 
VAL   CG1  C N N 455 
VAL   CG2  C N N 456 
VAL   OXT  O N N 457 
VAL   H    H N N 458 
VAL   H2   H N N 459 
VAL   HA   H N N 460 
VAL   HB   H N N 461 
VAL   HG11 H N N 462 
VAL   HG12 H N N 463 
VAL   HG13 H N N 464 
VAL   HG21 H N N 465 
VAL   HG22 H N N 466 
VAL   HG23 H N N 467 
VAL   HXT  H N N 468 
# 
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 
A1CAG C02 C01  sing N N 1   
A1CAG C04 C03  sing N N 2   
A1CAG C03 C02  sing N N 3   
A1CAG N05 C02  sing N N 4   
A1CAG C06 N05  sing N N 5   
A1CAG C08 O07  sing N N 6   
A1CAG C09 C08  sing N N 7   
A1CAG C10 C09  sing N N 8   
A1CAG C11 C10  sing N N 9   
A1CAG C12 C11  sing N N 10  
A1CAG C13 C11  sing N N 11  
A1CAG C14 C13  doub Y N 12  
A1CAG C15 C14  sing Y N 13  
A1CAG C17 N16  sing N N 14  
A1CAG C19 C18  sing N N 15  
A1CAG C20 C19  sing N N 16  
A1CAG C21 C20  doub Y N 17  
A1CAG N22 C21  sing Y N 18  
A1CAG C23 N22  doub Y N 19  
A1CAG C24 C23  sing Y N 20  
A1CAG C25 C24  doub Y N 21  
A1CAG C18 C17  sing N N 22  
A1CAG O26 C17  doub N N 23  
A1CAG N16 C15  sing N N 24  
A1CAG N27 C15  doub Y N 25  
A1CAG N28 N27  sing Y N 26  
A1CAG O07 C06  sing N N 27  
A1CAG O29 C06  doub N N 28  
A1CAG C02 C04  sing N N 29  
A1CAG C08 C12  sing N N 30  
A1CAG C13 N28  sing Y N 31  
A1CAG C20 C25  sing Y N 32  
A1CAG C11 H111 sing N N 33  
A1CAG C12 H122 sing N N 34  
A1CAG C12 H121 sing N N 35  
A1CAG C14 H141 sing N N 36  
A1CAG C18 H182 sing N N 37  
A1CAG C18 H181 sing N N 38  
A1CAG C19 H191 sing N N 39  
A1CAG C19 H192 sing N N 40  
A1CAG C21 H211 sing N N 41  
A1CAG C23 H231 sing N N 42  
A1CAG C24 H241 sing N N 43  
A1CAG C25 H251 sing N N 44  
A1CAG C01 H012 sing N N 45  
A1CAG C01 H011 sing N N 46  
A1CAG C01 H013 sing N N 47  
A1CAG C03 H032 sing N N 48  
A1CAG C03 H031 sing N N 49  
A1CAG C04 H041 sing N N 50  
A1CAG C04 H042 sing N N 51  
A1CAG C08 H081 sing N N 52  
A1CAG C09 H092 sing N N 53  
A1CAG C09 H091 sing N N 54  
A1CAG C10 H102 sing N N 55  
A1CAG C10 H101 sing N N 56  
A1CAG N05 H051 sing N N 57  
A1CAG N16 H161 sing N N 58  
A1CAG N28 H281 sing N N 59  
ALA   N   CA   sing N N 60  
ALA   N   H    sing N N 61  
ALA   N   H2   sing N N 62  
ALA   CA  C    sing N N 63  
ALA   CA  CB   sing N N 64  
ALA   CA  HA   sing N N 65  
ALA   C   O    doub N N 66  
ALA   C   OXT  sing N N 67  
ALA   CB  HB1  sing N N 68  
ALA   CB  HB2  sing N N 69  
ALA   CB  HB3  sing N N 70  
ALA   OXT HXT  sing N N 71  
ARG   N   CA   sing N N 72  
ARG   N   H    sing N N 73  
ARG   N   H2   sing N N 74  
ARG   CA  C    sing N N 75  
ARG   CA  CB   sing N N 76  
ARG   CA  HA   sing N N 77  
ARG   C   O    doub N N 78  
ARG   C   OXT  sing N N 79  
ARG   CB  CG   sing N N 80  
ARG   CB  HB2  sing N N 81  
ARG   CB  HB3  sing N N 82  
ARG   CG  CD   sing N N 83  
ARG   CG  HG2  sing N N 84  
ARG   CG  HG3  sing N N 85  
ARG   CD  NE   sing N N 86  
ARG   CD  HD2  sing N N 87  
ARG   CD  HD3  sing N N 88  
ARG   NE  CZ   sing N N 89  
ARG   NE  HE   sing N N 90  
ARG   CZ  NH1  sing N N 91  
ARG   CZ  NH2  doub N N 92  
ARG   NH1 HH11 sing N N 93  
ARG   NH1 HH12 sing N N 94  
ARG   NH2 HH21 sing N N 95  
ARG   NH2 HH22 sing N N 96  
ARG   OXT HXT  sing N N 97  
ASN   N   CA   sing N N 98  
ASN   N   H    sing N N 99  
ASN   N   H2   sing N N 100 
ASN   CA  C    sing N N 101 
ASN   CA  CB   sing N N 102 
ASN   CA  HA   sing N N 103 
ASN   C   O    doub N N 104 
ASN   C   OXT  sing N N 105 
ASN   CB  CG   sing N N 106 
ASN   CB  HB2  sing N N 107 
ASN   CB  HB3  sing N N 108 
ASN   CG  OD1  doub N N 109 
ASN   CG  ND2  sing N N 110 
ASN   ND2 HD21 sing N N 111 
ASN   ND2 HD22 sing N N 112 
ASN   OXT HXT  sing N N 113 
ASP   N   CA   sing N N 114 
ASP   N   H    sing N N 115 
ASP   N   H2   sing N N 116 
ASP   CA  C    sing N N 117 
ASP   CA  CB   sing N N 118 
ASP   CA  HA   sing N N 119 
ASP   C   O    doub N N 120 
ASP   C   OXT  sing N N 121 
ASP   CB  CG   sing N N 122 
ASP   CB  HB2  sing N N 123 
ASP   CB  HB3  sing N N 124 
ASP   CG  OD1  doub N N 125 
ASP   CG  OD2  sing N N 126 
ASP   OD2 HD2  sing N N 127 
ASP   OXT HXT  sing N N 128 
CYS   N   CA   sing N N 129 
CYS   N   H    sing N N 130 
CYS   N   H2   sing N N 131 
CYS   CA  C    sing N N 132 
CYS   CA  CB   sing N N 133 
CYS   CA  HA   sing N N 134 
CYS   C   O    doub N N 135 
CYS   C   OXT  sing N N 136 
CYS   CB  SG   sing N N 137 
CYS   CB  HB2  sing N N 138 
CYS   CB  HB3  sing N N 139 
CYS   SG  HG   sing N N 140 
CYS   OXT HXT  sing N N 141 
GLN   N   CA   sing N N 142 
GLN   N   H    sing N N 143 
GLN   N   H2   sing N N 144 
GLN   CA  C    sing N N 145 
GLN   CA  CB   sing N N 146 
GLN   CA  HA   sing N N 147 
GLN   C   O    doub N N 148 
GLN   C   OXT  sing N N 149 
GLN   CB  CG   sing N N 150 
GLN   CB  HB2  sing N N 151 
GLN   CB  HB3  sing N N 152 
GLN   CG  CD   sing N N 153 
GLN   CG  HG2  sing N N 154 
GLN   CG  HG3  sing N N 155 
GLN   CD  OE1  doub N N 156 
GLN   CD  NE2  sing N N 157 
GLN   NE2 HE21 sing N N 158 
GLN   NE2 HE22 sing N N 159 
GLN   OXT HXT  sing N N 160 
GLU   N   CA   sing N N 161 
GLU   N   H    sing N N 162 
GLU   N   H2   sing N N 163 
GLU   CA  C    sing N N 164 
GLU   CA  CB   sing N N 165 
GLU   CA  HA   sing N N 166 
GLU   C   O    doub N N 167 
GLU   C   OXT  sing N N 168 
GLU   CB  CG   sing N N 169 
GLU   CB  HB2  sing N N 170 
GLU   CB  HB3  sing N N 171 
GLU   CG  CD   sing N N 172 
GLU   CG  HG2  sing N N 173 
GLU   CG  HG3  sing N N 174 
GLU   CD  OE1  doub N N 175 
GLU   CD  OE2  sing N N 176 
GLU   OE2 HE2  sing N N 177 
GLU   OXT HXT  sing N N 178 
GLY   N   CA   sing N N 179 
GLY   N   H    sing N N 180 
GLY   N   H2   sing N N 181 
GLY   CA  C    sing N N 182 
GLY   CA  HA2  sing N N 183 
GLY   CA  HA3  sing N N 184 
GLY   C   O    doub N N 185 
GLY   C   OXT  sing N N 186 
GLY   OXT HXT  sing N N 187 
HIS   N   CA   sing N N 188 
HIS   N   H    sing N N 189 
HIS   N   H2   sing N N 190 
HIS   CA  C    sing N N 191 
HIS   CA  CB   sing N N 192 
HIS   CA  HA   sing N N 193 
HIS   C   O    doub N N 194 
HIS   C   OXT  sing N N 195 
HIS   CB  CG   sing N N 196 
HIS   CB  HB2  sing N N 197 
HIS   CB  HB3  sing N N 198 
HIS   CG  ND1  sing Y N 199 
HIS   CG  CD2  doub Y N 200 
HIS   ND1 CE1  doub Y N 201 
HIS   ND1 HD1  sing N N 202 
HIS   CD2 NE2  sing Y N 203 
HIS   CD2 HD2  sing N N 204 
HIS   CE1 NE2  sing Y N 205 
HIS   CE1 HE1  sing N N 206 
HIS   NE2 HE2  sing N N 207 
HIS   OXT HXT  sing N N 208 
HOH   O   H1   sing N N 209 
HOH   O   H2   sing N N 210 
ILE   N   CA   sing N N 211 
ILE   N   H    sing N N 212 
ILE   N   H2   sing N N 213 
ILE   CA  C    sing N N 214 
ILE   CA  CB   sing N N 215 
ILE   CA  HA   sing N N 216 
ILE   C   O    doub N N 217 
ILE   C   OXT  sing N N 218 
ILE   CB  CG1  sing N N 219 
ILE   CB  CG2  sing N N 220 
ILE   CB  HB   sing N N 221 
ILE   CG1 CD1  sing N N 222 
ILE   CG1 HG12 sing N N 223 
ILE   CG1 HG13 sing N N 224 
ILE   CG2 HG21 sing N N 225 
ILE   CG2 HG22 sing N N 226 
ILE   CG2 HG23 sing N N 227 
ILE   CD1 HD11 sing N N 228 
ILE   CD1 HD12 sing N N 229 
ILE   CD1 HD13 sing N N 230 
ILE   OXT HXT  sing N N 231 
LEU   N   CA   sing N N 232 
LEU   N   H    sing N N 233 
LEU   N   H2   sing N N 234 
LEU   CA  C    sing N N 235 
LEU   CA  CB   sing N N 236 
LEU   CA  HA   sing N N 237 
LEU   C   O    doub N N 238 
LEU   C   OXT  sing N N 239 
LEU   CB  CG   sing N N 240 
LEU   CB  HB2  sing N N 241 
LEU   CB  HB3  sing N N 242 
LEU   CG  CD1  sing N N 243 
LEU   CG  CD2  sing N N 244 
LEU   CG  HG   sing N N 245 
LEU   CD1 HD11 sing N N 246 
LEU   CD1 HD12 sing N N 247 
LEU   CD1 HD13 sing N N 248 
LEU   CD2 HD21 sing N N 249 
LEU   CD2 HD22 sing N N 250 
LEU   CD2 HD23 sing N N 251 
LEU   OXT HXT  sing N N 252 
LYS   N   CA   sing N N 253 
LYS   N   H    sing N N 254 
LYS   N   H2   sing N N 255 
LYS   CA  C    sing N N 256 
LYS   CA  CB   sing N N 257 
LYS   CA  HA   sing N N 258 
LYS   C   O    doub N N 259 
LYS   C   OXT  sing N N 260 
LYS   CB  CG   sing N N 261 
LYS   CB  HB2  sing N N 262 
LYS   CB  HB3  sing N N 263 
LYS   CG  CD   sing N N 264 
LYS   CG  HG2  sing N N 265 
LYS   CG  HG3  sing N N 266 
LYS   CD  CE   sing N N 267 
LYS   CD  HD2  sing N N 268 
LYS   CD  HD3  sing N N 269 
LYS   CE  NZ   sing N N 270 
LYS   CE  HE2  sing N N 271 
LYS   CE  HE3  sing N N 272 
LYS   NZ  HZ1  sing N N 273 
LYS   NZ  HZ2  sing N N 274 
LYS   NZ  HZ3  sing N N 275 
LYS   OXT HXT  sing N N 276 
MET   N   CA   sing N N 277 
MET   N   H    sing N N 278 
MET   N   H2   sing N N 279 
MET   CA  C    sing N N 280 
MET   CA  CB   sing N N 281 
MET   CA  HA   sing N N 282 
MET   C   O    doub N N 283 
MET   C   OXT  sing N N 284 
MET   CB  CG   sing N N 285 
MET   CB  HB2  sing N N 286 
MET   CB  HB3  sing N N 287 
MET   CG  SD   sing N N 288 
MET   CG  HG2  sing N N 289 
MET   CG  HG3  sing N N 290 
MET   SD  CE   sing N N 291 
MET   CE  HE1  sing N N 292 
MET   CE  HE2  sing N N 293 
MET   CE  HE3  sing N N 294 
MET   OXT HXT  sing N N 295 
PHE   N   CA   sing N N 296 
PHE   N   H    sing N N 297 
PHE   N   H2   sing N N 298 
PHE   CA  C    sing N N 299 
PHE   CA  CB   sing N N 300 
PHE   CA  HA   sing N N 301 
PHE   C   O    doub N N 302 
PHE   C   OXT  sing N N 303 
PHE   CB  CG   sing N N 304 
PHE   CB  HB2  sing N N 305 
PHE   CB  HB3  sing N N 306 
PHE   CG  CD1  doub Y N 307 
PHE   CG  CD2  sing Y N 308 
PHE   CD1 CE1  sing Y N 309 
PHE   CD1 HD1  sing N N 310 
PHE   CD2 CE2  doub Y N 311 
PHE   CD2 HD2  sing N N 312 
PHE   CE1 CZ   doub Y N 313 
PHE   CE1 HE1  sing N N 314 
PHE   CE2 CZ   sing Y N 315 
PHE   CE2 HE2  sing N N 316 
PHE   CZ  HZ   sing N N 317 
PHE   OXT HXT  sing N N 318 
PRO   N   CA   sing N N 319 
PRO   N   CD   sing N N 320 
PRO   N   H    sing N N 321 
PRO   CA  C    sing N N 322 
PRO   CA  CB   sing N N 323 
PRO   CA  HA   sing N N 324 
PRO   C   O    doub N N 325 
PRO   C   OXT  sing N N 326 
PRO   CB  CG   sing N N 327 
PRO   CB  HB2  sing N N 328 
PRO   CB  HB3  sing N N 329 
PRO   CG  CD   sing N N 330 
PRO   CG  HG2  sing N N 331 
PRO   CG  HG3  sing N N 332 
PRO   CD  HD2  sing N N 333 
PRO   CD  HD3  sing N N 334 
PRO   OXT HXT  sing N N 335 
SER   N   CA   sing N N 336 
SER   N   H    sing N N 337 
SER   N   H2   sing N N 338 
SER   CA  C    sing N N 339 
SER   CA  CB   sing N N 340 
SER   CA  HA   sing N N 341 
SER   C   O    doub N N 342 
SER   C   OXT  sing N N 343 
SER   CB  OG   sing N N 344 
SER   CB  HB2  sing N N 345 
SER   CB  HB3  sing N N 346 
SER   OG  HG   sing N N 347 
SER   OXT HXT  sing N N 348 
THR   N   CA   sing N N 349 
THR   N   H    sing N N 350 
THR   N   H2   sing N N 351 
THR   CA  C    sing N N 352 
THR   CA  CB   sing N N 353 
THR   CA  HA   sing N N 354 
THR   C   O    doub N N 355 
THR   C   OXT  sing N N 356 
THR   CB  OG1  sing N N 357 
THR   CB  CG2  sing N N 358 
THR   CB  HB   sing N N 359 
THR   OG1 HG1  sing N N 360 
THR   CG2 HG21 sing N N 361 
THR   CG2 HG22 sing N N 362 
THR   CG2 HG23 sing N N 363 
THR   OXT HXT  sing N N 364 
TPO   N   CA   sing N N 365 
TPO   N   H    sing N N 366 
TPO   N   H2   sing N N 367 
TPO   CA  CB   sing N N 368 
TPO   CA  C    sing N N 369 
TPO   CA  HA   sing N N 370 
TPO   CB  CG2  sing N N 371 
TPO   CB  OG1  sing N N 372 
TPO   CB  HB   sing N N 373 
TPO   CG2 HG21 sing N N 374 
TPO   CG2 HG22 sing N N 375 
TPO   CG2 HG23 sing N N 376 
TPO   OG1 P    sing N N 377 
TPO   P   O1P  doub N N 378 
TPO   P   O2P  sing N N 379 
TPO   P   O3P  sing N N 380 
TPO   O2P HOP2 sing N N 381 
TPO   O3P HOP3 sing N N 382 
TPO   C   O    doub N N 383 
TPO   C   OXT  sing N N 384 
TPO   OXT HXT  sing N N 385 
TRP   N   CA   sing N N 386 
TRP   N   H    sing N N 387 
TRP   N   H2   sing N N 388 
TRP   CA  C    sing N N 389 
TRP   CA  CB   sing N N 390 
TRP   CA  HA   sing N N 391 
TRP   C   O    doub N N 392 
TRP   C   OXT  sing N N 393 
TRP   CB  CG   sing N N 394 
TRP   CB  HB2  sing N N 395 
TRP   CB  HB3  sing N N 396 
TRP   CG  CD1  doub Y N 397 
TRP   CG  CD2  sing Y N 398 
TRP   CD1 NE1  sing Y N 399 
TRP   CD1 HD1  sing N N 400 
TRP   CD2 CE2  doub Y N 401 
TRP   CD2 CE3  sing Y N 402 
TRP   NE1 CE2  sing Y N 403 
TRP   NE1 HE1  sing N N 404 
TRP   CE2 CZ2  sing Y N 405 
TRP   CE3 CZ3  doub Y N 406 
TRP   CE3 HE3  sing N N 407 
TRP   CZ2 CH2  doub Y N 408 
TRP   CZ2 HZ2  sing N N 409 
TRP   CZ3 CH2  sing Y N 410 
TRP   CZ3 HZ3  sing N N 411 
TRP   CH2 HH2  sing N N 412 
TRP   OXT HXT  sing N N 413 
TYR   N   CA   sing N N 414 
TYR   N   H    sing N N 415 
TYR   N   H2   sing N N 416 
TYR   CA  C    sing N N 417 
TYR   CA  CB   sing N N 418 
TYR   CA  HA   sing N N 419 
TYR   C   O    doub N N 420 
TYR   C   OXT  sing N N 421 
TYR   CB  CG   sing N N 422 
TYR   CB  HB2  sing N N 423 
TYR   CB  HB3  sing N N 424 
TYR   CG  CD1  doub Y N 425 
TYR   CG  CD2  sing Y N 426 
TYR   CD1 CE1  sing Y N 427 
TYR   CD1 HD1  sing N N 428 
TYR   CD2 CE2  doub Y N 429 
TYR   CD2 HD2  sing N N 430 
TYR   CE1 CZ   doub Y N 431 
TYR   CE1 HE1  sing N N 432 
TYR   CE2 CZ   sing Y N 433 
TYR   CE2 HE2  sing N N 434 
TYR   CZ  OH   sing N N 435 
TYR   OH  HH   sing N N 436 
TYR   OXT HXT  sing N N 437 
VAL   N   CA   sing N N 438 
VAL   N   H    sing N N 439 
VAL   N   H2   sing N N 440 
VAL   CA  C    sing N N 441 
VAL   CA  CB   sing N N 442 
VAL   CA  HA   sing N N 443 
VAL   C   O    doub N N 444 
VAL   C   OXT  sing N N 445 
VAL   CB  CG1  sing N N 446 
VAL   CB  CG2  sing N N 447 
VAL   CB  HB   sing N N 448 
VAL   CG1 HG11 sing N N 449 
VAL   CG1 HG12 sing N N 450 
VAL   CG1 HG13 sing N N 451 
VAL   CG2 HG21 sing N N 452 
VAL   CG2 HG22 sing N N 453 
VAL   CG2 HG23 sing N N 454 
VAL   OXT HXT  sing N N 455 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Internal structure' 
# 
_space_group.name_H-M_alt     'P 41 21 2' 
_space_group.name_Hall        'P 4abw 2nw' 
_space_group.IT_number        92 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9OB5 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009845 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009845 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006602 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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 4   ? 52.59805 10.84263  -3.89323  1.000 135.02765 ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 4   ? 51.61461 11.87588  -3.59148  1.000 136.43153 ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 4   ? 52.27418 13.05302  -2.88163  1.000 152.70820 ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 4   ? 51.70783 13.63087  -1.95381  1.000 147.82168 ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 4   ? 50.48215 11.30570  -2.73449  1.000 128.94415 ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 4   ? 49.07507 11.59008  -3.25520  1.000 120.01322 ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 4   ? 48.48431 13.27163  -2.96396  1.000 117.08318 ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 4   ? 48.99769 14.10127  -4.46597  1.000 112.03305 ? 1   MET   A CE  1 
ATOM   9    N N   . GLU   A 1 5   ? 53.47586 13.40161  -3.32653  1.000 166.54575 ? 2   GLU   A N   1 
ATOM   10   C CA  . GLU   A 1 5   ? 54.24951 14.48194  -2.74308  1.000 163.98999 ? 2   GLU   A CA  1 
ATOM   11   C C   . GLU   A 1 5   ? 54.21343 15.69950  -3.66477  1.000 157.94985 ? 2   GLU   A C   1 
ATOM   12   O O   . GLU   A 1 5   ? 53.42396 15.76650  -4.61288  1.000 151.48120 ? 2   GLU   A O   1 
ATOM   13   C CB  . GLU   A 1 5   ? 55.67898 14.00798  -2.47599  1.000 165.00750 ? 2   GLU   A CB  1 
ATOM   14   C CG  . GLU   A 1 5   ? 56.45603 13.65603  -3.73425  1.000 170.98234 ? 2   GLU   A CG  1 
ATOM   15   C CD  . GLU   A 1 5   ? 57.37009 12.46387  -3.53856  1.000 180.01868 ? 2   GLU   A CD  1 
ATOM   16   O OE1 . GLU   A 1 5   ? 57.04021 11.59335  -2.70578  1.000 183.41200 ? 2   GLU   A OE1 1 
ATOM   17   O OE2 . GLU   A 1 5   ? 58.41728 12.39667  -4.21583  1.000 173.90890 ? 2   GLU   A OE2 1 
ATOM   18   N N   . ASN   A 1 6   ? 55.06104 16.68739  -3.36522  1.000 147.00807 ? 3   ASN   A N   1 
ATOM   19   C CA  . ASN   A 1 6   ? 55.22119 17.89885  -4.16649  1.000 137.76596 ? 3   ASN   A CA  1 
ATOM   20   C C   . ASN   A 1 6   ? 53.95142 18.74485  -4.20124  1.000 124.97828 ? 3   ASN   A C   1 
ATOM   21   O O   . ASN   A 1 6   ? 53.93562 19.81698  -4.81439  1.000 122.21418 ? 3   ASN   A O   1 
ATOM   22   C CB  . ASN   A 1 6   ? 55.65940 17.54684  -5.59251  1.000 139.19173 ? 3   ASN   A CB  1 
ATOM   23   C CG  . ASN   A 1 6   ? 56.49401 18.63933  -6.23479  1.000 136.24256 ? 3   ASN   A CG  1 
ATOM   24   O OD1 . ASN   A 1 6   ? 57.58451 18.38167  -6.74330  1.000 133.68661 ? 3   ASN   A OD1 1 
ATOM   25   N ND2 . ASN   A 1 6   ? 55.98809 19.86672  -6.21041  1.000 132.52608 ? 3   ASN   A ND2 1 
ATOM   26   N N   . PHE   A 1 7   ? 52.88882 18.28287  -3.54916  1.000 112.77929 ? 4   PHE   A N   1 
ATOM   27   C CA  . PHE   A 1 7   ? 51.63079 19.01122  -3.46733  1.000 99.92694  ? 4   PHE   A CA  1 
ATOM   28   C C   . PHE   A 1 7   ? 51.42019 19.49351  -2.03965  1.000 99.68979  ? 4   PHE   A C   1 
ATOM   29   O O   . PHE   A 1 7   ? 51.48718 18.70103  -1.09367  1.000 100.46442 ? 4   PHE   A O   1 
ATOM   30   C CB  . PHE   A 1 7   ? 50.45612 18.13923  -3.91706  1.000 103.32603 ? 4   PHE   A CB  1 
ATOM   31   C CG  . PHE   A 1 7   ? 50.21185 18.16868  -5.40027  1.000 102.06433 ? 4   PHE   A CG  1 
ATOM   32   C CD1 . PHE   A 1 7   ? 50.76532 19.16543  -6.18834  1.000 97.69001  ? 4   PHE   A CD1 1 
ATOM   33   C CD2 . PHE   A 1 7   ? 49.42149 17.20540  -6.00454  1.000 87.94793  ? 4   PHE   A CD2 1 
ATOM   34   C CE1 . PHE   A 1 7   ? 50.53919 19.19664  -7.55222  1.000 96.38818  ? 4   PHE   A CE1 1 
ATOM   35   C CE2 . PHE   A 1 7   ? 49.19132 17.22962  -7.36654  1.000 82.08972  ? 4   PHE   A CE2 1 
ATOM   36   C CZ  . PHE   A 1 7   ? 49.75064 18.22678  -8.14199  1.000 97.47191  ? 4   PHE   A CZ  1 
ATOM   37   N N   . GLN   A 1 8   ? 51.17133 20.79141  -1.89068  1.000 91.59569  ? 5   GLN   A N   1 
ATOM   38   C CA  . GLN   A 1 8   ? 50.98990 21.42371  -0.59088  1.000 91.23955  ? 5   GLN   A CA  1 
ATOM   39   C C   . GLN   A 1 8   ? 49.58415 22.00031  -0.52456  1.000 88.98374  ? 5   GLN   A C   1 
ATOM   40   O O   . GLN   A 1 8   ? 49.21926 22.84671  -1.34756  1.000 85.57147  ? 5   GLN   A O   1 
ATOM   41   C CB  . GLN   A 1 8   ? 52.03883 22.51511  -0.36653  1.000 92.11792  ? 5   GLN   A CB  1 
ATOM   42   C CG  . GLN   A 1 8   ? 51.92809 23.23911  0.96310   1.000 97.69310  ? 5   GLN   A CG  1 
ATOM   43   C CD  . GLN   A 1 8   ? 53.06148 24.22414  1.18048   1.000 111.49723 ? 5   GLN   A CD  1 
ATOM   44   O OE1 . GLN   A 1 8   ? 53.03618 25.02074  2.11811   1.000 116.44699 ? 5   GLN   A OE1 1 
ATOM   45   N NE2 . GLN   A 1 8   ? 54.06578 24.17169  0.31257   1.000 114.15607 ? 5   GLN   A NE2 1 
ATOM   46   N N   . LYS   A 1 9   ? 48.79795 21.53678  0.44517   1.000 87.40041  ? 6   LYS   A N   1 
ATOM   47   C CA  . LYS   A 1 9   ? 47.44200 22.04282  0.61210   1.000 86.26381  ? 6   LYS   A CA  1 
ATOM   48   C C   . LYS   A 1 9   ? 47.47363 23.51596  0.99656   1.000 78.87586  ? 6   LYS   A C   1 
ATOM   49   O O   . LYS   A 1 9   ? 48.23836 23.92659  1.87461   1.000 80.32596  ? 6   LYS   A O   1 
ATOM   50   C CB  . LYS   A 1 9   ? 46.69883 21.22885  1.67099   1.000 86.26169  ? 6   LYS   A CB  1 
ATOM   51   C CG  . LYS   A 1 9   ? 46.40488 19.79784  1.24882   1.000 81.10766  ? 6   LYS   A CG  1 
ATOM   52   C CD  . LYS   A 1 9   ? 45.74369 19.00949  2.36782   1.000 87.27777  ? 6   LYS   A CD  1 
ATOM   53   C CE  . LYS   A 1 9   ? 45.42640 17.58768  1.92756   1.000 94.20103  ? 6   LYS   A CE  1 
ATOM   54   N NZ  . LYS   A 1 9   ? 44.85753 16.77168  3.03680   1.000 99.24757  ? 6   LYS   A NZ  1 
ATOM   55   N N   . VAL   A 1 10  ? 46.64153 24.31124  0.32861   1.000 74.46012  ? 7   VAL   A N   1 
ATOM   56   C CA  . VAL   A 1 10  ? 46.62031 25.75382  0.50760   1.000 83.89252  ? 7   VAL   A CA  1 
ATOM   57   C C   . VAL   A 1 10  ? 45.33886 26.22070  1.18659   1.000 73.78057  ? 7   VAL   A C   1 
ATOM   58   O O   . VAL   A 1 10  ? 45.38116 27.07318  2.07677   1.000 84.35499  ? 7   VAL   A O   1 
ATOM   59   C CB  . VAL   A 1 10  ? 46.81994 26.47124  -0.84590  1.000 82.23916  ? 7   VAL   A CB  1 
ATOM   60   C CG1 . VAL   A 1 10  ? 46.66366 27.97844  -0.68693  1.000 79.86486  ? 7   VAL   A CG1 1 
ATOM   61   C CG2 . VAL   A 1 10  ? 48.18263 26.13352  -1.42741  1.000 86.98649  ? 7   VAL   A CG2 1 
ATOM   62   N N   . GLU   A 1 11  ? 44.19439 25.67119  0.78867   1.000 73.78879  ? 8   GLU   A N   1 
ATOM   63   C CA  . GLU   A 1 11  ? 42.91741 26.10327  1.33473   1.000 74.03078  ? 8   GLU   A CA  1 
ATOM   64   C C   . GLU   A 1 11  ? 41.88226 25.01681  1.08863   1.000 72.04759  ? 8   GLU   A C   1 
ATOM   65   O O   . GLU   A 1 11  ? 41.85947 24.40917  0.01622   1.000 72.67408  ? 8   GLU   A O   1 
ATOM   66   C CB  . GLU   A 1 11  ? 42.46536 27.42524  0.70151   1.000 73.96265  ? 8   GLU   A CB  1 
ATOM   67   C CG  . GLU   A 1 11  ? 41.13219 27.94289  1.21509   1.000 84.20186  ? 8   GLU   A CG  1 
ATOM   68   C CD  . GLU   A 1 11  ? 40.64080 29.14798  0.43922   1.000 85.41684  ? 8   GLU   A CD  1 
ATOM   69   O OE1 . GLU   A 1 11  ? 41.35797 29.59379  -0.48090  1.000 89.81572  ? 8   GLU   A OE1 1 
ATOM   70   O OE2 . GLU   A 1 11  ? 39.53809 29.64761  0.74652   1.000 95.75246  ? 8   GLU   A OE2 1 
ATOM   71   N N   . LYS   A 1 12  ? 41.03476 24.77653  2.08620   1.000 64.20333  ? 9   LYS   A N   1 
ATOM   72   C CA  . LYS   A 1 12  ? 39.92573 23.84584  1.93076   1.000 66.26549  ? 9   LYS   A CA  1 
ATOM   73   C C   . LYS   A 1 12  ? 38.82178 24.49165  1.10235   1.000 64.75342  ? 9   LYS   A C   1 
ATOM   74   O O   . LYS   A 1 12  ? 38.35756 25.59223  1.41797   1.000 71.06031  ? 9   LYS   A O   1 
ATOM   75   C CB  . LYS   A 1 12  ? 39.38352 23.42306  3.29537   1.000 66.31374  ? 9   LYS   A CB  1 
ATOM   76   C CG  . LYS   A 1 12  ? 38.33479 22.31934  3.23723   1.000 72.05189  ? 9   LYS   A CG  1 
ATOM   77   C CD  . LYS   A 1 12  ? 37.37950 22.40398  4.42070   1.000 80.24887  ? 9   LYS   A CD  1 
ATOM   78   C CE  . LYS   A 1 12  ? 36.43533 21.21009  4.48611   1.000 72.37057  ? 9   LYS   A CE  1 
ATOM   79   N NZ  . LYS   A 1 12  ? 37.00150 20.09055  5.29103   1.000 74.55688  ? 9   LYS   A NZ  1 
ATOM   80   N N   . ILE   A 1 13  ? 38.40575 23.80745  0.04107   1.000 62.34392  ? 10  ILE   A N   1 
ATOM   81   C CA  . ILE   A 1 13  ? 37.35242 24.32492  -0.82573  1.000 66.18213  ? 10  ILE   A CA  1 
ATOM   82   C C   . ILE   A 1 13  ? 35.97274 23.98970  -0.27794  1.000 64.56232  ? 10  ILE   A C   1 
ATOM   83   O O   . ILE   A 1 13  ? 35.06387 24.82175  -0.31606  1.000 77.61149  ? 10  ILE   A O   1 
ATOM   84   C CB  . ILE   A 1 13  ? 37.54393 23.78671  -2.25744  1.000 63.64148  ? 10  ILE   A CB  1 
ATOM   85   C CG1 . ILE   A 1 13  ? 38.83943 24.33779  -2.85807  1.000 67.13822  ? 10  ILE   A CG1 1 
ATOM   86   C CG2 . ILE   A 1 13  ? 36.35404 24.14373  -3.13407  1.000 62.98385  ? 10  ILE   A CG2 1 
ATOM   87   C CD1 . ILE   A 1 13  ? 39.12561 23.84347  -4.25869  1.000 60.20041  ? 10  ILE   A CD1 1 
ATOM   88   N N   A GLY   A 1 14  ? 35.79194 22.77580  0.22475   0.469 69.36620  ? 11  GLY   A N   1 
ATOM   89   N N   B GLY   A 1 14  ? 35.80098 22.79272  0.25743   0.531 71.73725  ? 11  GLY   A N   1 
ATOM   90   C CA  A GLY   A 1 14  ? 34.49293 22.35272  0.70478   0.469 72.32889  ? 11  GLY   A CA  1 
ATOM   91   C CA  B GLY   A 1 14  ? 34.55441 22.43558  0.90279   0.531 72.13323  ? 11  GLY   A CA  1 
ATOM   92   C C   A GLY   A 1 14  ? 34.50164 20.87321  1.01497   0.469 72.79339  ? 11  GLY   A C   1 
ATOM   93   C C   B GLY   A 1 14  ? 34.42299 20.93955  1.05068   0.531 74.80555  ? 11  GLY   A C   1 
ATOM   94   O O   A GLY   A 1 14  ? 35.53092 20.19717  0.92022   0.469 69.42504  ? 11  GLY   A O   1 
ATOM   95   O O   B GLY   A 1 14  ? 35.17239 20.15819  0.46687   0.531 71.06666  ? 11  GLY   A O   1 
ATOM   96   N N   A GLU   A 1 15  ? 33.32295 20.37765  1.38558   0.469 76.88351  ? 12  GLU   A N   1 
ATOM   97   N N   B GLU   A 1 15  ? 33.43986 20.54622  1.85572   0.531 76.98348  ? 12  GLU   A N   1 
ATOM   98   C CA  A GLU   A 1 15  ? 33.17062 18.98418  1.78058   0.469 77.14853  ? 12  GLU   A CA  1 
ATOM   99   C CA  B GLU   A 1 15  ? 33.08552 19.14319  2.02166   0.531 77.12076  ? 12  GLU   A CA  1 
ATOM   100  C C   A GLU   A 1 15  ? 31.90522 18.40667  1.16707   0.469 79.10685  ? 12  GLU   A C   1 
ATOM   101  C C   B GLU   A 1 15  ? 31.59395 18.97509  1.79031   0.531 78.88085  ? 12  GLU   A C   1 
ATOM   102  O O   A GLU   A 1 15  ? 30.85200 19.05081  1.18250   0.469 77.68128  ? 12  GLU   A O   1 
ATOM   103  O O   B GLU   A 1 15  ? 30.78889 19.65854  2.43493   0.531 78.11483  ? 12  GLU   A O   1 
ATOM   104  C CB  A GLU   A 1 15  ? 33.12701 18.84384  3.30735   0.469 74.64287  ? 12  GLU   A CB  1 
ATOM   105  C CB  B GLU   A 1 15  ? 33.46165 18.62862  3.42062   0.531 74.83727  ? 12  GLU   A CB  1 
ATOM   106  C CG  A GLU   A 1 15  ? 32.93662 17.41611  3.78954   0.469 75.49602  ? 12  GLU   A CG  1 
ATOM   107  C CG  B GLU   A 1 15  ? 33.33627 17.11431  3.54704   0.531 75.96669  ? 12  GLU   A CG  1 
ATOM   108  C CD  A GLU   A 1 15  ? 33.03123 17.29131  5.29502   0.469 78.16017  ? 12  GLU   A CD  1 
ATOM   109  C CD  B GLU   A 1 15  ? 33.13811 16.65465  4.97367   0.531 80.34401  ? 12  GLU   A CD  1 
ATOM   110  O OE1 A GLU   A 1 15  ? 33.17385 18.33203  5.97050   0.469 74.82387  ? 12  GLU   A OE1 1 
ATOM   111  O OE1 B GLU   A 1 15  ? 33.11701 17.52628  5.86626   0.531 77.09047  ? 12  GLU   A OE1 1 
ATOM   112  O OE2 A GLU   A 1 15  ? 32.96619 16.15184  5.80169   0.469 79.88390  ? 12  GLU   A OE2 1 
ATOM   113  O OE2 B GLU   A 1 15  ? 32.99937 15.43157  5.19935   0.531 79.98083  ? 12  GLU   A OE2 1 
ATOM   114  N N   A GLY   A 1 16  ? 32.01776 17.19290  0.62441   0.469 77.40426  ? 13  GLY   A N   1 
ATOM   115  N N   B GLY   A 1 16  ? 31.22509 18.08045  0.88883   0.531 77.09719  ? 13  GLY   A N   1 
ATOM   116  C CA  A GLY   A 1 16  ? 30.89307 16.44873  0.12689   0.469 78.93405  ? 13  GLY   A CA  1 
ATOM   117  C CA  B GLY   A 1 16  ? 29.82037 17.82776  0.64089   0.531 75.79752  ? 13  GLY   A CA  1 
ATOM   118  C C   A GLY   A 1 16  ? 30.60817 15.21364  0.95563   0.469 78.31450  ? 13  GLY   A C   1 
ATOM   119  C C   B GLY   A 1 16  ? 29.60251 16.43659  0.08717   0.531 75.37422  ? 13  GLY   A C   1 
ATOM   120  O O   A GLY   A 1 16  ? 31.07654 15.06692  2.09279   0.469 77.02080  ? 13  GLY   A O   1 
ATOM   121  O O   B GLY   A 1 16  ? 30.33298 15.50207  0.41651   0.531 78.33971  ? 13  GLY   A O   1 
ATOM   122  N N   A THR   A 1 17  ? 29.82588 14.30366  0.37442   0.469 78.34190  ? 14  THR   A N   1 
ATOM   123  N N   B THR   A 1 17  ? 28.58257 16.31060  -0.77248  0.531 75.24675  ? 14  THR   A N   1 
ATOM   124  C CA  A THR   A 1 17  ? 29.48665 13.06689  1.07100   0.469 72.76047  ? 14  THR   A CA  1 
ATOM   125  C CA  B THR   A 1 17  ? 28.29120 15.02014  -1.38892  0.531 74.86023  ? 14  THR   A CA  1 
ATOM   126  C C   A THR   A 1 17  ? 30.70900 12.16721  1.21601   0.469 74.60997  ? 14  THR   A C   1 
ATOM   127  C C   B THR   A 1 17  ? 29.44915 14.54912  -2.25474  0.531 75.66627  ? 14  THR   A C   1 
ATOM   128  O O   A THR   A 1 17  ? 31.13574 11.85056  2.33275   0.469 71.08839  ? 14  THR   A O   1 
ATOM   129  O O   B THR   A 1 17  ? 29.68134 13.34095  -2.38360  0.531 76.92627  ? 14  THR   A O   1 
ATOM   130  C CB  A THR   A 1 17  ? 28.36265 12.33761  0.33228   0.469 75.40590  ? 14  THR   A CB  1 
ATOM   131  C CB  B THR   A 1 17  ? 27.00878 15.10543  -2.21708  0.531 71.89033  ? 14  THR   A CB  1 
ATOM   132  O OG1 A THR   A 1 17  ? 27.15471 13.10403  0.41852   0.469 76.20129  ? 14  THR   A OG1 1 
ATOM   133  O OG1 B THR   A 1 17  ? 27.15046 16.11393  -3.22572  0.531 74.34160  ? 14  THR   A OG1 1 
ATOM   134  C CG2 A THR   A 1 17  ? 28.13132 10.96337  0.94176   0.469 75.22795  ? 14  THR   A CG2 1 
ATOM   135  C CG2 B THR   A 1 17  ? 25.81494 15.44229  -1.32723  0.531 76.69662  ? 14  THR   A CG2 1 
ATOM   136  N N   A TYR   A 1 18  ? 31.29040 11.74831  0.09201   0.469 80.72477  ? 15  TYR   A N   1 
ATOM   137  N N   B TYR   A 1 18  ? 30.20362 15.48613  -2.82896  0.531 73.87991  ? 15  TYR   A N   1 
ATOM   138  C CA  A TYR   A 1 18  ? 32.45019 10.86611  0.11873   0.469 80.02255  ? 15  TYR   A CA  1 
ATOM   139  C CA  B TYR   A 1 18  ? 31.37540 15.11514  -3.61458  0.531 73.07204  ? 15  TYR   A CA  1 
ATOM   140  C C   A TYR   A 1 18  ? 33.77403 11.61086  0.02826   0.469 81.74658  ? 15  TYR   A C   1 
ATOM   141  C C   B TYR   A 1 18  ? 32.44270 14.46091  -2.74388  0.531 78.87134  ? 15  TYR   A C   1 
ATOM   142  O O   A TYR   A 1 18  ? 34.79005 11.10432  0.51802   0.469 80.61575  ? 15  TYR   A O   1 
ATOM   143  O O   B TYR   A 1 18  ? 33.03893 13.44713  -3.13342  0.531 83.75011  ? 15  TYR   A O   1 
ATOM   144  C CB  A TYR   A 1 18  ? 32.37662 9.85137   -1.02650  0.469 76.49167  ? 15  TYR   A CB  1 
ATOM   145  C CB  B TYR   A 1 18  ? 31.93080 16.34645  -4.33326  0.531 76.18666  ? 15  TYR   A CB  1 
ATOM   146  C CG  A TYR   A 1 18  ? 31.22986 8.87338   -0.92312  0.469 75.24589  ? 15  TYR   A CG  1 
ATOM   147  C CG  B TYR   A 1 18  ? 31.70503 17.63823  -3.58251  0.531 71.52352  ? 15  TYR   A CG  1 
ATOM   148  C CD1 A TYR   A 1 18  ? 31.21737 7.89015   0.05666   0.469 72.33624  ? 15  TYR   A CD1 1 
ATOM   149  C CD1 B TYR   A 1 18  ? 32.60897 18.06572  -2.62476  0.531 66.25628  ? 15  TYR   A CD1 1 
ATOM   150  C CD2 A TYR   A 1 18  ? 30.16839 8.92156   -1.81709  0.469 73.11404  ? 15  TYR   A CD2 1 
ATOM   151  C CD2 B TYR   A 1 18  ? 30.58366 18.42605  -3.82634  0.531 68.42301  ? 15  TYR   A CD2 1 
ATOM   152  C CE1 A TYR   A 1 18  ? 30.17491 6.98932   0.15104   0.469 75.41321  ? 15  TYR   A CE1 1 
ATOM   153  C CE1 B TYR   A 1 18  ? 32.41094 19.23485  -1.92981  0.531 71.07736  ? 15  TYR   A CE1 1 
ATOM   154  C CE2 A TYR   A 1 18  ? 29.12092 8.02417   -1.73091  0.469 71.21050  ? 15  TYR   A CE2 1 
ATOM   155  C CE2 B TYR   A 1 18  ? 30.37489 19.60217  -3.13156  0.531 59.40909  ? 15  TYR   A CE2 1 
ATOM   156  C CZ  A TYR   A 1 18  ? 29.12942 7.06070   -0.74500  0.469 67.13540  ? 15  TYR   A CZ  1 
ATOM   157  C CZ  B TYR   A 1 18  ? 31.29388 20.00172  -2.18427  0.531 72.37327  ? 15  TYR   A CZ  1 
ATOM   158  O OH  A TYR   A 1 18  ? 28.08899 6.16529   -0.65498  0.469 68.83992  ? 15  TYR   A OH  1 
ATOM   159  O OH  B TYR   A 1 18  ? 31.09951 21.17192  -1.48613  0.531 68.88143  ? 15  TYR   A OH  1 
ATOM   160  N N   A GLY   A 1 19  ? 33.79375 12.78809  -0.57990  0.469 93.91015  ? 16  GLY   A N   1 
ATOM   161  N N   B GLY   A 1 19  ? 32.68486 15.01395  -1.55396  0.531 91.33240  ? 16  GLY   A N   1 
ATOM   162  C CA  A GLY   A 1 19  ? 35.03447 13.49645  -0.85875  0.469 83.16888  ? 16  GLY   A CA  1 
ATOM   163  C CA  B GLY   A 1 19  ? 33.80720 14.56319  -0.75193  0.531 85.31531  ? 16  GLY   A CA  1 
ATOM   164  C C   A GLY   A 1 19  ? 35.10236 14.85080  -0.18144  0.469 81.05757  ? 16  GLY   A C   1 
ATOM   165  C C   B GLY   A 1 19  ? 34.53622 15.70964  -0.07766  0.531 82.63165  ? 16  GLY   A C   1 
ATOM   166  O O   A GLY   A 1 19  ? 34.10363 15.56991  -0.11054  0.469 81.68421  ? 16  GLY   A O   1 
ATOM   167  O O   B GLY   A 1 19  ? 33.95226 16.78517  0.13016   0.531 80.61001  ? 16  GLY   A O   1 
ATOM   168  N N   A VAL   A 1 20  ? 36.28984 15.18638  0.31799   0.469 79.93978  ? 17  VAL   A N   1 
ATOM   169  N N   B VAL   A 1 20  ? 35.80204 15.50878  0.27214   0.531 79.37755  ? 17  VAL   A N   1 
ATOM   170  C CA  A VAL   A 1 20  ? 36.61296 16.51842  0.81470   0.469 73.56016  ? 17  VAL   A CA  1 
ATOM   171  C CA  B VAL   A 1 20  ? 36.61983 16.55623  0.86923   0.531 77.99436  ? 17  VAL   A CA  1 
ATOM   172  C C   A VAL   A 1 20  ? 37.57741 17.15152  -0.17683  0.469 73.50789  ? 17  VAL   A C   1 
ATOM   173  C C   B VAL   A 1 20  ? 37.51364 17.11540  -0.23113  0.531 74.08572  ? 17  VAL   A C   1 
ATOM   174  O O   A VAL   A 1 20  ? 38.59275 16.54370  -0.53783  0.469 75.27389  ? 17  VAL   A O   1 
ATOM   175  O O   B VAL   A 1 20  ? 38.41290 16.42859  -0.72790  0.531 74.92410  ? 17  VAL   A O   1 
ATOM   176  C CB  A VAL   A 1 20  ? 37.22240 16.46694  2.22654   0.469 75.69030  ? 17  VAL   A CB  1 
ATOM   177  C CB  B VAL   A 1 20  ? 37.43172 16.02798  2.06010   0.531 76.39379  ? 17  VAL   A CB  1 
ATOM   178  C CG1 A VAL   A 1 20  ? 37.64971 17.85972  2.67238   0.469 72.55069  ? 17  VAL   A CG1 1 
ATOM   179  C CG1 B VAL   A 1 20  ? 37.87266 17.17843  2.97181   0.531 73.10087  ? 17  VAL   A CG1 1 
ATOM   180  C CG2 A VAL   A 1 20  ? 36.23067 15.86652  3.20960   0.469 78.44110  ? 17  VAL   A CG2 1 
ATOM   181  C CG2 B VAL   A 1 20  ? 36.61098 15.01564  2.85374   0.531 81.48959  ? 17  VAL   A CG2 1 
ATOM   182  N N   . VAL   A 1 21  ? 37.25703 18.36040  -0.62655  1.000 64.25804  ? 18  VAL   A N   1 
ATOM   183  C CA  . VAL   A 1 21  ? 38.00030 19.02818  -1.69045  1.000 69.67858  ? 18  VAL   A CA  1 
ATOM   184  C C   . VAL   A 1 21  ? 38.93521 20.06317  -1.07772  1.000 71.76563  ? 18  VAL   A C   1 
ATOM   185  O O   . VAL   A 1 21  ? 38.49830 20.93338  -0.31368  1.000 62.05536  ? 18  VAL   A O   1 
ATOM   186  C CB  . VAL   A 1 21  ? 37.05410 19.67988  -2.71485  1.000 65.94611  ? 18  VAL   A CB  1 
ATOM   187  C CG1 . VAL   A 1 21  ? 37.85173 20.36574  -3.81479  1.000 64.49208  ? 18  VAL   A CG1 1 
ATOM   188  C CG2 . VAL   A 1 21  ? 36.11318 18.63839  -3.30507  1.000 65.33722  ? 18  VAL   A CG2 1 
ATOM   189  N N   . TYR   A 1 22  ? 40.21937 19.97148  -1.41905  1.000 60.26395  ? 19  TYR   A N   1 
ATOM   190  C CA  . TYR   A 1 22  ? 41.22465 20.94054  -1.01116  1.000 62.42827  ? 19  TYR   A CA  1 
ATOM   191  C C   . TYR   A 1 22  ? 41.81450 21.62129  -2.23868  1.000 68.25539  ? 19  TYR   A C   1 
ATOM   192  O O   . TYR   A 1 22  ? 41.78926 21.08210  -3.34856  1.000 71.14476  ? 19  TYR   A O   1 
ATOM   193  C CB  . TYR   A 1 22  ? 42.36296 20.28655  -0.21409  1.000 64.39058  ? 19  TYR   A CB  1 
ATOM   194  C CG  . TYR   A 1 22  ? 41.94774 19.64158  1.08494   1.000 68.25108  ? 19  TYR   A CG  1 
ATOM   195  C CD1 . TYR   A 1 22  ? 41.86084 20.38351  2.25453   1.000 80.46000  ? 19  TYR   A CD1 1 
ATOM   196  C CD2 . TYR   A 1 22  ? 41.66285 18.28449  1.14605   1.000 76.21758  ? 19  TYR   A CD2 1 
ATOM   197  C CE1 . TYR   A 1 22  ? 41.48821 19.79421  3.44801   1.000 83.82165  ? 19  TYR   A CE1 1 
ATOM   198  C CE2 . TYR   A 1 22  ? 41.29125 17.68573  2.33390   1.000 79.40409  ? 19  TYR   A CE2 1 
ATOM   199  C CZ  . TYR   A 1 22  ? 41.20422 18.44492  3.48198   1.000 75.33511  ? 19  TYR   A CZ  1 
ATOM   200  O OH  . TYR   A 1 22  ? 40.83294 17.85225  4.66737   1.000 92.32186  ? 19  TYR   A OH  1 
ATOM   201  N N   . LYS   A 1 23  ? 42.35771 22.81527  -2.02418  1.000 76.48600  ? 20  LYS   A N   1 
ATOM   202  C CA  . LYS   A 1 23  ? 43.13529 23.51750  -3.03630  1.000 66.53839  ? 20  LYS   A CA  1 
ATOM   203  C C   . LYS   A 1 23  ? 44.61274 23.30409  -2.73539  1.000 70.41469  ? 20  LYS   A C   1 
ATOM   204  O O   . LYS   A 1 23  ? 45.09438 23.70095  -1.66917  1.000 72.52857  ? 20  LYS   A O   1 
ATOM   205  C CB  . LYS   A 1 23  ? 42.80237 25.00925  -3.06017  1.000 62.59436  ? 20  LYS   A CB  1 
ATOM   206  C CG  . LYS   A 1 23  ? 43.72331 25.82820  -3.95587  1.000 65.12308  ? 20  LYS   A CG  1 
ATOM   207  C CD  . LYS   A 1 23  ? 43.42147 27.31637  -3.86121  1.000 71.75520  ? 20  LYS   A CD  1 
ATOM   208  C CE  . LYS   A 1 23  ? 44.36417 28.13305  -4.73377  1.000 68.43099  ? 20  LYS   A CE  1 
ATOM   209  N NZ  . LYS   A 1 23  ? 44.05567 29.59008  -4.67671  1.000 74.14325  ? 20  LYS   A NZ  1 
ATOM   210  N N   . ALA   A 1 24  ? 45.32396 22.67246  -3.66448  1.000 69.55594  ? 21  ALA   A N   1 
ATOM   211  C CA  . ALA   A 1 24  ? 46.73645 22.37257  -3.49614  1.000 70.62497  ? 21  ALA   A CA  1 
ATOM   212  C C   . ALA   A 1 24  ? 47.55989 23.15500  -4.51060  1.000 78.23646  ? 21  ALA   A C   1 
ATOM   213  O O   . ALA   A 1 24  ? 47.04513 23.63463  -5.52437  1.000 71.03607  ? 21  ALA   A O   1 
ATOM   214  C CB  . ALA   A 1 24  ? 47.00961 20.87097  -3.64333  1.000 74.55716  ? 21  ALA   A CB  1 
ATOM   215  N N   . ARG   A 1 25  ? 48.85461 23.27959  -4.22419  1.000 73.25912  ? 22  ARG   A N   1 
ATOM   216  C CA  . ARG   A 1 25  ? 49.77264 24.01749  -5.08374  1.000 81.12443  ? 22  ARG   A CA  1 
ATOM   217  C C   . ARG   A 1 25  ? 51.06226 23.22678  -5.22625  1.000 86.89739  ? 22  ARG   A C   1 
ATOM   218  O O   . ARG   A 1 25  ? 51.68576 22.86913  -4.22152  1.000 89.62845  ? 22  ARG   A O   1 
ATOM   219  C CB  . ARG   A 1 25  ? 50.06226 25.41199  -4.52181  1.000 85.82878  ? 22  ARG   A CB  1 
ATOM   220  C CG  . ARG   A 1 25  ? 50.95478 26.25873  -5.41241  1.000 88.59430  ? 22  ARG   A CG  1 
ATOM   221  C CD  . ARG   A 1 25  ? 51.38815 27.53708  -4.71728  1.000 91.44154  ? 22  ARG   A CD  1 
ATOM   222  N NE  . ARG   A 1 25  ? 52.25496 27.26507  -3.57665  1.000 103.34826 ? 22  ARG   A NE  1 
ATOM   223  C CZ  . ARG   A 1 25  ? 53.56571 27.08099  -3.65832  1.000 110.53334 ? 22  ARG   A CZ  1 
ATOM   224  N NH1 . ARG   A 1 25  ? 54.19865 27.12439  -4.81934  1.000 112.21445 ? 22  ARG   A NH1 1 
ATOM   225  N NH2 . ARG   A 1 25  ? 54.25856 26.84626  -2.54723  1.000 111.42166 ? 22  ARG   A NH2 1 
ATOM   226  N N   . ASN   A 1 26  ? 51.45606 22.95522  -6.46967  1.000 95.31449  ? 23  ASN   A N   1 
ATOM   227  C CA  . ASN   A 1 26  ? 52.75115 22.34071  -6.72518  1.000 98.19394  ? 23  ASN   A CA  1 
ATOM   228  C C   . ASN   A 1 26  ? 53.86152 23.30903  -6.33996  1.000 105.91888 ? 23  ASN   A C   1 
ATOM   229  O O   . ASN   A 1 26  ? 53.89999 24.44535  -6.81842  1.000 106.76303 ? 23  ASN   A O   1 
ATOM   230  C CB  . ASN   A 1 26  ? 52.87417 21.95156  -8.19706  1.000 103.22093 ? 23  ASN   A CB  1 
ATOM   231  C CG  . ASN   A 1 26  ? 54.10882 21.12419  -8.48208  1.000 113.18666 ? 23  ASN   A CG  1 
ATOM   232  O OD1 . ASN   A 1 26  ? 55.19948 21.65917  -8.68062  1.000 106.57021 ? 23  ASN   A OD1 1 
ATOM   233  N ND2 . ASN   A 1 26  ? 53.94320 19.80723  -8.50148  1.000 110.93591 ? 23  ASN   A ND2 1 
ATOM   234  N N   . LYS   A 1 27  ? 54.76640 22.86113  -5.46607  1.000 114.68544 ? 24  LYS   A N   1 
ATOM   235  C CA  . LYS   A 1 27  ? 55.79995 23.75877  -4.95825  1.000 113.73548 ? 24  LYS   A CA  1 
ATOM   236  C C   . LYS   A 1 27  ? 56.85071 24.07672  -6.01533  1.000 120.11486 ? 24  LYS   A C   1 
ATOM   237  O O   . LYS   A 1 27  ? 57.36399 25.20050  -6.05574  1.000 121.99852 ? 24  LYS   A O   1 
ATOM   238  C CB  . LYS   A 1 27  ? 56.45827 23.15492  -3.71688  1.000 124.30331 ? 24  LYS   A CB  1 
ATOM   239  C CG  . LYS   A 1 27  ? 57.40844 24.10280  -3.00311  1.000 131.74742 ? 24  LYS   A CG  1 
ATOM   240  C CD  . LYS   A 1 27  ? 57.98638 23.47586  -1.74605  1.000 130.22125 ? 24  LYS   A CD  1 
ATOM   241  C CE  . LYS   A 1 27  ? 58.93509 24.43463  -1.04227  1.000 134.92405 ? 24  LYS   A CE  1 
ATOM   242  N NZ  . LYS   A 1 27  ? 59.52043 23.83531  0.18894   1.000 140.41164 ? 24  LYS   A NZ  1 
ATOM   243  N N   . LEU   A 1 28  ? 57.18367 23.11381  -6.87473  1.000 128.22749 ? 25  LEU   A N   1 
ATOM   244  C CA  . LEU   A 1 28  ? 58.19887 23.35140  -7.89615  1.000 127.71371 ? 25  LEU   A CA  1 
ATOM   245  C C   . LEU   A 1 28  ? 57.64208 24.16835  -9.05698  1.000 122.66924 ? 25  LEU   A C   1 
ATOM   246  O O   . LEU   A 1 28  ? 58.13130 25.26403  -9.35248  1.000 120.30588 ? 25  LEU   A O   1 
ATOM   247  C CB  . LEU   A 1 28  ? 58.76075 22.02034  -8.40355  1.000 124.61590 ? 25  LEU   A CB  1 
ATOM   248  C CG  . LEU   A 1 28  ? 59.67627 21.24669  -7.45498  1.000 127.45803 ? 25  LEU   A CG  1 
ATOM   249  C CD1 . LEU   A 1 28  ? 60.17328 19.96978  -8.11551  1.000 120.17815 ? 25  LEU   A CD1 1 
ATOM   250  C CD2 . LEU   A 1 28  ? 60.84360 22.11489  -7.01353  1.000 121.81192 ? 25  LEU   A CD2 1 
ATOM   251  N N   . THR   A 1 29  ? 56.61540 23.64572  -9.72701  1.000 113.78659 ? 26  THR   A N   1 
ATOM   252  C CA  . THR   A 1 29  ? 56.08255 24.27425  -10.92837 1.000 106.09348 ? 26  THR   A CA  1 
ATOM   253  C C   . THR   A 1 29  ? 55.15854 25.44948  -10.63727 1.000 104.51909 ? 26  THR   A C   1 
ATOM   254  O O   . THR   A 1 29  ? 54.82167 26.19130  -11.56640 1.000 100.58670 ? 26  THR   A O   1 
ATOM   255  C CB  . THR   A 1 29  ? 55.32806 23.24070  -11.76937 1.000 99.95803  ? 26  THR   A CB  1 
ATOM   256  O OG1 . THR   A 1 29  ? 54.08153 22.92721  -11.13683 1.000 103.10950 ? 26  THR   A OG1 1 
ATOM   257  C CG2 . THR   A 1 29  ? 56.14659 21.96832  -11.90020 1.000 109.07219 ? 26  THR   A CG2 1 
ATOM   258  N N   . GLY   A 1 30  ? 54.74361 25.64197  -9.38677  1.000 105.86989 ? 27  GLY   A N   1 
ATOM   259  C CA  . GLY   A 1 30  ? 53.76028 26.65642  -9.07113  1.000 102.38409 ? 27  GLY   A CA  1 
ATOM   260  C C   . GLY   A 1 30  ? 52.34963 26.32974  -9.50364  1.000 89.44959  ? 27  GLY   A C   1 
ATOM   261  O O   . GLY   A 1 30  ? 51.45983 27.17390  -9.34742  1.000 91.16707  ? 27  GLY   A O   1 
ATOM   262  N N   . GLU   A 1 31  ? 52.11699 25.13395  -10.03586 1.000 88.08777  ? 28  GLU   A N   1 
ATOM   263  C CA  . GLU   A 1 31  ? 50.79790 24.75557  -10.51953 1.000 87.50203  ? 28  GLU   A CA  1 
ATOM   264  C C   . GLU   A 1 31  ? 49.85275 24.48597  -9.35440  1.000 90.41134  ? 28  GLU   A C   1 
ATOM   265  O O   . GLU   A 1 31  ? 50.23342 23.87566  -8.35146  1.000 87.21610  ? 28  GLU   A O   1 
ATOM   266  C CB  . GLU   A 1 31  ? 50.91383 23.51852  -11.41049 1.000 91.69724  ? 28  GLU   A CB  1 
ATOM   267  C CG  . GLU   A 1 31  ? 49.61852 23.05064  -12.04459 1.000 96.62441  ? 28  GLU   A CG  1 
ATOM   268  C CD  . GLU   A 1 31  ? 49.83584 21.88531  -12.99012 1.000 104.18130 ? 28  GLU   A CD  1 
ATOM   269  O OE1 . GLU   A 1 31  ? 51.00915 21.55597  -13.26589 1.000 95.07369  ? 28  GLU   A OE1 1 
ATOM   270  O OE2 . GLU   A 1 31  ? 48.83735 21.29861  -13.45633 1.000 104.09225 ? 28  GLU   A OE2 1 
ATOM   271  N N   . VAL   A 1 32  ? 48.61243 24.94941  -9.48984  1.000 74.73012  ? 29  VAL   A N   1 
ATOM   272  C CA  . VAL   A 1 32  ? 47.57452 24.74124  -8.48786  1.000 77.34211  ? 29  VAL   A CA  1 
ATOM   273  C C   . VAL   A 1 32  ? 46.54681 23.76836  -9.04785  1.000 71.80008  ? 29  VAL   A C   1 
ATOM   274  O O   . VAL   A 1 32  ? 46.20083 23.82453  -10.23397 1.000 75.18124  ? 29  VAL   A O   1 
ATOM   275  C CB  . VAL   A 1 32  ? 46.90968 26.06697  -8.06395  1.000 71.68218  ? 29  VAL   A CB  1 
ATOM   276  C CG1 . VAL   A 1 32  ? 47.92300 26.97492  -7.38356  1.000 74.37950  ? 29  VAL   A CG1 1 
ATOM   277  C CG2 . VAL   A 1 32  ? 46.28259 26.76620  -9.26064  1.000 74.47350  ? 29  VAL   A CG2 1 
ATOM   278  N N   . VAL   A 1 33  ? 46.07694 22.85864  -8.19521  1.000 65.57376  ? 30  VAL   A N   1 
ATOM   279  C CA  . VAL   A 1 33  ? 45.06966 21.87309  -8.55938  1.000 63.79598  ? 30  VAL   A CA  1 
ATOM   280  C C   . VAL   A 1 33  ? 44.03487 21.80831  -7.44279  1.000 66.88429  ? 30  VAL   A C   1 
ATOM   281  O O   . VAL   A 1 33  ? 44.16964 22.44869  -6.39983  1.000 66.11674  ? 30  VAL   A O   1 
ATOM   282  C CB  . VAL   A 1 33  ? 45.67381 20.47491  -8.81394  1.000 63.83083  ? 30  VAL   A CB  1 
ATOM   283  C CG1 . VAL   A 1 33  ? 46.70962 20.52383  -9.93220  1.000 64.49615  ? 30  VAL   A CG1 1 
ATOM   284  C CG2 . VAL   A 1 33  ? 46.27858 19.91474  -7.53323  1.000 72.75999  ? 30  VAL   A CG2 1 
ATOM   285  N N   . ALA   A 1 34  ? 42.98908 21.02185  -7.67899  1.000 66.71382  ? 31  ALA   A N   1 
ATOM   286  C CA  . ALA   A 1 34  ? 41.97411 20.73039  -6.67598  1.000 62.29140  ? 31  ALA   A CA  1 
ATOM   287  C C   . ALA   A 1 34  ? 42.02934 19.24762  -6.33664  1.000 66.46489  ? 31  ALA   A C   1 
ATOM   288  O O   . ALA   A 1 34  ? 41.96765 18.39971  -7.23338  1.000 68.66946  ? 31  ALA   A O   1 
ATOM   289  C CB  . ALA   A 1 34  ? 40.57921 21.11467  -7.17183  1.000 64.97012  ? 31  ALA   A CB  1 
ATOM   290  N N   . LEU   A 1 35  ? 42.15151 18.93913  -5.04875  1.000 62.41395  ? 32  LEU   A N   1 
ATOM   291  C CA  . LEU   A 1 35  ? 42.30378 17.56988  -4.57215  1.000 62.60891  ? 32  LEU   A CA  1 
ATOM   292  C C   . LEU   A 1 35  ? 41.02359 17.12332  -3.88113  1.000 72.10436  ? 32  LEU   A C   1 
ATOM   293  O O   . LEU   A 1 35  ? 40.64915 17.68067  -2.84438  1.000 68.86097  ? 32  LEU   A O   1 
ATOM   294  C CB  . LEU   A 1 35  ? 43.48552 17.45393  -3.60937  1.000 69.42932  ? 32  LEU   A CB  1 
ATOM   295  C CG  . LEU   A 1 35  ? 44.89443 17.36587  -4.19204  1.000 77.77048  ? 32  LEU   A CG  1 
ATOM   296  C CD1 . LEU   A 1 35  ? 45.91637 17.43249  -3.07206  1.000 70.08763  ? 32  LEU   A CD1 1 
ATOM   297  C CD2 . LEU   A 1 35  ? 45.05892 16.08388  -4.99039  1.000 78.64166  ? 32  LEU   A CD2 1 
ATOM   298  N N   . LYS   A 1 36  ? 40.36272 16.11733  -4.44726  1.000 67.10134  ? 33  LYS   A N   1 
ATOM   299  C CA  . LYS   A 1 36  ? 39.25538 15.44916  -3.77595  1.000 72.64851  ? 33  LYS   A CA  1 
ATOM   300  C C   . LYS   A 1 36  ? 39.79289 14.21666  -3.05725  1.000 73.83339  ? 33  LYS   A C   1 
ATOM   301  O O   . LYS   A 1 36  ? 40.28201 13.28043  -3.69900  1.000 71.44814  ? 33  LYS   A O   1 
ATOM   302  C CB  . LYS   A 1 36  ? 38.15506 15.06539  -4.76447  1.000 68.84981  ? 33  LYS   A CB  1 
ATOM   303  C CG  . LYS   A 1 36  ? 37.00954 14.29392  -4.12294  1.000 73.73079  ? 33  LYS   A CG  1 
ATOM   304  C CD  . LYS   A 1 36  ? 35.66844 14.63862  -4.75277  1.000 75.67005  ? 33  LYS   A CD  1 
ATOM   305  C CE  . LYS   A 1 36  ? 35.63266 14.27846  -6.22733  1.000 77.52291  ? 33  LYS   A CE  1 
ATOM   306  N NZ  . LYS   A 1 36  ? 34.30928 14.58746  -6.83750  1.000 80.73027  ? 33  LYS   A NZ  1 
ATOM   307  N N   . LYS   A 1 37  ? 39.70560 14.22127  -1.73068  1.000 70.89817  ? 34  LYS   A N   1 
ATOM   308  C CA  . LYS   A 1 37  ? 40.25750 13.16121  -0.89810  1.000 74.81189  ? 34  LYS   A CA  1 
ATOM   309  C C   . LYS   A 1 37  ? 39.15558 12.18630  -0.50389  1.000 81.16331  ? 34  LYS   A C   1 
ATOM   310  O O   . LYS   A 1 37  ? 38.07058 12.60474  -0.08695  1.000 81.89384  ? 34  LYS   A O   1 
ATOM   311  C CB  . LYS   A 1 37  ? 40.91925 13.75121  0.34780   1.000 78.94081  ? 34  LYS   A CB  1 
ATOM   312  C CG  . LYS   A 1 37  ? 41.56613 12.72777  1.26095   1.000 85.05973  ? 34  LYS   A CG  1 
ATOM   313  C CD  . LYS   A 1 37  ? 42.28756 13.40856  2.41097   1.000 86.98713  ? 34  LYS   A CD  1 
ATOM   314  C CE  . LYS   A 1 37  ? 42.94891 12.39543  3.32778   1.000 87.48562  ? 34  LYS   A CE  1 
ATOM   315  N NZ  . LYS   A 1 37  ? 43.72881 13.05727  4.40937   1.000 88.74197  ? 34  LYS   A NZ  1 
ATOM   316  N N   . ILE   A 1 38  ? 39.43591 10.89190  -0.63743  1.000 76.18329  ? 35  ILE   A N   1 
ATOM   317  C CA  . ILE   A 1 38  ? 38.48459 9.83318   -0.31417  1.000 79.84376  ? 35  ILE   A CA  1 
ATOM   318  C C   . ILE   A 1 38  ? 39.15250 8.90335   0.68807   1.000 88.32597  ? 35  ILE   A C   1 
ATOM   319  O O   . ILE   A 1 38  ? 40.10787 8.19313   0.34718   1.000 93.87433  ? 35  ILE   A O   1 
ATOM   320  C CB  . ILE   A 1 38  ? 38.02872 9.06136   -1.55969  1.000 80.62578  ? 35  ILE   A CB  1 
ATOM   321  C CG1 . ILE   A 1 38  ? 37.33098 9.99877   -2.54655  1.000 76.48525  ? 35  ILE   A CG1 1 
ATOM   322  C CG2 . ILE   A 1 38  ? 37.10574 7.91871   -1.16695  1.000 81.10496  ? 35  ILE   A CG2 1 
ATOM   323  C CD1 . ILE   A 1 38  ? 36.86220 9.31317   -3.81084  1.000 66.51358  ? 35  ILE   A CD1 1 
ATOM   324  N N   . ARG   A 1 39  ? 38.65474 8.90674   1.92272   1.000 83.21490  ? 36  ARG   A N   1 
ATOM   325  C CA  . ARG   A 1 39  ? 39.17521 8.03532   2.97203   1.000 86.57820  ? 36  ARG   A CA  1 
ATOM   326  C C   . ARG   A 1 39  ? 38.60806 6.63690   2.76059   1.000 85.49776  ? 36  ARG   A C   1 
ATOM   327  O O   . ARG   A 1 39  ? 37.41150 6.40853   2.96624   1.000 90.53567  ? 36  ARG   A O   1 
ATOM   328  C CB  . ARG   A 1 39  ? 38.80660 8.58353   4.34851   1.000 96.01015  ? 36  ARG   A CB  1 
ATOM   329  C CG  . ARG   A 1 39  ? 39.12765 10.05894  4.53115   1.000 98.43132  ? 36  ARG   A CG  1 
ATOM   330  C CD  . ARG   A 1 39  ? 38.39104 10.64193  5.72585   1.000 99.28436  ? 36  ARG   A CD  1 
ATOM   331  N NE  . ARG   A 1 39  ? 39.29503 11.02964  6.80202   1.000 105.88252 ? 36  ARG   A NE  1 
ATOM   332  C CZ  . ARG   A 1 39  ? 39.70016 10.21910  7.77011   1.000 111.38631 ? 36  ARG   A CZ  1 
ATOM   333  N NH1 . ARG   A 1 39  ? 39.31224 8.95532   7.82093   1.000 110.57038 ? 36  ARG   A NH1 1 
ATOM   334  N NH2 . ARG   A 1 39  ? 40.51488 10.68855  8.71123   1.000 109.92337 ? 36  ARG   A NH2 1 
ATOM   335  N N   . LEU   A 1 40  ? 39.45852 5.69943   2.33842   1.000 88.59393  ? 37  LEU   A N   1 
ATOM   336  C CA  . LEU   A 1 40  ? 38.96264 4.37251   1.99357   1.000 92.82568  ? 37  LEU   A CA  1 
ATOM   337  C C   . LEU   A 1 40  ? 38.72985 3.50999   3.22553   1.000 91.83570  ? 37  LEU   A C   1 
ATOM   338  O O   . LEU   A 1 40  ? 37.91995 2.57764   3.17653   1.000 94.63233  ? 37  LEU   A O   1 
ATOM   339  C CB  . LEU   A 1 40  ? 39.93841 3.67245   1.04493   1.000 91.24564  ? 37  LEU   A CB  1 
ATOM   340  C CG  . LEU   A 1 40  ? 40.14624 4.33780   -0.32036  1.000 84.26776  ? 37  LEU   A CG  1 
ATOM   341  C CD1 . LEU   A 1 40  ? 41.22046 3.60713   -1.10090  1.000 87.58279  ? 37  LEU   A CD1 1 
ATOM   342  C CD2 . LEU   A 1 40  ? 38.84476 4.38479   -1.10372  1.000 76.58863  ? 37  LEU   A CD2 1 
ATOM   343  N N   . ASP   A 1 41  ? 39.42984 3.79409   4.32833   1.000 92.10681  ? 38  ASP   A N   1 
ATOM   344  C CA  . ASP   A 1 41  ? 39.25007 3.01801   5.54918   1.000 93.07141  ? 38  ASP   A CA  1 
ATOM   345  C C   . ASP   A 1 41  ? 37.86697 3.20355   6.16298   1.000 88.92584  ? 38  ASP   A C   1 
ATOM   346  O O   . ASP   A 1 41  ? 37.43597 2.35807   6.95368   1.000 87.27668  ? 38  ASP   A O   1 
ATOM   347  C CB  . ASP   A 1 41  ? 40.33681 3.38636   6.55987   1.000 99.59673  ? 38  ASP   A CB  1 
ATOM   348  C CG  . ASP   A 1 41  ? 40.50974 4.88694   6.71788   1.000 101.31491 ? 38  ASP   A CG  1 
ATOM   349  O OD1 . ASP   A 1 41  ? 39.99039 5.64739   5.87615   1.000 103.10796 ? 38  ASP   A OD1 1 
ATOM   350  O OD2 . ASP   A 1 41  ? 41.16697 5.30533   7.69488   1.000 105.05868 ? 38  ASP   A OD2 1 
ATOM   351  N N   . THR   A 1 42  ? 37.16450 4.27916   5.81673   1.000 88.99098  ? 39  THR   A N   1 
ATOM   352  C CA  . THR   A 1 42  ? 35.81886 4.53329   6.30982   1.000 86.14917  ? 39  THR   A CA  1 
ATOM   353  C C   . THR   A 1 42  ? 34.73582 4.07180   5.34294   1.000 96.44801  ? 39  THR   A C   1 
ATOM   354  O O   . THR   A 1 42  ? 33.54954 4.26834   5.62379   1.000 82.94511  ? 39  THR   A O   1 
ATOM   355  C CB  . THR   A 1 42  ? 35.64098 6.02667   6.60357   1.000 92.14328  ? 39  THR   A CB  1 
ATOM   356  O OG1 . THR   A 1 42  ? 35.59478 6.75645   5.37133   1.000 98.14050  ? 39  THR   A OG1 1 
ATOM   357  C CG2 . THR   A 1 42  ? 36.79880 6.54384   7.43848   1.000 92.86022  ? 39  THR   A CG2 1 
ATOM   358  N N   . GLU   A 1 43  ? 35.11105 3.46286   4.22145   1.000 90.67743  ? 40  GLU   A N   1 
ATOM   359  C CA  . GLU   A 1 43  ? 34.17020 3.00778   3.20138   1.000 89.35381  ? 40  GLU   A CA  1 
ATOM   360  C C   . GLU   A 1 43  ? 34.09763 1.48580   3.26798   1.000 92.26600  ? 40  GLU   A C   1 
ATOM   361  O O   . GLU   A 1 43  ? 35.00779 0.79152   2.80562   1.000 88.12869  ? 40  GLU   A O   1 
ATOM   362  C CB  . GLU   A 1 43  ? 34.60169 3.48549   1.81865   1.000 87.19241  ? 40  GLU   A CB  1 
ATOM   363  C CG  . GLU   A 1 43  ? 34.77289 4.99144   1.70138   1.000 88.81311  ? 40  GLU   A CG  1 
ATOM   364  C CD  . GLU   A 1 43  ? 33.45508 5.73774   1.76096   1.000 93.24888  ? 40  GLU   A CD  1 
ATOM   365  O OE1 . GLU   A 1 43  ? 32.41616 5.14245   1.40622   1.000 92.09584  ? 40  GLU   A OE1 1 
ATOM   366  O OE2 . GLU   A 1 43  ? 33.45851 6.92014   2.16283   1.000 95.69313  ? 40  GLU   A OE2 1 
ATOM   367  N N   . THR   A 1 44  ? 33.00878 0.97060   3.84555   1.000 90.43479  ? 41  THR   A N   1 
ATOM   368  C CA  . THR   A 1 44  ? 32.83526 -0.47567  3.93683   1.000 97.97868  ? 41  THR   A CA  1 
ATOM   369  C C   . THR   A 1 44  ? 32.66732 -1.11273  2.56373   1.000 97.86882  ? 41  THR   A C   1 
ATOM   370  O O   . THR   A 1 44  ? 33.02919 -2.27940  2.37567   1.000 95.64871  ? 41  THR   A O   1 
ATOM   371  C CB  . THR   A 1 44  ? 31.63287 -0.81295  4.81966   1.000 94.67159  ? 41  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 44  ? 30.48925 -0.07369  4.37538   1.000 100.73147 ? 41  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 44  ? 31.92138 -0.46663  6.26617   1.000 101.20846 ? 41  THR   A CG2 1 
ATOM   374  N N   . GLU   A 1 45  ? 32.12451 -0.37250  1.59902   1.000 83.81165  ? 42  GLU   A N   1 
ATOM   375  C CA  . GLU   A 1 45  ? 31.89636 -0.88344  0.25619   1.000 85.42112  ? 42  GLU   A CA  1 
ATOM   376  C C   . GLU   A 1 45  ? 33.03710 -0.55350  -0.69964  1.000 84.48991  ? 42  GLU   A C   1 
ATOM   377  O O   . GLU   A 1 45  ? 32.83264 -0.55711  -1.91884  1.000 85.82382  ? 42  GLU   A O   1 
ATOM   378  C CB  . GLU   A 1 45  ? 30.57367 -0.34333  -0.29174  1.000 82.71434  ? 42  GLU   A CB  1 
ATOM   379  C CG  . GLU   A 1 45  ? 29.37044 -0.68950  0.57082   1.000 96.08496  ? 42  GLU   A CG  1 
ATOM   380  C CD  . GLU   A 1 45  ? 29.18164 -2.18481  0.72837   1.000 100.49628 ? 42  GLU   A CD  1 
ATOM   381  O OE1 . GLU   A 1 45  ? 29.28781 -2.90522  -0.28587  1.000 94.06244  ? 42  GLU   A OE1 1 
ATOM   382  O OE2 . GLU   A 1 45  ? 28.93809 -2.64057  1.86528   1.000 100.98958 ? 42  GLU   A OE2 1 
ATOM   383  N N   . GLY   A 1 46  ? 34.22984 -0.27330  -0.17606  1.000 85.87879  ? 43  GLY   A N   1 
ATOM   384  C CA  . GLY   A 1 46  ? 35.35111 0.05207   -1.03456  1.000 79.20758  ? 43  GLY   A CA  1 
ATOM   385  C C   . GLY   A 1 46  ? 35.19586 1.42006   -1.67633  1.000 76.88369  ? 43  GLY   A C   1 
ATOM   386  O O   . GLY   A 1 46  ? 34.58535 2.33652   -1.11946  1.000 83.27202  ? 43  GLY   A O   1 
ATOM   387  N N   . VAL   A 1 47  ? 35.76444 1.55670   -2.87013  1.000 75.05927  ? 44  VAL   A N   1 
ATOM   388  C CA  . VAL   A 1 47  ? 35.65135 2.82627   -3.59618  1.000 73.65326  ? 44  VAL   A CA  1 
ATOM   389  C C   . VAL   A 1 47  ? 34.18050 3.11078   -3.87516  1.000 72.23569  ? 44  VAL   A C   1 
ATOM   390  O O   . VAL   A 1 47  ? 33.47215 2.23589   -4.41199  1.000 67.07037  ? 44  VAL   A O   1 
ATOM   391  C CB  . VAL   A 1 47  ? 36.45986 2.77575   -4.90283  1.000 68.90872  ? 44  VAL   A CB  1 
ATOM   392  C CG1 . VAL   A 1 47  ? 36.47847 4.14263   -5.56852  1.000 71.93461  ? 44  VAL   A CG1 1 
ATOM   393  C CG2 . VAL   A 1 47  ? 37.87346 2.29221   -4.63022  1.000 63.71089  ? 44  VAL   A CG2 1 
ATOM   394  N N   . PRO   A 1 48  ? 33.66641 4.29029   -3.52543  1.000 68.63018  ? 45  PRO   A N   1 
ATOM   395  C CA  . PRO   A 1 48  ? 32.23548 4.55719   -3.71308  1.000 63.38135  ? 45  PRO   A CA  1 
ATOM   396  C C   . PRO   A 1 48  ? 31.83266 4.46652   -5.17690  1.000 70.21872  ? 45  PRO   A C   1 
ATOM   397  O O   . PRO   A 1 48  ? 32.61563 4.76655   -6.08098  1.000 68.12307  ? 45  PRO   A O   1 
ATOM   398  C CB  . PRO   A 1 48  ? 32.06547 5.98296   -3.17313  1.000 66.52770  ? 45  PRO   A CB  1 
ATOM   399  C CG  . PRO   A 1 48  ? 33.22720 6.18246   -2.25396  1.000 70.75376  ? 45  PRO   A CG  1 
ATOM   400  C CD  . PRO   A 1 48  ? 34.35614 5.40479   -2.85513  1.000 72.57151  ? 45  PRO   A CD  1 
ATOM   401  N N   . SER   A 1 49  ? 30.58817 4.03407   -5.39948  1.000 66.21154  ? 46  SER   A N   1 
ATOM   402  C CA  . SER   A 1 49  ? 30.08125 3.89551   -6.76113  1.000 63.93583  ? 46  SER   A CA  1 
ATOM   403  C C   . SER   A 1 49  ? 30.09083 5.23171   -7.49132  1.000 66.58373  ? 46  SER   A C   1 
ATOM   404  O O   . SER   A 1 49  ? 30.36067 5.28791   -8.69673  1.000 63.24433  ? 46  SER   A O   1 
ATOM   405  C CB  . SER   A 1 49  ? 28.67164 3.30660   -6.73636  1.000 65.07869  ? 46  SER   A CB  1 
ATOM   406  O OG  . SER   A 1 49  ? 27.78261 4.15093   -6.02779  1.000 87.46198  ? 46  SER   A OG  1 
ATOM   407  N N   . THR   A 1 50  ? 29.80075 6.32030   -6.77576  1.000 59.34527  ? 47  THR   A N   1 
ATOM   408  C CA  . THR   A 1 50  ? 29.87187 7.64475   -7.38153  1.000 66.29204  ? 47  THR   A CA  1 
ATOM   409  C C   . THR   A 1 50  ? 31.30346 8.02102   -7.74343  1.000 61.24686  ? 47  THR   A C   1 
ATOM   410  O O   . THR   A 1 50  ? 31.52168 8.78135   -8.69355  1.000 61.45163  ? 47  THR   A O   1 
ATOM   411  C CB  . THR   A 1 50  ? 29.27281 8.68545   -6.43618  1.000 63.53498  ? 47  THR   A CB  1 
ATOM   412  O OG1 . THR   A 1 50  ? 29.98412 8.66459   -5.19203  1.000 62.53147  ? 47  THR   A OG1 1 
ATOM   413  C CG2 . THR   A 1 50  ? 27.80279 8.38148   -6.18075  1.000 75.18613  ? 47  THR   A CG2 1 
ATOM   414  N N   . ALA   A 1 51  ? 32.28710 7.50570   -7.00354  1.000 58.73644  ? 48  ALA   A N   1 
ATOM   415  C CA  . ALA   A 1 51  ? 33.68065 7.79135   -7.32411  1.000 60.53033  ? 48  ALA   A CA  1 
ATOM   416  C C   . ALA   A 1 51  ? 34.14242 7.00575   -8.54554  1.000 64.53631  ? 48  ALA   A C   1 
ATOM   417  O O   . ALA   A 1 51  ? 34.85249 7.54540   -9.40116  1.000 60.78276  ? 48  ALA   A O   1 
ATOM   418  C CB  . ALA   A 1 51  ? 34.57201 7.48484   -6.11997  1.000 59.85163  ? 48  ALA   A CB  1 
ATOM   419  N N   . ILE   A 1 52  ? 33.74661 5.73453   -8.64541  1.000 65.50292  ? 49  ILE   A N   1 
ATOM   420  C CA  . ILE   A 1 52  ? 34.14100 4.92378   -9.79326  1.000 65.41049  ? 49  ILE   A CA  1 
ATOM   421  C C   . ILE   A 1 52  ? 33.49712 5.45414   -11.06800 1.000 59.43360  ? 49  ILE   A C   1 
ATOM   422  O O   . ILE   A 1 52  ? 34.12056 5.46156   -12.13705 1.000 60.08790  ? 49  ILE   A O   1 
ATOM   423  C CB  . ILE   A 1 52  ? 33.78666 3.44448   -9.55497  1.000 62.34418  ? 49  ILE   A CB  1 
ATOM   424  C CG1 . ILE   A 1 52  ? 34.27553 2.98995   -8.18083  1.000 66.33508  ? 49  ILE   A CG1 1 
ATOM   425  C CG2 . ILE   A 1 52  ? 34.40313 2.56981   -10.63299 1.000 68.66432  ? 49  ILE   A CG2 1 
ATOM   426  C CD1 . ILE   A 1 52  ? 33.98480 1.53485   -7.87948  1.000 67.22229  ? 49  ILE   A CD1 1 
ATOM   427  N N   . ARG   A 1 53  ? 32.24271 5.90580   -10.97741 1.000 63.25187  ? 50  ARG   A N   1 
ATOM   428  C CA  . ARG   A 1 53  ? 31.56194 6.45338   -12.14730 1.000 61.95778  ? 50  ARG   A CA  1 
ATOM   429  C C   . ARG   A 1 53  ? 32.23553 7.73135   -12.63062 1.000 60.03666  ? 50  ARG   A C   1 
ATOM   430  O O   . ARG   A 1 53  ? 32.54812 7.86962   -13.81819 1.000 61.25433  ? 50  ARG   A O   1 
ATOM   431  C CB  . ARG   A 1 53  ? 30.09168 6.72269   -11.82881 1.000 66.34513  ? 50  ARG   A CB  1 
ATOM   432  C CG  . ARG   A 1 53  ? 29.21563 5.48724   -11.72907 1.000 76.97526  ? 50  ARG   A CG  1 
ATOM   433  C CD  . ARG   A 1 53  ? 27.76967 5.88699   -11.48148 1.000 84.78888  ? 50  ARG   A CD  1 
ATOM   434  N NE  . ARG   A 1 53  ? 26.87887 4.74133   -11.34286 1.000 77.68251  ? 50  ARG   A NE  1 
ATOM   435  C CZ  . ARG   A 1 53  ? 25.57613 4.83360   -11.11300 1.000 83.42168  ? 50  ARG   A CZ  1 
ATOM   436  N NH1 . ARG   A 1 53  ? 24.97747 6.00739   -10.99427 1.000 69.97348  ? 50  ARG   A NH1 1 
ATOM   437  N NH2 . ARG   A 1 53  ? 24.85634 3.72066   -10.99884 1.000 75.48989  ? 50  ARG   A NH2 1 
ATOM   438  N N   . GLU   A 1 54  ? 32.46491 8.68155   -11.71919 1.000 54.83175  ? 51  GLU   A N   1 
ATOM   439  C CA  . GLU   A 1 54  ? 33.01181 9.97602   -12.11714 1.000 60.46952  ? 51  GLU   A CA  1 
ATOM   440  C C   . GLU   A 1 54  ? 34.40397 9.83707   -12.72102 1.000 60.94692  ? 51  GLU   A C   1 
ATOM   441  O O   . GLU   A 1 54  ? 34.72787 10.50854  -13.70742 1.000 61.99506  ? 51  GLU   A O   1 
ATOM   442  C CB  . GLU   A 1 54  ? 33.04327 10.92685  -10.92042 1.000 63.96422  ? 51  GLU   A CB  1 
ATOM   443  C CG  . GLU   A 1 54  ? 33.66002 12.28080  -11.24000 1.000 62.22504  ? 51  GLU   A CG  1 
ATOM   444  C CD  . GLU   A 1 54  ? 33.51292 13.28333  -10.11401 1.000 69.41207  ? 51  GLU   A CD  1 
ATOM   445  O OE1 . GLU   A 1 54  ? 33.30424 12.86258  -8.95694  1.000 80.07902  ? 51  GLU   A OE1 1 
ATOM   446  O OE2 . GLU   A 1 54  ? 33.60276 14.49723  -10.39193 1.000 75.50792  ? 51  GLU   A OE2 1 
ATOM   447  N N   . ILE   A 1 55  ? 35.24346 8.97591   -12.14221 1.000 60.59989  ? 52  ILE   A N   1 
ATOM   448  C CA  . ILE   A 1 55  ? 36.60247 8.80703   -12.65359 1.000 64.51963  ? 52  ILE   A CA  1 
ATOM   449  C C   . ILE   A 1 55  ? 36.57361 8.25767   -14.07529 1.000 64.00593  ? 52  ILE   A C   1 
ATOM   450  O O   . ILE   A 1 55  ? 37.23779 8.78282   -14.97714 1.000 61.64598  ? 52  ILE   A O   1 
ATOM   451  C CB  . ILE   A 1 55  ? 37.42171 7.90025   -11.71812 1.000 61.98433  ? 52  ILE   A CB  1 
ATOM   452  C CG1 . ILE   A 1 55  ? 37.66674 8.59311   -10.37632 1.000 58.30039  ? 52  ILE   A CG1 1 
ATOM   453  C CG2 . ILE   A 1 55  ? 38.73917 7.51867   -12.37063 1.000 67.21836  ? 52  ILE   A CG2 1 
ATOM   454  C CD1 . ILE   A 1 55  ? 38.34770 7.71120   -9.35375  1.000 62.08831  ? 52  ILE   A CD1 1 
ATOM   455  N N   . SER   A 1 56  ? 35.80003 7.19129   -14.29624 1.000 58.68440  ? 53  SER   A N   1 
ATOM   456  C CA  . SER   A 1 56  ? 35.76486 6.56286   -15.61310 1.000 63.83546  ? 53  SER   A CA  1 
ATOM   457  C C   . SER   A 1 56  ? 35.14614 7.48782   -16.65290 1.000 64.46964  ? 53  SER   A C   1 
ATOM   458  O O   . SER   A 1 56  ? 35.60909 7.53941   -17.79799 1.000 65.70746  ? 53  SER   A O   1 
ATOM   459  C CB  . SER   A 1 56  ? 34.99735 5.24238   -15.54726 1.000 68.86711  ? 53  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 56  ? 33.63269 5.46436   -15.23628 1.000 72.83230  ? 53  SER   A OG  1 
ATOM   461  N N   . LEU   A 1 57  ? 34.10322 8.22857   -16.27422 1.000 60.26715  ? 54  LEU   A N   1 
ATOM   462  C CA  . LEU   A 1 57  ? 33.46669 9.14542   -17.21507 1.000 63.79121  ? 54  LEU   A CA  1 
ATOM   463  C C   . LEU   A 1 57  ? 34.39235 10.30224  -17.57430 1.000 62.21707  ? 54  LEU   A C   1 
ATOM   464  O O   . LEU   A 1 57  ? 34.51275 10.66953  -18.74767 1.000 62.42130  ? 54  LEU   A O   1 
ATOM   465  C CB  . LEU   A 1 57  ? 32.15348 9.67207   -16.63406 1.000 51.95893  ? 54  LEU   A CB  1 
ATOM   466  C CG  . LEU   A 1 57  ? 31.00597 8.67355   -16.48021 1.000 62.92718  ? 54  LEU   A CG  1 
ATOM   467  C CD1 . LEU   A 1 57  ? 29.78934 9.33723   -15.85169 1.000 58.61437  ? 54  LEU   A CD1 1 
ATOM   468  C CD2 . LEU   A 1 57  ? 30.65225 8.05670   -17.82285 1.000 57.42417  ? 54  LEU   A CD2 1 
ATOM   469  N N   . LEU   A 1 58  ? 35.05616 10.89096  -16.57450 1.000 60.18964  ? 55  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 58  ? 35.89765 12.05674  -16.82768 1.000 62.21998  ? 55  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 58  ? 37.17960 11.68878  -17.56402 1.000 65.27553  ? 55  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 58  ? 37.74975 12.53365  -18.26278 1.000 70.67406  ? 55  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 58  ? 36.21828 12.76866  -15.51307 1.000 58.81054  ? 55  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 58  ? 35.05101 13.53714  -14.89161 1.000 62.62932  ? 55  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 58  ? 35.50962 14.30397  -13.66610 1.000 56.91891  ? 55  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 58  ? 34.43042 14.47504  -15.91476 1.000 63.88958  ? 55  LEU   A CD2 1 
ATOM   477  N N   . LYS   A 1 59  ? 37.65062 10.44723  -17.42630 1.000 62.79949  ? 56  LYS   A N   1 
ATOM   478  C CA  . LYS   A 1 59  ? 38.81777 10.02037  -18.18822 1.000 67.23150  ? 56  LYS   A CA  1 
ATOM   479  C C   . LYS   A 1 59  ? 38.51797 9.84920   -19.67010 1.000 74.24511  ? 56  LYS   A C   1 
ATOM   480  O O   . LYS   A 1 59  ? 39.45198 9.64969   -20.45394 1.000 83.82765  ? 56  LYS   A O   1 
ATOM   481  C CB  . LYS   A 1 59  ? 39.38266 8.71786   -17.61943 1.000 73.40150  ? 56  LYS   A CB  1 
ATOM   482  C CG  . LYS   A 1 59  ? 40.33563 8.92143   -16.45307 1.000 71.82486  ? 56  LYS   A CG  1 
ATOM   483  C CD  . LYS   A 1 59  ? 41.19019 7.68703   -16.21376 1.000 80.50188  ? 56  LYS   A CD  1 
ATOM   484  C CE  . LYS   A 1 59  ? 42.27507 7.95849   -15.18384 1.000 74.93090  ? 56  LYS   A CE  1 
ATOM   485  N NZ  . LYS   A 1 59  ? 43.16539 9.08025   -15.59496 1.000 77.18803  ? 56  LYS   A NZ  1 
ATOM   486  N N   . GLU   A 1 60  ? 37.24891 9.92342   -20.07023 1.000 72.84069  ? 57  GLU   A N   1 
ATOM   487  C CA  . GLU   A 1 60  ? 36.86878 9.88583   -21.47576 1.000 73.34168  ? 57  GLU   A CA  1 
ATOM   488  C C   . GLU   A 1 60  ? 36.07820 11.11946  -21.89336 1.000 67.76459  ? 57  GLU   A C   1 
ATOM   489  O O   . GLU   A 1 60  ? 35.56040 11.15943  -23.01560 1.000 71.41628  ? 57  GLU   A O   1 
ATOM   490  C CB  . GLU   A 1 60  ? 36.06626 8.61671   -21.77731 1.000 80.04175  ? 57  GLU   A CB  1 
ATOM   491  C CG  . GLU   A 1 60  ? 36.82058 7.33068   -21.47659 1.000 84.74144  ? 57  GLU   A CG  1 
ATOM   492  C CD  . GLU   A 1 60  ? 36.07256 6.09178   -21.92649 1.000 96.27938  ? 57  GLU   A CD  1 
ATOM   493  O OE1 . GLU   A 1 60  ? 34.90042 6.21799   -22.33744 1.000 97.30688  ? 57  GLU   A OE1 1 
ATOM   494  O OE2 . GLU   A 1 60  ? 36.65951 4.99088   -21.87129 1.000 94.55489  ? 57  GLU   A OE2 1 
ATOM   495  N N   . LEU   A 1 61  ? 35.96689 12.12274  -21.02159 1.000 62.57414  ? 58  LEU   A N   1 
ATOM   496  C CA  . LEU   A 1 61  ? 35.28343 13.36564  -21.35897 1.000 65.40897  ? 58  LEU   A CA  1 
ATOM   497  C C   . LEU   A 1 61  ? 36.24677 14.54348  -21.29884 1.000 70.06196  ? 58  LEU   A C   1 
ATOM   498  O O   . LEU   A 1 61  ? 36.07385 15.45234  -20.48048 1.000 74.64514  ? 58  LEU   A O   1 
ATOM   499  C CB  . LEU   A 1 61  ? 34.09864 13.60849  -20.41895 1.000 69.21796  ? 58  LEU   A CB  1 
ATOM   500  C CG  . LEU   A 1 61  ? 32.86993 12.71243  -20.58237 1.000 61.21027  ? 58  LEU   A CG  1 
ATOM   501  C CD1 . LEU   A 1 61  ? 31.77003 13.13796  -19.62172 1.000 55.52313  ? 58  LEU   A CD1 1 
ATOM   502  C CD2 . LEU   A 1 61  ? 32.37379 12.74109  -22.01604 1.000 56.85593  ? 58  LEU   A CD2 1 
ATOM   503  N N   . ASN   A 1 62  ? 37.26465 14.53896  -22.15416 1.000 66.25025  ? 59  ASN   A N   1 
ATOM   504  C CA  . ASN   A 1 62  ? 38.22787 15.63314  -22.21449 1.000 69.41354  ? 59  ASN   A CA  1 
ATOM   505  C C   . ASN   A 1 62  ? 37.67079 16.71369  -23.13649 1.000 59.69210  ? 59  ASN   A C   1 
ATOM   506  O O   . ASN   A 1 62  ? 37.52701 16.49560  -24.34433 1.000 64.34557  ? 59  ASN   A O   1 
ATOM   507  C CB  . ASN   A 1 62  ? 39.58396 15.12963  -22.70124 1.000 72.12629  ? 59  ASN   A CB  1 
ATOM   508  C CG  . ASN   A 1 62  ? 40.70532 16.11236  -22.42719 1.000 83.03295  ? 59  ASN   A CG  1 
ATOM   509  O OD1 . ASN   A 1 62  ? 41.27631 16.12983  -21.33581 1.000 94.09779  ? 59  ASN   A OD1 1 
ATOM   510  N ND2 . ASN   A 1 62  ? 41.03319 16.93007  -23.41999 1.000 84.46420  ? 59  ASN   A ND2 1 
ATOM   511  N N   . HIS   A 1 63  ? 37.35650 17.87683  -22.56941 1.000 59.87905  ? 60  HIS   A N   1 
ATOM   512  C CA  . HIS   A 1 63  ? 36.73792 18.96702  -23.31057 1.000 64.82687  ? 60  HIS   A CA  1 
ATOM   513  C C   . HIS   A 1 63  ? 37.10839 20.27893  -22.63918 1.000 57.16249  ? 60  HIS   A C   1 
ATOM   514  O O   . HIS   A 1 63  ? 37.26948 20.31926  -21.41333 1.000 56.63273  ? 60  HIS   A O   1 
ATOM   515  C CB  . HIS   A 1 63  ? 35.20959 18.80801  -23.36941 1.000 60.10198  ? 60  HIS   A CB  1 
ATOM   516  C CG  . HIS   A 1 63  ? 34.53435 19.76813  -24.29981 1.000 59.34097  ? 60  HIS   A CG  1 
ATOM   517  N ND1 . HIS   A 1 63  ? 34.00231 20.96664  -23.87574 1.000 57.91494  ? 60  HIS   A ND1 1 
ATOM   518  C CD2 . HIS   A 1 63  ? 34.31088 19.70955  -25.63420 1.000 58.77459  ? 60  HIS   A CD2 1 
ATOM   519  C CE1 . HIS   A 1 63  ? 33.47826 21.60382  -24.90770 1.000 65.15207  ? 60  HIS   A CE1 1 
ATOM   520  N NE2 . HIS   A 1 63  ? 33.65206 20.86244  -25.98671 1.000 59.83748  ? 60  HIS   A NE2 1 
ATOM   521  N N   . PRO   A 1 64  ? 37.26475 21.36182  -23.40710 1.000 61.74525  ? 61  PRO   A N   1 
ATOM   522  C CA  . PRO   A 1 64  ? 37.64545 22.64797  -22.79797 1.000 55.83695  ? 61  PRO   A CA  1 
ATOM   523  C C   . PRO   A 1 64  ? 36.63349 23.19473  -21.80475 1.000 66.13731  ? 61  PRO   A C   1 
ATOM   524  O O   . PRO   A 1 64  ? 37.00519 24.02683  -20.96839 1.000 59.49177  ? 61  PRO   A O   1 
ATOM   525  C CB  . PRO   A 1 64  ? 37.79107 23.57844  -24.01008 1.000 61.66754  ? 61  PRO   A CB  1 
ATOM   526  C CG  . PRO   A 1 64  ? 38.10081 22.66653  -25.14640 1.000 59.22253  ? 61  PRO   A CG  1 
ATOM   527  C CD  . PRO   A 1 64  ? 37.32680 21.40996  -24.87814 1.000 54.83363  ? 61  PRO   A CD  1 
ATOM   528  N N   . ASN   A 1 65  ? 35.37118 22.76916  -21.86577 1.000 62.13684  ? 62  ASN   A N   1 
ATOM   529  C CA  . ASN   A 1 65  ? 34.34610 23.26037  -20.95292 1.000 58.15405  ? 62  ASN   A CA  1 
ATOM   530  C C   . ASN   A 1 65  ? 33.93534 22.21457  -19.92123 1.000 56.31090  ? 62  ASN   A C   1 
ATOM   531  O O   . ASN   A 1 65  ? 32.82826 22.28312  -19.37838 1.000 54.49957  ? 62  ASN   A O   1 
ATOM   532  C CB  . ASN   A 1 65  ? 33.12785 23.75079  -21.73570 1.000 55.65415  ? 62  ASN   A CB  1 
ATOM   533  C CG  . ASN   A 1 65  ? 33.47614 24.85315  -22.71811 1.000 60.93798  ? 62  ASN   A CG  1 
ATOM   534  O OD1 . ASN   A 1 65  ? 33.54699 24.62276  -23.92490 1.000 66.51526  ? 62  ASN   A OD1 1 
ATOM   535  N ND2 . ASN   A 1 65  ? 33.70897 26.05712  -22.20282 1.000 58.86492  ? 62  ASN   A ND2 1 
ATOM   536  N N   . ILE   A 1 66  ? 34.80754 21.25176  -19.63641 1.000 60.56039  ? 63  ILE   A N   1 
ATOM   537  C CA  . ILE   A 1 66  ? 34.58701 20.26235  -18.58988 1.000 56.14657  ? 63  ILE   A CA  1 
ATOM   538  C C   . ILE   A 1 66  ? 35.81384 20.25762  -17.69084 1.000 54.77619  ? 63  ILE   A C   1 
ATOM   539  O O   . ILE   A 1 66  ? 36.94403 20.17212  -18.18397 1.000 63.14980  ? 63  ILE   A O   1 
ATOM   540  C CB  . ILE   A 1 66  ? 34.33241 18.85775  -19.16948 1.000 53.37829  ? 63  ILE   A CB  1 
ATOM   541  C CG1 . ILE   A 1 66  ? 33.10500 18.86759  -20.08265 1.000 54.49851  ? 63  ILE   A CG1 1 
ATOM   542  C CG2 . ILE   A 1 66  ? 34.15834 17.84404  -18.04972 1.000 52.29366  ? 63  ILE   A CG2 1 
ATOM   543  C CD1 . ILE   A 1 66  ? 32.77343 17.51638  -20.68014 1.000 63.57508  ? 63  ILE   A CD1 1 
ATOM   544  N N   . VAL   A 1 67  ? 35.59487 20.36292  -16.37833 1.000 57.02086  ? 64  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 67  ? 36.71139 20.37893  -15.43787 1.000 56.15152  ? 64  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 67  ? 37.46350 19.06123  -15.54440 1.000 61.59693  ? 64  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 67  ? 36.89050 17.98208  -15.34901 1.000 63.65128  ? 64  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 67  ? 36.21828 20.63461  -14.01127 1.000 58.20615  ? 64  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 67  ? 37.39490 20.66067  -13.04158 1.000 57.53930  ? 64  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 67  ? 35.44442 21.94048  -13.94660 1.000 54.33981  ? 64  VAL   A CG2 1 
ATOM   551  N N   . LYS   A 1 68  ? 38.75323 19.14384  -15.85680 1.000 58.39977  ? 65  LYS   A N   1 
ATOM   552  C CA  . LYS   A 1 68  ? 39.52844 17.95980  -16.19180 1.000 64.78636  ? 65  LYS   A CA  1 
ATOM   553  C C   . LYS   A 1 68  ? 39.94195 17.19060  -14.94481 1.000 60.55945  ? 65  LYS   A C   1 
ATOM   554  O O   . LYS   A 1 68  ? 40.31077 17.77731  -13.92260 1.000 64.80602  ? 65  LYS   A O   1 
ATOM   555  C CB  . LYS   A 1 68  ? 40.77561 18.34387  -16.98917 1.000 70.31096  ? 65  LYS   A CB  1 
ATOM   556  C CG  . LYS   A 1 68  ? 40.50283 19.16489  -18.23859 1.000 74.82722  ? 65  LYS   A CG  1 
ATOM   557  C CD  . LYS   A 1 68  ? 41.41553 18.76486  -19.39576 1.000 78.40460  ? 65  LYS   A CD  1 
ATOM   558  C CE  . LYS   A 1 68  ? 42.87352 18.64399  -18.96893 1.000 90.05250  ? 65  LYS   A CE  1 
ATOM   559  N NZ  . LYS   A 1 68  ? 43.26584 17.23601  -18.66496 1.000 97.42117  ? 65  LYS   A NZ  1 
ATOM   560  N N   . LEU   A 1 69  ? 39.87749 15.86578  -15.04108 1.000 60.80073  ? 66  LEU   A N   1 
ATOM   561  C CA  . LEU   A 1 69  ? 40.49481 14.97901  -14.06470 1.000 65.23123  ? 66  LEU   A CA  1 
ATOM   562  C C   . LEU   A 1 69  ? 41.92534 14.70230  -14.51209 1.000 68.56902  ? 66  LEU   A C   1 
ATOM   563  O O   . LEU   A 1 69  ? 42.14503 14.15177  -15.59671 1.000 69.75977  ? 66  LEU   A O   1 
ATOM   564  C CB  . LEU   A 1 69  ? 39.70491 13.67733  -13.93208 1.000 65.83707  ? 66  LEU   A CB  1 
ATOM   565  C CG  . LEU   A 1 69  ? 40.32696 12.58760  -13.05541 1.000 63.76932  ? 66  LEU   A CG  1 
ATOM   566  C CD1 . LEU   A 1 69  ? 40.45168 13.05927  -11.61492 1.000 61.17218  ? 66  LEU   A CD1 1 
ATOM   567  C CD2 . LEU   A 1 69  ? 39.52068 11.29777  -13.13886 1.000 67.51523  ? 66  LEU   A CD2 1 
ATOM   568  N N   . LEU   A 1 70  ? 42.89435 15.08784  -13.68318 1.000 69.02067  ? 67  LEU   A N   1 
ATOM   569  C CA  . LEU   A 1 70  ? 44.29679 15.00481  -14.07156 1.000 67.75179  ? 67  LEU   A CA  1 
ATOM   570  C C   . LEU   A 1 70  ? 44.94432 13.68358  -13.67366 1.000 66.94464  ? 67  LEU   A C   1 
ATOM   571  O O   . LEU   A 1 70  ? 45.71833 13.12003  -14.45466 1.000 76.33860  ? 67  LEU   A O   1 
ATOM   572  C CB  . LEU   A 1 70  ? 45.07755 16.17147  -13.46166 1.000 75.96927  ? 67  LEU   A CB  1 
ATOM   573  C CG  . LEU   A 1 70  ? 44.58196 17.56492  -13.85342 1.000 71.82367  ? 67  LEU   A CG  1 
ATOM   574  C CD1 . LEU   A 1 70  ? 45.45347 18.64203  -13.22898 1.000 69.70668  ? 67  LEU   A CD1 1 
ATOM   575  C CD2 . LEU   A 1 70  ? 44.54129 17.71168  -15.36718 1.000 76.95473  ? 67  LEU   A CD2 1 
ATOM   576  N N   . ASP   A 1 71  ? 44.64780 13.17244  -12.48053 1.000 69.87348  ? 68  ASP   A N   1 
ATOM   577  C CA  . ASP   A 1 71  ? 45.28534 11.94970  -12.01261 1.000 76.24207  ? 68  ASP   A CA  1 
ATOM   578  C C   . ASP   A 1 71  ? 44.44226 11.34040  -10.90214 1.000 73.38796  ? 68  ASP   A C   1 
ATOM   579  O O   . ASP   A 1 71  ? 43.62908 12.01817  -10.26889 1.000 71.65942  ? 68  ASP   A O   1 
ATOM   580  C CB  . ASP   A 1 71  ? 46.71415 12.21993  -11.52416 1.000 81.54021  ? 68  ASP   A CB  1 
ATOM   581  C CG  . ASP   A 1 71  ? 47.55668 10.96084  -11.45242 1.000 84.72822  ? 68  ASP   A CG  1 
ATOM   582  O OD1 . ASP   A 1 71  ? 47.11053 9.91364   -11.96564 1.000 80.71348  ? 68  ASP   A OD1 1 
ATOM   583  O OD2 . ASP   A 1 71  ? 48.66593 11.01913  -10.88082 1.000 89.65161  ? 68  ASP   A OD2 1 
ATOM   584  N N   . VAL   A 1 72  ? 44.64473 10.04418  -10.68079 1.000 72.02239  ? 69  VAL   A N   1 
ATOM   585  C CA  . VAL   A 1 72  ? 43.99378 9.30522   -9.60229  1.000 71.03923  ? 69  VAL   A CA  1 
ATOM   586  C C   . VAL   A 1 72  ? 45.10053 8.57911   -8.84916  1.000 79.42464  ? 69  VAL   A C   1 
ATOM   587  O O   . VAL   A 1 72  ? 45.59329 7.54155   -9.30600  1.000 75.33220  ? 69  VAL   A O   1 
ATOM   588  C CB  . VAL   A 1 72  ? 42.93512 8.32100   -10.11190 1.000 72.67930  ? 69  VAL   A CB  1 
ATOM   589  C CG1 . VAL   A 1 72  ? 42.29813 7.58192   -8.94346  1.000 65.38147  ? 69  VAL   A CG1 1 
ATOM   590  C CG2 . VAL   A 1 72  ? 41.87895 9.04735   -10.93125 1.000 66.73356  ? 69  VAL   A CG2 1 
ATOM   591  N N   . ILE   A 1 73  ? 45.49716 9.11839   -7.69887  1.000 80.02871  ? 70  ILE   A N   1 
ATOM   592  C CA  . ILE   A 1 73  ? 46.57893 8.55997   -6.89574  1.000 77.47114  ? 70  ILE   A CA  1 
ATOM   593  C C   . ILE   A 1 73  ? 45.97774 7.82832   -5.70462  1.000 79.74850  ? 70  ILE   A C   1 
ATOM   594  O O   . ILE   A 1 73  ? 45.10877 8.36664   -5.00644  1.000 82.42658  ? 70  ILE   A O   1 
ATOM   595  C CB  . ILE   A 1 73  ? 47.55515 9.65489   -6.43299  1.000 87.10348  ? 70  ILE   A CB  1 
ATOM   596  C CG1 . ILE   A 1 73  ? 47.94876 10.54922  -7.61002  1.000 82.78293  ? 70  ILE   A CG1 1 
ATOM   597  C CG2 . ILE   A 1 73  ? 48.79426 9.02953   -5.81308  1.000 78.31725  ? 70  ILE   A CG2 1 
ATOM   598  C CD1 . ILE   A 1 73  ? 48.88296 11.67873  -7.23440  1.000 94.60957  ? 70  ILE   A CD1 1 
ATOM   599  N N   . HIS   A 1 74  ? 46.43991 6.60340   -5.47154  1.000 77.65075  ? 71  HIS   A N   1 
ATOM   600  C CA  . HIS   A 1 74  ? 45.99725 5.78166   -4.35216  1.000 90.78677  ? 71  HIS   A CA  1 
ATOM   601  C C   . HIS   A 1 74  ? 47.18010 5.54096   -3.42528  1.000 92.40253  ? 71  HIS   A C   1 
ATOM   602  O O   . HIS   A 1 74  ? 48.21700 5.02768   -3.86029  1.000 97.38866  ? 71  HIS   A O   1 
ATOM   603  C CB  . HIS   A 1 74  ? 45.41820 4.45377   -4.83993  1.000 80.89781  ? 71  HIS   A CB  1 
ATOM   604  C CG  . HIS   A 1 74  ? 45.22432 3.44458   -3.75121  1.000 85.68312  ? 71  HIS   A CG  1 
ATOM   605  N ND1 . HIS   A 1 74  ? 45.74931 2.17173   -3.81342  1.000 89.32987  ? 71  HIS   A ND1 1 
ATOM   606  C CD2 . HIS   A 1 74  ? 44.56957 3.52365   -2.56863  1.000 87.10264  ? 71  HIS   A CD2 1 
ATOM   607  C CE1 . HIS   A 1 74  ? 45.42163 1.50839   -2.71889  1.000 89.80658  ? 71  HIS   A CE1 1 
ATOM   608  N NE2 . HIS   A 1 74  ? 44.70620 2.30629   -1.94690  1.000 92.46179  ? 71  HIS   A NE2 1 
ATOM   609  N N   . THR   A 1 75  ? 47.02277 5.90681   -2.15431  1.000 96.15368  ? 72  THR   A N   1 
ATOM   610  C CA  . THR   A 1 75  ? 48.09854 5.75524   -1.18545  1.000 101.58365 ? 72  THR   A CA  1 
ATOM   611  C C   . THR   A 1 75  ? 47.53079 5.83739   0.22587   1.000 100.39351 ? 72  THR   A C   1 
ATOM   612  O O   . THR   A 1 75  ? 46.68178 6.68599   0.51066   1.000 96.45021  ? 72  THR   A O   1 
ATOM   613  C CB  . THR   A 1 75  ? 49.18439 6.82305   -1.38801  1.000 104.67618 ? 72  THR   A CB  1 
ATOM   614  O OG1 . THR   A 1 75  ? 50.10561 6.79092   -0.29107  1.000 114.42706 ? 72  THR   A OG1 1 
ATOM   615  C CG2 . THR   A 1 75  ? 48.56862 8.21378   -1.49773  1.000 94.28647  ? 72  THR   A CG2 1 
ATOM   616  N N   . GLU   A 1 76  ? 47.99979 4.93598   1.09418   1.000 106.16428 ? 73  GLU   A N   1 
ATOM   617  C CA  . GLU   A 1 76  ? 47.70717 4.97302   2.53019   1.000 115.90691 ? 73  GLU   A CA  1 
ATOM   618  C C   . GLU   A 1 76  ? 46.21053 4.85387   2.81044   1.000 111.26623 ? 73  GLU   A C   1 
ATOM   619  O O   . GLU   A 1 76  ? 45.66455 5.56906   3.65249   1.000 108.88757 ? 73  GLU   A O   1 
ATOM   620  C CB  . GLU   A 1 76  ? 48.27148 6.24186   3.17364   1.000 121.30620 ? 73  GLU   A CB  1 
ATOM   621  C CG  . GLU   A 1 76  ? 49.75102 6.46526   2.91829   1.000 127.19807 ? 73  GLU   A CG  1 
ATOM   622  C CD  . GLU   A 1 76  ? 50.20246 7.86080   3.30343   1.000 134.75121 ? 73  GLU   A CD  1 
ATOM   623  O OE1 . GLU   A 1 76  ? 49.33380 8.70274   3.61478   1.000 133.83574 ? 73  GLU   A OE1 1 
ATOM   624  O OE2 . GLU   A 1 76  ? 51.42553 8.11609   3.29307   1.000 140.09758 ? 73  GLU   A OE2 1 
ATOM   625  N N   . ASN   A 1 77  ? 45.54241 3.93564   2.10850   1.000 97.66167  ? 74  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 77  ? 44.09312 3.75625   2.23285   1.000 102.34555 ? 74  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 77  ? 43.34634 5.05361   1.93264   1.000 93.13143  ? 74  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 77  ? 42.26179 5.30406   2.46351   1.000 89.05924  ? 74  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 77  ? 43.70903 3.21769   3.61475   1.000 97.96025  ? 74  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 77  ? 43.71616 1.70373   3.67399   1.000 110.44303 ? 74  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 77  ? 44.71051 1.08944   4.05785   1.000 114.60729 ? 74  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 77  ? 42.59720 1.09321   3.30100   1.000 93.15982  ? 74  ASN   A ND2 1 
ATOM   633  N N   . LYS   A 1 78  ? 43.93713 5.89465   1.08516   1.000 92.31019  ? 75  LYS   A N   1 
ATOM   634  C CA  . LYS   A 1 78  ? 43.31436 7.12205   0.61297   1.000 90.56355  ? 75  LYS   A CA  1 
ATOM   635  C C   . LYS   A 1 78  ? 43.34909 7.14393   -0.90650  1.000 90.96347  ? 75  LYS   A C   1 
ATOM   636  O O   . LYS   A 1 78  ? 44.30628 6.66594   -1.52273  1.000 87.30052  ? 75  LYS   A O   1 
ATOM   637  C CB  . LYS   A 1 78  ? 44.01184 8.37203   1.17100   1.000 96.31309  ? 75  LYS   A CB  1 
ATOM   638  C CG  . LYS   A 1 78  ? 43.41818 8.89423   2.47021   1.000 85.51604  ? 75  LYS   A CG  1 
ATOM   639  C CD  . LYS   A 1 78  ? 44.14794 8.34846   3.68239   1.000 101.53554 ? 75  LYS   A CD  1 
ATOM   640  C CE  . LYS   A 1 78  ? 45.60000 8.79950   3.69484   1.000 107.54728 ? 75  LYS   A CE  1 
ATOM   641  N NZ  . LYS   A 1 78  ? 45.72653 10.28324  3.73133   1.000 103.02428 ? 75  LYS   A NZ  1 
ATOM   642  N N   . LEU   A 1 79  ? 42.29508 7.69062   -1.50421  1.000 87.88389  ? 76  LEU   A N   1 
ATOM   643  C CA  . LEU   A 1 79  ? 42.18639 7.83003   -2.95168  1.000 81.23522  ? 76  LEU   A CA  1 
ATOM   644  C C   . LEU   A 1 79  ? 42.10193 9.31670   -3.26848  1.000 77.04665  ? 76  LEU   A C   1 
ATOM   645  O O   . LEU   A 1 79  ? 41.11656 9.97496   -2.91806  1.000 80.18601  ? 76  LEU   A O   1 
ATOM   646  C CB  . LEU   A 1 79  ? 40.96906 7.07759   -3.48611  1.000 73.86046  ? 76  LEU   A CB  1 
ATOM   647  C CG  . LEU   A 1 79  ? 40.92157 6.86539   -4.99979  1.000 76.64753  ? 76  LEU   A CG  1 
ATOM   648  C CD1 . LEU   A 1 79  ? 42.10353 6.02098   -5.45156  1.000 74.96215  ? 76  LEU   A CD1 1 
ATOM   649  C CD2 . LEU   A 1 79  ? 39.60482 6.22764   -5.41919  1.000 70.46724  ? 76  LEU   A CD2 1 
ATOM   650  N N   . TYR   A 1 80  ? 43.13551 9.84498   -3.91674  1.000 77.18853  ? 77  TYR   A N   1 
ATOM   651  C CA  . TYR   A 1 80  ? 43.20949 11.25831  -4.25978  1.000 76.25822  ? 77  TYR   A CA  1 
ATOM   652  C C   . TYR   A 1 80  ? 42.85222 11.45766  -5.72584  1.000 76.03287  ? 77  TYR   A C   1 
ATOM   653  O O   . TYR   A 1 80  ? 43.45128 10.83275  -6.60719  1.000 77.15024  ? 77  TYR   A O   1 
ATOM   654  C CB  . TYR   A 1 80  ? 44.60614 11.81444  -3.98038  1.000 78.86526  ? 77  TYR   A CB  1 
ATOM   655  C CG  . TYR   A 1 80  ? 44.89677 12.03398  -2.51469  1.000 85.41764  ? 77  TYR   A CG  1 
ATOM   656  C CD1 . TYR   A 1 80  ? 44.51140 13.20793  -1.88149  1.000 87.05349  ? 77  TYR   A CD1 1 
ATOM   657  C CD2 . TYR   A 1 80  ? 45.55874 11.07109  -1.76402  1.000 94.36670  ? 77  TYR   A CD2 1 
ATOM   658  C CE1 . TYR   A 1 80  ? 44.77479 13.41741  -0.54133  1.000 87.49114  ? 77  TYR   A CE1 1 
ATOM   659  C CE2 . TYR   A 1 80  ? 45.82700 11.27161  -0.42189  1.000 93.22843  ? 77  TYR   A CE2 1 
ATOM   660  C CZ  . TYR   A 1 80  ? 45.43287 12.44638  0.18401   1.000 93.67197  ? 77  TYR   A CZ  1 
ATOM   661  O OH  . TYR   A 1 80  ? 45.69808 12.65024  1.51930   1.000 103.62813 ? 77  TYR   A OH  1 
ATOM   662  N N   . LEU   A 1 81  ? 41.87961 12.32745  -5.97954  1.000 72.75902  ? 78  LEU   A N   1 
ATOM   663  C CA  . LEU   A 1 81  ? 41.48189 12.70812  -7.32857  1.000 71.66964  ? 78  LEU   A CA  1 
ATOM   664  C C   . LEU   A 1 81  ? 41.99280 14.11706  -7.59391  1.000 71.47019  ? 78  LEU   A C   1 
ATOM   665  O O   . LEU   A 1 81  ? 41.59036 15.06384  -6.90928  1.000 70.92186  ? 78  LEU   A O   1 
ATOM   666  C CB  . LEU   A 1 81  ? 39.96338 12.64439  -7.50027  1.000 71.06681  ? 78  LEU   A CB  1 
ATOM   667  C CG  . LEU   A 1 81  ? 39.27547 11.28873  -7.69192  1.000 70.74346  ? 78  LEU   A CG  1 
ATOM   668  C CD1 . LEU   A 1 81  ? 39.32111 10.44026  -6.42763  1.000 64.14635  ? 78  LEU   A CD1 1 
ATOM   669  C CD2 . LEU   A 1 81  ? 37.83852 11.49309  -8.14682  1.000 70.91507  ? 78  LEU   A CD2 1 
ATOM   670  N N   . VAL   A 1 82  ? 42.87717 14.25247  -8.57729  1.000 62.14008  ? 79  VAL   A N   1 
ATOM   671  C CA  . VAL   A 1 82  ? 43.50529 15.52740  -8.90446  1.000 61.74651  ? 79  VAL   A CA  1 
ATOM   672  C C   . VAL   A 1 82  ? 42.72194 16.16821  -10.04171 1.000 68.56784  ? 79  VAL   A C   1 
ATOM   673  O O   . VAL   A 1 82  ? 42.64464 15.61270  -11.14444 1.000 67.03705  ? 79  VAL   A O   1 
ATOM   674  C CB  . VAL   A 1 82  ? 44.98297 15.34368  -9.28366  1.000 71.30354  ? 79  VAL   A CB  1 
ATOM   675  C CG1 . VAL   A 1 82  ? 45.66381 16.69483  -9.43808  1.000 62.32920  ? 79  VAL   A CG1 1 
ATOM   676  C CG2 . VAL   A 1 82  ? 45.69657 14.49312  -8.24244  1.000 70.05753  ? 79  VAL   A CG2 1 
ATOM   677  N N   . PHE   A 1 83  ? 42.14841 17.33815  -9.77860  1.000 64.33506  ? 80  PHE   A N   1 
ATOM   678  C CA  . PHE   A 1 83  ? 41.32885 18.05447  -10.74235 1.000 61.58438  ? 80  PHE   A CA  1 
ATOM   679  C C   . PHE   A 1 83  ? 41.98766 19.36442  -11.15263 1.000 62.66904  ? 80  PHE   A C   1 
ATOM   680  O O   . PHE   A 1 83  ? 42.84763 19.90643  -10.45307 1.000 66.24562  ? 80  PHE   A O   1 
ATOM   681  C CB  . PHE   A 1 83  ? 39.93913 18.35674  -10.17157 1.000 63.48938  ? 80  PHE   A CB  1 
ATOM   682  C CG  . PHE   A 1 83  ? 39.06063 17.15232  -10.02789 1.000 60.72786  ? 80  PHE   A CG  1 
ATOM   683  C CD1 . PHE   A 1 83  ? 38.28222 16.71889  -11.08686 1.000 64.86283  ? 80  PHE   A CD1 1 
ATOM   684  C CD2 . PHE   A 1 83  ? 38.99683 16.46376  -8.82823  1.000 67.46016  ? 80  PHE   A CD2 1 
ATOM   685  C CE1 . PHE   A 1 83  ? 37.46523 15.61312  -10.95573 1.000 61.27680  ? 80  PHE   A CE1 1 
ATOM   686  C CE2 . PHE   A 1 83  ? 38.18049 15.35903  -8.69129  1.000 64.42187  ? 80  PHE   A CE2 1 
ATOM   687  C CZ  . PHE   A 1 83  ? 37.41469 14.93238  -9.75651  1.000 60.69435  ? 80  PHE   A CZ  1 
ATOM   688  N N   . GLU   A 1 84  ? 41.56076 19.86654  -12.30823 1.000 66.22193  ? 81  GLU   A N   1 
ATOM   689  C CA  . GLU   A 1 84  ? 41.86840 21.23483  -12.69653 1.000 57.03899  ? 81  GLU   A CA  1 
ATOM   690  C C   . GLU   A 1 84  ? 41.21369 22.20411  -11.71936 1.000 63.93712  ? 81  GLU   A C   1 
ATOM   691  O O   . GLU   A 1 84  ? 40.11459 21.95389  -11.21733 1.000 59.86452  ? 81  GLU   A O   1 
ATOM   692  C CB  . GLU   A 1 84  ? 41.37469 21.48853  -14.12266 1.000 62.66817  ? 81  GLU   A CB  1 
ATOM   693  C CG  . GLU   A 1 84  ? 41.49968 22.91889  -14.61419 1.000 74.23080  ? 81  GLU   A CG  1 
ATOM   694  C CD  . GLU   A 1 84  ? 40.74777 23.14480  -15.91157 1.000 71.95863  ? 81  GLU   A CD  1 
ATOM   695  O OE1 . GLU   A 1 84  ? 39.92357 22.28016  -16.27752 1.000 65.32905  ? 81  GLU   A OE1 1 
ATOM   696  O OE2 . GLU   A 1 84  ? 40.97881 24.18343  -16.56443 1.000 79.87738  ? 81  GLU   A OE2 1 
ATOM   697  N N   . PHE   A 1 85  ? 41.89408 23.31300  -11.44132 1.000 59.57660  ? 82  PHE   A N   1 
ATOM   698  C CA  . PHE   A 1 85  ? 41.42426 24.28166  -10.45981 1.000 61.88071  ? 82  PHE   A CA  1 
ATOM   699  C C   . PHE   A 1 85  ? 40.82974 25.50530  -11.14581 1.000 60.86362  ? 82  PHE   A C   1 
ATOM   700  O O   . PHE   A 1 85  ? 41.41093 26.04188  -12.09493 1.000 64.34944  ? 82  PHE   A O   1 
ATOM   701  C CB  . PHE   A 1 85  ? 42.55211 24.70939  -9.51934  1.000 62.38091  ? 82  PHE   A CB  1 
ATOM   702  C CG  . PHE   A 1 85  ? 42.15290 25.79467  -8.55799  1.000 63.32102  ? 82  PHE   A CG  1 
ATOM   703  C CD1 . PHE   A 1 85  ? 41.37727 25.50443  -7.44668  1.000 58.24062  ? 82  PHE   A CD1 1 
ATOM   704  C CD2 . PHE   A 1 85  ? 42.54613 27.10564  -8.77006  1.000 59.51883  ? 82  PHE   A CD2 1 
ATOM   705  C CE1 . PHE   A 1 85  ? 41.00222 26.50211  -6.56383  1.000 66.69544  ? 82  PHE   A CE1 1 
ATOM   706  C CE2 . PHE   A 1 85  ? 42.17442 28.10766  -7.89102  1.000 65.38165  ? 82  PHE   A CE2 1 
ATOM   707  C CZ  . PHE   A 1 85  ? 41.40213 27.80600  -6.78726  1.000 59.28399  ? 82  PHE   A CZ  1 
ATOM   708  N N   . LEU   A 1 86  ? 39.66968 25.93633  -10.65714 1.000 59.93092  ? 83  LEU   A N   1 
ATOM   709  C CA  . LEU   A 1 86  ? 39.03768 27.18342  -11.05573 1.000 59.16371  ? 83  LEU   A CA  1 
ATOM   710  C C   . LEU   A 1 86  ? 38.65421 27.94096  -9.79256  1.000 58.69072  ? 83  LEU   A C   1 
ATOM   711  O O   . LEU   A 1 86  ? 38.28479 27.34102  -8.77908  1.000 56.59133  ? 83  LEU   A O   1 
ATOM   712  C CB  . LEU   A 1 86  ? 37.80837 26.94785  -11.94359 1.000 62.47386  ? 83  LEU   A CB  1 
ATOM   713  C CG  . LEU   A 1 86  ? 38.06057 26.28105  -13.30060 1.000 70.77935  ? 83  LEU   A CG  1 
ATOM   714  C CD1 . LEU   A 1 86  ? 38.01622 24.76173  -13.19571 1.000 63.46219  ? 83  LEU   A CD1 1 
ATOM   715  C CD2 . LEU   A 1 86  ? 37.06936 26.78186  -14.33845 1.000 49.68266  ? 83  LEU   A CD2 1 
ATOM   716  N N   . HIS   A 1 87  ? 38.73995 29.26818  -9.85983  1.000 61.82327  ? 84  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 87  ? 38.75806 30.06819  -8.64221  1.000 61.44842  ? 84  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 87  ? 37.37461 30.39037  -8.08910  1.000 64.07173  ? 84  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 87  ? 37.28561 30.85815  -6.94896  1.000 66.28355  ? 84  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 87  ? 39.51938 31.37140  -8.88868  1.000 56.55361  ? 84  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 87  ? 38.67903 32.45849  -9.48167  1.000 63.43840  ? 84  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 87  ? 38.08588 32.35122  -10.72140 1.000 66.43481  ? 84  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 87  ? 38.33243 33.67666  -9.00273  1.000 70.67674  ? 84  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 87  ? 37.40977 33.45642  -10.98004 1.000 66.39956  ? 84  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 87  ? 37.54329 34.27675  -9.95326  1.000 78.29024  ? 84  HIS   A NE2 1 
ATOM   726  N N   . GLN   A 1 88  ? 36.30087 30.15762  -8.84074  1.000 63.10344  ? 85  GLN   A N   1 
ATOM   727  C CA  . GLN   A 1 88  ? 34.98440 30.56348  -8.36715  1.000 58.68838  ? 85  GLN   A CA  1 
ATOM   728  C C   . GLN   A 1 88  ? 33.90866 29.76190  -9.08452  1.000 59.34534  ? 85  GLN   A C   1 
ATOM   729  O O   . GLN   A 1 88  ? 34.06903 29.38343  -10.24740 1.000 57.95785  ? 85  GLN   A O   1 
ATOM   730  C CB  . GLN   A 1 88  ? 34.76159 32.06712  -8.57916  1.000 61.97613  ? 85  GLN   A CB  1 
ATOM   731  C CG  . GLN   A 1 88  ? 33.54149 32.63321  -7.86877  1.000 66.75224  ? 85  GLN   A CG  1 
ATOM   732  C CD  . GLN   A 1 88  ? 33.51399 34.14890  -7.87889  1.000 76.77700  ? 85  GLN   A CD  1 
ATOM   733  O OE1 . GLN   A 1 88  ? 33.67264 34.79088  -6.84050  1.000 86.42717  ? 85  GLN   A OE1 1 
ATOM   734  N NE2 . GLN   A 1 88  ? 33.31084 34.72955  -9.05573  1.000 73.55563  ? 85  GLN   A NE2 1 
ATOM   735  N N   . ASP   A 1 89  ? 32.81600 29.50250  -8.37124  1.000 56.48617  ? 86  ASP   A N   1 
ATOM   736  C CA  . ASP   A 1 89  ? 31.63796 28.88371  -8.95554  1.000 57.01816  ? 86  ASP   A CA  1 
ATOM   737  C C   . ASP   A 1 89  ? 30.67436 29.96390  -9.44089  1.000 62.89702  ? 86  ASP   A C   1 
ATOM   738  O O   . ASP   A 1 89  ? 30.79992 31.14309  -9.10185  1.000 60.58978  ? 86  ASP   A O   1 
ATOM   739  C CB  . ASP   A 1 89  ? 30.95682 27.95467  -7.94872  1.000 60.48600  ? 86  ASP   A CB  1 
ATOM   740  C CG  . ASP   A 1 89  ? 30.45692 28.68735  -6.71799  1.000 65.37886  ? 86  ASP   A CG  1 
ATOM   741  O OD1 . ASP   A 1 89  ? 29.37922 29.31485  -6.79143  1.000 64.05764  ? 86  ASP   A OD1 1 
ATOM   742  O OD2 . ASP   A 1 89  ? 31.14155 28.63257  -5.67527  1.000 91.28164  ? 86  ASP   A OD2 1 
ATOM   743  N N   . LEU   A 1 90  ? 29.69678 29.54654  -10.24944 1.000 58.21933  ? 87  LEU   A N   1 
ATOM   744  C CA  . LEU   A 1 90  ? 28.79163 30.51456  -10.86162 1.000 62.81056  ? 87  LEU   A CA  1 
ATOM   745  C C   . LEU   A 1 90  ? 27.89178 31.17694  -9.82439  1.000 58.59175  ? 87  LEU   A C   1 
ATOM   746  O O   . LEU   A 1 90  ? 27.63378 32.38290  -9.90727  1.000 63.77092  ? 87  LEU   A O   1 
ATOM   747  C CB  . LEU   A 1 90  ? 27.95374 29.84317  -11.94946 1.000 53.43733  ? 87  LEU   A CB  1 
ATOM   748  C CG  . LEU   A 1 90  ? 27.01790 30.77512  -12.72533 1.000 51.90254  ? 87  LEU   A CG  1 
ATOM   749  C CD1 . LEU   A 1 90  ? 27.81160 31.81554  -13.50801 1.000 60.39664  ? 87  LEU   A CD1 1 
ATOM   750  C CD2 . LEU   A 1 90  ? 26.09804 29.98379  -13.64568 1.000 57.95180  ? 87  LEU   A CD2 1 
ATOM   751  N N   . LYS   A 1 91  ? 27.41178 30.41207  -8.83840  1.000 59.82421  ? 88  LYS   A N   1 
ATOM   752  C CA  . LYS   A 1 91  ? 26.50257 30.97181  -7.84012  1.000 56.54373  ? 88  LYS   A CA  1 
ATOM   753  C C   . LYS   A 1 91  ? 27.15360 32.12196  -7.08174  1.000 60.33068  ? 88  LYS   A C   1 
ATOM   754  O O   . LYS   A 1 91  ? 26.53111 33.16766  -6.86299  1.000 61.80648  ? 88  LYS   A O   1 
ATOM   755  C CB  . LYS   A 1 91  ? 26.04381 29.88556  -6.86707  1.000 63.73540  ? 88  LYS   A CB  1 
ATOM   756  C CG  . LYS   A 1 91  ? 25.00013 30.37292  -5.87346  1.000 54.99816  ? 88  LYS   A CG  1 
ATOM   757  C CD  . LYS   A 1 91  ? 25.34713 29.96515  -4.45123  1.000 77.62092  ? 88  LYS   A CD  1 
ATOM   758  C CE  . LYS   A 1 91  ? 24.62390 28.69459  -4.04710  1.000 85.54059  ? 88  LYS   A CE  1 
ATOM   759  N NZ  . LYS   A 1 91  ? 24.96771 28.27216  -2.66139  1.000 80.98234  ? 88  LYS   A NZ  1 
ATOM   760  N N   . LYS   A 1 92  ? 28.40855 31.94199  -6.66377  1.000 58.29558  ? 89  LYS   A N   1 
ATOM   761  C CA  . LYS   A 1 92  ? 29.12807 33.02234  -5.99801  1.000 59.13953  ? 89  LYS   A CA  1 
ATOM   762  C C   . LYS   A 1 92  ? 29.33627 34.20722  -6.93220  1.000 65.05607  ? 89  LYS   A C   1 
ATOM   763  O O   . LYS   A 1 92  ? 29.35853 35.35940  -6.48360  1.000 59.69419  ? 89  LYS   A O   1 
ATOM   764  C CB  . LYS   A 1 92  ? 30.46843 32.50276  -5.47767  1.000 72.22179  ? 89  LYS   A CB  1 
ATOM   765  C CG  . LYS   A 1 92  ? 31.20475 33.44502  -4.54588  1.000 78.91778  ? 89  LYS   A CG  1 
ATOM   766  C CD  . LYS   A 1 92  ? 32.55565 32.85722  -4.16604  1.000 81.93338  ? 89  LYS   A CD  1 
ATOM   767  C CE  . LYS   A 1 92  ? 33.24747 33.66892  -3.08380  1.000 90.24343  ? 89  LYS   A CE  1 
ATOM   768  N NZ  . LYS   A 1 92  ? 34.57560 33.08325  -2.74632  1.000 93.70658  ? 89  LYS   A NZ  1 
ATOM   769  N N   . PHE   A 1 93  ? 29.48071 33.94400  -8.23214  1.000 63.08930  ? 90  PHE   A N   1 
ATOM   770  C CA  . PHE   A 1 93  ? 29.64233 35.02322  -9.19984  1.000 61.31789  ? 90  PHE   A CA  1 
ATOM   771  C C   . PHE   A 1 93  ? 28.32918 35.76124  -9.42945  1.000 62.42351  ? 90  PHE   A C   1 
ATOM   772  O O   . PHE   A 1 93  ? 28.31643 36.99049  -9.56219  1.000 62.24297  ? 90  PHE   A O   1 
ATOM   773  C CB  . PHE   A 1 93  ? 30.18641 34.45865  -10.51164 1.000 64.88799  ? 90  PHE   A CB  1 
ATOM   774  C CG  . PHE   A 1 93  ? 30.30058 35.47275  -11.61295 1.000 62.15226  ? 90  PHE   A CG  1 
ATOM   775  C CD1 . PHE   A 1 93  ? 31.33977 36.38783  -11.62396 1.000 62.43464  ? 90  PHE   A CD1 1 
ATOM   776  C CD2 . PHE   A 1 93  ? 29.37779 35.49971  -12.64716 1.000 62.11959  ? 90  PHE   A CD2 1 
ATOM   777  C CE1 . PHE   A 1 93  ? 31.45277 37.31966  -12.64032 1.000 61.43705  ? 90  PHE   A CE1 1 
ATOM   778  C CE2 . PHE   A 1 93  ? 29.48375 36.42946  -13.66761 1.000 70.82093  ? 90  PHE   A CE2 1 
ATOM   779  C CZ  . PHE   A 1 93  ? 30.52415 37.34055  -13.66410 1.000 65.82628  ? 90  PHE   A CZ  1 
ATOM   780  N N   . MET   A 1 94  ? 27.21433 35.02894  -9.48094  1.000 60.70429  ? 91  MET   A N   1 
ATOM   781  C CA  . MET   A 1 94  ? 25.91479 35.67330  -9.64192  1.000 63.75209  ? 91  MET   A CA  1 
ATOM   782  C C   . MET   A 1 94  ? 25.54765 36.49066  -8.40942  1.000 59.64539  ? 91  MET   A C   1 
ATOM   783  O O   . MET   A 1 94  ? 24.94987 37.56713  -8.52710  1.000 62.83268  ? 91  MET   A O   1 
ATOM   784  C CB  . MET   A 1 94  ? 24.84330 34.62279  -9.93019  1.000 61.35624  ? 91  MET   A CB  1 
ATOM   785  C CG  . MET   A 1 94  ? 25.16052 33.73863  -11.12326 1.000 70.34922  ? 91  MET   A CG  1 
ATOM   786  S SD  . MET   A 1 94  ? 24.15361 32.24583  -11.18463 1.000 84.93191  ? 91  MET   A SD  1 
ATOM   787  C CE  . MET   A 1 94  ? 22.65034 32.90781  -11.87890 1.000 65.94576  ? 91  MET   A CE  1 
ATOM   788  N N   . ASP   A 1 95  ? 25.89584 35.99577  -7.21852  1.000 60.02401  ? 92  ASP   A N   1 
ATOM   789  C CA  . ASP   A 1 95  ? 25.62476 36.74983  -5.99854  1.000 68.50216  ? 92  ASP   A CA  1 
ATOM   790  C C   . ASP   A 1 95  ? 26.44807 38.03049  -5.94991  1.000 63.52440  ? 92  ASP   A C   1 
ATOM   791  O O   . ASP   A 1 95  ? 25.94057 39.08811  -5.55830  1.000 64.81353  ? 92  ASP   A O   1 
ATOM   792  C CB  . ASP   A 1 95  ? 25.90349 35.88414  -4.76953  1.000 66.39702  ? 92  ASP   A CB  1 
ATOM   793  C CG  . ASP   A 1 95  ? 24.92794 34.73243  -4.63358  1.000 70.79964  ? 92  ASP   A CG  1 
ATOM   794  O OD1 . ASP   A 1 95  ? 23.98395 34.65429  -5.44672  1.000 73.03308  ? 92  ASP   A OD1 1 
ATOM   795  O OD2 . ASP   A 1 95  ? 25.10603 33.90550  -3.71425  1.000 71.97190  ? 92  ASP   A OD2 1 
ATOM   796  N N   . ALA   A 1 96  ? 27.71900 37.95660  -6.35108  1.000 59.79423  ? 93  ALA   A N   1 
ATOM   797  C CA  . ALA   A 1 96  ? 28.55325 39.14956  -6.41428  1.000 65.40683  ? 93  ALA   A CA  1 
ATOM   798  C C   . ALA   A 1 96  ? 28.09947 40.11464  -7.50005  1.000 64.68784  ? 93  ALA   A C   1 
ATOM   799  O O   . ALA   A 1 96  ? 28.40156 41.30949  -7.41598  1.000 70.69081  ? 93  ALA   A O   1 
ATOM   800  C CB  . ALA   A 1 96  ? 30.01334 38.75926  -6.64405  1.000 56.02167  ? 93  ALA   A CB  1 
ATOM   801  N N   . SER   A 1 97  ? 27.38828 39.62775  -8.51406  1.000 65.36325  ? 94  SER   A N   1 
ATOM   802  C CA  . SER   A 1 97  ? 26.89762 40.46372  -9.59893  1.000 64.68731  ? 94  SER   A CA  1 
ATOM   803  C C   . SER   A 1 97  ? 25.42278 40.80826  -9.45001  1.000 72.19227  ? 94  SER   A C   1 
ATOM   804  O O   . SER   A 1 97  ? 24.82994 41.35044  -10.38463 1.000 72.57459  ? 94  SER   A O   1 
ATOM   805  C CB  . SER   A 1 97  ? 27.13336 39.77266  -10.94411 1.000 68.74305  ? 94  SER   A CB  1 
ATOM   806  O OG  . SER   A 1 97  ? 28.48526 39.37437  -11.08614 1.000 68.20207  ? 94  SER   A OG  1 
ATOM   807  N N   . ALA   A 1 98  ? 24.82019 40.51389  -8.29550  1.000 67.92163  ? 95  ALA   A N   1 
ATOM   808  C CA  . ALA   A 1 98  ? 23.37595 40.67084  -8.15159  1.000 75.35870  ? 95  ALA   A CA  1 
ATOM   809  C C   . ALA   A 1 98  ? 22.94419 42.12914  -8.24965  1.000 79.68704  ? 95  ALA   A C   1 
ATOM   810  O O   . ALA   A 1 98  ? 21.86206 42.42087  -8.77202  1.000 79.89855  ? 95  ALA   A O   1 
ATOM   811  C CB  . ALA   A 1 98  ? 22.91716 40.06827  -6.82468  1.000 73.14071  ? 95  ALA   A CB  1 
ATOM   812  N N   . LEU   A 1 99  ? 23.76896 43.05510  -7.75799  1.000 72.40775  ? 96  LEU   A N   1 
ATOM   813  C CA  . LEU   A 1 99  ? 23.40280 44.46695  -7.78047  1.000 84.74568  ? 96  LEU   A CA  1 
ATOM   814  C C   . LEU   A 1 99  ? 23.52190 45.05102  -9.18295  1.000 86.86779  ? 96  LEU   A C   1 
ATOM   815  O O   . LEU   A 1 99  ? 22.55763 45.61351  -9.71449  1.000 86.47759  ? 96  LEU   A O   1 
ATOM   816  C CB  . LEU   A 1 99  ? 24.26878 45.25297  -6.79368  1.000 81.93958  ? 96  LEU   A CB  1 
ATOM   817  C CG  . LEU   A 1 99  ? 24.11663 44.89588  -5.31413  1.000 83.37019  ? 96  LEU   A CG  1 
ATOM   818  C CD1 . LEU   A 1 99  ? 24.95476 45.83332  -4.46251  1.000 82.50623  ? 96  LEU   A CD1 1 
ATOM   819  C CD2 . LEU   A 1 99  ? 22.65398 44.94073  -4.89344  1.000 84.75067  ? 96  LEU   A CD2 1 
ATOM   820  N N   . THR   A 1 100 ? 24.69533 44.92123  -9.79864  1.000 87.76108  ? 97  THR   A N   1 
ATOM   821  C CA  . THR   A 1 100 ? 24.91886 45.50263  -11.11572 1.000 88.74571  ? 97  THR   A CA  1 
ATOM   822  C C   . THR   A 1 100 ? 24.43175 44.61143  -12.25009 1.000 86.53423  ? 97  THR   A C   1 
ATOM   823  O O   . THR   A 1 100 ? 24.29003 45.09237  -13.37934 1.000 82.74566  ? 97  THR   A O   1 
ATOM   824  C CB  . THR   A 1 100 ? 26.40583 45.80213  -11.31760 1.000 90.70698  ? 97  THR   A CB  1 
ATOM   825  O OG1 . THR   A 1 100 ? 27.15784 44.58785  -11.19666 1.000 90.95382  ? 97  THR   A OG1 1 
ATOM   826  C CG2 . THR   A 1 100 ? 26.89060 46.79756  -10.27560 1.000 94.06161  ? 97  THR   A CG2 1 
ATOM   827  N N   . GLY   A 1 101 ? 24.17509 43.33460  -11.98380 1.000 87.29816  ? 98  GLY   A N   1 
ATOM   828  C CA  . GLY   A 1 101 ? 23.77916 42.41893  -13.03372 1.000 80.49132  ? 98  GLY   A CA  1 
ATOM   829  C C   . GLY   A 1 101 ? 24.96313 41.89803  -13.81627 1.000 75.80675  ? 98  GLY   A C   1 
ATOM   830  O O   . GLY   A 1 101 ? 26.00350 42.55799  -13.90099 1.000 78.15462  ? 98  GLY   A O   1 
ATOM   831  N N   . ILE   A 1 102 ? 24.82333 40.70553  -14.37477 1.000 82.50966  ? 99  ILE   A N   1 
ATOM   832  C CA  . ILE   A 1 102 ? 25.85064 40.16646  -15.26452 1.000 75.19119  ? 99  ILE   A CA  1 
ATOM   833  C C   . ILE   A 1 102 ? 25.65747 40.77753  -16.65280 1.000 76.68489  ? 99  ILE   A C   1 
ATOM   834  O O   . ILE   A 1 102 ? 24.52277 40.79936  -17.15295 1.000 81.31449  ? 99  ILE   A O   1 
ATOM   835  C CB  . ILE   A 1 102 ? 25.77481 38.64527  -15.32284 1.000 76.27806  ? 99  ILE   A CB  1 
ATOM   836  C CG1 . ILE   A 1 102 ? 25.87790 38.05274  -13.91549 1.000 69.63745  ? 99  ILE   A CG1 1 
ATOM   837  C CG2 . ILE   A 1 102 ? 26.88820 38.08543  -16.20245 1.000 70.42070  ? 99  ILE   A CG2 1 
ATOM   838  C CD1 . ILE   A 1 102 ? 25.85506 36.53796  -13.89390 1.000 63.69599  ? 99  ILE   A CD1 1 
ATOM   839  N N   . PRO   A 1 103 ? 26.71353 41.29145  -17.27754 1.000 77.80823  ? 100 PRO   A N   1 
ATOM   840  C CA  . PRO   A 1 103 ? 26.56691 41.85183  -18.62601 1.000 70.12147  ? 100 PRO   A CA  1 
ATOM   841  C C   . PRO   A 1 103 ? 26.01972 40.81970  -19.60111 1.000 71.21155  ? 100 PRO   A C   1 
ATOM   842  O O   . PRO   A 1 103 ? 26.39225 39.64507  -19.56679 1.000 71.76707  ? 100 PRO   A O   1 
ATOM   843  C CB  . PRO   A 1 103 ? 27.99541 42.27168  -18.98937 1.000 84.50257  ? 100 PRO   A CB  1 
ATOM   844  C CG  . PRO   A 1 103 ? 28.66507 42.49283  -17.67118 1.000 76.38145  ? 100 PRO   A CG  1 
ATOM   845  C CD  . PRO   A 1 103 ? 28.07351 41.47511  -16.74340 1.000 74.21846  ? 100 PRO   A CD  1 
ATOM   846  N N   . LEU   A 1 104 ? 25.11767 41.27450  -20.47086 1.000 71.47214  ? 101 LEU   A N   1 
ATOM   847  C CA  . LEU   A 1 104 ? 24.49378 40.36905  -21.43251 1.000 74.65388  ? 101 LEU   A CA  1 
ATOM   848  C C   . LEU   A 1 104 ? 25.49383 39.65567  -22.33892 1.000 76.09539  ? 101 LEU   A C   1 
ATOM   849  O O   . LEU   A 1 104 ? 25.29911 38.45272  -22.58861 1.000 67.65541  ? 101 LEU   A O   1 
ATOM   850  C CB  . LEU   A 1 104 ? 23.45261 41.13344  -22.26184 1.000 74.70083  ? 101 LEU   A CB  1 
ATOM   851  C CG  . LEU   A 1 104 ? 22.72861 40.32760  -23.34260 1.000 87.68706  ? 101 LEU   A CG  1 
ATOM   852  C CD1 . LEU   A 1 104 ? 21.99766 39.14102  -22.73105 1.000 77.46424  ? 101 LEU   A CD1 1 
ATOM   853  C CD2 . LEU   A 1 104 ? 21.76804 41.21415  -24.12058 1.000 87.59815  ? 101 LEU   A CD2 1 
ATOM   854  N N   . PRO   A 1 105 ? 26.54572 40.29825  -22.86603 1.000 76.35469  ? 102 PRO   A N   1 
ATOM   855  C CA  . PRO   A 1 105 ? 27.53884 39.53008  -23.63724 1.000 77.96815  ? 102 PRO   A CA  1 
ATOM   856  C C   . PRO   A 1 105 ? 28.20563 38.42672  -22.83471 1.000 71.54798  ? 102 PRO   A C   1 
ATOM   857  O O   . PRO   A 1 105 ? 28.61360 37.41222  -23.41434 1.000 69.15650  ? 102 PRO   A O   1 
ATOM   858  C CB  . PRO   A 1 105 ? 28.54841 40.60108  -24.07254 1.000 69.21490  ? 102 PRO   A CB  1 
ATOM   859  C CG  . PRO   A 1 105 ? 27.76466 41.86043  -24.09592 1.000 76.15874  ? 102 PRO   A CG  1 
ATOM   860  C CD  . PRO   A 1 105 ? 26.80322 41.74861  -22.95190 1.000 66.58617  ? 102 PRO   A CD  1 
ATOM   861  N N   . LEU   A 1 106 ? 28.32722 38.58956  -21.51535 1.000 67.09119  ? 103 LEU   A N   1 
ATOM   862  C CA  . LEU   A 1 106 ? 28.91754 37.54190  -20.69085 1.000 65.67999  ? 103 LEU   A CA  1 
ATOM   863  C C   . LEU   A 1 106 ? 27.92726 36.42072  -20.40189 1.000 70.87907  ? 103 LEU   A C   1 
ATOM   864  O O   . LEU   A 1 106 ? 28.33123 35.25700  -20.29840 1.000 67.33587  ? 103 LEU   A O   1 
ATOM   865  C CB  . LEU   A 1 106 ? 29.44595 38.13402  -19.38289 1.000 64.77792  ? 103 LEU   A CB  1 
ATOM   866  C CG  . LEU   A 1 106 ? 30.23381 37.18673  -18.47476 1.000 66.20315  ? 103 LEU   A CG  1 
ATOM   867  C CD1 . LEU   A 1 106 ? 31.40146 36.56989  -19.23202 1.000 69.10331  ? 103 LEU   A CD1 1 
ATOM   868  C CD2 . LEU   A 1 106 ? 30.72421 37.91449  -17.23266 1.000 65.23963  ? 103 LEU   A CD2 1 
ATOM   869  N N   . ILE   A 1 107 ? 26.63850 36.74591  -20.26604 1.000 69.33395  ? 104 ILE   A N   1 
ATOM   870  C CA  . ILE   A 1 107 ? 25.62163 35.70710  -20.11927 1.000 71.37882  ? 104 ILE   A CA  1 
ATOM   871  C C   . ILE   A 1 107 ? 25.56031 34.85113  -21.37682 1.000 66.42979  ? 104 ILE   A C   1 
ATOM   872  O O   . ILE   A 1 107 ? 25.49017 33.61706  -21.30807 1.000 60.77889  ? 104 ILE   A O   1 
ATOM   873  C CB  . ILE   A 1 107 ? 24.25133 36.33449  -19.79755 1.000 67.92780  ? 104 ILE   A CB  1 
ATOM   874  C CG1 . ILE   A 1 107 ? 24.29530 37.07870  -18.46279 1.000 69.70664  ? 104 ILE   A CG1 1 
ATOM   875  C CG2 . ILE   A 1 107 ? 23.16995 35.26623  -19.77190 1.000 61.68680  ? 104 ILE   A CG2 1 
ATOM   876  C CD1 . ILE   A 1 107 ? 22.97491 37.70899  -18.07427 1.000 69.07050  ? 104 ILE   A CD1 1 
ATOM   877  N N   . LYS   A 1 108 ? 25.59125 35.49452  -22.54570 1.000 61.86897  ? 105 LYS   A N   1 
ATOM   878  C CA  . LYS   A 1 108 ? 25.56680 34.75755  -23.80386 1.000 70.48928  ? 105 LYS   A CA  1 
ATOM   879  C C   . LYS   A 1 108 ? 26.82510 33.91641  -23.97498 1.000 67.20394  ? 105 LYS   A C   1 
ATOM   880  O O   . LYS   A 1 108 ? 26.75469 32.77192  -24.43854 1.000 69.50371  ? 105 LYS   A O   1 
ATOM   881  C CB  . LYS   A 1 108 ? 25.40290 35.72994  -24.97207 1.000 62.54095  ? 105 LYS   A CB  1 
ATOM   882  C CG  . LYS   A 1 108 ? 25.26763 35.06123  -26.32738 1.000 71.60390  ? 105 LYS   A CG  1 
ATOM   883  C CD  . LYS   A 1 108 ? 25.11238 36.08755  -27.43791 1.000 88.28658  ? 105 LYS   A CD  1 
ATOM   884  C CE  . LYS   A 1 108 ? 23.88602 36.95631  -27.22753 1.000 88.69610  ? 105 LYS   A CE  1 
ATOM   885  N NZ  . LYS   A 1 108 ? 23.66895 37.88693  -28.36929 1.000 94.25914  ? 105 LYS   A NZ  1 
ATOM   886  N N   . SER   A 1 109 ? 27.98456 34.46573  -23.60512 1.000 66.66472  ? 106 SER   A N   1 
ATOM   887  C CA  . SER   A 1 109 ? 29.22775 33.70958  -23.71604 1.000 62.97952  ? 106 SER   A CA  1 
ATOM   888  C C   . SER   A 1 109 ? 29.23442 32.51094  -22.77509 1.000 66.96806  ? 106 SER   A C   1 
ATOM   889  O O   . SER   A 1 109 ? 29.69799 31.42569  -23.14431 1.000 63.33571  ? 106 SER   A O   1 
ATOM   890  C CB  . SER   A 1 109 ? 30.42292 34.61819  -23.43157 1.000 64.61704  ? 106 SER   A CB  1 
ATOM   891  O OG  . SER   A 1 109 ? 31.62029 33.86705  -23.32491 1.000 74.99808  ? 106 SER   A OG  1 
ATOM   892  N N   . TYR   A 1 110 ? 28.71841 32.68470  -21.55623 1.000 60.40639  ? 107 TYR   A N   1 
ATOM   893  C CA  . TYR   A 1 110 ? 28.70090 31.58621  -20.59518 1.000 58.67372  ? 107 TYR   A CA  1 
ATOM   894  C C   . TYR   A 1 110 ? 27.72765 30.49397  -21.02260 1.000 59.53785  ? 107 TYR   A C   1 
ATOM   895  O O   . TYR   A 1 110 ? 28.06324 29.30462  -20.98862 1.000 55.55871  ? 107 TYR   A O   1 
ATOM   896  C CB  . TYR   A 1 110 ? 28.35070 32.11175  -19.20215 1.000 56.46477  ? 107 TYR   A CB  1 
ATOM   897  C CG  . TYR   A 1 110 ? 29.53537 32.65321  -18.43325 1.000 62.30922  ? 107 TYR   A CG  1 
ATOM   898  C CD1 . TYR   A 1 110 ? 30.83176 32.47071  -18.89717 1.000 61.54164  ? 107 TYR   A CD1 1 
ATOM   899  C CD2 . TYR   A 1 110 ? 29.35772 33.33504  -17.23704 1.000 61.49422  ? 107 TYR   A CD2 1 
ATOM   900  C CE1 . TYR   A 1 110 ? 31.91709 32.95897  -18.19510 1.000 63.42561  ? 107 TYR   A CE1 1 
ATOM   901  C CE2 . TYR   A 1 110 ? 30.43658 33.82676  -16.52791 1.000 63.37910  ? 107 TYR   A CE2 1 
ATOM   902  C CZ  . TYR   A 1 110 ? 31.71304 33.63593  -17.01136 1.000 63.81329  ? 107 TYR   A CZ  1 
ATOM   903  O OH  . TYR   A 1 110 ? 32.78817 34.12433  -16.30605 1.000 66.89938  ? 107 TYR   A OH  1 
ATOM   904  N N   . LEU   A 1 111 ? 26.51259 30.87851  -21.42419 1.000 57.34993  ? 108 LEU   A N   1 
ATOM   905  C CA  . LEU   A 1 111 ? 25.53625 29.89093  -21.87619 1.000 61.57046  ? 108 LEU   A CA  1 
ATOM   906  C C   . LEU   A 1 111 ? 26.03670 29.14159  -23.10478 1.000 63.55276  ? 108 LEU   A C   1 
ATOM   907  O O   . LEU   A 1 111 ? 25.81905 27.93090  -23.23533 1.000 63.58191  ? 108 LEU   A O   1 
ATOM   908  C CB  . LEU   A 1 111 ? 24.20059 30.57093  -22.17479 1.000 57.76866  ? 108 LEU   A CB  1 
ATOM   909  C CG  . LEU   A 1 111 ? 23.07013 29.65000  -22.63872 1.000 56.32797  ? 108 LEU   A CG  1 
ATOM   910  C CD1 . LEU   A 1 111 ? 22.62897 28.73256  -21.50807 1.000 53.37088  ? 108 LEU   A CD1 1 
ATOM   911  C CD2 . LEU   A 1 111 ? 21.89658 30.45630  -23.17577 1.000 59.92177  ? 108 LEU   A CD2 1 
ATOM   912  N N   . PHE   A 1 112 ? 26.71219 29.84655  -24.01505 1.000 54.92273  ? 109 PHE   A N   1 
ATOM   913  C CA  . PHE   A 1 112 ? 27.25156 29.20498  -25.20985 1.000 61.59565  ? 109 PHE   A CA  1 
ATOM   914  C C   . PHE   A 1 112 ? 28.28687 28.14827  -24.84155 1.000 59.70164  ? 109 PHE   A C   1 
ATOM   915  O O   . PHE   A 1 112 ? 28.29031 27.04362  -25.39689 1.000 61.37601  ? 109 PHE   A O   1 
ATOM   916  C CB  . PHE   A 1 112 ? 27.85354 30.26463  -26.13516 1.000 61.29532  ? 109 PHE   A CB  1 
ATOM   917  C CG  . PHE   A 1 112 ? 28.28990 29.73472  -27.47059 1.000 64.35669  ? 109 PHE   A CG  1 
ATOM   918  C CD1 . PHE   A 1 112 ? 27.36125 29.48412  -28.46771 1.000 60.23483  ? 109 PHE   A CD1 1 
ATOM   919  C CD2 . PHE   A 1 112 ? 29.62991 29.50415  -27.73554 1.000 67.07102  ? 109 PHE   A CD2 1 
ATOM   920  C CE1 . PHE   A 1 112 ? 27.75945 29.00194  -29.70275 1.000 71.84942  ? 109 PHE   A CE1 1 
ATOM   921  C CE2 . PHE   A 1 112 ? 30.03500 29.02178  -28.96930 1.000 72.52760  ? 109 PHE   A CE2 1 
ATOM   922  C CZ  . PHE   A 1 112 ? 29.09856 28.77079  -29.95338 1.000 69.17447  ? 109 PHE   A CZ  1 
ATOM   923  N N   . GLN   A 1 113 ? 29.17161 28.46899  -23.89445 1.000 58.17141  ? 110 GLN   A N   1 
ATOM   924  C CA  . GLN   A 1 113 ? 30.17072 27.49995  -23.45431 1.000 62.91170  ? 110 GLN   A CA  1 
ATOM   925  C C   . GLN   A 1 113 ? 29.52663 26.33070  -22.71933 1.000 60.50551  ? 110 GLN   A C   1 
ATOM   926  O O   . GLN   A 1 113 ? 29.94912 25.17982  -22.88429 1.000 60.54958  ? 110 GLN   A O   1 
ATOM   927  C CB  . GLN   A 1 113 ? 31.20660 28.18493  -22.56458 1.000 64.45589  ? 110 GLN   A CB  1 
ATOM   928  C CG  . GLN   A 1 113 ? 32.01401 29.26491  -23.26627 1.000 62.84030  ? 110 GLN   A CG  1 
ATOM   929  C CD  . GLN   A 1 113 ? 33.00027 29.93762  -22.33455 1.000 67.63344  ? 110 GLN   A CD  1 
ATOM   930  O OE1 . GLN   A 1 113 ? 33.78475 29.27001  -21.66203 1.000 64.89463  ? 110 GLN   A OE1 1 
ATOM   931  N NE2 . GLN   A 1 113 ? 32.95875 31.26499  -22.28065 1.000 69.48569  ? 110 GLN   A NE2 1 
ATOM   932  N N   . LEU   A 1 114 ? 28.50963 26.60609  -21.89748 1.000 54.98821  ? 111 LEU   A N   1 
ATOM   933  C CA  . LEU   A 1 114 ? 27.82625 25.53269  -21.18147 1.000 58.60692  ? 111 LEU   A CA  1 
ATOM   934  C C   . LEU   A 1 114 ? 27.13803 24.57669  -22.14716 1.000 55.48023  ? 111 LEU   A C   1 
ATOM   935  O O   . LEU   A 1 114 ? 27.16597 23.35534  -21.95035 1.000 55.30660  ? 111 LEU   A O   1 
ATOM   936  C CB  . LEU   A 1 114 ? 26.81172 26.11535  -20.19725 1.000 58.76779  ? 111 LEU   A CB  1 
ATOM   937  C CG  . LEU   A 1 114 ? 27.34848 26.87989  -18.98589 1.000 59.46579  ? 111 LEU   A CG  1 
ATOM   938  C CD1 . LEU   A 1 114 ? 26.21020 27.57480  -18.25324 1.000 49.67385  ? 111 LEU   A CD1 1 
ATOM   939  C CD2 . LEU   A 1 114 ? 28.10059 25.94977  -18.04631 1.000 55.78737  ? 111 LEU   A CD2 1 
ATOM   940  N N   . LEU   A 1 115 ? 26.51138 25.11494  -23.19696 1.000 53.31530  ? 112 LEU   A N   1 
ATOM   941  C CA  . LEU   A 1 115 ? 25.86338 24.26272  -24.18807 1.000 60.78121  ? 112 LEU   A CA  1 
ATOM   942  C C   . LEU   A 1 115 ? 26.87456 23.43926  -24.97444 1.000 57.55241  ? 112 LEU   A C   1 
ATOM   943  O O   . LEU   A 1 115 ? 26.57096 22.30948  -25.37381 1.000 56.99186  ? 112 LEU   A O   1 
ATOM   944  C CB  . LEU   A 1 115 ? 25.01921 25.10941  -25.13896 1.000 53.28496  ? 112 LEU   A CB  1 
ATOM   945  C CG  . LEU   A 1 115 ? 23.75158 25.73281  -24.55419 1.000 56.45553  ? 112 LEU   A CG  1 
ATOM   946  C CD1 . LEU   A 1 115 ? 23.18376 26.77292  -25.50323 1.000 58.40594  ? 112 LEU   A CD1 1 
ATOM   947  C CD2 . LEU   A 1 115 ? 22.71949 24.65744  -24.25926 1.000 51.25155  ? 112 LEU   A CD2 1 
ATOM   948  N N   . GLN   A 1 116 ? 28.07039 23.98547  -25.21321 1.000 54.01052  ? 113 GLN   A N   1 
ATOM   949  C CA  . GLN   A 1 116 ? 29.10949 23.22490  -25.90140 1.000 56.13651  ? 113 GLN   A CA  1 
ATOM   950  C C   . GLN   A 1 116 ? 29.58281 22.05017  -25.05460 1.000 58.06227  ? 113 GLN   A C   1 
ATOM   951  O O   . GLN   A 1 116 ? 29.73074 20.93168  -25.56063 1.000 51.86777  ? 113 GLN   A O   1 
ATOM   952  C CB  . GLN   A 1 116 ? 30.28478 24.13627  -26.25437 1.000 59.15761  ? 113 GLN   A CB  1 
ATOM   953  C CG  . GLN   A 1 116 ? 30.02667 25.05959  -27.43209 1.000 57.93068  ? 113 GLN   A CG  1 
ATOM   954  C CD  . GLN   A 1 116 ? 31.18199 26.00347  -27.68745 1.000 70.99306  ? 113 GLN   A CD  1 
ATOM   955  O OE1 . GLN   A 1 116 ? 31.69301 26.63985  -26.76522 1.000 73.11237  ? 113 GLN   A OE1 1 
ATOM   956  N NE2 . GLN   A 1 116 ? 31.60696 26.09363  -28.94179 1.000 69.04282  ? 113 GLN   A NE2 1 
ATOM   957  N N   . GLY   A 1 117 ? 29.82623 22.28295  -23.76292 1.000 55.22251  ? 114 GLY   A N   1 
ATOM   958  C CA  . GLY   A 1 117 ? 30.19989 21.19024  -22.88333 1.000 57.78989  ? 114 GLY   A CA  1 
ATOM   959  C C   . GLY   A 1 117 ? 29.09047 20.17712  -22.69235 1.000 54.26651  ? 114 GLY   A C   1 
ATOM   960  O O   . GLY   A 1 117 ? 29.36010 18.98571  -22.50549 1.000 56.23211  ? 114 GLY   A O   1 
ATOM   961  N N   . LEU   A 1 118 ? 27.83205 20.62635  -22.73272 1.000 57.40360  ? 115 LEU   A N   1 
ATOM   962  C CA  . LEU   A 1 118 ? 26.72258 19.68833  -22.58919 1.000 61.30800  ? 115 LEU   A CA  1 
ATOM   963  C C   . LEU   A 1 118 ? 26.50332 18.89376  -23.87246 1.000 53.60648  ? 115 LEU   A C   1 
ATOM   964  O O   . LEU   A 1 118 ? 26.17480 17.70145  -23.82282 1.000 58.88020  ? 115 LEU   A O   1 
ATOM   965  C CB  . LEU   A 1 118 ? 25.44954 20.43101  -22.19345 1.000 52.11166  ? 115 LEU   A CB  1 
ATOM   966  C CG  . LEU   A 1 118 ? 24.30015 19.55013  -21.69263 1.000 59.16130  ? 115 LEU   A CG  1 
ATOM   967  C CD1 . LEU   A 1 118 ? 24.71923 18.77711  -20.44792 1.000 53.48579  ? 115 LEU   A CD1 1 
ATOM   968  C CD2 . LEU   A 1 118 ? 23.06231 20.38904  -21.42293 1.000 52.36852  ? 115 LEU   A CD2 1 
ATOM   969  N N   . ALA   A 1 119 ? 26.68129 19.53637  -25.03226 1.000 51.39514  ? 116 ALA   A N   1 
ATOM   970  C CA  . ALA   A 1 119 ? 26.58580 18.81684  -26.29925 1.000 64.30655  ? 116 ALA   A CA  1 
ATOM   971  C C   . ALA   A 1 119 ? 27.67912 17.76350  -26.41483 1.000 57.51655  ? 116 ALA   A C   1 
ATOM   972  O O   . ALA   A 1 119 ? 27.45927 16.68859  -26.98443 1.000 54.29231  ? 116 ALA   A O   1 
ATOM   973  C CB  . ALA   A 1 119 ? 26.65714 19.79833  -27.46882 1.000 50.76299  ? 116 ALA   A CB  1 
ATOM   974  N N   . PHE   A 1 120 ? 28.86757 18.05889  -25.88428 1.000 58.72755  ? 117 PHE   A N   1 
ATOM   975  C CA  . PHE   A 1 120 ? 29.94140 17.07146  -25.86256 1.000 56.71028  ? 117 PHE   A CA  1 
ATOM   976  C C   . PHE   A 1 120 ? 29.59944 15.90750  -24.94090 1.000 59.27465  ? 117 PHE   A C   1 
ATOM   977  O O   . PHE   A 1 120 ? 29.93069 14.75378  -25.23922 1.000 65.83726  ? 117 PHE   A O   1 
ATOM   978  C CB  . PHE   A 1 120 ? 31.24904 17.73695  -25.43140 1.000 64.70257  ? 117 PHE   A CB  1 
ATOM   979  C CG  . PHE   A 1 120 ? 32.45055 16.84012  -25.51723 1.000 59.34152  ? 117 PHE   A CG  1 
ATOM   980  C CD1 . PHE   A 1 120 ? 33.13859 16.70353  -26.70945 1.000 64.48258  ? 117 PHE   A CD1 1 
ATOM   981  C CD2 . PHE   A 1 120 ? 32.90334 16.15037  -24.40295 1.000 59.63062  ? 117 PHE   A CD2 1 
ATOM   982  C CE1 . PHE   A 1 120 ? 34.25104 15.88921  -26.79564 1.000 65.35207  ? 117 PHE   A CE1 1 
ATOM   983  C CE2 . PHE   A 1 120 ? 34.01673 15.33241  -24.48298 1.000 62.97002  ? 117 PHE   A CE2 1 
ATOM   984  C CZ  . PHE   A 1 120 ? 34.69177 15.20371  -25.68100 1.000 58.86551  ? 117 PHE   A CZ  1 
ATOM   985  N N   . CYS   A 1 121 ? 28.93868 16.18907  -23.81591 1.000 55.92619  ? 118 CYS   A N   1 
ATOM   986  C CA  . CYS   A 1 121 ? 28.52974 15.11918  -22.91035 1.000 56.26432  ? 118 CYS   A CA  1 
ATOM   987  C C   . CYS   A 1 121 ? 27.47265 14.22963  -23.55164 1.000 57.70373  ? 118 CYS   A C   1 
ATOM   988  O O   . CYS   A 1 121 ? 27.55220 12.99928  -23.47798 1.000 61.08042  ? 118 CYS   A O   1 
ATOM   989  C CB  . CYS   A 1 121 ? 28.00204 15.70514  -21.60189 1.000 59.31061  ? 118 CYS   A CB  1 
ATOM   990  S SG  . CYS   A 1 121 ? 29.25669 16.39882  -20.50384 1.000 58.80064  ? 118 CYS   A SG  1 
ATOM   991  N N   . HIS   A 1 122 ? 26.47114 14.83934  -24.19024 1.000 55.43339  ? 119 HIS   A N   1 
ATOM   992  C CA  . HIS   A 1 122 ? 25.36723 14.07085  -24.75482 1.000 58.80269  ? 119 HIS   A CA  1 
ATOM   993  C C   . HIS   A 1 122 ? 25.79060 13.28145  -25.98740 1.000 52.36179  ? 119 HIS   A C   1 
ATOM   994  O O   . HIS   A 1 122 ? 25.27747 12.18091  -26.21775 1.000 56.71836  ? 119 HIS   A O   1 
ATOM   995  C CB  . HIS   A 1 122 ? 24.20692 15.00684  -25.08551 1.000 54.56448  ? 119 HIS   A CB  1 
ATOM   996  C CG  . HIS   A 1 122 ? 23.58142 15.63547  -23.87981 1.000 59.30709  ? 119 HIS   A CG  1 
ATOM   997  N ND1 . HIS   A 1 122 ? 22.60296 16.60169  -23.96649 1.000 62.70675  ? 119 HIS   A ND1 1 
ATOM   998  C CD2 . HIS   A 1 122 ? 23.79238 15.43168  -22.55774 1.000 55.31741  ? 119 HIS   A CD2 1 
ATOM   999  C CE1 . HIS   A 1 122 ? 22.23893 16.96728  -22.75030 1.000 64.75624  ? 119 HIS   A CE1 1 
ATOM   1000 N NE2 . HIS   A 1 122 ? 22.94544 16.27219  -21.87727 1.000 55.09013  ? 119 HIS   A NE2 1 
ATOM   1001 N N   . SER   A 1 123 ? 26.70827 13.82140  -26.79560 1.000 50.90280  ? 120 SER   A N   1 
ATOM   1002 C CA  . SER   A 1 123 ? 27.21183 13.05835  -27.93390 1.000 56.91099  ? 120 SER   A CA  1 
ATOM   1003 C C   . SER   A 1 123 ? 28.02174 11.85241  -27.47764 1.000 61.27630  ? 120 SER   A C   1 
ATOM   1004 O O   . SER   A 1 123 ? 28.07747 10.84035  -28.18596 1.000 64.26985  ? 120 SER   A O   1 
ATOM   1005 C CB  . SER   A 1 123 ? 28.05450 13.94963  -28.84707 1.000 60.38019  ? 120 SER   A CB  1 
ATOM   1006 O OG  . SER   A 1 123 ? 29.30409 14.26317  -28.25639 1.000 68.61776  ? 120 SER   A OG  1 
ATOM   1007 N N   . HIS   A 1 124 ? 28.65597 11.94279  -26.30882 1.000 55.14964  ? 121 HIS   A N   1 
ATOM   1008 C CA  . HIS   A 1 124 ? 29.30947 10.80362  -25.67811 1.000 59.29540  ? 121 HIS   A CA  1 
ATOM   1009 C C   . HIS   A 1 124 ? 28.34575 9.95816   -24.85906 1.000 56.92914  ? 121 HIS   A C   1 
ATOM   1010 O O   . HIS   A 1 124 ? 28.79075 9.04022   -24.16004 1.000 58.22628  ? 121 HIS   A O   1 
ATOM   1011 C CB  . HIS   A 1 124 ? 30.46458 11.27829  -24.79201 1.000 56.98201  ? 121 HIS   A CB  1 
ATOM   1012 C CG  . HIS   A 1 124 ? 31.68592 11.67826  -25.55799 1.000 62.78308  ? 121 HIS   A CG  1 
ATOM   1013 N ND1 . HIS   A 1 124 ? 31.67833 12.68855  -26.49534 1.000 66.36342  ? 121 HIS   A ND1 1 
ATOM   1014 C CD2 . HIS   A 1 124 ? 32.95195 11.19878  -25.53082 1.000 63.14494  ? 121 HIS   A CD2 1 
ATOM   1015 C CE1 . HIS   A 1 124 ? 32.88750 12.81496  -27.01173 1.000 65.31967  ? 121 HIS   A CE1 1 
ATOM   1016 N NE2 . HIS   A 1 124 ? 33.67919 11.92368  -26.44296 1.000 73.50240  ? 121 HIS   A NE2 1 
ATOM   1017 N N   . ARG   A 1 125 ? 27.04802 10.26128  -24.92678 1.000 56.77732  ? 122 ARG   A N   1 
ATOM   1018 C CA  . ARG   A 1 125 ? 26.00916 9.49775   -24.23696 1.000 59.00547  ? 122 ARG   A CA  1 
ATOM   1019 C C   . ARG   A 1 125 ? 26.20580 9.53105   -22.72088 1.000 63.39128  ? 122 ARG   A C   1 
ATOM   1020 O O   . ARG   A 1 125 ? 26.21060 8.49944   -22.04709 1.000 61.90765  ? 122 ARG   A O   1 
ATOM   1021 C CB  . ARG   A 1 125 ? 25.94839 8.06010   -24.76093 1.000 61.58465  ? 122 ARG   A CB  1 
ATOM   1022 C CG  . ARG   A 1 125 ? 25.40227 7.95445   -26.17693 1.000 64.03937  ? 122 ARG   A CG  1 
ATOM   1023 C CD  . ARG   A 1 125 ? 25.98429 6.76758   -26.93199 1.000 71.37780  ? 122 ARG   A CD  1 
ATOM   1024 N NE  . ARG   A 1 125 ? 25.70076 5.49014   -26.28944 1.000 69.28033  ? 122 ARG   A NE  1 
ATOM   1025 C CZ  . ARG   A 1 125 ? 26.59652 4.77031   -25.62821 1.000 78.86785  ? 122 ARG   A CZ  1 
ATOM   1026 N NH1 . ARG   A 1 125 ? 27.84811 5.17803   -25.49487 1.000 79.47929  ? 122 ARG   A NH1 1 
ATOM   1027 N NH2 . ARG   A 1 125 ? 26.22904 3.60926   -25.09332 1.000 85.00202  ? 122 ARG   A NH2 1 
ATOM   1028 N N   . VAL   A 1 126 ? 26.35792 10.73975  -22.18242 1.000 53.47823  ? 123 VAL   A N   1 
ATOM   1029 C CA  . VAL   A 1 126 ? 26.53687 10.95262  -20.75001 1.000 50.63845  ? 123 VAL   A CA  1 
ATOM   1030 C C   . VAL   A 1 126 ? 25.56277 12.03032  -20.29527 1.000 52.92866  ? 123 VAL   A C   1 
ATOM   1031 O O   . VAL   A 1 126 ? 25.56541 13.14275  -20.83625 1.000 54.43061  ? 123 VAL   A O   1 
ATOM   1032 C CB  . VAL   A 1 126 ? 27.97855 11.35654  -20.39880 1.000 51.10737  ? 123 VAL   A CB  1 
ATOM   1033 C CG1 . VAL   A 1 126 ? 28.06911 11.77313  -18.93902 1.000 55.76208  ? 123 VAL   A CG1 1 
ATOM   1034 C CG2 . VAL   A 1 126 ? 28.93722 10.21427  -20.68517 1.000 62.61283  ? 123 VAL   A CG2 1 
ATOM   1035 N N   . LEU   A 1 127 ? 24.73556 11.70353  -19.30620 1.000 55.43198  ? 124 LEU   A N   1 
ATOM   1036 C CA  . LEU   A 1 127 ? 23.88666 12.68463  -18.64619 1.000 55.61527  ? 124 LEU   A CA  1 
ATOM   1037 C C   . LEU   A 1 127 ? 24.60989 13.23151  -17.42401 1.000 55.10216  ? 124 LEU   A C   1 
ATOM   1038 O O   . LEU   A 1 127 ? 25.24178 12.47807  -16.68232 1.000 57.37198  ? 124 LEU   A O   1 
ATOM   1039 C CB  . LEU   A 1 127 ? 22.55924 12.05489  -18.22067 1.000 54.02918  ? 124 LEU   A CB  1 
ATOM   1040 C CG  . LEU   A 1 127 ? 21.81118 11.24021  -19.27343 1.000 65.71765  ? 124 LEU   A CG  1 
ATOM   1041 C CD1 . LEU   A 1 127 ? 20.54362 10.63654  -18.68528 1.000 61.38112  ? 124 LEU   A CD1 1 
ATOM   1042 C CD2 . LEU   A 1 127 ? 21.49061 12.11110  -20.46951 1.000 57.36159  ? 124 LEU   A CD2 1 
ATOM   1043 N N   . HIS   A 1 128 ? 24.51732 14.54542  -17.21378 1.000 53.00787  ? 125 HIS   A N   1 
ATOM   1044 C CA  . HIS   A 1 128 ? 25.13741 15.13478  -16.03036 1.000 48.32259  ? 125 HIS   A CA  1 
ATOM   1045 C C   . HIS   A 1 128 ? 24.25145 14.95884  -14.80064 1.000 51.60545  ? 125 HIS   A C   1 
ATOM   1046 O O   . HIS   A 1 128 ? 24.70724 14.46742  -13.76114 1.000 52.12214  ? 125 HIS   A O   1 
ATOM   1047 C CB  . HIS   A 1 128 ? 25.44038 16.61403  -16.27317 1.000 47.68139  ? 125 HIS   A CB  1 
ATOM   1048 C CG  . HIS   A 1 128 ? 26.24104 17.24801  -15.18043 1.000 55.49704  ? 125 HIS   A CG  1 
ATOM   1049 N ND1 . HIS   A 1 128 ? 25.69149 17.60534  -13.96795 1.000 52.32862  ? 125 HIS   A ND1 1 
ATOM   1050 C CD2 . HIS   A 1 128 ? 27.55219 17.57832  -15.11170 1.000 53.00458  ? 125 HIS   A CD2 1 
ATOM   1051 C CE1 . HIS   A 1 128 ? 26.62846 18.13262  -13.20084 1.000 55.18007  ? 125 HIS   A CE1 1 
ATOM   1052 N NE2 . HIS   A 1 128 ? 27.76674 18.12789  -13.87118 1.000 56.51208  ? 125 HIS   A NE2 1 
ATOM   1053 N N   . ARG   A 1 129 ? 22.98740 15.37071  -14.90442 1.000 47.86527  ? 126 ARG   A N   1 
ATOM   1054 C CA  . ARG   A 1 129 ? 21.92612 15.14550  -13.92509 1.000 54.66012  ? 126 ARG   A CA  1 
ATOM   1055 C C   . ARG   A 1 129 ? 22.09893 15.93744  -12.63589 1.000 48.34982  ? 126 ARG   A C   1 
ATOM   1056 O O   . ARG   A 1 129 ? 21.43116 15.62908  -11.64281 1.000 52.75701  ? 126 ARG   A O   1 
ATOM   1057 C CB  . ARG   A 1 129 ? 21.77277 13.65929  -13.57982 1.000 54.64801  ? 126 ARG   A CB  1 
ATOM   1058 C CG  . ARG   A 1 129 ? 21.54185 12.76305  -14.78384 1.000 55.22749  ? 126 ARG   A CG  1 
ATOM   1059 C CD  . ARG   A 1 129 ? 21.09906 11.37512  -14.35774 1.000 60.66755  ? 126 ARG   A CD  1 
ATOM   1060 N NE  . ARG   A 1 129 ? 22.05248 10.75244  -13.44736 1.000 60.85781  ? 126 ARG   A NE  1 
ATOM   1061 C CZ  . ARG   A 1 129 ? 21.88800 9.55953   -12.89171 1.000 66.94022  ? 126 ARG   A CZ  1 
ATOM   1062 N NH1 . ARG   A 1 129 ? 20.81002 8.83069   -13.12774 1.000 58.75867  ? 126 ARG   A NH1 1 
ATOM   1063 N NH2 . ARG   A 1 129 ? 22.82882 9.08599   -12.07843 1.000 64.59740  ? 126 ARG   A NH2 1 
ATOM   1064 N N   . ASP   A 1 130 ? 22.96340 16.94618  -12.61341 1.000 50.37621  ? 127 ASP   A N   1 
ATOM   1065 C CA  . ASP   A 1 130 ? 23.05543 17.83740  -11.46039 1.000 52.33199  ? 127 ASP   A CA  1 
ATOM   1066 C C   . ASP   A 1 130 ? 23.64002 19.17967  -11.89377 1.000 53.47101  ? 127 ASP   A C   1 
ATOM   1067 O O   . ASP   A 1 130 ? 24.59930 19.68589  -11.30883 1.000 57.20723  ? 127 ASP   A O   1 
ATOM   1068 C CB  . ASP   A 1 130 ? 23.87886 17.20995  -10.33521 1.000 51.80777  ? 127 ASP   A CB  1 
ATOM   1069 C CG  . ASP   A 1 130 ? 23.50523 17.75853  -8.96798  1.000 64.55156  ? 127 ASP   A CG  1 
ATOM   1070 O OD1 . ASP   A 1 130 ? 22.40844 18.34438  -8.84601  1.000 59.45836  ? 127 ASP   A OD1 1 
ATOM   1071 O OD2 . ASP   A 1 130 ? 24.30190 17.60899  -8.01788  1.000 68.82109  ? 127 ASP   A OD2 1 
ATOM   1072 N N   . LEU   A 1 131 ? 23.05844 19.77228  -12.93465 1.000 52.40531  ? 128 LEU   A N   1 
ATOM   1073 C CA  . LEU   A 1 131 ? 23.48844 21.07974  -13.41821 1.000 49.96585  ? 128 LEU   A CA  1 
ATOM   1074 C C   . LEU   A 1 131 ? 22.87478 22.15740  -12.53337 1.000 58.11588  ? 128 LEU   A C   1 
ATOM   1075 O O   . LEU   A 1 131 ? 21.65977 22.37627  -12.55771 1.000 58.76286  ? 128 LEU   A O   1 
ATOM   1076 C CB  . LEU   A 1 131 ? 23.09076 21.27026  -14.87897 1.000 49.18011  ? 128 LEU   A CB  1 
ATOM   1077 C CG  . LEU   A 1 131 ? 23.81988 20.39025  -15.89505 1.000 58.89102  ? 128 LEU   A CG  1 
ATOM   1078 C CD1 . LEU   A 1 131 ? 23.32442 20.67343  -17.30328 1.000 56.05647  ? 128 LEU   A CD1 1 
ATOM   1079 C CD2 . LEU   A 1 131 ? 25.32287 20.60515  -15.79814 1.000 51.89475  ? 128 LEU   A CD2 1 
ATOM   1080 N N   . LYS   A 1 132 ? 23.71126 22.81543  -11.74082 1.000 54.24591  ? 129 LYS   A N   1 
ATOM   1081 C CA  . LYS   A 1 132 ? 23.30174 23.91661  -10.88408 1.000 58.59938  ? 129 LYS   A CA  1 
ATOM   1082 C C   . LYS   A 1 132 ? 24.46252 24.88844  -10.78711 1.000 52.43620  ? 129 LYS   A C   1 
ATOM   1083 O O   . LYS   A 1 132 ? 25.61545 24.50769  -11.03505 1.000 57.26876  ? 129 LYS   A O   1 
ATOM   1084 C CB  . LYS   A 1 132 ? 22.88074 23.42053  -9.49251  1.000 54.78064  ? 129 LYS   A CB  1 
ATOM   1085 C CG  . LYS   A 1 132 ? 23.88380 22.50086  -8.81943  1.000 54.75947  ? 129 LYS   A CG  1 
ATOM   1086 C CD  . LYS   A 1 132 ? 23.37708 22.04504  -7.46081  1.000 54.50271  ? 129 LYS   A CD  1 
ATOM   1087 C CE  . LYS   A 1 132 ? 24.35097 21.08523  -6.79960  1.000 62.20893  ? 129 LYS   A CE  1 
ATOM   1088 N NZ  . LYS   A 1 132 ? 23.89807 20.68987  -5.43772  1.000 65.28099  ? 129 LYS   A NZ  1 
ATOM   1089 N N   . PRO   A 1 133 ? 24.20278 26.15759  -10.45106 1.000 56.07064  ? 130 PRO   A N   1 
ATOM   1090 C CA  . PRO   A 1 133 ? 25.29186 27.14841  -10.41057 1.000 53.35775  ? 130 PRO   A CA  1 
ATOM   1091 C C   . PRO   A 1 133 ? 26.46550 26.75119  -9.53171  1.000 53.74089  ? 130 PRO   A C   1 
ATOM   1092 O O   . PRO   A 1 133 ? 27.60006 27.15633  -9.81513  1.000 58.54080  ? 130 PRO   A O   1 
ATOM   1093 C CB  . PRO   A 1 133 ? 24.59388 28.40658  -9.87726  1.000 53.41830  ? 130 PRO   A CB  1 
ATOM   1094 C CG  . PRO   A 1 133 ? 23.18398 28.25579  -10.31448 1.000 61.05226  ? 130 PRO   A CG  1 
ATOM   1095 C CD  . PRO   A 1 133 ? 22.88843 26.78388  -10.21853 1.000 55.83306  ? 130 PRO   A CD  1 
ATOM   1096 N N   . GLN   A 1 134 ? 26.23383 25.97161  -8.47224  1.000 52.64288  ? 131 GLN   A N   1 
ATOM   1097 C CA  . GLN   A 1 134 ? 27.33775 25.51472  -7.63618  1.000 55.66994  ? 131 GLN   A CA  1 
ATOM   1098 C C   . GLN   A 1 134 ? 28.27347 24.56573  -8.37364  1.000 53.55641  ? 131 GLN   A C   1 
ATOM   1099 O O   . GLN   A 1 134 ? 29.44456 24.45772  -7.99518  1.000 54.58113  ? 131 GLN   A O   1 
ATOM   1100 C CB  . GLN   A 1 134 ? 26.80997 24.82781  -6.37584  1.000 60.58325  ? 131 GLN   A CB  1 
ATOM   1101 C CG  . GLN   A 1 134 ? 25.98121 25.71965  -5.46465  1.000 65.04860  ? 131 GLN   A CG  1 
ATOM   1102 C CD  . GLN   A 1 134 ? 24.48649 25.54420  -5.66989  1.000 75.94398  ? 131 GLN   A CD  1 
ATOM   1103 O OE1 . GLN   A 1 134 ? 23.98217 25.64568  -6.78788  1.000 56.25709  ? 131 GLN   A OE1 1 
ATOM   1104 N NE2 . GLN   A 1 134 ? 23.77020 25.27750  -4.58418  1.000 75.20432  ? 131 GLN   A NE2 1 
ATOM   1105 N N   . ASN   A 1 135 ? 27.79003 23.87620  -9.40737  1.000 48.59298  ? 132 ASN   A N   1 
ATOM   1106 C CA  . ASN   A 1 135 ? 28.60076 22.93637  -10.17088 1.000 53.24100  ? 132 ASN   A CA  1 
ATOM   1107 C C   . ASN   A 1 135 ? 29.15663 23.53992  -11.45569 1.000 57.80573  ? 132 ASN   A C   1 
ATOM   1108 O O   . ASN   A 1 135 ? 29.74000 22.81416  -12.26754 1.000 51.30800  ? 132 ASN   A O   1 
ATOM   1109 C CB  . ASN   A 1 135 ? 27.79044 21.67758  -10.49007 1.000 56.15960  ? 132 ASN   A CB  1 
ATOM   1110 C CG  . ASN   A 1 135 ? 27.50510 20.84372  -9.25732  1.000 53.37074  ? 132 ASN   A CG  1 
ATOM   1111 O OD1 . ASN   A 1 135 ? 28.24530 20.89890  -8.27615  1.000 64.33200  ? 132 ASN   A OD1 1 
ATOM   1112 N ND2 . ASN   A 1 135 ? 26.42930 20.06510  -9.30065  1.000 55.13938  ? 132 ASN   A ND2 1 
ATOM   1113 N N   . LEU   A 1 136 ? 28.99322 24.84427  -11.65646 1.000 58.43472  ? 133 LEU   A N   1 
ATOM   1114 C CA  . LEU   A 1 136 ? 29.52040 25.54431  -12.82105 1.000 55.13704  ? 133 LEU   A CA  1 
ATOM   1115 C C   . LEU   A 1 136 ? 30.65492 26.44915  -12.36076 1.000 58.47672  ? 133 LEU   A C   1 
ATOM   1116 O O   . LEU   A 1 136 ? 30.42764 27.39390  -11.59782 1.000 56.57609  ? 133 LEU   A O   1 
ATOM   1117 C CB  . LEU   A 1 136 ? 28.42183 26.34893  -13.51544 1.000 52.54317  ? 133 LEU   A CB  1 
ATOM   1118 C CG  . LEU   A 1 136 ? 27.13382 25.56802  -13.78757 1.000 55.33411  ? 133 LEU   A CG  1 
ATOM   1119 C CD1 . LEU   A 1 136 ? 26.12321 26.42811  -14.52915 1.000 60.08369  ? 133 LEU   A CD1 1 
ATOM   1120 C CD2 . LEU   A 1 136 ? 27.43258 24.29522  -14.56530 1.000 49.96015  ? 133 LEU   A CD2 1 
ATOM   1121 N N   . LEU   A 1 137 ? 31.86928 26.15541  -12.81630 1.000 53.88640  ? 134 LEU   A N   1 
ATOM   1122 C CA  . LEU   A 1 137 ? 33.07334 26.82186  -12.34172 1.000 58.08702  ? 134 LEU   A CA  1 
ATOM   1123 C C   . LEU   A 1 137 ? 33.63322 27.73425  -13.42269 1.000 59.01065  ? 134 LEU   A C   1 
ATOM   1124 O O   . LEU   A 1 137 ? 33.65293 27.37493  -14.60369 1.000 61.54380  ? 134 LEU   A O   1 
ATOM   1125 C CB  . LEU   A 1 137 ? 34.13351 25.80184  -11.92465 1.000 52.53658  ? 134 LEU   A CB  1 
ATOM   1126 C CG  . LEU   A 1 137 ? 33.67923 24.81670  -10.84872 1.000 51.45816  ? 134 LEU   A CG  1 
ATOM   1127 C CD1 . LEU   A 1 137 ? 34.78123 23.82223  -10.54244 1.000 63.18970  ? 134 LEU   A CD1 1 
ATOM   1128 C CD2 . LEU   A 1 137 ? 33.25845 25.56528  -9.59526  1.000 58.98500  ? 134 LEU   A CD2 1 
ATOM   1129 N N   . ILE   A 1 138 ? 34.09485 28.91144  -13.00847 1.000 53.99001  ? 135 ILE   A N   1 
ATOM   1130 C CA  . ILE   A 1 138 ? 34.64385 29.91312  -13.91249 1.000 52.17209  ? 135 ILE   A CA  1 
ATOM   1131 C C   . ILE   A 1 138 ? 36.08574 30.19899  -13.51384 1.000 65.76173  ? 135 ILE   A C   1 
ATOM   1132 O O   . ILE   A 1 138 ? 36.48033 30.00734  -12.35800 1.000 65.49226  ? 135 ILE   A O   1 
ATOM   1133 C CB  . ILE   A 1 138 ? 33.80651 31.21142  -13.90397 1.000 60.68290  ? 135 ILE   A CB  1 
ATOM   1134 C CG1 . ILE   A 1 138 ? 33.87122 31.87603  -12.52736 1.000 67.84773  ? 135 ILE   A CG1 1 
ATOM   1135 C CG2 . ILE   A 1 138 ? 32.36283 30.92166  -14.27577 1.000 63.16356  ? 135 ILE   A CG2 1 
ATOM   1136 C CD1 . ILE   A 1 138 ? 33.08717 33.16523  -12.42511 1.000 70.20363  ? 135 ILE   A CD1 1 
ATOM   1137 N N   . ASN   A 1 139 ? 36.87387 30.65831  -14.48052 1.000 62.53682  ? 136 ASN   A N   1 
ATOM   1138 C CA  . ASN   A 1 139 ? 38.23894 31.10401  -14.24170 1.000 66.64083  ? 136 ASN   A CA  1 
ATOM   1139 C C   . ASN   A 1 139 ? 38.35199 32.58884  -14.57803 1.000 68.19138  ? 136 ASN   A C   1 
ATOM   1140 O O   . ASN   A 1 139 ? 37.37779 33.24037  -14.96440 1.000 66.02531  ? 136 ASN   A O   1 
ATOM   1141 C CB  . ASN   A 1 139 ? 39.24596 30.27482  -15.04821 1.000 76.70757  ? 136 ASN   A CB  1 
ATOM   1142 C CG  . ASN   A 1 139 ? 39.03715 30.37902  -16.55281 1.000 71.47926  ? 136 ASN   A CG  1 
ATOM   1143 O OD1 . ASN   A 1 139 ? 38.12919 31.06076  -17.03031 1.000 71.45942  ? 136 ASN   A OD1 1 
ATOM   1144 N ND2 . ASN   A 1 139 ? 39.89287 29.69948  -17.30838 1.000 74.28609  ? 136 ASN   A ND2 1 
ATOM   1145 N N   . THR   A 1 140 ? 39.56224 33.12267  -14.43398 1.000 71.59476  ? 137 THR   A N   1 
ATOM   1146 C CA  . THR   A 1 140 ? 39.82382 34.53228  -14.69769 1.000 74.57552  ? 137 THR   A CA  1 
ATOM   1147 C C   . THR   A 1 140 ? 40.08558 34.82524  -16.17124 1.000 73.87330  ? 137 THR   A C   1 
ATOM   1148 O O   . THR   A 1 140 ? 40.57034 35.91410  -16.49544 1.000 79.42492  ? 137 THR   A O   1 
ATOM   1149 C CB  . THR   A 1 140 ? 41.00965 35.01168  -13.85583 1.000 75.41270  ? 137 THR   A CB  1 
ATOM   1150 O OG1 . THR   A 1 140 ? 42.16759 34.22418  -14.16241 1.000 82.96213  ? 137 THR   A OG1 1 
ATOM   1151 C CG2 . THR   A 1 140 ? 40.69687 34.89065  -12.37227 1.000 64.26033  ? 137 THR   A CG2 1 
ATOM   1152 N N   . GLU   A 1 141 ? 39.76980 33.89025  -17.06824 1.000 79.58969  ? 138 GLU   A N   1 
ATOM   1153 C CA  . GLU   A 1 141 ? 39.98041 34.07761  -18.49873 1.000 74.79235  ? 138 GLU   A CA  1 
ATOM   1154 C C   . GLU   A 1 141 ? 38.67769 33.98426  -19.28581 1.000 72.54829  ? 138 GLU   A C   1 
ATOM   1155 O O   . GLU   A 1 141 ? 38.70193 33.70818  -20.48879 1.000 70.01643  ? 138 GLU   A O   1 
ATOM   1156 C CB  . GLU   A 1 141 ? 41.00085 33.06484  -19.02168 1.000 74.90163  ? 138 GLU   A CB  1 
ATOM   1157 C CG  . GLU   A 1 141 ? 42.35394 33.15795  -18.33439 1.000 79.27382  ? 138 GLU   A CG  1 
ATOM   1158 C CD  . GLU   A 1 141 ? 43.34942 32.14463  -18.85760 1.000 94.44367  ? 138 GLU   A CD  1 
ATOM   1159 O OE1 . GLU   A 1 141 ? 42.93517 31.22195  -19.59051 1.000 87.56478  ? 138 GLU   A OE1 1 
ATOM   1160 O OE2 . GLU   A 1 141 ? 44.54884 32.27383  -18.53578 1.000 87.90945  ? 138 GLU   A OE2 1 
ATOM   1161 N N   . GLY   A 1 142 ? 37.54071 34.20404  -18.62914 1.000 75.62588  ? 139 GLY   A N   1 
ATOM   1162 C CA  . GLY   A 1 142 ? 36.26090 34.23920  -19.30588 1.000 61.92557  ? 139 GLY   A CA  1 
ATOM   1163 C C   . GLY   A 1 142 ? 35.64074 32.89547  -19.60997 1.000 59.36902  ? 139 GLY   A C   1 
ATOM   1164 O O   . GLY   A 1 142 ? 34.64268 32.84596  -20.33732 1.000 67.31955  ? 139 GLY   A O   1 
ATOM   1165 N N   . ALA   A 1 143 ? 36.18488 31.80730  -19.07769 1.000 64.83408  ? 140 ALA   A N   1 
ATOM   1166 C CA  . ALA   A 1 143 ? 35.68181 30.47308  -19.36358 1.000 65.72126  ? 140 ALA   A CA  1 
ATOM   1167 C C   . ALA   A 1 143 ? 34.82685 29.95865  -18.21170 1.000 65.40256  ? 140 ALA   A C   1 
ATOM   1168 O O   . ALA   A 1 143 ? 34.98441 30.37595  -17.06224 1.000 62.20997  ? 140 ALA   A O   1 
ATOM   1169 C CB  . ALA   A 1 143 ? 36.83415 29.50275  -19.63070 1.000 64.23368  ? 140 ALA   A CB  1 
ATOM   1170 N N   . ILE   A 1 144 ? 33.91228 29.04673  -18.53840 1.000 58.78461  ? 141 ILE   A N   1 
ATOM   1171 C CA  . ILE   A 1 144 ? 33.05563 28.38405  -17.56005 1.000 57.11833  ? 141 ILE   A CA  1 
ATOM   1172 C C   . ILE   A 1 144 ? 33.00252 26.90140  -17.90996 1.000 64.28524  ? 141 ILE   A C   1 
ATOM   1173 O O   . ILE   A 1 144 ? 32.96469 26.53286  -19.08924 1.000 61.43589  ? 141 ILE   A O   1 
ATOM   1174 C CB  . ILE   A 1 144 ? 31.64340 29.00989  -17.51913 1.000 56.31861  ? 141 ILE   A CB  1 
ATOM   1175 C CG1 . ILE   A 1 144 ? 30.80252 28.38032  -16.40504 1.000 55.30846  ? 141 ILE   A CG1 1 
ATOM   1176 C CG2 . ILE   A 1 144 ? 30.95015 28.88416  -18.87201 1.000 57.26073  ? 141 ILE   A CG2 1 
ATOM   1177 C CD1 . ILE   A 1 144 ? 29.46492 29.05766  -16.19476 1.000 50.26405  ? 141 ILE   A CD1 1 
ATOM   1178 N N   . LYS   A 1 145 ? 33.02390 26.04601  -16.88617 1.000 58.96616  ? 142 LYS   A N   1 
ATOM   1179 C CA  . LYS   A 1 145 ? 33.20086 24.61538  -17.09441 1.000 57.56221  ? 142 LYS   A CA  1 
ATOM   1180 C C   . LYS   A 1 145 ? 32.26055 23.82520  -16.19516 1.000 59.95857  ? 142 LYS   A C   1 
ATOM   1181 O O   . LYS   A 1 145 ? 31.94174 24.24399  -15.07919 1.000 55.63180  ? 142 LYS   A O   1 
ATOM   1182 C CB  . LYS   A 1 145 ? 34.65544 24.19041  -16.83270 1.000 53.50689  ? 142 LYS   A CB  1 
ATOM   1183 C CG  . LYS   A 1 145 ? 35.68535 25.03373  -17.57425 1.000 53.43945  ? 142 LYS   A CG  1 
ATOM   1184 C CD  . LYS   A 1 145 ? 37.07041 24.41750  -17.53843 1.000 57.19456  ? 142 LYS   A CD  1 
ATOM   1185 C CE  . LYS   A 1 145 ? 38.06869 25.30305  -18.26589 1.000 52.75239  ? 142 LYS   A CE  1 
ATOM   1186 N NZ  . LYS   A 1 145 ? 39.34453 24.58736  -18.53885 1.000 62.09337  ? 142 LYS   A NZ  1 
ATOM   1187 N N   . LEU   A 1 146 ? 31.82378 22.67076  -16.69801 1.000 54.72541  ? 143 LEU   A N   1 
ATOM   1188 C CA  . LEU   A 1 146 ? 30.97438 21.76757  -15.93254 1.000 53.90730  ? 143 LEU   A CA  1 
ATOM   1189 C C   . LEU   A 1 146 ? 31.81171 20.97153  -14.94034 1.000 55.00302  ? 143 LEU   A C   1 
ATOM   1190 O O   . LEU   A 1 146 ? 32.89917 20.49121  -15.27119 1.000 55.30916  ? 143 LEU   A O   1 
ATOM   1191 C CB  . LEU   A 1 146 ? 30.23244 20.80507  -16.86258 1.000 53.42393  ? 143 LEU   A CB  1 
ATOM   1192 C CG  . LEU   A 1 146 ? 29.36467 21.37133  -17.98759 1.000 60.00105  ? 143 LEU   A CG  1 
ATOM   1193 C CD1 . LEU   A 1 146 ? 28.74671 20.24141  -18.80294 1.000 52.33623  ? 143 LEU   A CD1 1 
ATOM   1194 C CD2 . LEU   A 1 146 ? 28.28537 22.27874  -17.42756 1.000 58.72750  ? 143 LEU   A CD2 1 
ATOM   1195 N N   . ALA   A 1 147 ? 31.29431 20.81865  -13.72283 1.000 53.46152  ? 144 ALA   A N   1 
ATOM   1196 C CA  . ALA   A 1 147 ? 32.01395 20.12270  -12.66667 1.000 51.45702  ? 144 ALA   A CA  1 
ATOM   1197 C C   . ALA   A 1 147 ? 31.07002 19.17468  -11.94087 1.000 62.72718  ? 144 ALA   A C   1 
ATOM   1198 O O   . ALA   A 1 147 ? 29.85206 19.20014  -12.13903 1.000 51.79401  ? 144 ALA   A O   1 
ATOM   1199 C CB  . ALA   A 1 147 ? 32.64806 21.10667  -11.67644 1.000 55.87605  ? 144 ALA   A CB  1 
ATOM   1200 N N   . ASP   A 1 148 ? 31.66042 18.33161  -11.08940 1.000 59.35084  ? 145 ASP   A N   1 
ATOM   1201 C CA  . ASP   A 1 148 ? 30.93909 17.36511  -10.26643 1.000 60.78384  ? 145 ASP   A CA  1 
ATOM   1202 C C   . ASP   A 1 148 ? 30.11284 16.40838  -11.11751 1.000 59.39735  ? 145 ASP   A C   1 
ATOM   1203 O O   . ASP   A 1 148 ? 28.92657 16.64871  -11.36314 1.000 58.26308  ? 145 ASP   A O   1 
ATOM   1204 C CB  . ASP   A 1 148 ? 30.04495 18.08030  -9.24861  1.000 56.30180  ? 145 ASP   A CB  1 
ATOM   1205 C CG  . ASP   A 1 148 ? 29.64191 17.18062  -8.09153  1.000 71.21099  ? 145 ASP   A CG  1 
ATOM   1206 O OD1 . ASP   A 1 148 ? 29.91290 15.96226  -8.15858  1.000 64.96633  ? 145 ASP   A OD1 1 
ATOM   1207 O OD2 . ASP   A 1 148 ? 29.06159 17.69294  -7.11077  1.000 69.26698  ? 145 ASP   A OD2 1 
ATOM   1208 N N   . PHE   A 1 149 ? 30.73227 15.31489  -11.56192 1.000 61.24706  ? 146 PHE   A N   1 
ATOM   1209 C CA  . PHE   A 1 149 ? 30.05444 14.26964  -12.31639 1.000 58.17700  ? 146 PHE   A CA  1 
ATOM   1210 C C   . PHE   A 1 149 ? 29.71005 13.05993  -11.45353 1.000 58.99262  ? 146 PHE   A C   1 
ATOM   1211 O O   . PHE   A 1 149 ? 29.54362 11.95496  -11.98326 1.000 59.17661  ? 146 PHE   A O   1 
ATOM   1212 C CB  . PHE   A 1 149 ? 30.90981 13.83944  -13.50896 1.000 54.28185  ? 146 PHE   A CB  1 
ATOM   1213 C CG  . PHE   A 1 149 ? 30.83082 14.77336  -14.68106 1.000 56.75008  ? 146 PHE   A CG  1 
ATOM   1214 C CD1 . PHE   A 1 149 ? 31.44823 16.01239  -14.64179 1.000 57.79425  ? 146 PHE   A CD1 1 
ATOM   1215 C CD2 . PHE   A 1 149 ? 30.14576 14.40697  -15.82738 1.000 50.90764  ? 146 PHE   A CD2 1 
ATOM   1216 C CE1 . PHE   A 1 149 ? 31.37765 16.87174  -15.72260 1.000 55.42088  ? 146 PHE   A CE1 1 
ATOM   1217 C CE2 . PHE   A 1 149 ? 30.07235 15.26026  -16.91051 1.000 47.56477  ? 146 PHE   A CE2 1 
ATOM   1218 C CZ  . PHE   A 1 149 ? 30.68984 16.49445  -16.85808 1.000 55.22796  ? 146 PHE   A CZ  1 
ATOM   1219 N N   . GLY   A 1 150 ? 29.60382 13.24634  -10.13524 1.000 58.16188  ? 147 GLY   A N   1 
ATOM   1220 C CA  . GLY   A 1 150 ? 29.27468 12.13402  -9.26048  1.000 62.11238  ? 147 GLY   A CA  1 
ATOM   1221 C C   . GLY   A 1 150 ? 27.87074 11.60478  -9.46595  1.000 60.87770  ? 147 GLY   A C   1 
ATOM   1222 O O   . GLY   A 1 150 ? 27.61104 10.41922  -9.23934  1.000 60.99834  ? 147 GLY   A O   1 
ATOM   1223 N N   . LEU   A 1 151 ? 26.94982 12.46604  -9.89080  1.000 58.97667  ? 148 LEU   A N   1 
ATOM   1224 C CA  . LEU   A 1 151 ? 25.58577 12.06844  -10.20473 1.000 60.30787  ? 148 LEU   A CA  1 
ATOM   1225 C C   . LEU   A 1 151 ? 25.38431 11.81556  -11.69226 1.000 57.21559  ? 148 LEU   A C   1 
ATOM   1226 O O   . LEU   A 1 151 ? 24.24818 11.60579  -12.12939 1.000 59.75861  ? 148 LEU   A O   1 
ATOM   1227 C CB  . LEU   A 1 151 ? 24.60128 13.13015  -9.71194  1.000 57.97996  ? 148 LEU   A CB  1 
ATOM   1228 C CG  . LEU   A 1 151 ? 24.52362 13.29668  -8.19376  1.000 71.10187  ? 148 LEU   A CG  1 
ATOM   1229 C CD1 . LEU   A 1 151 ? 23.58421 14.43017  -7.82398  1.000 74.28931  ? 148 LEU   A CD1 1 
ATOM   1230 C CD2 . LEU   A 1 151 ? 24.08299 11.99807  -7.53797  1.000 65.72660  ? 148 LEU   A CD2 1 
ATOM   1231 N N   . ALA   A 1 152 ? 26.45809 11.83148  -12.47546 1.000 56.08503  ? 149 ALA   A N   1 
ATOM   1232 C CA  . ALA   A 1 152 ? 26.36323 11.59370  -13.90468 1.000 56.77508  ? 149 ALA   A CA  1 
ATOM   1233 C C   . ALA   A 1 152 ? 26.19504 10.10529  -14.19274 1.000 53.02969  ? 149 ALA   A C   1 
ATOM   1234 O O   . ALA   A 1 152 ? 26.54165 9.24361   -13.38086 1.000 56.21428  ? 149 ALA   A O   1 
ATOM   1235 C CB  . ALA   A 1 152 ? 27.60133 12.13183  -14.62344 1.000 48.71488  ? 149 ALA   A CB  1 
ATOM   1236 N N   . ARG   A 1 153 ? 25.65212 9.80909   -15.37155 1.000 58.00155  ? 150 ARG   A N   1 
ATOM   1237 C CA  . ARG   A 1 153 ? 25.47087 8.42897   -15.79362 1.000 58.94885  ? 150 ARG   A CA  1 
ATOM   1238 C C   . ARG   A 1 153 ? 25.51548 8.34602   -17.31107 1.000 62.61587  ? 150 ARG   A C   1 
ATOM   1239 O O   . ARG   A 1 153 ? 24.91364 9.16954   -18.00521 1.000 62.03943  ? 150 ARG   A O   1 
ATOM   1240 C CB  . ARG   A 1 153 ? 24.14732 7.84881   -15.28128 1.000 62.62723  ? 150 ARG   A CB  1 
ATOM   1241 C CG  . ARG   A 1 153 ? 23.96079 6.37742   -15.62338 1.000 76.37195  ? 150 ARG   A CG  1 
ATOM   1242 C CD  . ARG   A 1 153 ? 22.55915 5.88618   -15.29929 1.000 82.27170  ? 150 ARG   A CD  1 
ATOM   1243 N NE  . ARG   A 1 153 ? 22.41195 4.46283   -15.58058 1.000 84.61036  ? 150 ARG   A NE  1 
ATOM   1244 C CZ  . ARG   A 1 153 ? 22.62680 3.49669   -14.69761 1.000 84.91480  ? 150 ARG   A CZ  1 
ATOM   1245 N NH1 . ARG   A 1 153 ? 22.97724 3.76475   -13.45042 1.000 91.71932  ? 150 ARG   A NH1 1 
ATOM   1246 N NH2 . ARG   A 1 153 ? 22.48896 2.22906   -15.07626 1.000 90.20397  ? 150 ARG   A NH2 1 
ATOM   1247 N N   . ALA   A 1 154 ? 26.23013 7.34516   -17.81620 1.000 61.70843  ? 151 ALA   A N   1 
ATOM   1248 C CA  . ALA   A 1 154 ? 26.21427 7.04736   -19.23996 1.000 66.05288  ? 151 ALA   A CA  1 
ATOM   1249 C C   . ALA   A 1 154 ? 24.94139 6.28619   -19.58681 1.000 66.73701  ? 151 ALA   A C   1 
ATOM   1250 O O   . ALA   A 1 154 ? 24.61987 5.27727   -18.95107 1.000 75.17860  ? 151 ALA   A O   1 
ATOM   1251 C CB  . ALA   A 1 154 ? 27.44680 6.23319   -19.63242 1.000 57.48975  ? 151 ALA   A CB  1 
ATOM   1252 N N   . PHE   A 1 155 ? 24.21134 6.77229   -20.58601 1.000 64.79566  ? 152 PHE   A N   1 
ATOM   1253 C CA  . PHE   A 1 155 ? 22.97419 6.13436   -21.01023 1.000 64.52990  ? 152 PHE   A CA  1 
ATOM   1254 C C   . PHE   A 1 155 ? 23.20387 5.34318   -22.28970 1.000 69.24732  ? 152 PHE   A C   1 
ATOM   1255 O O   . PHE   A 1 155 ? 23.96608 5.76165   -23.16567 1.000 71.70321  ? 152 PHE   A O   1 
ATOM   1256 C CB  . PHE   A 1 155 ? 21.85095 7.15924   -21.21361 1.000 67.13112  ? 152 PHE   A CB  1 
ATOM   1257 C CG  . PHE   A 1 155 ? 22.07593 8.11553   -22.36000 1.000 66.51902  ? 152 PHE   A CG  1 
ATOM   1258 C CD1 . PHE   A 1 155 ? 21.64253 7.80638   -23.64210 1.000 63.75718  ? 152 PHE   A CD1 1 
ATOM   1259 C CD2 . PHE   A 1 155 ? 22.68785 9.33878   -22.14678 1.000 61.49115  ? 152 PHE   A CD2 1 
ATOM   1260 C CE1 . PHE   A 1 155 ? 21.83816 8.68965   -24.69253 1.000 69.54559  ? 152 PHE   A CE1 1 
ATOM   1261 C CE2 . PHE   A 1 155 ? 22.87853 10.22996  -23.18954 1.000 67.32672  ? 152 PHE   A CE2 1 
ATOM   1262 C CZ  . PHE   A 1 155 ? 22.45711 9.90186   -24.46599 1.000 64.50314  ? 152 PHE   A CZ  1 
ATOM   1263 N N   . GLY   A 1 156 ? 22.54366 4.19041   -22.38544 1.000 69.31372  ? 153 GLY   A N   1 
ATOM   1264 C CA  . GLY   A 1 156 ? 22.63841 3.36638   -23.56972 1.000 81.41795  ? 153 GLY   A CA  1 
ATOM   1265 C C   . GLY   A 1 156 ? 21.64206 3.77294   -24.63763 1.000 83.52765  ? 153 GLY   A C   1 
ATOM   1266 O O   . GLY   A 1 156 ? 20.81095 4.65852   -24.44898 1.000 81.54042  ? 153 GLY   A O   1 
ATOM   1267 N N   . VAL   A 1 157 ? 21.74091 3.10682   -25.77919 1.000 92.36117  ? 154 VAL   A N   1 
ATOM   1268 C CA  . VAL   A 1 157 ? 20.85458 3.33195   -26.91144 1.000 94.14618  ? 154 VAL   A CA  1 
ATOM   1269 C C   . VAL   A 1 157 ? 20.18324 2.00883   -27.25820 1.000 94.33005  ? 154 VAL   A C   1 
ATOM   1270 O O   . VAL   A 1 157 ? 20.78429 1.14272   -27.89379 1.000 97.62573  ? 154 VAL   A O   1 
ATOM   1271 C CB  . VAL   A 1 157 ? 21.61605 3.90453   -28.12093 1.000 94.00009  ? 154 VAL   A CB  1 
ATOM   1272 C CG1 . VAL   A 1 157 ? 20.65818 4.17732   -29.27013 1.000 91.28392  ? 154 VAL   A CG1 1 
ATOM   1273 C CG2 . VAL   A 1 157 ? 22.35928 5.17452   -27.72744 1.000 85.26489  ? 154 VAL   A CG2 1 
ATOM   1274 N N   . PRO   A 1 158 ? 18.92243 1.81269   -26.85108 1.000 91.78695  ? 155 PRO   A N   1 
ATOM   1275 C CA  . PRO   A 1 158 ? 18.05265 2.74387   -26.11943 1.000 89.45754  ? 155 PRO   A CA  1 
ATOM   1276 C C   . PRO   A 1 158 ? 18.34690 2.77745   -24.62243 1.000 88.59110  ? 155 PRO   A C   1 
ATOM   1277 O O   . PRO   A 1 158 ? 19.10734 1.96016   -24.11074 1.000 82.63083  ? 155 PRO   A O   1 
ATOM   1278 C CB  . PRO   A 1 158 ? 16.65623 2.18632   -26.40986 1.000 90.53052  ? 155 PRO   A CB  1 
ATOM   1279 C CG  . PRO   A 1 158 ? 16.88391 0.70006   -26.46471 1.000 92.66271  ? 155 PRO   A CG  1 
ATOM   1280 C CD  . PRO   A 1 158 ? 18.24075 0.53158   -27.11619 1.000 95.34667  ? 155 PRO   A CD  1 
ATOM   1281 N N   . VAL   A 1 159 ? 17.75155 3.72332   -23.89784 1.000 83.87294  ? 156 VAL   A N   1 
ATOM   1282 C CA  . VAL   A 1 159 ? 17.95002 3.83620   -22.45797 1.000 79.69619  ? 156 VAL   A CA  1 
ATOM   1283 C C   . VAL   A 1 159 ? 16.98554 2.89738   -21.74822 1.000 81.37062  ? 156 VAL   A C   1 
ATOM   1284 O O   . VAL   A 1 159 ? 16.05054 2.36810   -22.36008 1.000 83.79943  ? 156 VAL   A O   1 
ATOM   1285 C CB  . VAL   A 1 159 ? 17.75344 5.28553   -21.97575 1.000 74.25827  ? 156 VAL   A CB  1 
ATOM   1286 C CG1 . VAL   A 1 159 ? 18.46503 6.25878   -22.90235 1.000 69.95672  ? 156 VAL   A CG1 1 
ATOM   1287 C CG2 . VAL   A 1 159 ? 16.27030 5.61628   -21.87357 1.000 74.02643  ? 156 VAL   A CG2 1 
ATOM   1288 N N   . ARG   A 1 160 ? 17.21036 2.68091   -20.45580 1.000 80.42153  ? 157 ARG   A N   1 
ATOM   1289 C CA  . ARG   A 1 160 ? 16.28113 1.95561   -19.60385 1.000 82.99527  ? 157 ARG   A CA  1 
ATOM   1290 C C   . ARG   A 1 160 ? 15.98014 2.81398   -18.38059 1.000 78.94978  ? 157 ARG   A C   1 
ATOM   1291 O O   . ARG   A 1 160 ? 16.45174 3.94947   -18.26173 1.000 77.50185  ? 157 ARG   A O   1 
ATOM   1292 C CB  . ARG   A 1 160 ? 16.83754 0.58073   -19.20666 1.000 79.89915  ? 157 ARG   A CB  1 
ATOM   1293 C CG  . ARG   A 1 160 ? 17.95001 0.61340   -18.17085 1.000 78.42972  ? 157 ARG   A CG  1 
ATOM   1294 C CD  . ARG   A 1 160 ? 18.32876 -0.79639  -17.74039 1.000 80.57642  ? 157 ARG   A CD  1 
ATOM   1295 N NE  . ARG   A 1 160 ? 19.05490 -0.81198  -16.47607 1.000 89.77584  ? 157 ARG   A NE  1 
ATOM   1296 C CZ  . ARG   A 1 160 ? 20.37647 -0.83160  -16.36805 1.000 82.25311  ? 157 ARG   A CZ  1 
ATOM   1297 N NH1 . ARG   A 1 160 ? 21.15796 -0.83634  -17.43621 1.000 79.53172  ? 157 ARG   A NH1 1 
ATOM   1298 N NH2 . ARG   A 1 160 ? 20.92818 -0.84900  -15.15747 1.000 75.43978  ? 157 ARG   A NH2 1 
ATOM   1299 N N   . THR   A 1 161 ? 15.17969 2.26867   -17.46823 1.000 73.16881  ? 158 THR   A N   1 
ATOM   1300 C CA  . THR   A 1 161 ? 14.78391 3.01333   -16.27952 1.000 77.89910  ? 158 THR   A CA  1 
ATOM   1301 C C   . THR   A 1 161 ? 15.99484 3.29443   -15.40097 1.000 81.91524  ? 158 THR   A C   1 
ATOM   1302 O O   . THR   A 1 161 ? 16.63878 2.36813   -14.89943 1.000 81.83890  ? 158 THR   A O   1 
ATOM   1303 C CB  . THR   A 1 161 ? 13.72585 2.23787   -15.49705 1.000 70.68110  ? 158 THR   A CB  1 
ATOM   1304 O OG1 . THR   A 1 161 ? 12.58743 2.00958   -16.33590 1.000 81.73539  ? 158 THR   A OG1 1 
ATOM   1305 C CG2 . THR   A 1 161 ? 13.29128 3.02680   -14.26932 1.000 79.64114  ? 158 THR   A CG2 1 
ATOM   1306 N N   . TYR   A 1 162 ? 16.30370 4.57458   -15.21925 1.000 78.80951  ? 159 TYR   A N   1 
ATOM   1307 C CA  . TYR   A 1 162 ? 17.44928 4.98041   -14.41087 1.000 77.74953  ? 159 TYR   A CA  1 
ATOM   1308 C C   . TYR   A 1 162 ? 17.00566 5.46784   -13.03389 1.000 74.20222  ? 159 TYR   A C   1 
ATOM   1309 O O   . TYR   A 1 162 ? 15.82930 5.36814   -12.68728 1.000 71.76523  ? 159 TYR   A O   1 
ATOM   1310 C CB  . TYR   A 1 162 ? 18.25252 6.06678   -15.13086 1.000 80.63457  ? 159 TYR   A CB  1 
ATOM   1311 C CG  . TYR   A 1 162 ? 18.87762 5.59294   -16.42295 1.000 73.85347  ? 159 TYR   A CG  1 
ATOM   1312 C CD1 . TYR   A 1 162 ? 19.24677 4.26439   -16.58845 1.000 71.06963  ? 159 TYR   A CD1 1 
ATOM   1313 C CD2 . TYR   A 1 162 ? 19.08995 6.46879   -17.48026 1.000 74.78083  ? 159 TYR   A CD2 1 
ATOM   1314 C CE1 . TYR   A 1 162 ? 19.81463 3.82114   -17.76673 1.000 78.28014  ? 159 TYR   A CE1 1 
ATOM   1315 C CE2 . TYR   A 1 162 ? 19.65766 6.03345   -18.66466 1.000 67.45211  ? 159 TYR   A CE2 1 
ATOM   1316 C CZ  . TYR   A 1 162 ? 20.01806 4.70774   -18.80121 1.000 76.40035  ? 159 TYR   A CZ  1 
ATOM   1317 O OH  . TYR   A 1 162 ? 20.58265 4.26243   -19.97478 1.000 72.27680  ? 159 TYR   A OH  1 
HETATM 1318 N N   . TPO   A 1 163 ? 17.95355 5.98971   -12.25767 1.000 73.05347  ? 160 TPO   A N   1 
HETATM 1319 C CA  . TPO   A 1 163 ? 17.68525 6.43771   -10.89223 1.000 76.02136  ? 160 TPO   A CA  1 
HETATM 1320 C CB  . TPO   A 1 163 ? 18.97438 6.92473   -10.20035 1.000 79.80042  ? 160 TPO   A CB  1 
HETATM 1321 C CG2 . TPO   A 1 163 ? 18.68841 7.45005   -8.79788  1.000 71.59600  ? 160 TPO   A CG2 1 
HETATM 1322 O OG1 . TPO   A 1 163 ? 19.86845 5.84235   -10.13738 1.000 80.20356  ? 160 TPO   A OG1 1 
HETATM 1323 P P   . TPO   A 1 163 ? 21.37033 5.96647   -10.95536 1.000 73.90219  ? 160 TPO   A P   1 
HETATM 1324 O O1P . TPO   A 1 163 ? 21.95671 4.59222   -10.65706 1.000 78.17225  ? 160 TPO   A O1P 1 
HETATM 1325 O O2P . TPO   A 1 163 ? 21.00435 6.20670   -12.41868 1.000 68.98807  ? 160 TPO   A O2P 1 
HETATM 1326 O O3P . TPO   A 1 163 ? 22.09439 7.13887   -10.29703 1.000 74.96695  ? 160 TPO   A O3P 1 
HETATM 1327 C C   . TPO   A 1 163 ? 16.63911 7.55038   -10.85212 1.000 74.15147  ? 160 TPO   A C   1 
HETATM 1328 O O   . TPO   A 1 163 ? 16.72797 8.53165   -11.58934 1.000 78.30708  ? 160 TPO   A O   1 
ATOM   1329 N N   . HIS   A 1 164 ? 15.64201 7.37936   -9.99074  1.000 73.54801  ? 161 HIS   A N   1 
ATOM   1330 C CA  . HIS   A 1 164 ? 14.55996 8.34595   -9.85604  1.000 85.76019  ? 161 HIS   A CA  1 
ATOM   1331 C C   . HIS   A 1 164 ? 14.93566 9.50205   -8.93431  1.000 87.76513  ? 161 HIS   A C   1 
ATOM   1332 O O   . HIS   A 1 164 ? 15.85928 9.38856   -8.12673  1.000 82.53865  ? 161 HIS   A O   1 
ATOM   1333 C CB  . HIS   A 1 164 ? 13.30434 7.65262   -9.33028  1.000 89.25686  ? 161 HIS   A CB  1 
ATOM   1334 C CG  . HIS   A 1 164 ? 13.50258 6.96848   -8.01304  1.000 89.30715  ? 161 HIS   A CG  1 
ATOM   1335 N ND1 . HIS   A 1 164 ? 13.20552 7.57086   -6.80940  1.000 96.93139  ? 161 HIS   A ND1 1 
ATOM   1336 C CD2 . HIS   A 1 164 ? 13.97714 5.73675   -7.70998  1.000 91.52045  ? 161 HIS   A CD2 1 
ATOM   1337 C CE1 . HIS   A 1 164 ? 13.48275 6.73810   -5.82205  1.000 99.03565  ? 161 HIS   A CE1 1 
ATOM   1338 N NE2 . HIS   A 1 164 ? 13.95285 5.61824   -6.34140  1.000 107.21022 ? 161 HIS   A NE2 1 
ATOM   1339 N N   . GLU   A 1 165 ? 14.20785 10.61277  -9.07377  1.000 85.67773  ? 162 GLU   A N   1 
ATOM   1340 C CA  . GLU   A 1 165 ? 14.35031 11.78020  -8.20164  1.000 84.60612  ? 162 GLU   A CA  1 
ATOM   1341 C C   . GLU   A 1 165 ? 15.77227 12.33803  -8.24240  1.000 77.47889  ? 162 GLU   A C   1 
ATOM   1342 O O   . GLU   A 1 165 ? 16.38600 12.61837  -7.21095  1.000 87.20413  ? 162 GLU   A O   1 
ATOM   1343 C CB  . GLU   A 1 165 ? 13.93228 11.44529  -6.76739  1.000 84.20287  ? 162 GLU   A CB  1 
ATOM   1344 C CG  . GLU   A 1 165 ? 12.54289 10.84266  -6.66157  1.000 88.76109  ? 162 GLU   A CG  1 
ATOM   1345 C CD  . GLU   A 1 165 ? 12.18366 10.45015  -5.24407  1.000 101.05735 ? 162 GLU   A CD  1 
ATOM   1346 O OE1 . GLU   A 1 165 ? 12.73900 11.05176  -4.30176  1.000 103.40801 ? 162 GLU   A OE1 1 
ATOM   1347 O OE2 . GLU   A 1 165 ? 11.34946 9.53656   -5.07188  1.000 100.57826 ? 162 GLU   A OE2 1 
ATOM   1348 N N   . VAL   A 1 166 ? 16.29763 12.49886  -9.45496  1.000 73.74151  ? 163 VAL   A N   1 
ATOM   1349 C CA  . VAL   A 1 166 ? 17.62939 13.06353  -9.64069  1.000 75.65625  ? 163 VAL   A CA  1 
ATOM   1350 C C   . VAL   A 1 166 ? 17.51846 14.57626  -9.77403  1.000 69.25123  ? 163 VAL   A C   1 
ATOM   1351 O O   . VAL   A 1 166 ? 16.41066 15.12537  -9.79983  1.000 71.12059  ? 163 VAL   A O   1 
ATOM   1352 C CB  . VAL   A 1 166 ? 18.33512 12.44902  -10.86378 1.000 73.23634  ? 163 VAL   A CB  1 
ATOM   1353 C CG1 . VAL   A 1 166 ? 18.67277 10.99099  -10.60305 1.000 76.31512  ? 163 VAL   A CG1 1 
ATOM   1354 C CG2 . VAL   A 1 166 ? 17.46665 12.58700  -12.10582 1.000 58.14983  ? 163 VAL   A CG2 1 
ATOM   1355 N N   . VAL   A 1 167 ? 18.67141 15.24890  -9.85073  1.000 63.28784  ? 164 VAL   A N   1 
ATOM   1356 C CA  . VAL   A 1 167 ? 18.79564 16.69651  -10.02333 1.000 63.19818  ? 164 VAL   A CA  1 
ATOM   1357 C C   . VAL   A 1 167 ? 18.31704 17.43332  -8.77686  1.000 61.03830  ? 164 VAL   A C   1 
ATOM   1358 O O   . VAL   A 1 167 ? 17.31144 17.05915  -8.16316  1.000 60.10144  ? 164 VAL   A O   1 
ATOM   1359 C CB  . VAL   A 1 167 ? 18.04173 17.18697  -11.27572 1.000 60.55435  ? 164 VAL   A CB  1 
ATOM   1360 C CG1 . VAL   A 1 167 ? 18.33530 18.65512  -11.52950 1.000 60.82975  ? 164 VAL   A CG1 1 
ATOM   1361 C CG2 . VAL   A 1 167 ? 18.41689 16.35032  -12.49150 1.000 61.72184  ? 164 VAL   A CG2 1 
ATOM   1362 N N   . THR   A 1 168 ? 19.04437 18.48063  -8.38972  1.000 58.51627  ? 165 THR   A N   1 
ATOM   1363 C CA  . THR   A 1 168 ? 18.60436 19.33556  -7.29590  1.000 54.24171  ? 165 THR   A CA  1 
ATOM   1364 C C   . THR   A 1 168 ? 17.23754 19.93304  -7.62257  1.000 61.44188  ? 165 THR   A C   1 
ATOM   1365 O O   . THR   A 1 168 ? 16.90128 20.17102  -8.78548  1.000 57.52481  ? 165 THR   A O   1 
ATOM   1366 C CB  . THR   A 1 168 ? 19.63628 20.43848  -7.03812  1.000 60.29333  ? 165 THR   A CB  1 
ATOM   1367 O OG1 . THR   A 1 168 ? 20.94161 19.85166  -6.95340  1.000 62.19251  ? 165 THR   A OG1 1 
ATOM   1368 C CG2 . THR   A 1 168 ? 19.34330 21.16846  -5.73533  1.000 50.99372  ? 165 THR   A CG2 1 
ATOM   1369 N N   . LEU   A 1 169 ? 16.44598 20.17529  -6.57411  1.000 47.52671  ? 166 LEU   A N   1 
ATOM   1370 C CA  . LEU   A 1 169 ? 15.01579 20.42062  -6.74933  1.000 56.78105  ? 166 LEU   A CA  1 
ATOM   1371 C C   . LEU   A 1 169 ? 14.74090 21.64140  -7.62343  1.000 60.42974  ? 166 LEU   A C   1 
ATOM   1372 O O   . LEU   A 1 169 ? 13.86982 21.59830  -8.50021  1.000 56.12374  ? 166 LEU   A O   1 
ATOM   1373 C CB  . LEU   A 1 169 ? 14.34626 20.57506  -5.38340  1.000 51.70084  ? 166 LEU   A CB  1 
ATOM   1374 C CG  . LEU   A 1 169 ? 12.81961 20.63380  -5.40106  1.000 58.04558  ? 166 LEU   A CG  1 
ATOM   1375 C CD1 . LEU   A 1 169 ? 12.25283 19.39169  -6.07166  1.000 57.85140  ? 166 LEU   A CD1 1 
ATOM   1376 C CD2 . LEU   A 1 169 ? 12.26888 20.78885  -3.99370  1.000 52.07050  ? 166 LEU   A CD2 1 
ATOM   1377 N N   . TRP   A 1 170 ? 15.47216 22.73704  -7.40594  1.000 56.90059  ? 167 TRP   A N   1 
ATOM   1378 C CA  . TRP   A 1 170 ? 15.21236 23.96835  -8.14684  1.000 55.52946  ? 167 TRP   A CA  1 
ATOM   1379 C C   . TRP   A 1 170 ? 15.44954 23.82286  -9.64369  1.000 57.34119  ? 167 TRP   A C   1 
ATOM   1380 O O   . TRP   A 1 170 ? 14.86026 24.57412  -10.42783 1.000 52.93952  ? 167 TRP   A O   1 
ATOM   1381 C CB  . TRP   A 1 170 ? 16.07983 25.10333  -7.60426  1.000 55.07356  ? 167 TRP   A CB  1 
ATOM   1382 C CG  . TRP   A 1 170 ? 15.64058 25.60965  -6.27566  1.000 59.19629  ? 167 TRP   A CG  1 
ATOM   1383 C CD1 . TRP   A 1 170 ? 14.63912 25.10897  -5.49589  1.000 60.37038  ? 167 TRP   A CD1 1 
ATOM   1384 C CD2 . TRP   A 1 170 ? 16.18085 26.72922  -5.56707  1.000 60.93840  ? 167 TRP   A CD2 1 
ATOM   1385 N NE1 . TRP   A 1 170 ? 14.52595 25.84611  -4.34334  1.000 61.85928  ? 167 TRP   A NE1 1 
ATOM   1386 C CE2 . TRP   A 1 170 ? 15.46134 26.84689  -4.36253  1.000 61.49612  ? 167 TRP   A CE2 1 
ATOM   1387 C CE3 . TRP   A 1 170 ? 17.20498 27.64222  -5.83346  1.000 58.64349  ? 167 TRP   A CE3 1 
ATOM   1388 C CZ2 . TRP   A 1 170 ? 15.73162 27.84063  -3.42630  1.000 67.13900  ? 167 TRP   A CZ2 1 
ATOM   1389 C CZ3 . TRP   A 1 170 ? 17.47240 28.62706  -4.90359  1.000 67.19907  ? 167 TRP   A CZ3 1 
ATOM   1390 C CH2 . TRP   A 1 170 ? 16.73822 28.71962  -3.71489  1.000 65.37051  ? 167 TRP   A CH2 1 
ATOM   1391 N N   . TYR   A 1 171 ? 16.29017 22.87846  -10.05863 1.000 48.85805  ? 168 TYR   A N   1 
ATOM   1392 C CA  . TYR   A 1 171 ? 16.65258 22.71749  -11.45980 1.000 52.26734  ? 168 TYR   A CA  1 
ATOM   1393 C C   . TYR   A 1 171 ? 16.17706 21.38396  -12.02366 1.000 48.40371  ? 168 TYR   A C   1 
ATOM   1394 O O   . TYR   A 1 171 ? 16.69630 20.92216  -13.04484 1.000 51.36462  ? 168 TYR   A O   1 
ATOM   1395 C CB  . TYR   A 1 171 ? 18.16528 22.87643  -11.62240 1.000 53.95700  ? 168 TYR   A CB  1 
ATOM   1396 C CG  . TYR   A 1 171 ? 18.68363 24.12369  -10.94219 1.000 55.19998  ? 168 TYR   A CG  1 
ATOM   1397 C CD1 . TYR   A 1 171 ? 18.69436 25.34600  -11.60263 1.000 51.40550  ? 168 TYR   A CD1 1 
ATOM   1398 C CD2 . TYR   A 1 171 ? 19.13153 24.08541  -9.62738  1.000 53.07183  ? 168 TYR   A CD2 1 
ATOM   1399 C CE1 . TYR   A 1 171 ? 19.15057 26.49060  -10.97814 1.000 53.97841  ? 168 TYR   A CE1 1 
ATOM   1400 C CE2 . TYR   A 1 171 ? 19.58867 25.22382  -8.99484  1.000 48.63010  ? 168 TYR   A CE2 1 
ATOM   1401 C CZ  . TYR   A 1 171 ? 19.59465 26.42339  -9.67426  1.000 55.20859  ? 168 TYR   A CZ  1 
ATOM   1402 O OH  . TYR   A 1 171 ? 20.05110 27.56083  -9.04946  1.000 57.40375  ? 168 TYR   A OH  1 
ATOM   1403 N N   . ARG   A 1 172 ? 15.18142 20.77205  -11.38740 1.000 49.55560  ? 169 ARG   A N   1 
ATOM   1404 C CA  . ARG   A 1 172 ? 14.69197 19.45567  -11.76824 1.000 51.12662  ? 169 ARG   A CA  1 
ATOM   1405 C C   . ARG   A 1 172 ? 13.59740 19.59250  -12.81834 1.000 50.27837  ? 169 ARG   A C   1 
ATOM   1406 O O   . ARG   A 1 172 ? 12.64015 20.34990  -12.63004 1.000 49.77687  ? 169 ARG   A O   1 
ATOM   1407 C CB  . ARG   A 1 172 ? 14.16310 18.71915  -10.53814 1.000 50.92411  ? 169 ARG   A CB  1 
ATOM   1408 C CG  . ARG   A 1 172 ? 13.79539 17.27258  -10.77927 1.000 56.90519  ? 169 ARG   A CG  1 
ATOM   1409 C CD  . ARG   A 1 172 ? 13.32992 16.62348  -9.49057  1.000 54.11428  ? 169 ARG   A CD  1 
ATOM   1410 N NE  . ARG   A 1 172 ? 14.32648 16.73993  -8.43282  1.000 56.88248  ? 169 ARG   A NE  1 
ATOM   1411 C CZ  . ARG   A 1 172 ? 14.14537 16.32564  -7.18692  1.000 65.24545  ? 169 ARG   A CZ  1 
ATOM   1412 N NH1 . ARG   A 1 172 ? 13.01017 15.76489  -6.80477  1.000 50.23168  ? 169 ARG   A NH1 1 
ATOM   1413 N NH2 . ARG   A 1 172 ? 15.12728 16.47897  -6.30265  1.000 55.46963  ? 169 ARG   A NH2 1 
ATOM   1414 N N   . ALA   A 1 173 ? 13.73868 18.84998  -13.91395 1.000 50.84287  ? 170 ALA   A N   1 
ATOM   1415 C CA  . ALA   A 1 173 ? 12.79103 18.93598  -15.01375 1.000 48.91480  ? 170 ALA   A CA  1 
ATOM   1416 C C   . ALA   A 1 173 ? 11.40989 18.44388  -14.57461 1.000 51.64837  ? 170 ALA   A C   1 
ATOM   1417 O O   . ALA   A 1 173 ? 11.29389 17.64344  -13.64126 1.000 56.42478  ? 170 ALA   A O   1 
ATOM   1418 C CB  . ALA   A 1 173 ? 13.29501 18.11943  -16.20293 1.000 54.11525  ? 170 ALA   A CB  1 
ATOM   1419 N N   . PRO   A 1 174 ? 10.33917 18.91344  -15.22577 1.000 55.87666  ? 171 PRO   A N   1 
ATOM   1420 C CA  . PRO   A 1 174 ? 8.99420  18.50641  -14.78810 1.000 53.41564  ? 171 PRO   A CA  1 
ATOM   1421 C C   . PRO   A 1 174 ? 8.69460  17.03755  -15.02583 1.000 55.58834  ? 171 PRO   A C   1 
ATOM   1422 O O   . PRO   A 1 174 ? 7.87802  16.46473  -14.29451 1.000 57.23826  ? 171 PRO   A O   1 
ATOM   1423 C CB  . PRO   A 1 174 ? 8.06763  19.41350  -15.61013 1.000 57.79244  ? 171 PRO   A CB  1 
ATOM   1424 C CG  . PRO   A 1 174 ? 8.86651  19.76819  -16.81421 1.000 51.53735  ? 171 PRO   A CG  1 
ATOM   1425 C CD  . PRO   A 1 174 ? 10.28496 19.87894  -16.33813 1.000 51.19463  ? 171 PRO   A CD  1 
ATOM   1426 N N   . GLU   A 1 175 ? 9.32233  16.40501  -16.02077 1.000 57.31902  ? 172 GLU   A N   1 
ATOM   1427 C CA  . GLU   A 1 175 ? 9.07783  14.98271  -16.23776 1.000 61.47082  ? 172 GLU   A CA  1 
ATOM   1428 C C   . GLU   A 1 175 ? 9.63110  14.14066  -15.09471 1.000 60.86597  ? 172 GLU   A C   1 
ATOM   1429 O O   . GLU   A 1 175 ? 9.08720  13.07153  -14.79477 1.000 59.32948  ? 172 GLU   A O   1 
ATOM   1430 C CB  . GLU   A 1 175 ? 9.67221  14.53336  -17.57433 1.000 55.61427  ? 172 GLU   A CB  1 
ATOM   1431 C CG  . GLU   A 1 175 ? 11.17866 14.71541  -17.70368 1.000 59.08273  ? 172 GLU   A CG  1 
ATOM   1432 C CD  . GLU   A 1 175 ? 11.56214 16.05536  -18.30371 1.000 54.66534  ? 172 GLU   A CD  1 
ATOM   1433 O OE1 . GLU   A 1 175 ? 10.75794 17.00602  -18.20858 1.000 58.04170  ? 172 GLU   A OE1 1 
ATOM   1434 O OE2 . GLU   A 1 175 ? 12.66941 16.15677  -18.87429 1.000 48.98455  ? 172 GLU   A OE2 1 
ATOM   1435 N N   . ILE   A 1 176 ? 10.70066 14.60460  -14.44498 1.000 57.48205  ? 173 ILE   A N   1 
ATOM   1436 C CA  . ILE   A 1 176 ? 11.20124 13.92149  -13.25708 1.000 55.46193  ? 173 ILE   A CA  1 
ATOM   1437 C C   . ILE   A 1 176 ? 10.22071 14.08204  -12.10256 1.000 58.93583  ? 173 ILE   A C   1 
ATOM   1438 O O   . ILE   A 1 176 ? 9.93330  13.12495  -11.37375 1.000 61.40417  ? 173 ILE   A O   1 
ATOM   1439 C CB  . ILE   A 1 176 ? 12.59986 14.44892  -12.88801 1.000 55.57418  ? 173 ILE   A CB  1 
ATOM   1440 C CG1 . ILE   A 1 176 ? 13.55116 14.32481  -14.08012 1.000 57.86623  ? 173 ILE   A CG1 1 
ATOM   1441 C CG2 . ILE   A 1 176 ? 13.15042 13.69906  -11.68276 1.000 53.89076  ? 173 ILE   A CG2 1 
ATOM   1442 C CD1 . ILE   A 1 176 ? 13.83552 12.89783  -14.48874 1.000 60.24109  ? 173 ILE   A CD1 1 
ATOM   1443 N N   . LEU   A 1 177 ? 9.68821  15.29330  -11.92225 1.000 56.74454  ? 174 LEU   A N   1 
ATOM   1444 C CA  . LEU   A 1 177 ? 8.74871  15.54955  -10.83582 1.000 60.69859  ? 174 LEU   A CA  1 
ATOM   1445 C C   . LEU   A 1 177 ? 7.45083  14.76916  -11.00779 1.000 65.93326  ? 174 LEU   A C   1 
ATOM   1446 O O   . LEU   A 1 177 ? 6.78960  14.44519  -10.01450 1.000 66.14851  ? 174 LEU   A O   1 
ATOM   1447 C CB  . LEU   A 1 177 ? 8.46078  17.04878  -10.74343 1.000 61.79772  ? 174 LEU   A CB  1 
ATOM   1448 C CG  . LEU   A 1 177 ? 9.63461  17.95239  -10.36343 1.000 60.66112  ? 174 LEU   A CG  1 
ATOM   1449 C CD1 . LEU   A 1 177 ? 9.33371  19.40453  -10.71296 1.000 48.23468  ? 174 LEU   A CD1 1 
ATOM   1450 C CD2 . LEU   A 1 177 ? 9.95045  17.81378  -8.88292  1.000 58.30188  ? 174 LEU   A CD2 1 
ATOM   1451 N N   . LEU   A 1 178 ? 7.07310  14.45595  -12.24439 1.000 68.29055  ? 175 LEU   A N   1 
ATOM   1452 C CA  . LEU   A 1 178 ? 5.85362  13.70666  -12.51525 1.000 70.03272  ? 175 LEU   A CA  1 
ATOM   1453 C C   . LEU   A 1 178 ? 6.07587  12.19981  -12.55887 1.000 69.19479  ? 175 LEU   A C   1 
ATOM   1454 O O   . LEU   A 1 178 ? 5.11397  11.45253  -12.76645 1.000 73.86343  ? 175 LEU   A O   1 
ATOM   1455 C CB  . LEU   A 1 178 ? 5.22291  14.18101  -13.82914 1.000 67.43444  ? 175 LEU   A CB  1 
ATOM   1456 C CG  . LEU   A 1 178 ? 4.56734  15.56254  -13.76664 1.000 71.95090  ? 175 LEU   A CG  1 
ATOM   1457 C CD1 . LEU   A 1 178 ? 4.06497  15.99378  -15.13512 1.000 68.82641  ? 175 LEU   A CD1 1 
ATOM   1458 C CD2 . LEU   A 1 178 ? 3.43232  15.56272  -12.75424 1.000 67.31648  ? 175 LEU   A CD2 1 
ATOM   1459 N N   . GLY   A 1 179 ? 7.30978  11.73863  -12.37059 1.000 70.83205  ? 176 GLY   A N   1 
ATOM   1460 C CA  . GLY   A 1 179 ? 7.57808  10.32122  -12.22566 1.000 68.49797  ? 176 GLY   A CA  1 
ATOM   1461 C C   . GLY   A 1 179 ? 7.66575  9.54884   -13.52517 1.000 66.78221  ? 176 GLY   A C   1 
ATOM   1462 O O   . GLY   A 1 179 ? 7.08243  8.46799   -13.64438 1.000 75.53375  ? 176 GLY   A O   1 
ATOM   1463 N N   . CYS   A 1 180 ? 8.39754  10.07973  -14.50091 1.000 57.80358  ? 177 CYS   A N   1 
ATOM   1464 C CA  . CYS   A 1 180 ? 8.54982  9.38829   -15.77352 1.000 69.49918  ? 177 CYS   A CA  1 
ATOM   1465 C C   . CYS   A 1 180 ? 9.41438  8.14501   -15.60888 1.000 71.95085  ? 177 CYS   A C   1 
ATOM   1466 O O   . CYS   A 1 180 ? 10.35227 8.12317   -14.80712 1.000 63.89736  ? 177 CYS   A O   1 
ATOM   1467 C CB  . CYS   A 1 180 ? 9.16080  10.32236  -16.81832 1.000 67.46615  ? 177 CYS   A CB  1 
ATOM   1468 S SG  . CYS   A 1 180 ? 10.82395 10.91182  -16.42789 1.000 74.74631  ? 177 CYS   A SG  1 
ATOM   1469 N N   . LYS   A 1 181 ? 9.08438  7.09873   -16.36860 1.000 75.65186  ? 178 LYS   A N   1 
ATOM   1470 C CA  . LYS   A 1 181 ? 9.87655  5.87384   -16.32550 1.000 76.90363  ? 178 LYS   A CA  1 
ATOM   1471 C C   . LYS   A 1 181 ? 11.26003 6.09750   -16.92387 1.000 76.55870  ? 178 LYS   A C   1 
ATOM   1472 O O   . LYS   A 1 181 ? 12.28325 5.85088   -16.27414 1.000 80.42717  ? 178 LYS   A O   1 
ATOM   1473 C CB  . LYS   A 1 181 ? 9.14937  4.74897   -17.06333 1.000 81.12873  ? 178 LYS   A CB  1 
ATOM   1474 C CG  . LYS   A 1 181 ? 8.10156  4.01771   -16.24033 1.000 88.45249  ? 178 LYS   A CG  1 
ATOM   1475 C CD  . LYS   A 1 181 ? 7.43605  2.91957   -17.06017 1.000 101.48920 ? 178 LYS   A CD  1 
ATOM   1476 C CE  . LYS   A 1 181 ? 8.46730  1.99935   -17.70011 1.000 101.10879 ? 178 LYS   A CE  1 
ATOM   1477 N NZ  . LYS   A 1 181 ? 9.33960  1.33963   -16.68954 1.000 99.47213  ? 178 LYS   A NZ  1 
ATOM   1478 N N   . TYR   A 1 182 ? 11.30918 6.56836   -18.16433 1.000 72.56970  ? 179 TYR   A N   1 
ATOM   1479 C CA  . TYR   A 1 182 ? 12.55682 6.78544   -18.87682 1.000 74.56623  ? 179 TYR   A CA  1 
ATOM   1480 C C   . TYR   A 1 182 ? 12.84075 8.27670   -19.00006 1.000 75.36216  ? 179 TYR   A C   1 
ATOM   1481 O O   . TYR   A 1 182 ? 11.92208 9.09963   -19.04746 1.000 78.05012  ? 179 TYR   A O   1 
ATOM   1482 C CB  . TYR   A 1 182 ? 12.50692 6.15597   -20.27201 1.000 67.75905  ? 179 TYR   A CB  1 
ATOM   1483 C CG  . TYR   A 1 182 ? 12.10716 4.69776   -20.28456 1.000 74.12709  ? 179 TYR   A CG  1 
ATOM   1484 C CD1 . TYR   A 1 182 ? 12.72787 3.77663   -19.45141 1.000 73.77583  ? 179 TYR   A CD1 1 
ATOM   1485 C CD2 . TYR   A 1 182 ? 11.10055 4.24438   -21.12679 1.000 77.22745  ? 179 TYR   A CD2 1 
ATOM   1486 C CE1 . TYR   A 1 182 ? 12.36169 2.44152   -19.46413 1.000 78.18030  ? 179 TYR   A CE1 1 
ATOM   1487 C CE2 . TYR   A 1 182 ? 10.72709 2.91410   -21.14575 1.000 80.19353  ? 179 TYR   A CE2 1 
ATOM   1488 C CZ  . TYR   A 1 182 ? 11.35959 2.01704   -20.31307 1.000 83.73574  ? 179 TYR   A CZ  1 
ATOM   1489 O OH  . TYR   A 1 182 ? 10.98686 0.69200   -20.33213 1.000 84.80680  ? 179 TYR   A OH  1 
ATOM   1490 N N   . TYR   A 1 183 ? 14.12666 8.61568   -19.04925 1.000 68.82577  ? 180 TYR   A N   1 
ATOM   1491 C CA  . TYR   A 1 183 ? 14.55278 9.98628   -19.29484 1.000 71.28418  ? 180 TYR   A CA  1 
ATOM   1492 C C   . TYR   A 1 183 ? 15.96621 9.95817   -19.85411 1.000 62.50054  ? 180 TYR   A C   1 
ATOM   1493 O O   . TYR   A 1 183 ? 16.68031 8.95903   -19.73458 1.000 67.92736  ? 180 TYR   A O   1 
ATOM   1494 C CB  . TYR   A 1 183 ? 14.48627 10.84642  -18.02492 1.000 73.88121  ? 180 TYR   A CB  1 
ATOM   1495 C CG  . TYR   A 1 183 ? 15.43759 10.43201  -16.92066 1.000 69.82473  ? 180 TYR   A CG  1 
ATOM   1496 C CD1 . TYR   A 1 183 ? 16.73896 10.92146  -16.87373 1.000 64.01443  ? 180 TYR   A CD1 1 
ATOM   1497 C CD2 . TYR   A 1 183 ? 15.02773 9.56784   -15.91431 1.000 71.84494  ? 180 TYR   A CD2 1 
ATOM   1498 C CE1 . TYR   A 1 183 ? 17.60612 10.54944  -15.86529 1.000 67.73343  ? 180 TYR   A CE1 1 
ATOM   1499 C CE2 . TYR   A 1 183 ? 15.88836 9.19232   -14.90035 1.000 61.56907  ? 180 TYR   A CE2 1 
ATOM   1500 C CZ  . TYR   A 1 183 ? 17.17510 9.68610   -14.88101 1.000 61.35314  ? 180 TYR   A CZ  1 
ATOM   1501 O OH  . TYR   A 1 183 ? 18.03332 9.31367   -13.87260 1.000 69.35550  ? 180 TYR   A OH  1 
ATOM   1502 N N   . SER   A 1 184 ? 16.36283 11.07417  -20.46505 1.000 62.59597  ? 181 SER   A N   1 
ATOM   1503 C CA  . SER   A 1 184 ? 17.70409 11.18259  -21.02401 1.000 69.79111  ? 181 SER   A CA  1 
ATOM   1504 C C   . SER   A 1 184 ? 18.19167 12.62661  -21.03496 1.000 63.34392  ? 181 SER   A C   1 
ATOM   1505 O O   . SER   A 1 184 ? 18.17537 13.30336  -20.00167 1.000 64.00615  ? 181 SER   A O   1 
ATOM   1506 C CB  . SER   A 1 184 ? 17.74498 10.59938  -22.43800 1.000 67.08195  ? 181 SER   A CB  1 
ATOM   1507 O OG  . SER   A 1 184 ? 16.91076 11.33081  -23.31877 1.000 75.00024  ? 181 SER   A OG  1 
ATOM   1508 N N   . THR   A 1 185 ? 18.61707 13.10643  -22.20623 1.000 59.75981  ? 182 THR   A N   1 
ATOM   1509 C CA  . THR   A 1 185 ? 19.35288 14.36308  -22.29305 1.000 61.25525  ? 182 THR   A CA  1 
ATOM   1510 C C   . THR   A 1 185 ? 18.49699 15.58640  -21.98953 1.000 53.80670  ? 182 THR   A C   1 
ATOM   1511 O O   . THR   A 1 185 ? 19.05255 16.65038  -21.69567 1.000 55.75495  ? 182 THR   A O   1 
ATOM   1512 C CB  . THR   A 1 185 ? 19.96965 14.50921  -23.68503 1.000 54.88314  ? 182 THR   A CB  1 
ATOM   1513 O OG1 . THR   A 1 185 ? 18.93038 14.48722  -24.67105 1.000 56.79575  ? 182 THR   A OG1 1 
ATOM   1514 C CG2 . THR   A 1 185 ? 20.94500 13.37398  -23.96036 1.000 59.53455  ? 182 THR   A CG2 1 
ATOM   1515 N N   . ALA   A 1 186 ? 17.16810 15.46585  -22.05021 1.000 52.94110  ? 183 ALA   A N   1 
ATOM   1516 C CA  . ALA   A 1 186 ? 16.31458 16.64045  -21.89645 1.000 53.18723  ? 183 ALA   A CA  1 
ATOM   1517 C C   . ALA   A 1 186 ? 16.39615 17.23075  -20.49371 1.000 52.03401  ? 183 ALA   A C   1 
ATOM   1518 O O   . ALA   A 1 186 ? 16.16909 18.43283  -20.31598 1.000 52.89798  ? 183 ALA   A O   1 
ATOM   1519 C CB  . ALA   A 1 186 ? 14.86677 16.28728  -22.23898 1.000 50.48965  ? 183 ALA   A CB  1 
ATOM   1520 N N   . VAL   A 1 187 ? 16.72149 16.41382  -19.48847 1.000 50.20746  ? 184 VAL   A N   1 
ATOM   1521 C CA  . VAL   A 1 187 ? 16.73345 16.91393  -18.11663 1.000 52.46400  ? 184 VAL   A CA  1 
ATOM   1522 C C   . VAL   A 1 187 ? 17.87589 17.90117  -17.90383 1.000 49.75487  ? 184 VAL   A C   1 
ATOM   1523 O O   . VAL   A 1 187 ? 17.76016 18.82742  -17.09176 1.000 52.98637  ? 184 VAL   A O   1 
ATOM   1524 C CB  . VAL   A 1 187 ? 16.79507 15.74187  -17.11770 1.000 57.37635  ? 184 VAL   A CB  1 
ATOM   1525 C CG1 . VAL   A 1 187 ? 15.60981 14.81196  -17.32328 1.000 54.54509  ? 184 VAL   A CG1 1 
ATOM   1526 C CG2 . VAL   A 1 187 ? 18.10315 14.98022  -17.25349 1.000 59.53847  ? 184 VAL   A CG2 1 
ATOM   1527 N N   . ASP   A 1 188 ? 18.98578 17.73912  -18.62790 1.000 55.18094  ? 185 ASP   A N   1 
ATOM   1528 C CA  . ASP   A 1 188 ? 20.08904 18.68391  -18.49240 1.000 51.94988  ? 185 ASP   A CA  1 
ATOM   1529 C C   . ASP   A 1 188 ? 19.77011 20.01807  -19.15340 1.000 55.48349  ? 185 ASP   A C   1 
ATOM   1530 O O   . ASP   A 1 188 ? 20.19467 21.06971  -18.66110 1.000 55.83321  ? 185 ASP   A O   1 
ATOM   1531 C CB  . ASP   A 1 188 ? 21.36569 18.08908  -19.08395 1.000 55.58440  ? 185 ASP   A CB  1 
ATOM   1532 C CG  . ASP   A 1 188 ? 21.90802 16.94096  -18.25983 1.000 56.87936  ? 185 ASP   A CG  1 
ATOM   1533 O OD1 . ASP   A 1 188 ? 21.61317 16.88741  -17.04781 1.000 54.00612  ? 185 ASP   A OD1 1 
ATOM   1534 O OD2 . ASP   A 1 188 ? 22.63464 16.09626  -18.82316 1.000 56.07237  ? 185 ASP   A OD2 1 
ATOM   1535 N N   . ILE   A 1 189 ? 19.02696 19.99545  -20.26136 1.000 54.06911  ? 186 ILE   A N   1 
ATOM   1536 C CA  . ILE   A 1 189 ? 18.67308 21.23198  -20.95152 1.000 52.10295  ? 186 ILE   A CA  1 
ATOM   1537 C C   . ILE   A 1 189 ? 17.73328 22.07458  -20.09784 1.000 54.03766  ? 186 ILE   A C   1 
ATOM   1538 O O   . ILE   A 1 189 ? 17.85539 23.30519  -20.04627 1.000 53.71922  ? 186 ILE   A O   1 
ATOM   1539 C CB  . ILE   A 1 189 ? 18.06107 20.91157  -22.32679 1.000 48.67667  ? 186 ILE   A CB  1 
ATOM   1540 C CG1 . ILE   A 1 189 ? 19.11212 20.27660  -23.23718 1.000 54.47987  ? 186 ILE   A CG1 1 
ATOM   1541 C CG2 . ILE   A 1 189 ? 17.48719 22.16513  -22.96577 1.000 55.29415  ? 186 ILE   A CG2 1 
ATOM   1542 C CD1 . ILE   A 1 189 ? 20.24134 21.21325  -23.60599 1.000 53.13259  ? 186 ILE   A CD1 1 
ATOM   1543 N N   . TRP   A 1 190 ? 16.77990 21.43063  -19.41973 1.000 46.38104  ? 187 TRP   A N   1 
ATOM   1544 C CA  . TRP   A 1 190 ? 15.89386 22.15561  -18.51369 1.000 53.62053  ? 187 TRP   A CA  1 
ATOM   1545 C C   . TRP   A 1 190 ? 16.68742 22.86113  -17.42150 1.000 52.07469  ? 187 TRP   A C   1 
ATOM   1546 O O   . TRP   A 1 190 ? 16.40327 24.01478  -17.07785 1.000 51.38475  ? 187 TRP   A O   1 
ATOM   1547 C CB  . TRP   A 1 190 ? 14.87241 21.19849  -17.89996 1.000 48.81567  ? 187 TRP   A CB  1 
ATOM   1548 C CG  . TRP   A 1 190 ? 13.95689 21.85069  -16.90671 1.000 47.67728  ? 187 TRP   A CG  1 
ATOM   1549 C CD1 . TRP   A 1 190 ? 14.20624 22.07421  -15.58249 1.000 50.33721  ? 187 TRP   A CD1 1 
ATOM   1550 C CD2 . TRP   A 1 190 ? 12.64103 22.35934  -17.15730 1.000 51.24859  ? 187 TRP   A CD2 1 
ATOM   1551 N NE1 . TRP   A 1 190 ? 13.12885 22.69300  -14.99502 1.000 49.69691  ? 187 TRP   A NE1 1 
ATOM   1552 C CE2 . TRP   A 1 190 ? 12.15426 22.87784  -15.94018 1.000 51.04801  ? 187 TRP   A CE2 1 
ATOM   1553 C CE3 . TRP   A 1 190 ? 11.82721 22.42676  -18.29265 1.000 55.01531  ? 187 TRP   A CE3 1 
ATOM   1554 C CZ2 . TRP   A 1 190 ? 10.89187 23.45575  -15.82736 1.000 50.11646  ? 187 TRP   A CZ2 1 
ATOM   1555 C CZ3 . TRP   A 1 190 ? 10.57356 23.00123  -18.17787 1.000 55.89434  ? 187 TRP   A CZ3 1 
ATOM   1556 C CH2 . TRP   A 1 190 ? 10.11889 23.50657  -16.95460 1.000 54.18723  ? 187 TRP   A CH2 1 
ATOM   1557 N N   . SER   A 1 191 ? 17.68575 22.17509  -16.85750 1.000 48.76888  ? 188 SER   A N   1 
ATOM   1558 C CA  . SER   A 1 191 ? 18.52029 22.79130  -15.83161 1.000 51.28198  ? 188 SER   A CA  1 
ATOM   1559 C C   . SER   A 1 191 ? 19.25090 24.01144  -16.37576 1.000 52.76043  ? 188 SER   A C   1 
ATOM   1560 O O   . SER   A 1 191 ? 19.33585 25.04363  -15.70049 1.000 54.59316  ? 188 SER   A O   1 
ATOM   1561 C CB  . SER   A 1 191 ? 19.51605 21.77152  -15.28266 1.000 48.11911  ? 188 SER   A CB  1 
ATOM   1562 O OG  . SER   A 1 191 ? 18.84221 20.66655  -14.70822 1.000 50.67102  ? 188 SER   A OG  1 
ATOM   1563 N N   . LEU   A 1 192 ? 19.77727 23.91758  -17.60066 1.000 43.68916  ? 189 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 192 ? 20.46079 25.06377  -18.18978 1.000 53.35400  ? 189 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 192 ? 19.49247 26.20029  -18.49037 1.000 53.69750  ? 189 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 192 ? 19.86873 27.37323  -18.38850 1.000 53.82543  ? 189 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 192 ? 21.20402 24.64885  -19.45839 1.000 50.17117  ? 189 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 192 ? 22.50583 23.86545  -19.27155 1.000 64.07604  ? 189 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 192 ? 23.30300 23.88488  -20.55996 1.000 54.54575  ? 189 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 192 ? 23.32970 24.41752  -18.11499 1.000 58.47173  ? 189 LEU   A CD2 1 
ATOM   1571 N N   . GLY   A 1 193 ? 18.25045 25.87851  -18.86018 1.000 54.76889  ? 190 GLY   A N   1 
ATOM   1572 C CA  . GLY   A 1 193 ? 17.24998 26.91960  -19.02951 1.000 53.31071  ? 190 GLY   A CA  1 
ATOM   1573 C C   . GLY   A 1 193 ? 16.96540 27.66199  -17.73799 1.000 53.05786  ? 190 GLY   A C   1 
ATOM   1574 O O   . GLY   A 1 193 ? 16.81202 28.88576  -17.73473 1.000 54.12545  ? 190 GLY   A O   1 
ATOM   1575 N N   . CYS   A 1 194 ? 16.88813 26.93189  -16.62221 1.000 47.92339  ? 191 CYS   A N   1 
ATOM   1576 C CA  . CYS   A 1 194 ? 16.72415 27.58574  -15.32815 1.000 54.57311  ? 191 CYS   A CA  1 
ATOM   1577 C C   . CYS   A 1 194 ? 17.93924 28.44108  -14.99143 1.000 52.77539  ? 191 CYS   A C   1 
ATOM   1578 O O   . CYS   A 1 194 ? 17.79923 29.56691  -14.49790 1.000 49.90948  ? 191 CYS   A O   1 
ATOM   1579 C CB  . CYS   A 1 194 ? 16.47971 26.54145  -14.23823 1.000 51.14871  ? 191 CYS   A CB  1 
ATOM   1580 S SG  . CYS   A 1 194 ? 15.00201 25.52636  -14.48292 1.000 55.12334  ? 191 CYS   A SG  1 
ATOM   1581 N N   . ILE   A 1 195 ? 19.14102 27.92460  -15.26051 1.000 54.52254  ? 192 ILE   A N   1 
ATOM   1582 C CA  . ILE   A 1 195 ? 20.35937 28.68855  -15.00855 1.000 61.84243  ? 192 ILE   A CA  1 
ATOM   1583 C C   . ILE   A 1 195 ? 20.43945 29.89016  -15.94321 1.000 62.38172  ? 192 ILE   A C   1 
ATOM   1584 O O   . ILE   A 1 195 ? 20.90954 30.96733  -15.55470 1.000 60.45449  ? 192 ILE   A O   1 
ATOM   1585 C CB  . ILE   A 1 195 ? 21.59135 27.77410  -15.14271 1.000 58.63322  ? 192 ILE   A CB  1 
ATOM   1586 C CG1 . ILE   A 1 195 ? 21.53444 26.65378  -14.10199 1.000 56.00076  ? 192 ILE   A CG1 1 
ATOM   1587 C CG2 . ILE   A 1 195 ? 22.87818 28.56990  -14.98919 1.000 61.05571  ? 192 ILE   A CG2 1 
ATOM   1588 C CD1 . ILE   A 1 195 ? 22.56903 25.56892  -14.30846 1.000 59.99996  ? 192 ILE   A CD1 1 
ATOM   1589 N N   . PHE   A 1 196 ? 19.97907 29.72561  -17.18627 1.000 57.62451  ? 193 PHE   A N   1 
ATOM   1590 C CA  . PHE   A 1 196 ? 19.94206 30.83812  -18.13181 1.000 57.37030  ? 193 PHE   A CA  1 
ATOM   1591 C C   . PHE   A 1 196 ? 19.09601 31.98558  -17.59117 1.000 62.34145  ? 193 PHE   A C   1 
ATOM   1592 O O   . PHE   A 1 196 ? 19.55701 33.13065  -17.51486 1.000 56.55081  ? 193 PHE   A O   1 
ATOM   1593 C CB  . PHE   A 1 196 ? 19.40482 30.34752  -19.48096 1.000 55.82552  ? 193 PHE   A CB  1 
ATOM   1594 C CG  . PHE   A 1 196 ? 19.39617 31.39434  -20.56472 1.000 57.70695  ? 193 PHE   A CG  1 
ATOM   1595 C CD1 . PHE   A 1 196 ? 20.21698 32.51148  -20.49443 1.000 61.11834  ? 193 PHE   A CD1 1 
ATOM   1596 C CD2 . PHE   A 1 196 ? 18.55879 31.25493  -21.66032 1.000 62.31126  ? 193 PHE   A CD2 1 
ATOM   1597 C CE1 . PHE   A 1 196 ? 20.19781 33.46803  -21.49408 1.000 60.09394  ? 193 PHE   A CE1 1 
ATOM   1598 C CE2 . PHE   A 1 196 ? 18.53676 32.20696  -22.66321 1.000 60.29244  ? 193 PHE   A CE2 1 
ATOM   1599 C CZ  . PHE   A 1 196 ? 19.35762 33.31460  -22.57951 1.000 58.85740  ? 193 PHE   A CZ  1 
ATOM   1600 N N   . ALA   A 1 197 ? 17.84965 31.69459  -17.21100 1.000 58.55008  ? 194 ALA   A N   1 
ATOM   1601 C CA  . ALA   A 1 197 ? 16.97779 32.73538  -16.67895 1.000 60.12842  ? 194 ALA   A CA  1 
ATOM   1602 C C   . ALA   A 1 197 ? 17.49973 33.28732  -15.36107 1.000 60.78763  ? 194 ALA   A C   1 
ATOM   1603 O O   . ALA   A 1 197 ? 17.31061 34.47419  -15.06816 1.000 63.24741  ? 194 ALA   A O   1 
ATOM   1604 C CB  . ALA   A 1 197 ? 15.55815 32.19574  -16.49975 1.000 57.61418  ? 194 ALA   A CB  1 
ATOM   1605 N N   . GLU   A 1 198 ? 18.15736 32.45122  -14.55541 1.000 54.93865  ? 195 GLU   A N   1 
ATOM   1606 C CA  . GLU   A 1 198 ? 18.67384 32.92757  -13.27697 1.000 62.77605  ? 195 GLU   A CA  1 
ATOM   1607 C C   . GLU   A 1 198 ? 19.80229 33.93310  -13.47810 1.000 65.27899  ? 195 GLU   A C   1 
ATOM   1608 O O   . GLU   A 1 198 ? 19.95473 34.86542  -12.68265 1.000 65.77606  ? 195 GLU   A O   1 
ATOM   1609 C CB  . GLU   A 1 198 ? 19.14462 31.74647  -12.42863 1.000 57.74841  ? 195 GLU   A CB  1 
ATOM   1610 C CG  . GLU   A 1 198 ? 19.36218 32.07612  -10.95751 1.000 60.40893  ? 195 GLU   A CG  1 
ATOM   1611 C CD  . GLU   A 1 198 ? 19.73763 30.85916  -10.13415 1.000 69.15748  ? 195 GLU   A CD  1 
ATOM   1612 O OE1 . GLU   A 1 198 ? 19.37044 29.73464  -10.52871 1.000 64.53162  ? 195 GLU   A OE1 1 
ATOM   1613 O OE2 . GLU   A 1 198 ? 20.40915 31.02605  -9.09472  1.000 60.86785  ? 195 GLU   A OE2 1 
ATOM   1614 N N   . MET   A 1 199 ? 20.60974 33.75742  -14.53076 1.000 59.35073  ? 196 MET   A N   1 
ATOM   1615 C CA  . MET   A 1 199 ? 21.62281 34.75514  -14.86165 1.000 61.92752  ? 196 MET   A CA  1 
ATOM   1616 C C   . MET   A 1 199 ? 20.99267 36.06282  -15.32302 1.000 67.11697  ? 196 MET   A C   1 
ATOM   1617 O O   . MET   A 1 199 ? 21.55889 37.13632  -15.09223 1.000 66.86508  ? 196 MET   A O   1 
ATOM   1618 C CB  . MET   A 1 199 ? 22.56608 34.21078  -15.93591 1.000 62.59351  ? 196 MET   A CB  1 
ATOM   1619 C CG  . MET   A 1 199 ? 23.56015 33.18003  -15.42891 1.000 64.88967  ? 196 MET   A CG  1 
ATOM   1620 S SD  . MET   A 1 199 ? 24.81966 32.77651  -16.65364 1.000 68.42159  ? 196 MET   A SD  1 
ATOM   1621 C CE  . MET   A 1 199 ? 23.82722 32.02026  -17.93924 1.000 50.12505  ? 196 MET   A CE  1 
ATOM   1622 N N   . VAL   A 1 200 ? 19.82554 35.99489  -15.96278 1.000 66.45052  ? 197 VAL   A N   1 
ATOM   1623 C CA  . VAL   A 1 200 ? 19.17194 37.19691  -16.47044 1.000 71.74730  ? 197 VAL   A CA  1 
ATOM   1624 C C   . VAL   A 1 200 ? 18.48336 37.95832  -15.34410 1.000 72.15887  ? 197 VAL   A C   1 
ATOM   1625 O O   . VAL   A 1 200 ? 18.64811 39.17599  -15.20667 1.000 71.66920  ? 197 VAL   A O   1 
ATOM   1626 C CB  . VAL   A 1 200 ? 18.18088 36.82562  -17.58975 1.000 64.72282  ? 197 VAL   A CB  1 
ATOM   1627 C CG1 . VAL   A 1 200 ? 17.39617 38.04794  -18.03826 1.000 72.00457  ? 197 VAL   A CG1 1 
ATOM   1628 C CG2 . VAL   A 1 200 ? 18.91785 36.19806  -18.76220 1.000 60.00596  ? 197 VAL   A CG2 1 
ATOM   1629 N N   . THR   A 1 201 ? 17.70538 37.25557  -14.52160 1.000 69.76838  ? 198 THR   A N   1 
ATOM   1630 C CA  . THR   A 1 201 ? 16.90691 37.88524  -13.47760 1.000 73.53706  ? 198 THR   A CA  1 
ATOM   1631 C C   . THR   A 1 201 ? 17.63094 37.99857  -12.14150 1.000 68.29739  ? 198 THR   A C   1 
ATOM   1632 O O   . THR   A 1 201 ? 17.09149 38.61928  -11.21875 1.000 71.52935  ? 198 THR   A O   1 
ATOM   1633 C CB  . THR   A 1 201 ? 15.59882 37.11078  -13.27269 1.000 74.11485  ? 198 THR   A CB  1 
ATOM   1634 O OG1 . THR   A 1 201 ? 15.89277 35.76165  -12.88802 1.000 71.06778  ? 198 THR   A OG1 1 
ATOM   1635 C CG2 . THR   A 1 201 ? 14.78017 37.09952  -14.55306 1.000 62.51107  ? 198 THR   A CG2 1 
ATOM   1636 N N   . ARG   A 1 202 ? 18.82399 37.41540  -12.01514 1.000 74.92183  ? 199 ARG   A N   1 
ATOM   1637 C CA  . ARG   A 1 202 ? 19.61320 37.41987  -10.78210 1.000 75.53345  ? 199 ARG   A CA  1 
ATOM   1638 C C   . ARG   A 1 202 ? 18.88745 36.75423  -9.61509  1.000 73.99558  ? 199 ARG   A C   1 
ATOM   1639 O O   . ARG   A 1 202 ? 19.21685 37.00509  -8.45145  1.000 74.01928  ? 199 ARG   A O   1 
ATOM   1640 C CB  . ARG   A 1 202 ? 20.04667 38.83979  -10.39494 1.000 80.77110  ? 199 ARG   A CB  1 
ATOM   1641 C CG  . ARG   A 1 202 ? 21.26850 39.33631  -11.15171 1.000 86.83587  ? 199 ARG   A CG  1 
ATOM   1642 C CD  . ARG   A 1 202 ? 20.89473 40.26984  -12.29151 1.000 80.01079  ? 199 ARG   A CD  1 
ATOM   1643 N NE  . ARG   A 1 202 ? 20.72789 41.64542  -11.83691 1.000 81.19050  ? 199 ARG   A NE  1 
ATOM   1644 C CZ  . ARG   A 1 202 ? 19.55797 42.23497  -11.63320 1.000 89.06070  ? 199 ARG   A CZ  1 
ATOM   1645 N NH1 . ARG   A 1 202 ? 18.41738 41.60003  -11.84667 1.000 93.15740  ? 199 ARG   A NH1 1 
ATOM   1646 N NH2 . ARG   A 1 202 ? 19.53214 43.49573  -11.20983 1.000 94.99279  ? 199 ARG   A NH2 1 
ATOM   1647 N N   . ARG   A 1 203 ? 17.90642 35.90189  -9.90309  1.000 68.88598  ? 200 ARG   A N   1 
ATOM   1648 C CA  . ARG   A 1 203 ? 17.23648 35.12005  -8.87493  1.000 73.06462  ? 200 ARG   A CA  1 
ATOM   1649 C C   . ARG   A 1 203 ? 16.77472 33.80854  -9.49111  1.000 66.61836  ? 200 ARG   A C   1 
ATOM   1650 O O   . ARG   A 1 203 ? 16.59069 33.70346  -10.70725 1.000 67.39830  ? 200 ARG   A O   1 
ATOM   1651 C CB  . ARG   A 1 203 ? 16.05239 35.87546  -8.25720  1.000 75.96807  ? 200 ARG   A CB  1 
ATOM   1652 C CG  . ARG   A 1 203 ? 14.88681 36.09867  -9.20390  1.000 78.29546  ? 200 ARG   A CG  1 
ATOM   1653 C CD  . ARG   A 1 203 ? 13.73853 36.79675  -8.49645  1.000 91.21241  ? 200 ARG   A CD  1 
ATOM   1654 N NE  . ARG   A 1 203 ? 12.58742 36.97956  -9.37190  1.000 92.13175  ? 200 ARG   A NE  1 
ATOM   1655 C CZ  . ARG   A 1 203 ? 12.40500 38.03109  -10.15849 1.000 100.04736 ? 200 ARG   A CZ  1 
ATOM   1656 N NH1 . ARG   A 1 203 ? 13.28410 39.01877  -10.20673 1.000 103.42544 ? 200 ARG   A NH1 1 
ATOM   1657 N NH2 . ARG   A 1 203 ? 11.31392 38.09263  -10.91668 1.000 103.77683 ? 200 ARG   A NH2 1 
ATOM   1658 N N   . ALA   A 1 204 ? 16.59874 32.80413  -8.63325  1.000 64.61232  ? 201 ALA   A N   1 
ATOM   1659 C CA  . ALA   A 1 204 ? 16.21104 31.47866  -9.09804  1.000 64.75334  ? 201 ALA   A CA  1 
ATOM   1660 C C   . ALA   A 1 204 ? 14.86352 31.52887  -9.80676  1.000 55.34794  ? 201 ALA   A C   1 
ATOM   1661 O O   . ALA   A 1 204 ? 13.97119 32.29261  -9.42894  1.000 54.62917  ? 201 ALA   A O   1 
ATOM   1662 C CB  . ALA   A 1 204 ? 16.15572 30.50014  -7.92491  1.000 61.34872  ? 201 ALA   A CB  1 
ATOM   1663 N N   . LEU   A 1 205 ? 14.71990 30.70309  -10.84508 1.000 53.39205  ? 202 LEU   A N   1 
ATOM   1664 C CA  . LEU   A 1 205 ? 13.50574 30.72938  -11.65344 1.000 52.51461  ? 202 LEU   A CA  1 
ATOM   1665 C C   . LEU   A 1 205 ? 12.34544 30.04044  -10.94336 1.000 55.76044  ? 202 LEU   A C   1 
ATOM   1666 O O   . LEU   A 1 205 ? 11.24997 30.60288  -10.84303 1.000 60.56318  ? 202 LEU   A O   1 
ATOM   1667 C CB  . LEU   A 1 205 ? 13.77061 30.08239  -13.01435 1.000 53.87779  ? 202 LEU   A CB  1 
ATOM   1668 C CG  . LEU   A 1 205 ? 12.65687 30.15925  -14.06231 1.000 58.26030  ? 202 LEU   A CG  1 
ATOM   1669 C CD1 . LEU   A 1 205 ? 12.20987 31.59692  -14.28266 1.000 58.57508  ? 202 LEU   A CD1 1 
ATOM   1670 C CD2 . LEU   A 1 205 ? 13.12175 29.53670  -15.37120 1.000 52.79749  ? 202 LEU   A CD2 1 
ATOM   1671 N N   . PHE   A 1 206 ? 12.56147 28.82198  -10.45037 1.000 53.92085  ? 203 PHE   A N   1 
ATOM   1672 C CA  . PHE   A 1 206 ? 11.53924 28.06468  -9.72780  1.000 54.74872  ? 203 PHE   A CA  1 
ATOM   1673 C C   . PHE   A 1 206 ? 12.13094 27.61045  -8.40150  1.000 57.90528  ? 203 PHE   A C   1 
ATOM   1674 O O   . PHE   A 1 206 ? 12.60999 26.47518  -8.27870  1.000 55.45553  ? 203 PHE   A O   1 
ATOM   1675 C CB  . PHE   A 1 206 ? 11.04488 26.86420  -10.53656 1.000 57.01641  ? 203 PHE   A CB  1 
ATOM   1676 C CG  . PHE   A 1 206 ? 10.69749 27.18447  -11.96215 1.000 58.05972  ? 203 PHE   A CG  1 
ATOM   1677 C CD1 . PHE   A 1 206 ? 9.66227  28.05541  -12.26120 1.000 57.88870  ? 203 PHE   A CD1 1 
ATOM   1678 C CD2 . PHE   A 1 206 ? 11.39199 26.59273  -13.00483 1.000 58.54741  ? 203 PHE   A CD2 1 
ATOM   1679 C CE1 . PHE   A 1 206 ? 9.33654  28.34388  -13.57462 1.000 61.84486  ? 203 PHE   A CE1 1 
ATOM   1680 C CE2 . PHE   A 1 206 ? 11.07086 26.87440  -14.32147 1.000 60.22519  ? 203 PHE   A CE2 1 
ATOM   1681 C CZ  . PHE   A 1 206 ? 10.04223 27.75143  -14.60751 1.000 63.55052  ? 203 PHE   A CZ  1 
ATOM   1682 N N   . PRO   A 1 207 ? 12.12303 28.47454  -7.38542  1.000 56.71286  ? 204 PRO   A N   1 
ATOM   1683 C CA  . PRO   A 1 207 ? 12.69773 28.10634  -6.07146  1.000 59.23090  ? 204 PRO   A CA  1 
ATOM   1684 C C   . PRO   A 1 207 ? 11.68777 27.42101  -5.15397  1.000 69.10162  ? 204 PRO   A C   1 
ATOM   1685 O O   . PRO   A 1 207 ? 11.15968 28.00143  -4.19291  1.000 65.46390  ? 204 PRO   A O   1 
ATOM   1686 C CB  . PRO   A 1 207 ? 13.15738 29.46202  -5.53166  1.000 60.80129  ? 204 PRO   A CB  1 
ATOM   1687 C CG  . PRO   A 1 207 ? 12.14641 30.42196  -6.07903  1.000 61.18712  ? 204 PRO   A CG  1 
ATOM   1688 C CD  . PRO   A 1 207 ? 11.73692 29.89661  -7.43715  1.000 54.17203  ? 204 PRO   A CD  1 
ATOM   1689 N N   . GLY   A 1 208 ? 11.40785 26.15050  -5.44713  1.000 60.26006  ? 205 GLY   A N   1 
ATOM   1690 C CA  . GLY   A 1 208 ? 10.46424 25.40127  -4.64697  1.000 63.63635  ? 205 GLY   A CA  1 
ATOM   1691 C C   . GLY   A 1 208 ? 11.10443 24.74652  -3.43842  1.000 63.49337  ? 205 GLY   A C   1 
ATOM   1692 O O   . GLY   A 1 208 ? 12.31036 24.51469  -3.39077  1.000 62.38721  ? 205 GLY   A O   1 
ATOM   1693 N N   . ASP   A 1 209 ? 10.26921 24.45716  -2.43814  1.000 65.97199  ? 206 ASP   A N   1 
ATOM   1694 C CA  . ASP   A 1 209 ? 10.71567 23.80313  -1.21647  1.000 73.16295  ? 206 ASP   A CA  1 
ATOM   1695 C C   . ASP   A 1 209 ? 10.19594 22.37817  -1.07503  1.000 67.35143  ? 206 ASP   A C   1 
ATOM   1696 O O   . ASP   A 1 209 ? 10.47881 21.72655  -0.06373  1.000 72.07969  ? 206 ASP   A O   1 
ATOM   1697 C CB  . ASP   A 1 209 ? 10.31071 24.63403  0.00931   1.000 70.57276  ? 206 ASP   A CB  1 
ATOM   1698 C CG  . ASP   A 1 209 ? 8.82108  24.91808  0.06384   1.000 72.92202  ? 206 ASP   A CG  1 
ATOM   1699 O OD1 . ASP   A 1 209 ? 8.07727  24.40591  -0.79862  1.000 81.66068  ? 206 ASP   A OD1 1 
ATOM   1700 O OD2 . ASP   A 1 209 ? 8.39449  25.66206  0.97210   1.000 92.99398  ? 206 ASP   A OD2 1 
ATOM   1701 N N   . SER   A 1 210 ? 9.44345  21.88082  -2.05226  1.000 70.28638  ? 207 SER   A N   1 
ATOM   1702 C CA  . SER   A 1 210 ? 8.98821  20.49923  -2.05639  1.000 69.55524  ? 207 SER   A CA  1 
ATOM   1703 C C   . SER   A 1 210 ? 8.75979  20.08145  -3.50098  1.000 66.51005  ? 207 SER   A C   1 
ATOM   1704 O O   . SER   A 1 210 ? 8.83495  20.89794  -4.42222  1.000 71.81391  ? 207 SER   A O   1 
ATOM   1705 C CB  . SER   A 1 210 ? 7.71731  20.31804  -1.21693  1.000 68.16917  ? 207 SER   A CB  1 
ATOM   1706 O OG  . SER   A 1 210 ? 6.59985  20.94119  -1.82797  1.000 71.17536  ? 207 SER   A OG  1 
ATOM   1707 N N   . GLU   A 1 211 ? 8.48340  18.78930  -3.69434  1.000 65.65317  ? 208 GLU   A N   1 
ATOM   1708 C CA  . GLU   A 1 211 ? 8.25393  18.28863  -5.04633  1.000 64.46883  ? 208 GLU   A CA  1 
ATOM   1709 C C   . GLU   A 1 211 ? 6.97948  18.87121  -5.64334  1.000 64.75323  ? 208 GLU   A C   1 
ATOM   1710 O O   . GLU   A 1 211 ? 6.95396  19.24253  -6.82268  1.000 67.56078  ? 208 GLU   A O   1 
ATOM   1711 C CB  . GLU   A 1 211 ? 8.19205  16.76109  -5.04749  1.000 67.07746  ? 208 GLU   A CB  1 
ATOM   1712 C CG  . GLU   A 1 211 ? 9.51581  16.07804  -4.75004  1.000 66.80012  ? 208 GLU   A CG  1 
ATOM   1713 C CD  . GLU   A 1 211 ? 9.46083  14.58034  -4.98447  1.000 92.38384  ? 208 GLU   A CD  1 
ATOM   1714 O OE1 . GLU   A 1 211 ? 9.39944  14.15991  -6.15969  1.000 88.53411  ? 208 GLU   A OE1 1 
ATOM   1715 O OE2 . GLU   A 1 211 ? 9.47220  13.82284  -3.99236  1.000 101.77098 ? 208 GLU   A OE2 1 
ATOM   1716 N N   . ILE   A 1 212 ? 5.91073  18.95927  -4.84791  1.000 65.60724  ? 209 ILE   A N   1 
ATOM   1717 C CA  . ILE   A 1 212 ? 4.65612  19.48702  -5.37307  1.000 70.21525  ? 209 ILE   A CA  1 
ATOM   1718 C C   . ILE   A 1 212 ? 4.71553  21.00447  -5.50426  1.000 71.94472  ? 209 ILE   A C   1 
ATOM   1719 O O   . ILE   A 1 212 ? 4.10049  21.57837  -6.41175  1.000 67.90385  ? 209 ILE   A O   1 
ATOM   1720 C CB  . ILE   A 1 212 ? 3.47418  19.03052  -4.49535  1.000 66.04017  ? 209 ILE   A CB  1 
ATOM   1721 C CG1 . ILE   A 1 212 ? 2.14299  19.37033  -5.16853  1.000 77.70522  ? 209 ILE   A CG1 1 
ATOM   1722 C CG2 . ILE   A 1 212 ? 3.54928  19.65365  -3.10733  1.000 71.22104  ? 209 ILE   A CG2 1 
ATOM   1723 C CD1 . ILE   A 1 212 ? 1.93528  18.66451  -6.49446  1.000 76.79019  ? 209 ILE   A CD1 1 
ATOM   1724 N N   . ASP   A 1 213 ? 5.46014  21.67951  -4.62384  1.000 66.24930  ? 210 ASP   A N   1 
ATOM   1725 C CA  . ASP   A 1 213 ? 5.59349  23.12939  -4.72904  1.000 62.60907  ? 210 ASP   A CA  1 
ATOM   1726 C C   . ASP   A 1 213 ? 6.48840  23.51762  -5.89838  1.000 62.84588  ? 210 ASP   A C   1 
ATOM   1727 O O   . ASP   A 1 213 ? 6.23902  24.52484  -6.57047  1.000 62.75494  ? 210 ASP   A O   1 
ATOM   1728 C CB  . ASP   A 1 213 ? 6.13959  23.70112  -3.42262  1.000 61.54106  ? 210 ASP   A CB  1 
ATOM   1729 C CG  . ASP   A 1 213 ? 6.30213  25.20164  -3.47059  1.000 71.88794  ? 210 ASP   A CG  1 
ATOM   1730 O OD1 . ASP   A 1 213 ? 5.27368  25.91007  -3.46979  1.000 70.31925  ? 210 ASP   A OD1 1 
ATOM   1731 O OD2 . ASP   A 1 213 ? 7.45847  25.67111  -3.50810  1.000 67.85812  ? 210 ASP   A OD2 1 
ATOM   1732 N N   . GLN   A 1 214 ? 7.54365  22.73866  -6.14565  1.000 59.36678  ? 211 GLN   A N   1 
ATOM   1733 C CA  . GLN   A 1 214 ? 8.37921  22.97467  -7.31760  1.000 53.81935  ? 211 GLN   A CA  1 
ATOM   1734 C C   . GLN   A 1 214 ? 7.57371  22.82315  -8.60045  1.000 60.80099  ? 211 GLN   A C   1 
ATOM   1735 O O   . GLN   A 1 214 ? 7.72112  23.61907  -9.53561  1.000 57.24053  ? 211 GLN   A O   1 
ATOM   1736 C CB  . GLN   A 1 214 ? 9.56477  22.01031  -7.31513  1.000 55.79075  ? 211 GLN   A CB  1 
ATOM   1737 C CG  . GLN   A 1 214 ? 10.50822 22.17812  -8.49180  1.000 56.71485  ? 211 GLN   A CG  1 
ATOM   1738 C CD  . GLN   A 1 214 ? 11.40100 23.39138  -8.34948  1.000 63.00022  ? 211 GLN   A CD  1 
ATOM   1739 O OE1 . GLN   A 1 214 ? 11.61115 23.89488  -7.24666  1.000 60.09515  ? 211 GLN   A OE1 1 
ATOM   1740 N NE2 . GLN   A 1 214 ? 11.93674 23.86580  -9.46660  1.000 55.34679  ? 211 GLN   A NE2 1 
ATOM   1741 N N   . LEU   A 1 215 ? 6.71004  21.80691  -8.65704  1.000 63.28748  ? 212 LEU   A N   1 
ATOM   1742 C CA  . LEU   A 1 215 ? 5.88792  21.58757  -9.84164  1.000 65.00118  ? 212 LEU   A CA  1 
ATOM   1743 C C   . LEU   A 1 215 ? 4.87773  22.71301  -10.02888 1.000 66.92269  ? 212 LEU   A C   1 
ATOM   1744 O O   . LEU   A 1 215 ? 4.60306  23.12678  -11.16153 1.000 68.02798  ? 212 LEU   A O   1 
ATOM   1745 C CB  . LEU   A 1 215 ? 5.17920  20.23726  -9.73405  1.000 62.14247  ? 212 LEU   A CB  1 
ATOM   1746 C CG  . LEU   A 1 215 ? 4.50297  19.67773  -10.98595 1.000 69.28519  ? 212 LEU   A CG  1 
ATOM   1747 C CD1 . LEU   A 1 215 ? 5.53363  19.26580  -12.02721 1.000 58.59533  ? 212 LEU   A CD1 1 
ATOM   1748 C CD2 . LEU   A 1 215 ? 3.60440  18.50680  -10.62381 1.000 72.73078  ? 212 LEU   A CD2 1 
ATOM   1749 N N   . PHE   A 1 216 ? 4.31804  23.22547  -8.92993  1.000 61.92379  ? 213 PHE   A N   1 
ATOM   1750 C CA  . PHE   A 1 216 ? 3.33491  24.29817  -9.04050  1.000 62.06019  ? 213 PHE   A CA  1 
ATOM   1751 C C   . PHE   A 1 216 ? 3.98530  25.62502  -9.40973  1.000 67.82492  ? 213 PHE   A C   1 
ATOM   1752 O O   . PHE   A 1 216 ? 3.35743  26.45416  -10.07858 1.000 67.80137  ? 213 PHE   A O   1 
ATOM   1753 C CB  . PHE   A 1 216 ? 2.54803  24.43811  -7.73674  1.000 67.70164  ? 213 PHE   A CB  1 
ATOM   1754 C CG  . PHE   A 1 216 ? 1.50200  23.37468  -7.53906  1.000 65.76304  ? 213 PHE   A CG  1 
ATOM   1755 C CD1 . PHE   A 1 216 ? 1.36878  22.33399  -8.44475  1.000 70.01685  ? 213 PHE   A CD1 1 
ATOM   1756 C CD2 . PHE   A 1 216 ? 0.64104  23.42530  -6.45397  1.000 66.47256  ? 213 PHE   A CD2 1 
ATOM   1757 C CE1 . PHE   A 1 216 ? 0.40682  21.35721  -8.26582  1.000 81.11814  ? 213 PHE   A CE1 1 
ATOM   1758 C CE2 . PHE   A 1 216 ? -0.32593 22.45138  -6.26953  1.000 71.65496  ? 213 PHE   A CE2 1 
ATOM   1759 C CZ  . PHE   A 1 216 ? -0.44303 21.41701  -7.17571  1.000 80.21206  ? 213 PHE   A CZ  1 
ATOM   1760 N N   . ARG   A 1 217 ? 5.22989  25.85026  -8.98084  1.000 58.63924  ? 214 ARG   A N   1 
ATOM   1761 C CA  . ARG   A 1 217 ? 5.94391  27.05016  -9.40552  1.000 60.31433  ? 214 ARG   A CA  1 
ATOM   1762 C C   . ARG   A 1 217 ? 6.23508  27.01152  -10.89976 1.000 62.50137  ? 214 ARG   A C   1 
ATOM   1763 O O   . ARG   A 1 217 ? 6.22293  28.05189  -11.56826 1.000 66.08049  ? 214 ARG   A O   1 
ATOM   1764 C CB  . ARG   A 1 217 ? 7.23826  27.20731  -8.60822  1.000 57.74544  ? 214 ARG   A CB  1 
ATOM   1765 C CG  . ARG   A 1 217 ? 7.02507  27.58157  -7.15249  1.000 60.20299  ? 214 ARG   A CG  1 
ATOM   1766 C CD  . ARG   A 1 217 ? 8.34576  27.83304  -6.44603  1.000 70.09570  ? 214 ARG   A CD  1 
ATOM   1767 N NE  . ARG   A 1 217 ? 8.15447  28.16057  -5.03803  1.000 74.20036  ? 214 ARG   A NE  1 
ATOM   1768 C CZ  . ARG   A 1 217 ? 7.96408  29.38785  -4.57389  1.000 78.37825  ? 214 ARG   A CZ  1 
ATOM   1769 N NH1 . ARG   A 1 217 ? 7.93348  30.43479  -5.38192  1.000 83.83202  ? 214 ARG   A NH1 1 
ATOM   1770 N NH2 . ARG   A 1 217 ? 7.79851  29.56887  -3.26658  1.000 78.25878  ? 214 ARG   A NH2 1 
ATOM   1771 N N   . ILE   A 1 218 ? 6.50222  25.81982  -11.43883 1.000 59.63191  ? 215 ILE   A N   1 
ATOM   1772 C CA  . ILE   A 1 218 ? 6.66452  25.67392  -12.88139 1.000 61.74053  ? 215 ILE   A CA  1 
ATOM   1773 C C   . ILE   A 1 218 ? 5.33803  25.91059  -13.58870 1.000 59.14150  ? 215 ILE   A C   1 
ATOM   1774 O O   . ILE   A 1 218 ? 5.28550  26.56125  -14.63968 1.000 65.94796  ? 215 ILE   A O   1 
ATOM   1775 C CB  . ILE   A 1 218 ? 7.24470  24.28766  -13.21637 1.000 57.66773  ? 215 ILE   A CB  1 
ATOM   1776 C CG1 . ILE   A 1 218 ? 8.63266  24.12667  -12.59606 1.000 58.79154  ? 215 ILE   A CG1 1 
ATOM   1777 C CG2 . ILE   A 1 218 ? 7.30346  24.07895  -14.72411 1.000 61.83246  ? 215 ILE   A CG2 1 
ATOM   1778 C CD1 . ILE   A 1 218 ? 9.19912  22.73319  -12.72757 1.000 48.60773  ? 215 ILE   A CD1 1 
ATOM   1779 N N   . PHE   A 1 219 ? 4.24532  25.39345  -13.02077 1.000 64.28661  ? 216 PHE   A N   1 
ATOM   1780 C CA  . PHE   A 1 219 ? 2.93249  25.58546  -13.62816 1.000 63.11740  ? 216 PHE   A CA  1 
ATOM   1781 C C   . PHE   A 1 219 ? 2.53404  27.05615  -13.62843 1.000 72.81335  ? 216 PHE   A C   1 
ATOM   1782 O O   . PHE   A 1 219 ? 1.93314  27.54357  -14.59209 1.000 71.28289  ? 216 PHE   A O   1 
ATOM   1783 C CB  . PHE   A 1 219 ? 1.87758  24.75735  -12.89244 1.000 66.18137  ? 216 PHE   A CB  1 
ATOM   1784 C CG  . PHE   A 1 219 ? 2.00171  23.27054  -13.09733 1.000 61.27648  ? 216 PHE   A CG  1 
ATOM   1785 C CD1 . PHE   A 1 219 ? 2.99351  22.73679  -13.90403 1.000 58.70993  ? 216 PHE   A CD1 1 
ATOM   1786 C CD2 . PHE   A 1 219 ? 1.10723  22.40603  -12.48560 1.000 62.67069  ? 216 PHE   A CD2 1 
ATOM   1787 C CE1 . PHE   A 1 219 ? 3.09895  21.37010  -14.08288 1.000 59.47343  ? 216 PHE   A CE1 1 
ATOM   1788 C CE2 . PHE   A 1 219 ? 1.20430  21.04147  -12.66488 1.000 64.46898  ? 216 PHE   A CE2 1 
ATOM   1789 C CZ  . PHE   A 1 219 ? 2.19914  20.52238  -13.46692 1.000 62.81688  ? 216 PHE   A CZ  1 
ATOM   1790 N N   . ARG   A 1 220 ? 2.85594  27.77934  -12.55278 1.000 68.62497  ? 217 ARG   A N   1 
ATOM   1791 C CA  . ARG   A 1 220 ? 2.46304  29.18021  -12.44514 1.000 71.92848  ? 217 ARG   A CA  1 
ATOM   1792 C C   . ARG   A 1 220 ? 3.15212  30.06508  -13.47563 1.000 69.00567  ? 217 ARG   A C   1 
ATOM   1793 O O   . ARG   A 1 220 ? 2.61760  31.12467  -13.81964 1.000 74.17691  ? 217 ARG   A O   1 
ATOM   1794 C CB  . ARG   A 1 220 ? 2.75553  29.69915  -11.03637 1.000 71.14917  ? 217 ARG   A CB  1 
ATOM   1795 C CG  . ARG   A 1 220 ? 1.70432  29.31969  -10.00857 1.000 85.90280  ? 217 ARG   A CG  1 
ATOM   1796 C CD  . ARG   A 1 220 ? 2.05944  29.84178  -8.62500  1.000 88.50266  ? 217 ARG   A CD  1 
ATOM   1797 N NE  . ARG   A 1 220 ? 2.72717  31.13800  -8.67074  1.000 93.64038  ? 217 ARG   A NE  1 
ATOM   1798 C CZ  . ARG   A 1 220 ? 2.12216  32.29245  -8.91718  1.000 97.07527  ? 217 ARG   A CZ  1 
ATOM   1799 N NH1 . ARG   A 1 220 ? 0.82900  32.35232  -9.18941  1.000 92.09114  ? 217 ARG   A NH1 1 
ATOM   1800 N NH2 . ARG   A 1 220 ? 2.83553  33.41477  -8.89878  1.000 101.11129 ? 217 ARG   A NH2 1 
ATOM   1801 N N   . THR   A 1 221 ? 4.31579  29.65774  -13.97855 1.000 60.79913  ? 218 THR   A N   1 
ATOM   1802 C CA  . THR   A 1 221 ? 5.06409  30.44710  -14.94924 1.000 72.74643  ? 218 THR   A CA  1 
ATOM   1803 C C   . THR   A 1 221 ? 4.82527  29.99306  -16.38377 1.000 67.06137  ? 218 THR   A C   1 
ATOM   1804 O O   . THR   A 1 221 ? 4.61158  30.82505  -17.26943 1.000 74.67227  ? 218 THR   A O   1 
ATOM   1805 C CB  . THR   A 1 221 ? 6.56344  30.38864  -14.63007 1.000 68.13005  ? 218 THR   A CB  1 
ATOM   1806 O OG1 . THR   A 1 221 ? 6.78038  30.79664  -13.27405 1.000 68.42083  ? 218 THR   A OG1 1 
ATOM   1807 C CG2 . THR   A 1 221 ? 7.34694  31.30651  -15.55834 1.000 74.17838  ? 218 THR   A CG2 1 
ATOM   1808 N N   . LEU   A 1 222 ? 4.85351  28.68587  -16.63046 1.000 67.75711  ? 219 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 222 ? 4.71670  28.13995  -17.97337 1.000 68.55726  ? 219 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 222 ? 3.31641  27.62122  -18.26918 1.000 70.54466  ? 219 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 222 ? 3.07817  27.11931  -19.37192 1.000 73.58539  ? 219 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 222 ? 5.73485  27.01544  -18.19039 1.000 63.24755  ? 219 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 222 ? 7.20753  27.39192  -18.02100 1.000 66.30329  ? 219 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 222 ? 8.08538  26.15160  -18.04786 1.000 62.19276  ? 219 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 222 ? 7.63725  28.37840  -19.09579 1.000 73.80550  ? 219 LEU   A CD2 1 
ATOM   1816 N N   . GLY   A 1 223 ? 2.39335  27.72766  -17.32701 1.000 69.70013  ? 220 GLY   A N   1 
ATOM   1817 C CA  . GLY   A 1 223 ? 1.05256  27.21643  -17.56238 1.000 67.79850  ? 220 GLY   A CA  1 
ATOM   1818 C C   . GLY   A 1 223 ? 0.93577  25.74120  -17.23808 1.000 64.54230  ? 220 GLY   A C   1 
ATOM   1819 O O   . GLY   A 1 223 ? 1.86741  24.95566  -17.41098 1.000 69.33898  ? 220 GLY   A O   1 
ATOM   1820 N N   . THR   A 1 224 ? -0.23456 25.36187  -16.74681 1.000 66.75560  ? 221 THR   A N   1 
ATOM   1821 C CA  . THR   A 1 224 ? -0.51174 23.96369  -16.43732 1.000 71.88842  ? 221 THR   A CA  1 
ATOM   1822 C C   . THR   A 1 224 ? -0.56882 23.15500  -17.72574 1.000 66.20609  ? 221 THR   A C   1 
ATOM   1823 O O   . THR   A 1 224 ? -1.46812 23.38558  -18.54497 1.000 68.43571  ? 221 THR   A O   1 
ATOM   1824 C CB  . THR   A 1 224 ? -1.82720 23.83478  -15.67095 1.000 69.45147  ? 221 THR   A CB  1 
ATOM   1825 O OG1 . THR   A 1 224 ? -1.76391 24.61957  -14.47393 1.000 75.28520  ? 221 THR   A OG1 1 
ATOM   1826 C CG2 . THR   A 1 224 ? -2.08692 22.38265  -15.29940 1.000 69.37447  ? 221 THR   A CG2 1 
ATOM   1827 N N   . PRO   A 1 225 ? 0.34457  22.21401  -17.94940 1.000 63.81887  ? 222 PRO   A N   1 
ATOM   1828 C CA  . PRO   A 1 225 ? 0.37732  21.51100  -19.23471 1.000 72.95536  ? 222 PRO   A CA  1 
ATOM   1829 C C   . PRO   A 1 225 ? -0.79705 20.56069  -19.39281 1.000 70.36320  ? 222 PRO   A C   1 
ATOM   1830 O O   . PRO   A 1 225 ? -1.36955 20.06767  -18.41794 1.000 69.49400  ? 222 PRO   A O   1 
ATOM   1831 C CB  . PRO   A 1 225 ? 1.70430  20.74658  -19.18391 1.000 69.09662  ? 222 PRO   A CB  1 
ATOM   1832 C CG  . PRO   A 1 225 ? 1.94776  20.53385  -17.72763 1.000 69.89452  ? 222 PRO   A CG  1 
ATOM   1833 C CD  . PRO   A 1 225 ? 1.40982  21.75863  -17.04036 1.000 65.52997  ? 222 PRO   A CD  1 
ATOM   1834 N N   . ASP   A 1 226 ? -1.15514 20.31102  -20.64895 1.000 71.72589  ? 223 ASP   A N   1 
ATOM   1835 C CA  . ASP   A 1 226 ? -2.21953 19.37581  -20.98380 1.000 71.93498  ? 223 ASP   A CA  1 
ATOM   1836 C C   . ASP   A 1 226 ? -1.72911 18.49163  -22.12558 1.000 74.99099  ? 223 ASP   A C   1 
ATOM   1837 O O   . ASP   A 1 226 ? -0.55894 18.54287  -22.51681 1.000 67.54828  ? 223 ASP   A O   1 
ATOM   1838 C CB  . ASP   A 1 226 ? -3.51625 20.12463  -21.32210 1.000 72.02498  ? 223 ASP   A CB  1 
ATOM   1839 C CG  . ASP   A 1 226 ? -3.32676 21.16861  -22.40734 1.000 73.33509  ? 223 ASP   A CG  1 
ATOM   1840 O OD1 . ASP   A 1 226 ? -2.19060 21.32971  -22.89983 1.000 87.95818  ? 223 ASP   A OD1 1 
ATOM   1841 O OD2 . ASP   A 1 226 ? -4.32120 21.83222  -22.76908 1.000 84.37903  ? 223 ASP   A OD2 1 
ATOM   1842 N N   . GLU   A 1 227 ? -2.63727 17.67838  -22.67092 1.000 69.77373  ? 224 GLU   A N   1 
ATOM   1843 C CA  . GLU   A 1 227 ? -2.24324 16.70323  -23.68359 1.000 75.47013  ? 224 GLU   A CA  1 
ATOM   1844 C C   . GLU   A 1 227 ? -1.78472 17.36753  -24.97491 1.000 76.30632  ? 224 GLU   A C   1 
ATOM   1845 O O   . GLU   A 1 227 ? -0.99210 16.78382  -25.72258 1.000 73.87650  ? 224 GLU   A O   1 
ATOM   1846 C CB  . GLU   A 1 227 ? -3.39884 15.74259  -23.96452 1.000 70.93017  ? 224 GLU   A CB  1 
ATOM   1847 C CG  . GLU   A 1 227 ? -3.59757 14.69354  -22.88479 1.000 73.81553  ? 224 GLU   A CG  1 
ATOM   1848 C CD  . GLU   A 1 227 ? -2.43954 13.71476  -22.80649 1.000 83.44115  ? 224 GLU   A CD  1 
ATOM   1849 O OE1 . GLU   A 1 227 ? -1.73762 13.53718  -23.82452 1.000 78.53952  ? 224 GLU   A OE1 1 
ATOM   1850 O OE2 . GLU   A 1 227 ? -2.23019 13.12099  -21.72842 1.000 82.38796  ? 224 GLU   A OE2 1 
ATOM   1851 N N   . VAL   A 1 228 ? -2.26203 18.58003  -25.25509 1.000 74.89859  ? 225 VAL   A N   1 
ATOM   1852 C CA  . VAL   A 1 228 ? -1.88861 19.25310  -26.49544 1.000 76.53696  ? 225 VAL   A CA  1 
ATOM   1853 C C   . VAL   A 1 228 ? -0.43511 19.70940  -26.44107 1.000 76.82398  ? 225 VAL   A C   1 
ATOM   1854 O O   . VAL   A 1 228 ? 0.34924  19.45208  -27.36178 1.000 77.79353  ? 225 VAL   A O   1 
ATOM   1855 C CB  . VAL   A 1 228 ? -2.83967 20.42990  -26.77259 1.000 82.66534  ? 225 VAL   A CB  1 
ATOM   1856 C CG1 . VAL   A 1 228 ? -2.29446 21.28552  -27.89799 1.000 83.94717  ? 225 VAL   A CG1 1 
ATOM   1857 C CG2 . VAL   A 1 228 ? -4.23082 19.91590  -27.11788 1.000 75.60230  ? 225 VAL   A CG2 1 
ATOM   1858 N N   . VAL   A 1 229 ? -0.05441 20.39845  -25.36362 1.000 78.91113  ? 226 VAL   A N   1 
ATOM   1859 C CA  . VAL   A 1 229 ? 1.31263  20.89619  -25.24706 1.000 74.60764  ? 226 VAL   A CA  1 
ATOM   1860 C C   . VAL   A 1 229 ? 2.29564  19.81294  -24.82165 1.000 73.86862  ? 226 VAL   A C   1 
ATOM   1861 O O   . VAL   A 1 229 ? 3.50756  19.98089  -25.00949 1.000 73.39923  ? 226 VAL   A O   1 
ATOM   1862 C CB  . VAL   A 1 229 ? 1.38372  22.07789  -24.26384 1.000 75.86084  ? 226 VAL   A CB  1 
ATOM   1863 C CG1 . VAL   A 1 229 ? 0.22447  23.04149  -24.49557 1.000 79.63739  ? 226 VAL   A CG1 1 
ATOM   1864 C CG2 . VAL   A 1 229 ? 1.40762  21.59244  -22.82003 1.000 79.93280  ? 226 VAL   A CG2 1 
ATOM   1865 N N   . TRP   A 1 230 ? 1.81153  18.70647  -24.26349 1.000 72.93720  ? 227 TRP   A N   1 
ATOM   1866 C CA  . TRP   A 1 230 ? 2.65683  17.62472  -23.77334 1.000 64.98408  ? 227 TRP   A CA  1 
ATOM   1867 C C   . TRP   A 1 230 ? 1.89511  16.30660  -23.86171 1.000 70.56195  ? 227 TRP   A C   1 
ATOM   1868 O O   . TRP   A 1 230 ? 1.21218  15.92955  -22.90201 1.000 66.12680  ? 227 TRP   A O   1 
ATOM   1869 C CB  . TRP   A 1 230 ? 3.09549  17.92540  -22.33727 1.000 68.06513  ? 227 TRP   A CB  1 
ATOM   1870 C CG  . TRP   A 1 230 ? 4.08686  16.95651  -21.76653 1.000 69.97222  ? 227 TRP   A CG  1 
ATOM   1871 C CD1 . TRP   A 1 230 ? 4.59707  15.84631  -22.37544 1.000 67.96116  ? 227 TRP   A CD1 1 
ATOM   1872 C CD2 . TRP   A 1 230 ? 4.68687  17.01521  -20.46493 1.000 67.70212  ? 227 TRP   A CD2 1 
ATOM   1873 N NE1 . TRP   A 1 230 ? 5.47514  15.20937  -21.53013 1.000 66.64797  ? 227 TRP   A NE1 1 
ATOM   1874 C CE2 . TRP   A 1 230 ? 5.54862  15.90760  -20.35244 1.000 62.69458  ? 227 TRP   A CE2 1 
ATOM   1875 C CE3 . TRP   A 1 230 ? 4.57752  17.89697  -19.38707 1.000 70.71171  ? 227 TRP   A CE3 1 
ATOM   1876 C CZ2 . TRP   A 1 230 ? 6.29590  15.65742  -19.20533 1.000 63.29971  ? 227 TRP   A CZ2 1 
ATOM   1877 C CZ3 . TRP   A 1 230 ? 5.32088  17.64621  -18.24862 1.000 63.72427  ? 227 TRP   A CZ3 1 
ATOM   1878 C CH2 . TRP   A 1 230 ? 6.16892  16.53461  -18.16815 1.000 67.09602  ? 227 TRP   A CH2 1 
ATOM   1879 N N   . PRO   A 1 231 ? 1.96052  15.59819  -24.98864 1.000 73.94620  ? 228 PRO   A N   1 
ATOM   1880 C CA  . PRO   A 1 231 ? 1.18260  14.36059  -25.11435 1.000 71.39629  ? 228 PRO   A CA  1 
ATOM   1881 C C   . PRO   A 1 231 ? 1.60266  13.31927  -24.08575 1.000 64.67427  ? 228 PRO   A C   1 
ATOM   1882 O O   . PRO   A 1 231 ? 2.78622  13.00227  -23.93864 1.000 67.82414  ? 228 PRO   A O   1 
ATOM   1883 C CB  . PRO   A 1 231 ? 1.48608  13.89667  -26.54146 1.000 70.06990  ? 228 PRO   A CB  1 
ATOM   1884 C CG  . PRO   A 1 231 ? 1.93258  15.11060  -27.26280 1.000 71.54518  ? 228 PRO   A CG  1 
ATOM   1885 C CD  . PRO   A 1 231 ? 2.66172  15.93901  -26.24311 1.000 74.16375  ? 228 PRO   A CD  1 
ATOM   1886 N N   . GLY   A 1 232 ? 0.61043  12.77688  -23.38212 1.000 72.48352  ? 229 GLY   A N   1 
ATOM   1887 C CA  . GLY   A 1 232 ? 0.83545  11.76616  -22.37361 1.000 71.53279  ? 229 GLY   A CA  1 
ATOM   1888 C C   . GLY   A 1 232 ? 1.02913  12.28683  -20.96677 1.000 71.05657  ? 229 GLY   A C   1 
ATOM   1889 O O   . GLY   A 1 232 ? 1.31938  11.48933  -20.06605 1.000 83.06758  ? 229 GLY   A O   1 
ATOM   1890 N N   . VAL   A 1 233 ? 0.86985  13.59347  -20.74196 1.000 69.45558  ? 230 VAL   A N   1 
ATOM   1891 C CA  . VAL   A 1 233 ? 1.12237  14.14829  -19.41487 1.000 77.01999  ? 230 VAL   A CA  1 
ATOM   1892 C C   . VAL   A 1 233 ? 0.03287  13.73539  -18.43129 1.000 77.66528  ? 230 VAL   A C   1 
ATOM   1893 O O   . VAL   A 1 233 ? 0.30445  13.54346  -17.23933 1.000 68.58217  ? 230 VAL   A O   1 
ATOM   1894 C CB  . VAL   A 1 233 ? 1.26806  15.68193  -19.49118 1.000 69.24653  ? 230 VAL   A CB  1 
ATOM   1895 C CG1 . VAL   A 1 233 ? -0.02729 16.33111  -19.96077 1.000 71.48136  ? 230 VAL   A CG1 1 
ATOM   1896 C CG2 . VAL   A 1 233 ? 1.69392  16.24648  -18.14508 1.000 68.34691  ? 230 VAL   A CG2 1 
ATOM   1897 N N   . THR   A 1 234 ? -1.20562 13.57651  -18.90184 1.000 72.62341  ? 231 THR   A N   1 
ATOM   1898 C CA  . THR   A 1 234 ? -2.29757 13.19883  -18.01411 1.000 72.72545  ? 231 THR   A CA  1 
ATOM   1899 C C   . THR   A 1 234 ? -2.21289 11.74828  -17.56005 1.000 76.17915  ? 231 THR   A C   1 
ATOM   1900 O O   . THR   A 1 234 ? -2.92984 11.36712  -16.62867 1.000 85.71043  ? 231 THR   A O   1 
ATOM   1901 C CB  . THR   A 1 234 ? -3.64381 13.44650  -18.69868 1.000 86.24322  ? 231 THR   A CB  1 
ATOM   1902 O OG1 . THR   A 1 234 ? -3.73647 12.64448  -19.88203 1.000 81.67748  ? 231 THR   A OG1 1 
ATOM   1903 C CG2 . THR   A 1 234 ? -3.78491 14.91272  -19.07715 1.000 82.91407  ? 231 THR   A CG2 1 
ATOM   1904 N N   . SER   A 1 235 ? -1.36046 10.93925  -18.18476 1.000 82.37008  ? 232 SER   A N   1 
ATOM   1905 C CA  . SER   A 1 235 ? -1.19860 9.53833   -17.82511 1.000 84.55568  ? 232 SER   A CA  1 
ATOM   1906 C C   . SER   A 1 235 ? 0.04157  9.28189   -16.98059 1.000 86.42199  ? 232 SER   A C   1 
ATOM   1907 O O   . SER   A 1 235 ? 0.31216  8.12697   -16.63830 1.000 92.77973  ? 232 SER   A O   1 
ATOM   1908 C CB  . SER   A 1 235 ? -1.14583 8.67341   -19.08931 1.000 82.79915  ? 232 SER   A CB  1 
ATOM   1909 O OG  . SER   A 1 235 ? -2.32180 8.82772   -19.86481 1.000 88.47656  ? 232 SER   A OG  1 
ATOM   1910 N N   . MET   A 1 236 ? 0.79587  10.32168  -16.63696 1.000 76.78032  ? 233 MET   A N   1 
ATOM   1911 C CA  . MET   A 1 236 ? 2.01799  10.13305  -15.87633 1.000 75.13417  ? 233 MET   A CA  1 
ATOM   1912 C C   . MET   A 1 236 ? 1.69209  9.80531   -14.41793 1.000 77.91006  ? 233 MET   A C   1 
ATOM   1913 O O   . MET   A 1 236 ? 0.64525  10.20731  -13.90247 1.000 83.57904  ? 233 MET   A O   1 
ATOM   1914 C CB  . MET   A 1 236 ? 2.89367  11.37973  -15.96787 1.000 74.05312  ? 233 MET   A CB  1 
ATOM   1915 C CG  . MET   A 1 236 ? 3.24684  11.75435  -17.40133 1.000 77.55476  ? 233 MET   A CG  1 
ATOM   1916 S SD  . MET   A 1 236 ? 4.52736  13.01383  -17.52711 1.000 77.34162  ? 233 MET   A SD  1 
ATOM   1917 C CE  . MET   A 1 236 ? 5.94294  12.12777  -16.87772 1.000 74.21625  ? 233 MET   A CE  1 
ATOM   1918 N N   . PRO   A 1 237 ? 2.57457  9.06523   -13.73455 1.000 75.47515  ? 234 PRO   A N   1 
ATOM   1919 C CA  . PRO   A 1 237 ? 2.21385  8.53992   -12.40359 1.000 81.65510  ? 234 PRO   A CA  1 
ATOM   1920 C C   . PRO   A 1 237 ? 1.87954  9.60838   -11.37573 1.000 75.08450  ? 234 PRO   A C   1 
ATOM   1921 O O   . PRO   A 1 237 ? 0.95077  9.41906   -10.58042 1.000 81.81230  ? 234 PRO   A O   1 
ATOM   1922 C CB  . PRO   A 1 237 ? 3.46059  7.73801   -12.00130 1.000 78.52747  ? 234 PRO   A CB  1 
ATOM   1923 C CG  . PRO   A 1 237 ? 4.11297  7.37913   -13.29466 1.000 76.81139  ? 234 PRO   A CG  1 
ATOM   1924 C CD  . PRO   A 1 237 ? 3.87837  8.55479   -14.19357 1.000 76.59382  ? 234 PRO   A CD  1 
ATOM   1925 N N   . ASP   A 1 238 ? 2.60416  10.72332  -11.35991 1.000 76.36203  ? 235 ASP   A N   1 
ATOM   1926 C CA  . ASP   A 1 238 ? 2.37160  11.76318  -10.36659 1.000 81.73944  ? 235 ASP   A CA  1 
ATOM   1927 C C   . ASP   A 1 238 ? 1.41843  12.84946  -10.84615 1.000 79.43185  ? 235 ASP   A C   1 
ATOM   1928 O O   . ASP   A 1 238 ? 1.20799  13.82889  -10.12302 1.000 80.93823  ? 235 ASP   A O   1 
ATOM   1929 C CB  . ASP   A 1 238 ? 3.69943  12.39565  -9.93951  1.000 75.80798  ? 235 ASP   A CB  1 
ATOM   1930 C CG  . ASP   A 1 238 ? 4.57292  11.43925  -9.15268  1.000 84.30291  ? 235 ASP   A CG  1 
ATOM   1931 O OD1 . ASP   A 1 238 ? 4.02184  10.63113  -8.37524  1.000 91.66191  ? 235 ASP   A OD1 1 
ATOM   1932 O OD2 . ASP   A 1 238 ? 5.81004  11.49557  -9.31128  1.000 87.33628  ? 235 ASP   A OD2 1 
ATOM   1933 N N   . TYR   A 1 239 ? 0.83944  12.70900  -12.03519 1.000 80.77394  ? 236 TYR   A N   1 
ATOM   1934 C CA  . TYR   A 1 239 ? -0.14046 13.68332  -12.49137 1.000 84.67607  ? 236 TYR   A CA  1 
ATOM   1935 C C   . TYR   A 1 239 ? -1.44817 13.51264  -11.73004 1.000 77.07417  ? 236 TYR   A C   1 
ATOM   1936 O O   . TYR   A 1 239 ? -1.88711 12.39230  -11.45593 1.000 77.84340  ? 236 TYR   A O   1 
ATOM   1937 C CB  . TYR   A 1 239 ? -0.38921 13.54487  -13.99345 1.000 81.24051  ? 236 TYR   A CB  1 
ATOM   1938 C CG  . TYR   A 1 239 ? -1.39951 14.54027  -14.52739 1.000 78.34970  ? 236 TYR   A CG  1 
ATOM   1939 C CD1 . TYR   A 1 239 ? -1.00498 15.80924  -14.93237 1.000 78.93898  ? 236 TYR   A CD1 1 
ATOM   1940 C CD2 . TYR   A 1 239 ? -2.74810 14.21445  -14.61861 1.000 75.66021  ? 236 TYR   A CD2 1 
ATOM   1941 C CE1 . TYR   A 1 239 ? -1.92354 16.72373  -15.41648 1.000 70.43562  ? 236 TYR   A CE1 1 
ATOM   1942 C CE2 . TYR   A 1 239 ? -3.67360 15.12323  -15.10010 1.000 82.07115  ? 236 TYR   A CE2 1 
ATOM   1943 C CZ  . TYR   A 1 239 ? -3.25599 16.37588  -15.49835 1.000 78.19986  ? 236 TYR   A CZ  1 
ATOM   1944 O OH  . TYR   A 1 239 ? -4.17232 17.28306  -15.97882 1.000 75.32629  ? 236 TYR   A OH  1 
ATOM   1945 N N   . LYS   A 1 240 ? -2.07227 14.63851  -11.39103 1.000 76.73052  ? 237 LYS   A N   1 
ATOM   1946 C CA  . LYS   A 1 240 ? -3.34800 14.65058  -10.69631 1.000 83.83767  ? 237 LYS   A CA  1 
ATOM   1947 C C   . LYS   A 1 240 ? -4.30982 15.54766  -11.46596 1.000 89.11465  ? 237 LYS   A C   1 
ATOM   1948 O O   . LYS   A 1 240 ? -3.93728 16.67225  -11.84444 1.000 84.50238  ? 237 LYS   A O   1 
ATOM   1949 C CB  . LYS   A 1 240 ? -3.18861 15.14971  -9.25319  1.000 86.92450  ? 237 LYS   A CB  1 
ATOM   1950 C CG  . LYS   A 1 240 ? -2.32232 14.26337  -8.37288  1.000 88.56320  ? 237 LYS   A CG  1 
ATOM   1951 C CD  . LYS   A 1 240 ? -3.05447 12.99179  -7.98012  1.000 96.10073  ? 237 LYS   A CD  1 
ATOM   1952 C CE  . LYS   A 1 240 ? -2.19362 12.10855  -7.09208  1.000 94.89308  ? 237 LYS   A CE  1 
ATOM   1953 N NZ  . LYS   A 1 240 ? -1.00902 11.57667  -7.82041  1.000 95.79788  ? 237 LYS   A NZ  1 
ATOM   1954 N N   . PRO   A 1 241 ? -5.53967 15.09650  -11.72957 1.000 91.18596  ? 238 PRO   A N   1 
ATOM   1955 C CA  . PRO   A 1 241 ? -6.52710 15.98454  -12.36570 1.000 92.96138  ? 238 PRO   A CA  1 
ATOM   1956 C C   . PRO   A 1 241 ? -6.88768 17.19286  -11.51799 1.000 97.40287  ? 238 PRO   A C   1 
ATOM   1957 O O   . PRO   A 1 241 ? -7.50445 18.13051  -12.04036 1.000 88.29367  ? 238 PRO   A O   1 
ATOM   1958 C CB  . PRO   A 1 241 ? -7.74345 15.07073  -12.57508 1.000 88.12859  ? 238 PRO   A CB  1 
ATOM   1959 C CG  . PRO   A 1 241 ? -7.19066 13.67910  -12.53957 1.000 92.82892  ? 238 PRO   A CG  1 
ATOM   1960 C CD  . PRO   A 1 241 ? -6.05213 13.72625  -11.56570 1.000 90.97220  ? 238 PRO   A CD  1 
ATOM   1961 N N   . SER   A 1 242 ? -6.52496 17.19993  -10.23609 1.000 93.52111  ? 239 SER   A N   1 
ATOM   1962 C CA  . SER   A 1 242 ? -6.81444 18.31080  -9.33995  1.000 95.94064  ? 239 SER   A CA  1 
ATOM   1963 C C   . SER   A 1 242 ? -5.80060 19.44284  -9.44390  1.000 89.88352  ? 239 SER   A C   1 
ATOM   1964 O O   . SER   A 1 242 ? -5.88707 20.39818  -8.66445  1.000 93.43914  ? 239 SER   A O   1 
ATOM   1965 C CB  . SER   A 1 242 ? -6.87592 17.81023  -7.89433  1.000 106.98934 ? 239 SER   A CB  1 
ATOM   1966 O OG  . SER   A 1 242 ? -5.64078 17.23190  -7.50646  1.000 105.18652 ? 239 SER   A OG  1 
ATOM   1967 N N   . PHE   A 1 243 ? -4.85043 19.36075  -10.36930 1.000 83.56840  ? 240 PHE   A N   1 
ATOM   1968 C CA  . PHE   A 1 243 ? -3.87567 20.43001  -10.53214 1.000 87.57713  ? 240 PHE   A CA  1 
ATOM   1969 C C   . PHE   A 1 243 ? -4.58523 21.72852  -10.90470 1.000 90.49034  ? 240 PHE   A C   1 
ATOM   1970 O O   . PHE   A 1 243 ? -5.45166 21.72331  -11.79066 1.000 96.33779  ? 240 PHE   A O   1 
ATOM   1971 C CB  . PHE   A 1 243 ? -2.85098 20.07229  -11.60847 1.000 84.20403  ? 240 PHE   A CB  1 
ATOM   1972 C CG  . PHE   A 1 243 ? -1.82505 19.06720  -11.16707 1.000 84.95884  ? 240 PHE   A CG  1 
ATOM   1973 C CD1 . PHE   A 1 243 ? -1.68774 18.73468  -9.82965  1.000 80.58641  ? 240 PHE   A CD1 1 
ATOM   1974 C CD2 . PHE   A 1 243 ? -0.98916 18.46145  -12.09283 1.000 85.24434  ? 240 PHE   A CD2 1 
ATOM   1975 C CE1 . PHE   A 1 243 ? -0.74038 17.81199  -9.42350  1.000 75.10759  ? 240 PHE   A CE1 1 
ATOM   1976 C CE2 . PHE   A 1 243 ? -0.03870 17.53876  -11.69390 1.000 79.47916  ? 240 PHE   A CE2 1 
ATOM   1977 C CZ  . PHE   A 1 243 ? 0.08532  17.21315  -10.35744 1.000 85.30585  ? 240 PHE   A CZ  1 
ATOM   1978 N N   . PRO   A 1 244 ? -4.26225 22.84626  -10.25848 1.000 87.98668  ? 241 PRO   A N   1 
ATOM   1979 C CA  . PRO   A 1 244 ? -4.88829 24.11730  -10.63469 1.000 84.06486  ? 241 PRO   A CA  1 
ATOM   1980 C C   . PRO   A 1 244 ? -4.48037 24.54778  -12.03411 1.000 89.16690  ? 241 PRO   A C   1 
ATOM   1981 O O   . PRO   A 1 244 ? -3.39887 24.21443  -12.52605 1.000 78.35293  ? 241 PRO   A O   1 
ATOM   1982 C CB  . PRO   A 1 244 ? -4.36870 25.09900  -9.57688  1.000 84.74527  ? 241 PRO   A CB  1 
ATOM   1983 C CG  . PRO   A 1 244 ? -3.92482 24.23636  -8.43530  1.000 86.47739  ? 241 PRO   A CG  1 
ATOM   1984 C CD  . PRO   A 1 244 ? -3.40713 22.98248  -9.06813  1.000 85.22227  ? 241 PRO   A CD  1 
ATOM   1985 N N   . LYS   A 1 245 ? -5.37214 25.29821  -12.67769 1.000 79.71258  ? 242 LYS   A N   1 
ATOM   1986 C CA  . LYS   A 1 245 ? -5.15365 25.77859  -14.03850 1.000 79.16530  ? 242 LYS   A CA  1 
ATOM   1987 C C   . LYS   A 1 245 ? -4.57612 27.18802  -13.97755 1.000 80.60400  ? 242 LYS   A C   1 
ATOM   1988 O O   . LYS   A 1 245 ? -5.29254 28.14887  -13.67633 1.000 92.67161  ? 242 LYS   A O   1 
ATOM   1989 C CB  . LYS   A 1 245 ? -6.45537 25.75228  -14.83744 1.000 82.60613  ? 242 LYS   A CB  1 
ATOM   1990 C CG  . LYS   A 1 245 ? -7.08729 24.37425  -14.95163 1.000 83.50668  ? 242 LYS   A CG  1 
ATOM   1991 C CD  . LYS   A 1 245 ? -6.16912 23.39724  -15.66811 1.000 80.30491  ? 242 LYS   A CD  1 
ATOM   1992 C CE  . LYS   A 1 245 ? -6.84072 22.04592  -15.84971 1.000 82.02659  ? 242 LYS   A CE  1 
ATOM   1993 N NZ  . LYS   A 1 245 ? -5.96223 21.08377  -16.57010 1.000 88.76305  ? 242 LYS   A NZ  1 
ATOM   1994 N N   . TRP   A 1 246 ? -3.28250 27.30942  -14.25795 1.000 75.36397  ? 243 TRP   A N   1 
ATOM   1995 C CA  . TRP   A 1 246 ? -2.61308 28.59725  -14.35910 1.000 78.59814  ? 243 TRP   A CA  1 
ATOM   1996 C C   . TRP   A 1 246 ? -2.32040 28.91230  -15.81874 1.000 79.29817  ? 243 TRP   A C   1 
ATOM   1997 O O   . TRP   A 1 246 ? -2.00998 28.01370  -16.60764 1.000 80.28846  ? 243 TRP   A O   1 
ATOM   1998 C CB  . TRP   A 1 246 ? -1.30906 28.61027  -13.55662 1.000 79.70016  ? 243 TRP   A CB  1 
ATOM   1999 C CG  . TRP   A 1 246 ? -1.50470 28.67341  -12.07233 1.000 85.13682  ? 243 TRP   A CG  1 
ATOM   2000 C CD1 . TRP   A 1 246 ? -1.94462 29.74436  -11.34878 1.000 78.81539  ? 243 TRP   A CD1 1 
ATOM   2001 C CD2 . TRP   A 1 246 ? -1.25043 27.62758  -11.12553 1.000 79.02101  ? 243 TRP   A CD2 1 
ATOM   2002 N NE1 . TRP   A 1 246 ? -1.98803 29.42738  -10.01297 1.000 86.05207  ? 243 TRP   A NE1 1 
ATOM   2003 C CE2 . TRP   A 1 246 ? -1.56667 28.13405  -9.84937  1.000 82.63942  ? 243 TRP   A CE2 1 
ATOM   2004 C CE3 . TRP   A 1 246 ? -0.79004 26.31181  -11.23318 1.000 75.70601  ? 243 TRP   A CE3 1 
ATOM   2005 C CZ2 . TRP   A 1 246 ? -1.43666 27.37146  -8.68994  1.000 80.60088  ? 243 TRP   A CZ2 1 
ATOM   2006 C CZ3 . TRP   A 1 246 ? -0.66208 25.55630  -10.08015 1.000 87.47806  ? 243 TRP   A CZ3 1 
ATOM   2007 C CH2 . TRP   A 1 246 ? -0.98299 26.08855  -8.82639  1.000 83.83917  ? 243 TRP   A CH2 1 
ATOM   2008 N N   . ALA   A 1 247 ? -2.41856 30.18791  -16.17311 1.000 78.21383  ? 244 ALA   A N   1 
ATOM   2009 C CA  . ALA   A 1 247 ? -2.13066 30.62573  -17.52922 1.000 80.29374  ? 244 ALA   A CA  1 
ATOM   2010 C C   . ALA   A 1 247 ? -0.64026 30.89231  -17.69101 1.000 73.85471  ? 244 ALA   A C   1 
ATOM   2011 O O   . ALA   A 1 247 ? 0.02004  31.38279  -16.77018 1.000 79.41945  ? 244 ALA   A O   1 
ATOM   2012 C CB  . ALA   A 1 247 ? -2.92846 31.88250  -17.87278 1.000 79.13411  ? 244 ALA   A CB  1 
ATOM   2013 N N   . ARG   A 1 248 ? -0.11500 30.56002  -18.86830 1.000 72.79206  ? 245 ARG   A N   1 
ATOM   2014 C CA  . ARG   A 1 248 ? 1.28724  30.82249  -19.15891 1.000 70.54281  ? 245 ARG   A CA  1 
ATOM   2015 C C   . ARG   A 1 248 ? 1.55259  32.32252  -19.15976 1.000 74.78798  ? 245 ARG   A C   1 
ATOM   2016 O O   . ARG   A 1 248 ? 0.79390  33.10602  -19.73757 1.000 91.35325  ? 245 ARG   A O   1 
ATOM   2017 C CB  . ARG   A 1 248 ? 1.67270  30.21522  -20.50876 1.000 79.63145  ? 245 ARG   A CB  1 
ATOM   2018 C CG  . ARG   A 1 248 ? 3.14268  30.37665  -20.86917 1.000 73.62807  ? 245 ARG   A CG  1 
ATOM   2019 C CD  . ARG   A 1 248 ? 3.41769  29.87806  -22.27762 1.000 84.51553  ? 245 ARG   A CD  1 
ATOM   2020 N NE  . ARG   A 1 248 ? 4.82645  29.99026  -22.63657 1.000 80.27049  ? 245 ARG   A NE  1 
ATOM   2021 C CZ  . ARG   A 1 248 ? 5.70756  29.00520  -22.53041 1.000 77.93541  ? 245 ARG   A CZ  1 
ATOM   2022 N NH1 . ARG   A 1 248 ? 5.35945  27.81271  -22.07597 1.000 74.15082  ? 245 ARG   A NH1 1 
ATOM   2023 N NH2 . ARG   A 1 248 ? 6.96837  29.22048  -22.89491 1.000 79.79551  ? 245 ARG   A NH2 1 
ATOM   2024 N N   . GLN   A 1 249 ? 2.63401  32.72119  -18.50024 1.000 87.38205  ? 246 GLN   A N   1 
ATOM   2025 C CA  . GLN   A 1 249 ? 2.97854  34.12804  -18.37844 1.000 89.58445  ? 246 GLN   A CA  1 
ATOM   2026 C C   . GLN   A 1 249 ? 3.83206  34.57953  -19.55602 1.000 89.32192  ? 246 GLN   A C   1 
ATOM   2027 O O   . GLN   A 1 249 ? 4.65713  33.82559  -20.07907 1.000 87.74227  ? 246 GLN   A O   1 
ATOM   2028 C CB  . GLN   A 1 249 ? 3.71742  34.39262  -17.06555 1.000 86.92147  ? 246 GLN   A CB  1 
ATOM   2029 C CG  . GLN   A 1 249 ? 2.87262  34.15716  -15.82401 1.000 89.45056  ? 246 GLN   A CG  1 
ATOM   2030 C CD  . GLN   A 1 249 ? 3.62402  34.44726  -14.53930 1.000 97.00386  ? 246 GLN   A CD  1 
ATOM   2031 O OE1 . GLN   A 1 249 ? 4.83296  34.67954  -14.55116 1.000 97.27608  ? 246 GLN   A OE1 1 
ATOM   2032 N NE2 . GLN   A 1 249 ? 2.90784  34.43669  -13.42080 1.000 103.56707 ? 246 GLN   A NE2 1 
ATOM   2033 N N   . ASP   A 1 250 ? 3.61684  35.82575  -19.97159 1.000 92.74046  ? 247 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 250 ? 4.39647  36.40199  -21.05792 1.000 94.08874  ? 247 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 250 ? 5.85663  36.51831  -20.64097 1.000 93.21315  ? 247 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 250 ? 6.17024  37.08617  -19.59048 1.000 96.73476  ? 247 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 250 ? 3.83708  37.77594  -21.43264 1.000 98.42908  ? 247 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 250 ? 4.23894  38.21326  -22.82905 1.000 103.57705 ? 247 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 250 ? 5.32581  37.81400  -23.29626 1.000 110.51811 ? 247 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 250 ? 3.46259  38.95984  -23.46162 1.000 106.15831 ? 247 ASP   A OD2 1 
ATOM   2041 N N   . PHE   A 1 251 ? 6.75404  35.97533  -21.46811 1.000 91.17445  ? 248 PHE   A N   1 
ATOM   2042 C CA  . PHE   A 1 251 ? 8.17699  36.01780  -21.14921 1.000 92.83960  ? 248 PHE   A CA  1 
ATOM   2043 C C   . PHE   A 1 251 ? 8.73450  37.43404  -21.12420 1.000 98.42812  ? 248 PHE   A C   1 
ATOM   2044 O O   . PHE   A 1 251 ? 9.85964  37.62792  -20.65027 1.000 96.49154  ? 248 PHE   A O   1 
ATOM   2045 C CB  . PHE   A 1 251 ? 8.97203  35.16273  -22.13793 1.000 90.44440  ? 248 PHE   A CB  1 
ATOM   2046 C CG  . PHE   A 1 251 ? 9.06729  33.71574  -21.74432 1.000 83.20718  ? 248 PHE   A CG  1 
ATOM   2047 C CD1 . PHE   A 1 251 ? 8.12053  33.14735  -20.90768 1.000 83.74635  ? 248 PHE   A CD1 1 
ATOM   2048 C CD2 . PHE   A 1 251 ? 10.11590 32.92977  -22.19231 1.000 78.51513  ? 248 PHE   A CD2 1 
ATOM   2049 C CE1 . PHE   A 1 251 ? 8.20789  31.81847  -20.53841 1.000 83.72813  ? 248 PHE   A CE1 1 
ATOM   2050 C CE2 . PHE   A 1 251 ? 10.21115 31.60066  -21.82361 1.000 72.60582  ? 248 PHE   A CE2 1 
ATOM   2051 C CZ  . PHE   A 1 251 ? 9.25505  31.04419  -20.99651 1.000 81.14367  ? 248 PHE   A CZ  1 
ATOM   2052 N N   . SER   A 1 252 ? 7.98605  38.42260  -21.62015 1.000 101.93422 ? 249 SER   A N   1 
ATOM   2053 C CA  . SER   A 1 252 ? 8.37769  39.81227  -21.42350 1.000 102.59003 ? 249 SER   A CA  1 
ATOM   2054 C C   . SER   A 1 252 ? 8.37916  40.19326  -19.94999 1.000 102.67910 ? 249 SER   A C   1 
ATOM   2055 O O   . SER   A 1 252 ? 9.06444  41.14753  -19.56658 1.000 107.32473 ? 249 SER   A O   1 
ATOM   2056 C CB  . SER   A 1 252 ? 7.44496  40.74100  -22.20299 1.000 108.42698 ? 249 SER   A CB  1 
ATOM   2057 O OG  . SER   A 1 252 ? 7.47269  40.44966  -23.58933 1.000 118.04194 ? 249 SER   A OG  1 
ATOM   2058 N N   . LYS   A 1 253 ? 7.62724  39.47048  -19.11982 1.000 101.70448 ? 250 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 253 ? 7.62021  39.68501  -17.67908 1.000 101.72613 ? 250 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 253 ? 8.47617  38.68068  -16.92161 1.000 100.46071 ? 250 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 253 ? 8.99106  39.00973  -15.84810 1.000 106.40634 ? 250 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 253 ? 6.18682  39.62576  -17.13768 1.000 104.15027 ? 250 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 253 ? 5.20795  40.54401  -17.85187 1.000 112.19126 ? 250 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 253 ? 3.89665  40.65519  -17.08739 1.000 118.28381 ? 250 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 253 ? 3.25619  39.29265  -16.86989 1.000 117.60663 ? 250 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 253 ? 2.87048  38.64335  -18.15300 1.000 106.41878 ? 250 LYS   A NZ  1 
ATOM   2067 N N   . VAL   A 1 254 ? 8.63847  37.46616  -17.45092 1.000 89.51745  ? 251 VAL   A N   1 
ATOM   2068 C CA  . VAL   A 1 254 ? 9.46366  36.46477  -16.78076 1.000 87.70886  ? 251 VAL   A CA  1 
ATOM   2069 C C   . VAL   A 1 254 ? 10.93786 36.83618  -16.88340 1.000 87.38907  ? 251 VAL   A C   1 
ATOM   2070 O O   . VAL   A 1 254 ? 11.66338 36.85162  -15.88196 1.000 88.37084  ? 251 VAL   A O   1 
ATOM   2071 C CB  . VAL   A 1 254 ? 9.19080  35.06658  -17.36368 1.000 84.64876  ? 251 VAL   A CB  1 
ATOM   2072 C CG1 . VAL   A 1 254 ? 10.11868 34.03938  -16.73416 1.000 77.92977  ? 251 VAL   A CG1 1 
ATOM   2073 C CG2 . VAL   A 1 254 ? 7.73613  34.67838  -17.14919 1.000 88.66962  ? 251 VAL   A CG2 1 
ATOM   2074 N N   . VAL   A 1 255 ? 11.40112 37.13951  -18.09174 1.000 86.50186  ? 252 VAL   A N   1 
ATOM   2075 C CA  . VAL   A 1 255 ? 12.77630 37.58135  -18.30996 1.000 85.45836  ? 252 VAL   A CA  1 
ATOM   2076 C C   . VAL   A 1 255 ? 12.74966 38.92469  -19.03233 1.000 87.83837  ? 252 VAL   A C   1 
ATOM   2077 O O   . VAL   A 1 255 ? 12.95044 38.97627  -20.25462 1.000 93.44204  ? 252 VAL   A O   1 
ATOM   2078 C CB  . VAL   A 1 255 ? 13.58166 36.52914  -19.08933 1.000 81.51853  ? 252 VAL   A CB  1 
ATOM   2079 C CG1 . VAL   A 1 255 ? 14.12550 35.47560  -18.13786 1.000 81.17809  ? 252 VAL   A CG1 1 
ATOM   2080 C CG2 . VAL   A 1 255 ? 12.71195 35.87232  -20.15554 1.000 82.71559  ? 252 VAL   A CG2 1 
ATOM   2081 N N   . PRO   A 1 256 ? 12.50161 40.02546  -18.32597 1.000 91.22080  ? 253 PRO   A N   1 
ATOM   2082 C CA  . PRO   A 1 256 ? 12.39073 41.33996  -18.98482 1.000 89.81044  ? 253 PRO   A CA  1 
ATOM   2083 C C   . PRO   A 1 256 ? 13.64307 41.72876  -19.75814 1.000 88.94096  ? 253 PRO   A C   1 
ATOM   2084 O O   . PRO   A 1 256 ? 13.52483 42.22099  -20.89065 1.000 94.65666  ? 253 PRO   A O   1 
ATOM   2085 C CB  . PRO   A 1 256 ? 12.12745 42.29937  -17.81335 1.000 86.88529  ? 253 PRO   A CB  1 
ATOM   2086 C CG  . PRO   A 1 256 ? 11.45847 41.44528  -16.79010 1.000 90.60626  ? 253 PRO   A CG  1 
ATOM   2087 C CD  . PRO   A 1 256 ? 12.08944 40.08291  -16.91092 1.000 84.60739  ? 253 PRO   A CD  1 
ATOM   2088 N N   . PRO   A 1 257 ? 14.85650 41.55338  -19.21006 1.000 90.34237  ? 254 PRO   A N   1 
ATOM   2089 C CA  . PRO   A 1 257 ? 16.04336 41.99863  -19.96473 1.000 87.18373  ? 254 PRO   A CA  1 
ATOM   2090 C C   . PRO   A 1 257 ? 16.27816 41.23854  -21.25886 1.000 95.51379  ? 254 PRO   A C   1 
ATOM   2091 O O   . PRO   A 1 257 ? 17.01885 41.73082  -22.11909 1.000 91.63898  ? 254 PRO   A O   1 
ATOM   2092 C CB  . PRO   A 1 257 ? 17.19846 41.77644  -18.97676 1.000 88.61537  ? 254 PRO   A CB  1 
ATOM   2093 C CG  . PRO   A 1 257 ? 16.56229 41.74166  -17.64615 1.000 82.40245  ? 254 PRO   A CG  1 
ATOM   2094 C CD  . PRO   A 1 257 ? 15.25407 41.06608  -17.87463 1.000 79.19908  ? 254 PRO   A CD  1 
ATOM   2095 N N   . LEU   A 1 258 ? 15.67445 40.06679  -21.43142 1.000 94.84287  ? 255 LEU   A N   1 
ATOM   2096 C CA  . LEU   A 1 258 ? 15.95632 39.23392  -22.59143 1.000 94.43096  ? 255 LEU   A CA  1 
ATOM   2097 C C   . LEU   A 1 258 ? 15.23584 39.75757  -23.82870 1.000 95.82658  ? 255 LEU   A C   1 
ATOM   2098 O O   . LEU   A 1 258 ? 14.07046 40.16002  -23.76592 1.000 96.89860  ? 255 LEU   A O   1 
ATOM   2099 C CB  . LEU   A 1 258 ? 15.54807 37.78797  -22.31081 1.000 88.23052  ? 255 LEU   A CB  1 
ATOM   2100 C CG  . LEU   A 1 258 ? 16.57521 36.72055  -22.68839 1.000 86.65746  ? 255 LEU   A CG  1 
ATOM   2101 C CD1 . LEU   A 1 258 ? 17.96992 37.13818  -22.24906 1.000 79.70672  ? 255 LEU   A CD1 1 
ATOM   2102 C CD2 . LEU   A 1 258 ? 16.20067 35.38255  -22.07202 1.000 79.44612  ? 255 LEU   A CD2 1 
ATOM   2103 N N   . ASP   A 1 259 ? 15.94036 39.74801  -24.95836 1.000 93.75542  ? 256 ASP   A N   1 
ATOM   2104 C CA  . ASP   A 1 259 ? 15.39312 40.24082  -26.21560 1.000 99.37434  ? 256 ASP   A CA  1 
ATOM   2105 C C   . ASP   A 1 259 ? 14.56243 39.14346  -26.88123 1.000 96.36329  ? 256 ASP   A C   1 
ATOM   2106 O O   . ASP   A 1 259 ? 14.20368 38.13815  -26.26264 1.000 99.42517  ? 256 ASP   A O   1 
ATOM   2107 C CB  . ASP   A 1 259 ? 16.51681 40.74398  -27.11885 1.000 97.82123  ? 256 ASP   A CB  1 
ATOM   2108 C CG  . ASP   A 1 259 ? 17.58260 39.69320  -27.36793 1.000 103.27561 ? 256 ASP   A CG  1 
ATOM   2109 O OD1 . ASP   A 1 259 ? 17.34113 38.77863  -28.18333 1.000 101.49975 ? 256 ASP   A OD1 1 
ATOM   2110 O OD2 . ASP   A 1 259 ? 18.66307 39.78217  -26.74796 1.000 113.67879 ? 256 ASP   A OD2 1 
ATOM   2111 N N   . GLU   A 1 260 ? 14.25115 39.32697  -28.16648 1.000 96.57871  ? 257 GLU   A N   1 
ATOM   2112 C CA  . GLU   A 1 260 ? 13.38757 38.37954  -28.86570 1.000 95.36678  ? 257 GLU   A CA  1 
ATOM   2113 C C   . GLU   A 1 260 ? 14.07012 37.02822  -29.03950 1.000 87.65990  ? 257 GLU   A C   1 
ATOM   2114 O O   . GLU   A 1 260 ? 13.46315 35.97970  -28.79183 1.000 84.17018  ? 257 GLU   A O   1 
ATOM   2115 C CB  . GLU   A 1 260 ? 12.97098 38.95008  -30.22156 1.000 94.67789  ? 257 GLU   A CB  1 
ATOM   2116 C CG  . GLU   A 1 260 ? 12.18935 37.97470  -31.08901 1.000 103.42464 ? 257 GLU   A CG  1 
ATOM   2117 C CD  . GLU   A 1 260 ? 11.83807 38.55282  -32.44606 1.000 113.78557 ? 257 GLU   A CD  1 
ATOM   2118 O OE1 . GLU   A 1 260 ? 11.88209 39.79211  -32.59619 1.000 112.04024 ? 257 GLU   A OE1 1 
ATOM   2119 O OE2 . GLU   A 1 260 ? 11.52096 37.76817  -33.36432 1.000 124.99459 ? 257 GLU   A OE2 1 
ATOM   2120 N N   . ASP   A 1 261 ? 15.33250 37.03106  -29.47392 1.000 81.88103  ? 258 ASP   A N   1 
ATOM   2121 C CA  . ASP   A 1 261 ? 16.04730 35.77206  -29.65556 1.000 79.40286  ? 258 ASP   A CA  1 
ATOM   2122 C C   . ASP   A 1 261 ? 16.30120 35.06995  -28.32781 1.000 79.42295  ? 258 ASP   A C   1 
ATOM   2123 O O   . ASP   A 1 261 ? 16.37781 33.83660  -28.28638 1.000 70.33360  ? 258 ASP   A O   1 
ATOM   2124 C CB  . ASP   A 1 261 ? 17.36561 36.01466  -30.38958 1.000 84.01301  ? 258 ASP   A CB  1 
ATOM   2125 C CG  . ASP   A 1 261 ? 17.16584 36.32065  -31.86027 1.000 86.75941  ? 258 ASP   A CG  1 
ATOM   2126 O OD1 . ASP   A 1 261 ? 16.24987 35.73196  -32.47316 1.000 94.61324  ? 258 ASP   A OD1 1 
ATOM   2127 O OD2 . ASP   A 1 261 ? 17.92580 37.14953  -32.40315 1.000 89.95794  ? 258 ASP   A OD2 1 
ATOM   2128 N N   . GLY   A 1 262 ? 16.42735 35.82932  -27.23825 1.000 82.80779  ? 259 GLY   A N   1 
ATOM   2129 C CA  . GLY   A 1 262 ? 16.64985 35.21052  -25.94213 1.000 75.97893  ? 259 GLY   A CA  1 
ATOM   2130 C C   . GLY   A 1 262 ? 15.41522 34.51295  -25.40337 1.000 72.83750  ? 259 GLY   A C   1 
ATOM   2131 O O   . GLY   A 1 262 ? 15.50000 33.39529  -24.88593 1.000 64.98640  ? 259 GLY   A O   1 
ATOM   2132 N N   . ARG   A 1 263 ? 14.25191 35.16194  -25.51174 1.000 76.77831  ? 260 ARG   A N   1 
ATOM   2133 C CA  . ARG   A 1 263 ? 13.01364 34.53901  -25.05482 1.000 76.24161  ? 260 ARG   A CA  1 
ATOM   2134 C C   . ARG   A 1 263 ? 12.68158 33.29271  -25.86321 1.000 75.98164  ? 260 ARG   A C   1 
ATOM   2135 O O   . ARG   A 1 263 ? 12.12754 32.32957  -25.31984 1.000 77.42317  ? 260 ARG   A O   1 
ATOM   2136 C CB  . ARG   A 1 263 ? 11.85778 35.53522  -25.13495 1.000 86.39868  ? 260 ARG   A CB  1 
ATOM   2137 C CG  . ARG   A 1 263 ? 12.06423 36.81226  -24.34258 1.000 86.76755  ? 260 ARG   A CG  1 
ATOM   2138 C CD  . ARG   A 1 263 ? 10.80296 37.66074  -24.35982 1.000 95.35355  ? 260 ARG   A CD  1 
ATOM   2139 N NE  . ARG   A 1 263 ? 10.17585 37.67703  -25.67704 1.000 98.60742  ? 260 ARG   A NE  1 
ATOM   2140 C CZ  . ARG   A 1 263 ? 10.39683 38.59923  -26.60417 1.000 99.87864  ? 260 ARG   A CZ  1 
ATOM   2141 N NH1 . ARG   A 1 263 ? 11.22118 39.61137  -26.38946 1.000 101.44694 ? 260 ARG   A NH1 1 
ATOM   2142 N NH2 . ARG   A 1 263 ? 9.77519  38.50314  -27.77663 1.000 99.75781  ? 260 ARG   A NH2 1 
ATOM   2143 N N   . SER   A 1 264 ? 13.00582 33.29354  -27.15805 1.000 73.16302  ? 261 SER   A N   1 
ATOM   2144 C CA  . SER   A 1 264 ? 12.73302 32.12877  -27.99330 1.000 73.93077  ? 261 SER   A CA  1 
ATOM   2145 C C   . SER   A 1 264 ? 13.56821 30.93308  -27.55626 1.000 69.62096  ? 261 SER   A C   1 
ATOM   2146 O O   . SER   A 1 264 ? 13.04765 29.82177  -27.40506 1.000 67.59825  ? 261 SER   A O   1 
ATOM   2147 C CB  . SER   A 1 264 ? 12.99818 32.46073  -29.46149 1.000 68.66117  ? 261 SER   A CB  1 
ATOM   2148 O OG  . SER   A 1 264 ? 12.91431 31.29705  -30.26604 1.000 72.78690  ? 261 SER   A OG  1 
ATOM   2149 N N   . LEU   A 1 265 ? 14.87024 31.14387  -27.34854 1.000 67.03923  ? 262 LEU   A N   1 
ATOM   2150 C CA  . LEU   A 1 265 ? 15.73697 30.05100  -26.92108 1.000 58.55047  ? 262 LEU   A CA  1 
ATOM   2151 C C   . LEU   A 1 265 ? 15.33570 29.53334  -25.54623 1.000 65.70117  ? 262 LEU   A C   1 
ATOM   2152 O O   . LEU   A 1 265 ? 15.30325 28.31857  -25.31936 1.000 57.96177  ? 262 LEU   A O   1 
ATOM   2153 C CB  . LEU   A 1 265 ? 17.19536 30.50789  -26.91760 1.000 66.36475  ? 262 LEU   A CB  1 
ATOM   2154 C CG  . LEU   A 1 265 ? 18.21243 29.49611  -26.38712 1.000 64.98968  ? 262 LEU   A CG  1 
ATOM   2155 C CD1 . LEU   A 1 265 ? 18.20383 28.23193  -27.23415 1.000 60.52095  ? 262 LEU   A CD1 1 
ATOM   2156 C CD2 . LEU   A 1 265 ? 19.60575 30.11065  -26.33553 1.000 59.77610  ? 262 LEU   A CD2 1 
ATOM   2157 N N   . LEU   A 1 266 ? 15.02294 30.44087  -24.61653 1.000 63.41167  ? 263 LEU   A N   1 
ATOM   2158 C CA  . LEU   A 1 266 ? 14.61801 30.02245  -23.27756 1.000 63.70918  ? 263 LEU   A CA  1 
ATOM   2159 C C   . LEU   A 1 266 ? 13.33114 29.20757  -23.31860 1.000 59.74583  ? 263 LEU   A C   1 
ATOM   2160 O O   . LEU   A 1 266 ? 13.18025 28.23528  -22.56937 1.000 56.96563  ? 263 LEU   A O   1 
ATOM   2161 C CB  . LEU   A 1 266 ? 14.45098 31.24335  -22.37156 1.000 58.87009  ? 263 LEU   A CB  1 
ATOM   2162 C CG  . LEU   A 1 266 ? 14.04689 30.95360  -20.92438 1.000 59.86497  ? 263 LEU   A CG  1 
ATOM   2163 C CD1 . LEU   A 1 266 ? 15.12783 30.15005  -20.21894 1.000 58.71849  ? 263 LEU   A CD1 1 
ATOM   2164 C CD2 . LEU   A 1 266 ? 13.75603 32.24395  -20.17448 1.000 57.03978  ? 263 LEU   A CD2 1 
ATOM   2165 N N   . SER   A 1 267 ? 12.39208 29.58729  -24.19006 1.000 61.50201  ? 264 SER   A N   1 
ATOM   2166 C CA  . SER   A 1 267 ? 11.15191 28.82797  -24.31798 1.000 64.38397  ? 264 SER   A CA  1 
ATOM   2167 C C   . SER   A 1 267 ? 11.42292 27.40852  -24.79817 1.000 62.48426  ? 264 SER   A C   1 
ATOM   2168 O O   . SER   A 1 267 ? 10.82999 26.44883  -24.29079 1.000 66.02621  ? 264 SER   A O   1 
ATOM   2169 C CB  . SER   A 1 267 ? 10.19388 29.54075  -25.27259 1.000 65.18123  ? 264 SER   A CB  1 
ATOM   2170 O OG  . SER   A 1 267 ? 9.85065  30.82656  -24.78902 1.000 84.43380  ? 264 SER   A OG  1 
ATOM   2171 N N   . GLN   A 1 268 ? 12.32700 27.25465  -25.76855 1.000 56.08451  ? 265 GLN   A N   1 
ATOM   2172 C CA  . GLN   A 1 268 ? 12.61984 25.92969  -26.30192 1.000 58.77804  ? 265 GLN   A CA  1 
ATOM   2173 C C   . GLN   A 1 268 ? 13.41031 25.08538  -25.31155 1.000 54.42820  ? 265 GLN   A C   1 
ATOM   2174 O O   . GLN   A 1 268 ? 13.32670 23.85269  -25.34903 1.000 57.95605  ? 265 GLN   A O   1 
ATOM   2175 C CB  . GLN   A 1 268 ? 13.37195 26.05544  -27.62642 1.000 58.98100  ? 265 GLN   A CB  1 
ATOM   2176 C CG  . GLN   A 1 268 ? 12.63340 26.88831  -28.66153 1.000 57.68733  ? 265 GLN   A CG  1 
ATOM   2177 C CD  . GLN   A 1 268 ? 13.38892 27.01210  -29.96924 1.000 63.83327  ? 265 GLN   A CD  1 
ATOM   2178 O OE1 . GLN   A 1 268 ? 13.53556 28.10684  -30.51199 1.000 72.89339  ? 265 GLN   A OE1 1 
ATOM   2179 N NE2 . GLN   A 1 268 ? 13.86180 25.88640  -30.48952 1.000 64.79782  ? 265 GLN   A NE2 1 
ATOM   2180 N N   . MET   A 1 269 ? 14.18001 25.72104  -24.42513 1.000 57.89998  ? 266 MET   A N   1 
ATOM   2181 C CA  . MET   A 1 269 ? 14.86410 24.98839  -23.36708 1.000 58.09422  ? 266 MET   A CA  1 
ATOM   2182 C C   . MET   A 1 269 ? 13.93402 24.62500  -22.21809 1.000 58.19563  ? 266 MET   A C   1 
ATOM   2183 O O   . MET   A 1 269 ? 14.25684 23.72209  -21.43826 1.000 56.14410  ? 266 MET   A O   1 
ATOM   2184 C CB  . MET   A 1 269 ? 16.04391 25.80346  -22.83138 1.000 56.99918  ? 266 MET   A CB  1 
ATOM   2185 C CG  . MET   A 1 269 ? 17.08366 26.14896  -23.88054 1.000 52.67002  ? 266 MET   A CG  1 
ATOM   2186 S SD  . MET   A 1 269 ? 18.42051 27.17221  -23.23187 1.000 60.91264  ? 266 MET   A SD  1 
ATOM   2187 C CE  . MET   A 1 269 ? 19.33266 25.96985  -22.27077 1.000 47.23190  ? 266 MET   A CE  1 
ATOM   2188 N N   . LEU   A 1 270 ? 12.79260 25.30522  -22.09797 1.000 53.91434  ? 267 LEU   A N   1 
ATOM   2189 C CA  . LEU   A 1 270 ? 11.81504 25.03773  -21.05131 1.000 47.85354  ? 267 LEU   A CA  1 
ATOM   2190 C C   . LEU   A 1 270 ? 10.52911 24.42997  -21.60387 1.000 55.11390  ? 267 LEU   A C   1 
ATOM   2191 O O   . LEU   A 1 270 ? 9.46969  24.55270  -20.98056 1.000 52.75342  ? 267 LEU   A O   1 
ATOM   2192 C CB  . LEU   A 1 270 ? 11.51261 26.31907  -20.27308 1.000 51.34619  ? 267 LEU   A CB  1 
ATOM   2193 C CG  . LEU   A 1 270 ? 12.68902 26.91910  -19.49930 1.000 57.25876  ? 267 LEU   A CG  1 
ATOM   2194 C CD1 . LEU   A 1 270 ? 12.24986 28.15444  -18.72862 1.000 51.93179  ? 267 LEU   A CD1 1 
ATOM   2195 C CD2 . LEU   A 1 270 ? 13.29261 25.88394  -18.56213 1.000 50.73674  ? 267 LEU   A CD2 1 
ATOM   2196 N N   . HIS   A 1 271 ? 10.60098 23.78267  -22.76490 1.000 58.87784  ? 268 HIS   A N   1 
ATOM   2197 C CA  . HIS   A 1 271 ? 9.44261  23.08565  -23.30440 1.000 58.72128  ? 268 HIS   A CA  1 
ATOM   2198 C C   . HIS   A 1 271 ? 9.05190  21.93711  -22.38261 1.000 64.52696  ? 268 HIS   A C   1 
ATOM   2199 O O   . HIS   A 1 271 ? 9.90912  21.21970  -21.86034 1.000 57.43612  ? 268 HIS   A O   1 
ATOM   2200 C CB  . HIS   A 1 271 ? 9.75302  22.56070  -24.70738 1.000 60.15738  ? 268 HIS   A CB  1 
ATOM   2201 C CG  . HIS   A 1 271 ? 8.53838  22.30408  -25.54468 1.000 67.17312  ? 268 HIS   A CG  1 
ATOM   2202 N ND1 . HIS   A 1 271 ? 7.53939  21.43382  -25.16374 1.000 67.81975  ? 268 HIS   A ND1 1 
ATOM   2203 C CD2 . HIS   A 1 271 ? 8.16937  22.79517  -26.75168 1.000 67.83647  ? 268 HIS   A CD2 1 
ATOM   2204 C CE1 . HIS   A 1 271 ? 6.60386  21.40586  -26.09604 1.000 81.91340  ? 268 HIS   A CE1 1 
ATOM   2205 N NE2 . HIS   A 1 271 ? 6.96209  22.22268  -27.07049 1.000 85.11928  ? 268 HIS   A NE2 1 
ATOM   2206 N N   . TYR   A 1 272 ? 7.74480  21.77034  -22.17388 1.000 56.85053  ? 269 TYR   A N   1 
ATOM   2207 C CA  . TYR   A 1 272 ? 7.26953  20.70249  -21.29875 1.000 60.04311  ? 269 TYR   A CA  1 
ATOM   2208 C C   . TYR   A 1 272 ? 7.62065  19.33009  -21.86125 1.000 61.90508  ? 269 TYR   A C   1 
ATOM   2209 O O   . TYR   A 1 272 ? 8.16371  18.47545  -21.15139 1.000 60.06565  ? 269 TYR   A O   1 
ATOM   2210 C CB  . TYR   A 1 272 ? 5.76014  20.82497  -21.08537 1.000 57.14772  ? 269 TYR   A CB  1 
ATOM   2211 C CG  . TYR   A 1 272 ? 5.36557  21.77286  -19.97643 1.000 58.92463  ? 269 TYR   A CG  1 
ATOM   2212 C CD1 . TYR   A 1 272 ? 5.76744  21.54519  -18.66582 1.000 63.31514  ? 269 TYR   A CD1 1 
ATOM   2213 C CD2 . TYR   A 1 272 ? 4.57625  22.88446  -20.23562 1.000 63.43670  ? 269 TYR   A CD2 1 
ATOM   2214 C CE1 . TYR   A 1 272 ? 5.40304  22.40621  -17.64507 1.000 59.55225  ? 269 TYR   A CE1 1 
ATOM   2215 C CE2 . TYR   A 1 272 ? 4.20519  23.75060  -19.22323 1.000 58.56332  ? 269 TYR   A CE2 1 
ATOM   2216 C CZ  . TYR   A 1 272 ? 4.62071  23.50698  -17.92946 1.000 68.96291  ? 269 TYR   A CZ  1 
ATOM   2217 O OH  . TYR   A 1 272 ? 4.25310  24.36692  -16.91799 1.000 64.32323  ? 269 TYR   A OH  1 
ATOM   2218 N N   . ASP   A 1 273 ? 7.31433  19.10214  -23.13081 1.000 56.48912  ? 270 ASP   A N   1 
ATOM   2219 C CA  . ASP   A 1 273 ? 7.56921  17.81046  -23.75872 1.000 62.23159  ? 270 ASP   A CA  1 
ATOM   2220 C C   . ASP   A 1 273 ? 9.07058  17.57805  -23.86634 1.000 61.89674  ? 270 ASP   A C   1 
ATOM   2221 O O   . ASP   A 1 273 ? 9.76169  18.35936  -24.53343 1.000 57.32191  ? 270 ASP   A O   1 
ATOM   2222 C CB  . ASP   A 1 273 ? 6.91774  17.76088  -25.14141 1.000 64.71062  ? 270 ASP   A CB  1 
ATOM   2223 C CG  . ASP   A 1 273 ? 6.84841  16.35252  -25.71329 1.000 66.81227  ? 270 ASP   A CG  1 
ATOM   2224 O OD1 . ASP   A 1 273 ? 7.67878  15.49861  -25.33549 1.000 63.67879  ? 270 ASP   A OD1 1 
ATOM   2225 O OD2 . ASP   A 1 273 ? 5.95904  16.10210  -26.55293 1.000 72.35604  ? 270 ASP   A OD2 1 
ATOM   2226 N N   . PRO   A 1 274 ? 9.61798  16.53730  -23.23380 1.000 61.35456  ? 271 PRO   A N   1 
ATOM   2227 C CA  . PRO   A 1 274 ? 11.05394 16.26440  -23.39727 1.000 61.17107  ? 271 PRO   A CA  1 
ATOM   2228 C C   . PRO   A 1 274 ? 11.43462 15.91579  -24.82350 1.000 63.79192  ? 271 PRO   A C   1 
ATOM   2229 O O   . PRO   A 1 274 ? 12.59340 16.11116  -25.20983 1.000 60.85746  ? 271 PRO   A O   1 
ATOM   2230 C CB  . PRO   A 1 274 ? 11.29965 15.08610  -22.44230 1.000 57.48774  ? 271 PRO   A CB  1 
ATOM   2231 C CG  . PRO   A 1 274 ? 10.14713 15.10463  -21.49530 1.000 59.77604  ? 271 PRO   A CG  1 
ATOM   2232 C CD  . PRO   A 1 274 ? 8.98438  15.60071  -22.29361 1.000 57.91038  ? 271 PRO   A CD  1 
ATOM   2233 N N   . ASN   A 1 275 ? 10.49366 15.40449  -25.62189 1.000 64.98276  ? 272 ASN   A N   1 
ATOM   2234 C CA  . ASN   A 1 275 ? 10.80260 15.08578  -27.01144 1.000 65.04232  ? 272 ASN   A CA  1 
ATOM   2235 C C   . ASN   A 1 275 ? 10.89664 16.34329  -27.86662 1.000 63.92521  ? 272 ASN   A C   1 
ATOM   2236 O O   . ASN   A 1 275 ? 11.59908 16.34852  -28.88367 1.000 70.42557  ? 272 ASN   A O   1 
ATOM   2237 C CB  . ASN   A 1 275 ? 9.75097  14.12930  -27.57554 1.000 66.01160  ? 272 ASN   A CB  1 
ATOM   2238 C CG  . ASN   A 1 275 ? 9.62331  12.85838  -26.75754 1.000 80.10833  ? 272 ASN   A CG  1 
ATOM   2239 O OD1 . ASN   A 1 275 ? 10.61914 12.30239  -26.29524 1.000 79.12484  ? 272 ASN   A OD1 1 
ATOM   2240 N ND2 . ASN   A 1 275 ? 8.39254  12.39796  -26.56567 1.000 83.10014  ? 272 ASN   A ND2 1 
ATOM   2241 N N   . LYS   A 1 276 ? 10.20648 17.41387  -27.47149 1.000 62.57051  ? 273 LYS   A N   1 
ATOM   2242 C CA  . LYS   A 1 276 ? 10.23907 18.67375  -28.20151 1.000 61.30685  ? 273 LYS   A CA  1 
ATOM   2243 C C   . LYS   A 1 276 ? 11.25442 19.66248  -27.64947 1.000 63.33482  ? 273 LYS   A C   1 
ATOM   2244 O O   . LYS   A 1 276 ? 11.59707 20.62575  -28.34487 1.000 61.99958  ? 273 LYS   A O   1 
ATOM   2245 C CB  . LYS   A 1 276 ? 8.85380  19.33031  -28.18788 1.000 58.91135  ? 273 LYS   A CB  1 
ATOM   2246 C CG  . LYS   A 1 276 ? 7.76885  18.51944  -28.87246 1.000 74.80372  ? 273 LYS   A CG  1 
ATOM   2247 C CD  . LYS   A 1 276 ? 7.97270  18.47583  -30.37815 1.000 74.68129  ? 273 LYS   A CD  1 
ATOM   2248 C CE  . LYS   A 1 276 ? 6.77023  17.85644  -31.07222 1.000 78.82784  ? 273 LYS   A CE  1 
ATOM   2249 N NZ  . LYS   A 1 276 ? 6.88611  17.91739  -32.55527 1.000 89.20058  ? 273 LYS   A NZ  1 
ATOM   2250 N N   . ARG   A 1 277 ? 11.73036 19.45252  -26.42394 1.000 56.81464  ? 274 ARG   A N   1 
ATOM   2251 C CA  . ARG   A 1 277 ? 12.69451 20.36265  -25.82245 1.000 56.64539  ? 274 ARG   A CA  1 
ATOM   2252 C C   . ARG   A 1 277 ? 13.96123 20.41384  -26.66534 1.000 57.65366  ? 274 ARG   A C   1 
ATOM   2253 O O   . ARG   A 1 277 ? 14.47465 19.37882  -27.10031 1.000 56.32148  ? 274 ARG   A O   1 
ATOM   2254 C CB  . ARG   A 1 277 ? 13.01410 19.91392  -24.39717 1.000 54.32928  ? 274 ARG   A CB  1 
ATOM   2255 C CG  . ARG   A 1 277 ? 13.64469 20.98044  -23.51758 1.000 50.00929  ? 274 ARG   A CG  1 
ATOM   2256 C CD  . ARG   A 1 277 ? 13.72660 20.48573  -22.08562 1.000 54.16602  ? 274 ARG   A CD  1 
ATOM   2257 N NE  . ARG   A 1 277 ? 12.41285 20.10190  -21.58193 1.000 54.66202  ? 274 ARG   A NE  1 
ATOM   2258 C CZ  . ARG   A 1 277 ? 12.21047 19.24254  -20.59297 1.000 54.43492  ? 274 ARG   A CZ  1 
ATOM   2259 N NH1 . ARG   A 1 277 ? 13.21885 18.63723  -19.98690 1.000 50.23675  ? 274 ARG   A NH1 1 
ATOM   2260 N NH2 . ARG   A 1 277 ? 10.96482 18.97778  -20.20833 1.000 50.10472  ? 274 ARG   A NH2 1 
ATOM   2261 N N   . ILE   A 1 278 ? 14.45971 21.62960  -26.89872 1.000 54.01690  ? 275 ILE   A N   1 
ATOM   2262 C CA  . ILE   A 1 278 ? 15.58582 21.81016  -27.80356 1.000 54.79028  ? 275 ILE   A CA  1 
ATOM   2263 C C   . ILE   A 1 278 ? 16.81033 21.08360  -27.26411 1.000 58.43845  ? 275 ILE   A C   1 
ATOM   2264 O O   . ILE   A 1 278 ? 17.01799 20.97956  -26.04773 1.000 52.51945  ? 275 ILE   A O   1 
ATOM   2265 C CB  . ILE   A 1 278 ? 15.85916 23.30907  -28.01754 1.000 60.78561  ? 275 ILE   A CB  1 
ATOM   2266 C CG1 . ILE   A 1 278 ? 16.83780 23.52093  -29.17393 1.000 58.83721  ? 275 ILE   A CG1 1 
ATOM   2267 C CG2 . ILE   A 1 278 ? 16.38889 23.95447  -26.74403 1.000 57.41669  ? 275 ILE   A CG2 1 
ATOM   2268 C CD1 . ILE   A 1 278 ? 17.00188 24.97166  -29.57146 1.000 55.81773  ? 275 ILE   A CD1 1 
ATOM   2269 N N   . SER   A 1 279 ? 17.61581 20.54901  -28.17580 1.000 60.12122  ? 276 SER   A N   1 
ATOM   2270 C CA  . SER   A 1 279 ? 18.83483 19.86408  -27.78659 1.000 61.80349  ? 276 SER   A CA  1 
ATOM   2271 C C   . SER   A 1 279 ? 19.97263 20.86606  -27.60821 1.000 58.55823  ? 276 SER   A C   1 
ATOM   2272 O O   . SER   A 1 279 ? 19.88404 22.02939  -28.01011 1.000 56.43319  ? 276 SER   A O   1 
ATOM   2273 C CB  . SER   A 1 279 ? 19.20890 18.81172  -28.82579 1.000 59.22797  ? 276 SER   A CB  1 
ATOM   2274 O OG  . SER   A 1 279 ? 19.51636 19.41141  -30.07176 1.000 60.89403  ? 276 SER   A OG  1 
ATOM   2275 N N   . ALA   A 1 280 ? 21.05852 20.39707  -26.98909 1.000 50.60674  ? 277 ALA   A N   1 
ATOM   2276 C CA  . ALA   A 1 280 ? 22.22195 21.25573  -26.79468 1.000 59.86487  ? 277 ALA   A CA  1 
ATOM   2277 C C   . ALA   A 1 280 ? 22.85772 21.62995  -28.12714 1.000 63.12246  ? 277 ALA   A C   1 
ATOM   2278 O O   . ALA   A 1 280 ? 23.25972 22.78086  -28.33050 1.000 59.97541  ? 277 ALA   A O   1 
ATOM   2279 C CB  . ALA   A 1 280 ? 23.23881 20.56593  -25.88492 1.000 54.46442  ? 277 ALA   A CB  1 
ATOM   2280 N N   . LYS   A 1 281 ? 22.94323 20.67361  -29.05392 1.000 64.12394  ? 278 LYS   A N   1 
ATOM   2281 C CA  . LYS   A 1 281 ? 23.52429 20.95905  -30.36118 1.000 63.53451  ? 278 LYS   A CA  1 
ATOM   2282 C C   . LYS   A 1 281 ? 22.66626 21.94797  -31.14162 1.000 66.18685  ? 278 LYS   A C   1 
ATOM   2283 O O   . LYS   A 1 281 ? 23.19118 22.86803  -31.77958 1.000 59.91757  ? 278 LYS   A O   1 
ATOM   2284 C CB  . LYS   A 1 281 ? 23.70104 19.65869  -31.14533 1.000 73.10540  ? 278 LYS   A CB  1 
ATOM   2285 C CG  . LYS   A 1 281 ? 24.38287 19.83541  -32.48749 1.000 70.56365  ? 278 LYS   A CG  1 
ATOM   2286 C CD  . LYS   A 1 281 ? 24.36195 18.54101  -33.28074 1.000 86.91911  ? 278 LYS   A CD  1 
ATOM   2287 C CE  . LYS   A 1 281 ? 25.12559 18.68308  -34.58628 1.000 95.69665  ? 278 LYS   A CE  1 
ATOM   2288 N NZ  . LYS   A 1 281 ? 26.58514 18.85988  -34.35607 1.000 97.23236  ? 278 LYS   A NZ  1 
ATOM   2289 N N   . ALA   A 1 282 ? 21.34195 21.77317  -31.10343 1.000 60.82146  ? 279 ALA   A N   1 
ATOM   2290 C CA  . ALA   A 1 282 ? 20.45257 22.68969  -31.80736 1.000 62.41068  ? 279 ALA   A CA  1 
ATOM   2291 C C   . ALA   A 1 282 ? 20.43371 24.06469  -31.15738 1.000 61.31436  ? 279 ALA   A C   1 
ATOM   2292 O O   . ALA   A 1 282 ? 20.27863 25.07553  -31.85366 1.000 65.68550  ? 279 ALA   A O   1 
ATOM   2293 C CB  . ALA   A 1 282 ? 19.03791 22.11285  -31.86535 1.000 54.32842  ? 279 ALA   A CB  1 
ATOM   2294 N N   . ALA   A 1 283 ? 20.58590 24.12452  -29.83289 1.000 61.74429  ? 280 ALA   A N   1 
ATOM   2295 C CA  . ALA   A 1 283 ? 20.60841 25.41531  -29.15324 1.000 68.35756  ? 280 ALA   A CA  1 
ATOM   2296 C C   . ALA   A 1 283 ? 21.82602 26.23341  -29.56245 1.000 65.12421  ? 280 ALA   A C   1 
ATOM   2297 O O   . ALA   A 1 283 ? 21.76150 27.46592  -29.62592 1.000 63.67163  ? 280 ALA   A O   1 
ATOM   2298 C CB  . ALA   A 1 283 ? 20.58641 25.21381  -27.63955 1.000 61.51362  ? 280 ALA   A CB  1 
ATOM   2299 N N   . LEU   A 1 284 ? 22.95004 25.56279  -29.83362 1.000 66.23080  ? 281 LEU   A N   1 
ATOM   2300 C CA  . LEU   A 1 284 ? 24.14054 26.25446  -30.31530 1.000 62.59894  ? 281 LEU   A CA  1 
ATOM   2301 C C   . LEU   A 1 284 ? 23.89383 26.93101  -31.65737 1.000 70.36042  ? 281 LEU   A C   1 
ATOM   2302 O O   . LEU   A 1 284 ? 24.52838 27.94567  -31.96348 1.000 68.74739  ? 281 LEU   A O   1 
ATOM   2303 C CB  . LEU   A 1 284 ? 25.30581 25.26801  -30.41607 1.000 69.22849  ? 281 LEU   A CB  1 
ATOM   2304 C CG  . LEU   A 1 284 ? 25.88087 24.74765  -29.09691 1.000 66.39682  ? 281 LEU   A CG  1 
ATOM   2305 C CD1 . LEU   A 1 284 ? 26.89853 23.64952  -29.35223 1.000 61.51743  ? 281 LEU   A CD1 1 
ATOM   2306 C CD2 . LEU   A 1 284 ? 26.51123 25.88763  -28.31593 1.000 61.59015  ? 281 LEU   A CD2 1 
ATOM   2307 N N   . ALA   A 1 285 ? 22.98508 26.39129  -32.46687 1.000 72.31366  ? 282 ALA   A N   1 
ATOM   2308 C CA  . ALA   A 1 285 ? 22.65606 26.96729  -33.76285 1.000 66.04898  ? 282 ALA   A CA  1 
ATOM   2309 C C   . ALA   A 1 285 ? 21.51827 27.97738  -33.69322 1.000 68.52145  ? 282 ALA   A C   1 
ATOM   2310 O O   . ALA   A 1 285 ? 21.09442 28.48163  -34.73829 1.000 72.51329  ? 282 ALA   A O   1 
ATOM   2311 C CB  . ALA   A 1 285 ? 22.29824 25.85765  -34.75615 1.000 67.74968  ? 282 ALA   A CB  1 
ATOM   2312 N N   . HIS   A 1 286 ? 21.01750 28.28342  -32.49859 1.000 69.22155  ? 283 HIS   A N   1 
ATOM   2313 C CA  . HIS   A 1 286 ? 19.92616 29.23371  -32.36711 1.000 74.59436  ? 283 HIS   A CA  1 
ATOM   2314 C C   . HIS   A 1 286 ? 20.39600 30.63674  -32.75440 1.000 72.35445  ? 283 HIS   A C   1 
ATOM   2315 O O   . HIS   A 1 286 ? 21.55956 30.99048  -32.54391 1.000 78.04931  ? 283 HIS   A O   1 
ATOM   2316 C CB  . HIS   A 1 286 ? 19.39338 29.23450  -30.93502 1.000 69.22687  ? 283 HIS   A CB  1 
ATOM   2317 C CG  . HIS   A 1 286 ? 18.07742 29.93075  -30.77584 1.000 74.28237  ? 283 HIS   A CG  1 
ATOM   2318 N ND1 . HIS   A 1 286 ? 17.97675 31.27028  -30.46773 1.000 72.35447  ? 283 HIS   A ND1 1 
ATOM   2319 C CD2 . HIS   A 1 286 ? 16.80732 29.47379  -30.88563 1.000 78.12593  ? 283 HIS   A CD2 1 
ATOM   2320 C CE1 . HIS   A 1 286 ? 16.70195 31.60872  -30.39437 1.000 75.37479  ? 283 HIS   A CE1 1 
ATOM   2321 N NE2 . HIS   A 1 286 ? 15.97145 30.53673  -30.64290 1.000 77.84820  ? 283 HIS   A NE2 1 
ATOM   2322 N N   . PRO   A 1 287 ? 19.51149 31.45203  -33.33914 1.000 77.00732  ? 284 PRO   A N   1 
ATOM   2323 C CA  . PRO   A 1 287 ? 19.90099 32.82672  -33.70134 1.000 86.15222  ? 284 PRO   A CA  1 
ATOM   2324 C C   . PRO   A 1 287 ? 20.31188 33.69239  -32.51754 1.000 81.38782  ? 284 PRO   A C   1 
ATOM   2325 O O   . PRO   A 1 287 ? 20.74523 34.83082  -32.73307 1.000 81.70621  ? 284 PRO   A O   1 
ATOM   2326 C CB  . PRO   A 1 287 ? 18.64185 33.38114  -34.38104 1.000 86.91174  ? 284 PRO   A CB  1 
ATOM   2327 C CG  . PRO   A 1 287 ? 17.93117 32.17267  -34.89110 1.000 86.23178  ? 284 PRO   A CG  1 
ATOM   2328 C CD  . PRO   A 1 287 ? 18.19030 31.09186  -33.88366 1.000 79.10138  ? 284 PRO   A CD  1 
ATOM   2329 N N   . PHE   A 1 288 ? 20.18661 33.20391  -31.28178 1.000 77.27933  ? 285 PHE   A N   1 
ATOM   2330 C CA  . PHE   A 1 288 ? 20.67684 33.96997  -30.14211 1.000 79.72109  ? 285 PHE   A CA  1 
ATOM   2331 C C   . PHE   A 1 288 ? 22.19845 34.02727  -30.12591 1.000 77.08322  ? 285 PHE   A C   1 
ATOM   2332 O O   . PHE   A 1 288 ? 22.77590 34.98589  -29.60085 1.000 76.48217  ? 285 PHE   A O   1 
ATOM   2333 C CB  . PHE   A 1 288 ? 20.14657 33.37004  -28.83957 1.000 70.41271  ? 285 PHE   A CB  1 
ATOM   2334 C CG  . PHE   A 1 288 ? 20.51941 34.15326  -27.61182 1.000 77.95452  ? 285 PHE   A CG  1 
ATOM   2335 C CD1 . PHE   A 1 288 ? 19.96901 35.40267  -27.37873 1.000 82.22453  ? 285 PHE   A CD1 1 
ATOM   2336 C CD2 . PHE   A 1 288 ? 21.41078 33.63607  -26.68562 1.000 67.51711  ? 285 PHE   A CD2 1 
ATOM   2337 C CE1 . PHE   A 1 288 ? 20.30696 36.12750  -26.24935 1.000 75.73787  ? 285 PHE   A CE1 1 
ATOM   2338 C CE2 . PHE   A 1 288 ? 21.75172 34.35541  -25.55191 1.000 76.40773  ? 285 PHE   A CE2 1 
ATOM   2339 C CZ  . PHE   A 1 288 ? 21.19861 35.60248  -25.33422 1.000 76.33166  ? 285 PHE   A CZ  1 
ATOM   2340 N N   . PHE   A 1 289 ? 22.86024 33.02103  -30.69612 1.000 84.44378  ? 286 PHE   A N   1 
ATOM   2341 C CA  . PHE   A 1 289 ? 24.31217 32.98694  -30.79422 1.000 86.17505  ? 286 PHE   A CA  1 
ATOM   2342 C C   . PHE   A 1 289 ? 24.80953 33.27702  -32.20458 1.000 101.08845 ? 286 PHE   A C   1 
ATOM   2343 O O   . PHE   A 1 289 ? 25.97633 33.00587  -32.50509 1.000 109.24396 ? 286 PHE   A O   1 
ATOM   2344 C CB  . PHE   A 1 289 ? 24.84684 31.62927  -30.32956 1.000 79.06888  ? 286 PHE   A CB  1 
ATOM   2345 C CG  . PHE   A 1 289 ? 24.37706 31.22293  -28.96108 1.000 73.95529  ? 286 PHE   A CG  1 
ATOM   2346 C CD1 . PHE   A 1 289 ? 24.87068 31.84775  -27.82844 1.000 67.35121  ? 286 PHE   A CD1 1 
ATOM   2347 C CD2 . PHE   A 1 289 ? 23.45303 30.20340  -28.80885 1.000 62.49033  ? 286 PHE   A CD2 1 
ATOM   2348 C CE1 . PHE   A 1 289 ? 24.44164 31.47142  -26.57051 1.000 67.35425  ? 286 PHE   A CE1 1 
ATOM   2349 C CE2 . PHE   A 1 289 ? 23.02071 29.82183  -27.55561 1.000 66.67767  ? 286 PHE   A CE2 1 
ATOM   2350 C CZ  . PHE   A 1 289 ? 23.51528 30.45624  -26.43406 1.000 67.85049  ? 286 PHE   A CZ  1 
ATOM   2351 N N   . GLN   A 1 290 ? 23.95385 33.81909  -33.07643 1.000 105.53594 ? 287 GLN   A N   1 
ATOM   2352 C CA  . GLN   A 1 290 ? 24.36300 34.08489  -34.45186 1.000 112.85772 ? 287 GLN   A CA  1 
ATOM   2353 C C   . GLN   A 1 290 ? 25.48046 35.11564  -34.53242 1.000 125.30360 ? 287 GLN   A C   1 
ATOM   2354 O O   . GLN   A 1 290 ? 26.20800 35.14849  -35.53094 1.000 131.36076 ? 287 GLN   A O   1 
ATOM   2355 C CB  . GLN   A 1 290 ? 23.16441 34.55055  -35.28108 1.000 113.84692 ? 287 GLN   A CB  1 
ATOM   2356 C CG  . GLN   A 1 290 ? 22.66781 35.94445  -34.93303 1.000 117.90477 ? 287 GLN   A CG  1 
ATOM   2357 C CD  . GLN   A 1 290 ? 21.30872 36.24439  -35.53415 1.000 124.54212 ? 287 GLN   A CD  1 
ATOM   2358 O OE1 . GLN   A 1 290 ? 20.85134 35.54915  -36.44096 1.000 132.47857 ? 287 GLN   A OE1 1 
ATOM   2359 N NE2 . GLN   A 1 290 ? 20.65153 37.27993  -35.02483 1.000 121.12035 ? 287 GLN   A NE2 1 
ATOM   2360 N N   . ASP   A 1 291 ? 25.63225 35.95594  -33.50964 1.000 123.46734 ? 288 ASP   A N   1 
ATOM   2361 C CA  . ASP   A 1 291 ? 26.73034 36.90998  -33.45792 1.000 126.18554 ? 288 ASP   A CA  1 
ATOM   2362 C C   . ASP   A 1 291 ? 27.98559 36.33129  -32.82190 1.000 129.25845 ? 288 ASP   A C   1 
ATOM   2363 O O   . ASP   A 1 291 ? 29.07504 36.88067  -33.02138 1.000 135.86078 ? 288 ASP   A O   1 
ATOM   2364 C CB  . ASP   A 1 291 ? 26.30277 38.16439  -32.68942 1.000 126.96509 ? 288 ASP   A CB  1 
ATOM   2365 C CG  . ASP   A 1 291 ? 25.73494 37.84218  -31.32091 1.000 126.19986 ? 288 ASP   A CG  1 
ATOM   2366 O OD1 . ASP   A 1 291 ? 25.19528 36.72879  -31.14887 1.000 123.87077 ? 288 ASP   A OD1 1 
ATOM   2367 O OD2 . ASP   A 1 291 ? 25.82496 38.70047  -30.41821 1.000 125.85003 ? 288 ASP   A OD2 1 
ATOM   2368 N N   . VAL   A 1 292 ? 27.86000 35.24278  -32.06805 1.000 128.11013 ? 289 VAL   A N   1 
ATOM   2369 C CA  . VAL   A 1 292 ? 29.01393 34.61928  -31.42833 1.000 124.67968 ? 289 VAL   A CA  1 
ATOM   2370 C C   . VAL   A 1 292 ? 29.66094 33.58266  -32.33746 1.000 128.16673 ? 289 VAL   A C   1 
ATOM   2371 O O   . VAL   A 1 292 ? 30.88776 33.53082  -32.45383 1.000 134.53213 ? 289 VAL   A O   1 
ATOM   2372 C CB  . VAL   A 1 292 ? 28.59387 34.00273  -30.07863 1.000 116.22055 ? 289 VAL   A CB  1 
ATOM   2373 C CG1 . VAL   A 1 292 ? 29.73946 33.20685  -29.47352 1.000 104.80894 ? 289 VAL   A CG1 1 
ATOM   2374 C CG2 . VAL   A 1 292 ? 28.13893 35.09018  -29.12218 1.000 114.53312 ? 289 VAL   A CG2 1 
ATOM   2375 N N   . THR   A 1 293 ? 28.85839 32.75232  -32.99611 1.000 121.36517 ? 290 THR   A N   1 
ATOM   2376 C CA  . THR   A 1 293 ? 29.36574 31.69118  -33.84927 1.000 122.46930 ? 290 THR   A CA  1 
ATOM   2377 C C   . THR   A 1 293 ? 28.88103 31.88563  -35.27971 1.000 132.37731 ? 290 THR   A C   1 
ATOM   2378 O O   . THR   A 1 293 ? 27.88213 32.56340  -35.53764 1.000 133.01864 ? 290 THR   A O   1 
ATOM   2379 C CB  . THR   A 1 293 ? 28.93347 30.30805  -33.34082 1.000 113.26639 ? 290 THR   A CB  1 
ATOM   2380 O OG1 . THR   A 1 293 ? 29.53711 29.29017  -34.14869 1.000 116.10023 ? 290 THR   A OG1 1 
ATOM   2381 C CG2 . THR   A 1 293 ? 27.41961 30.16361  -33.40506 1.000 108.18403 ? 290 THR   A CG2 1 
ATOM   2382 N N   . LYS   A 1 294 ? 29.61459 31.28049  -36.21228 1.000 133.88143 ? 291 LYS   A N   1 
ATOM   2383 C CA  . LYS   A 1 294 ? 29.25203 31.25788  -37.61513 1.000 135.63507 ? 291 LYS   A CA  1 
ATOM   2384 C C   . LYS   A 1 294 ? 29.10368 29.81676  -38.08721 1.000 138.36623 ? 291 LYS   A C   1 
ATOM   2385 O O   . LYS   A 1 294 ? 29.87332 28.94638  -37.66544 1.000 136.32285 ? 291 LYS   A O   1 
ATOM   2386 C CB  . LYS   A 1 294 ? 30.30205 31.98055  -38.47298 1.000 142.60346 ? 291 LYS   A CB  1 
ATOM   2387 C CG  . LYS   A 1 294 ? 29.75112 33.17368  -39.23873 1.000 137.75407 ? 291 LYS   A CG  1 
ATOM   2388 C CD  . LYS   A 1 294 ? 29.05850 34.15446  -38.30489 1.000 140.64689 ? 291 LYS   A CD  1 
ATOM   2389 C CE  . LYS   A 1 294 ? 28.41625 35.29627  -39.07572 1.000 141.81664 ? 291 LYS   A CE  1 
ATOM   2390 N NZ  . LYS   A 1 294 ? 27.69611 36.23668  -38.17310 1.000 137.55737 ? 291 LYS   A NZ  1 
ATOM   2391 N N   . PRO   A 1 295 ? 28.13132 29.53192  -38.95020 1.000 143.04950 ? 292 PRO   A N   1 
ATOM   2392 C CA  . PRO   A 1 295 ? 27.86517 28.13901  -39.32191 1.000 140.85834 ? 292 PRO   A CA  1 
ATOM   2393 C C   . PRO   A 1 295 ? 28.96507 27.55762  -40.19491 1.000 143.37694 ? 292 PRO   A C   1 
ATOM   2394 O O   . PRO   A 1 295 ? 29.65389 28.26712  -40.93235 1.000 139.80212 ? 292 PRO   A O   1 
ATOM   2395 C CB  . PRO   A 1 295 ? 26.53975 28.22564  -40.08593 1.000 140.07459 ? 292 PRO   A CB  1 
ATOM   2396 C CG  . PRO   A 1 295 ? 26.53963 29.60535  -40.65792 1.000 145.22175 ? 292 PRO   A CG  1 
ATOM   2397 C CD  . PRO   A 1 295 ? 27.22369 30.47129  -39.63234 1.000 143.12449 ? 292 PRO   A CD  1 
ATOM   2398 N N   . VAL   A 1 296 ? 29.12156 26.24133  -40.09851 1.000 143.03848 ? 293 VAL   A N   1 
ATOM   2399 C CA  . VAL   A 1 296 ? 30.08211 25.50595  -40.91564 1.000 140.54947 ? 293 VAL   A CA  1 
ATOM   2400 C C   . VAL   A 1 296 ? 29.35790 24.99506  -42.15589 1.000 136.59995 ? 293 VAL   A C   1 
ATOM   2401 O O   . VAL   A 1 296 ? 28.13264 24.80762  -42.12144 1.000 141.10700 ? 293 VAL   A O   1 
ATOM   2402 C CB  . VAL   A 1 296 ? 30.72488 24.35438  -40.12430 1.000 133.38582 ? 293 VAL   A CB  1 
ATOM   2403 C CG1 . VAL   A 1 296 ? 31.26743 24.86159  -38.79978 1.000 129.28086 ? 293 VAL   A CG1 1 
ATOM   2404 C CG2 . VAL   A 1 296 ? 29.72492 23.22871  -39.89909 1.000 132.37849 ? 293 VAL   A CG2 1 
ATOM   2405 N N   . PRO   A 1 297 ? 30.05402 24.77578  -43.27102 1.000 130.80257 ? 294 PRO   A N   1 
ATOM   2406 C CA  . PRO   A 1 297 ? 29.39107 24.18876  -44.44354 1.000 130.00862 ? 294 PRO   A CA  1 
ATOM   2407 C C   . PRO   A 1 297 ? 29.00598 22.74066  -44.17513 1.000 127.52575 ? 294 PRO   A C   1 
ATOM   2408 O O   . PRO   A 1 297 ? 29.80829 21.95284  -43.66898 1.000 131.14790 ? 294 PRO   A O   1 
ATOM   2409 C CB  . PRO   A 1 297 ? 30.45024 24.30165  -45.54615 1.000 127.80218 ? 294 PRO   A CB  1 
ATOM   2410 C CG  . PRO   A 1 297 ? 31.74950 24.37188  -44.81218 1.000 125.54783 ? 294 PRO   A CG  1 
ATOM   2411 C CD  . PRO   A 1 297 ? 31.46078 25.11748  -43.54367 1.000 131.87987 ? 294 PRO   A CD  1 
ATOM   2412 N N   . HIS   A 1 298 ? 27.76735 22.39621  -44.51575 1.000 127.87333 ? 295 HIS   A N   1 
ATOM   2413 C CA  . HIS   A 1 298 ? 27.22484 21.06753  -44.26408 1.000 129.35677 ? 295 HIS   A CA  1 
ATOM   2414 C C   . HIS   A 1 298 ? 27.29256 20.23817  -45.53972 1.000 122.49976 ? 295 HIS   A C   1 
ATOM   2415 O O   . HIS   A 1 298 ? 26.71493 20.61724  -46.56432 1.000 131.04383 ? 295 HIS   A O   1 
ATOM   2416 C CB  . HIS   A 1 298 ? 25.78620 21.15324  -43.75527 1.000 136.09525 ? 295 HIS   A CB  1 
ATOM   2417 C CG  . HIS   A 1 298 ? 25.67396 21.63055  -42.34105 1.000 136.83585 ? 295 HIS   A CG  1 
ATOM   2418 N ND1 . HIS   A 1 298 ? 26.75681 21.69920  -41.49099 1.000 141.20824 ? 295 HIS   A ND1 1 
ATOM   2419 C CD2 . HIS   A 1 298 ? 24.60760 22.06268  -41.62733 1.000 141.98526 ? 295 HIS   A CD2 1 
ATOM   2420 C CE1 . HIS   A 1 298 ? 26.36257 22.15278  -40.31463 1.000 140.62324 ? 295 HIS   A CE1 1 
ATOM   2421 N NE2 . HIS   A 1 298 ? 25.06288 22.38140  -40.37092 1.000 142.27950 ? 295 HIS   A NE2 1 
ATOM   2422 N N   . LEU   A 1 299 ? 27.99616 19.11142  -45.47195 1.000 121.18843 ? 296 LEU   A N   1 
ATOM   2423 C CA  . LEU   A 1 299 ? 28.06151 18.18883  -46.59725 1.000 121.93746 ? 296 LEU   A CA  1 
ATOM   2424 C C   . LEU   A 1 299 ? 26.71117 17.50717  -46.78056 1.000 134.04078 ? 296 LEU   A C   1 
ATOM   2425 O O   . LEU   A 1 299 ? 26.20247 16.86322  -45.85700 1.000 134.31608 ? 296 LEU   A O   1 
ATOM   2426 C CB  . LEU   A 1 299 ? 29.16032 17.15532  -46.36524 1.000 110.07566 ? 296 LEU   A CB  1 
ATOM   2427 C CG  . LEU   A 1 299 ? 29.26273 16.01239  -47.37700 1.000 119.26190 ? 296 LEU   A CG  1 
ATOM   2428 C CD1 . LEU   A 1 299 ? 29.65662 16.53264  -48.75033 1.000 110.85075 ? 296 LEU   A CD1 1 
ATOM   2429 C CD2 . LEU   A 1 299 ? 30.24654 14.95728  -46.89433 1.000 107.20721 ? 296 LEU   A CD2 1 
ATOM   2430 N N   . ARG   A 1 300 ? 26.12895 17.64753  -47.96963 1.000 158.56480 ? 297 ARG   A N   1 
ATOM   2431 C CA  . ARG   A 1 300 ? 24.82785 17.04745  -48.26571 1.000 159.94993 ? 297 ARG   A CA  1 
ATOM   2432 C C   . ARG   A 1 300 ? 25.00788 15.60046  -48.73051 1.000 159.32143 ? 297 ARG   A C   1 
ATOM   2433 O O   . ARG   A 1 300 ? 24.58296 15.19684  -49.81273 1.000 157.05996 ? 297 ARG   A O   1 
ATOM   2434 C CB  . ARG   A 1 300 ? 24.08512 17.88094  -49.30433 1.000 159.49478 ? 297 ARG   A CB  1 
ATOM   2435 C CG  . ARG   A 1 300 ? 24.29457 19.38418  -49.16723 1.000 159.26973 ? 297 ARG   A CG  1 
ATOM   2436 C CD  . ARG   A 1 300 ? 23.76245 19.92763  -47.84658 1.000 167.79238 ? 297 ARG   A CD  1 
ATOM   2437 N NE  . ARG   A 1 300 ? 22.31743 20.12346  -47.86304 1.000 177.87097 ? 297 ARG   A NE  1 
ATOM   2438 C CZ  . ARG   A 1 300 ? 21.43860 19.28679  -47.32839 1.000 180.01078 ? 297 ARG   A CZ  1 
ATOM   2439 N NH1 . ARG   A 1 300 ? 21.82222 18.17520  -46.72234 1.000 174.87705 ? 297 ARG   A NH1 1 
ATOM   2440 N NH2 . ARG   A 1 300 ? 20.14206 19.57487  -47.40026 1.000 181.98854 ? 297 ARG   A NH2 1 
ATOM   2441 N N   . LEU   A 1 301 ? 25.65997 14.81758  -47.87624 1.000 141.89798 ? 298 LEU   A N   1 
ATOM   2442 C CA  . LEU   A 1 301 ? 25.96745 13.42578  -48.18317 1.000 143.82564 ? 298 LEU   A CA  1 
ATOM   2443 C C   . LEU   A 1 301 ? 26.13139 12.60697  -46.90699 1.000 145.10261 ? 298 LEU   A C   1 
ATOM   2444 O O   . LEU   A 1 301 ? 25.29981 11.75578  -46.59236 1.000 148.91445 ? 298 LEU   A O   1 
ATOM   2445 C CB  . LEU   A 1 301 ? 27.23553 13.33486  -49.03488 1.000 136.88971 ? 298 LEU   A CB  1 
ATOM   2446 C CG  . LEU   A 1 301 ? 27.77274 11.93376  -49.33285 1.000 136.23804 ? 298 LEU   A CG  1 
ATOM   2447 C CD1 . LEU   A 1 301 ? 26.74203 11.10919  -50.08763 1.000 141.56418 ? 298 LEU   A CD1 1 
ATOM   2448 C CD2 . LEU   A 1 301 ? 29.07593 12.01576  -50.11356 1.000 129.31301 ? 298 LEU   A CD2 1 
ATOM   2449 N N   . GLY   B 2 9   ? 29.76149 1.88276   -42.28240 1.000 99.05034  ? 102 GLY   B N   1 
ATOM   2450 C CA  . GLY   B 2 9   ? 28.51847 2.63106   -42.31681 1.000 107.29345 ? 102 GLY   B CA  1 
ATOM   2451 C C   . GLY   B 2 9   ? 27.93401 2.88943   -40.94170 1.000 105.41916 ? 102 GLY   B C   1 
ATOM   2452 O O   . GLY   B 2 9   ? 28.42034 2.36191   -39.94143 1.000 102.04720 ? 102 GLY   B O   1 
ATOM   2453 N N   . SER   B 2 10  ? 26.88410 3.70582   -40.89308 1.000 104.93117 ? 103 SER   B N   1 
ATOM   2454 C CA  . SER   B 2 10  ? 26.21865 4.05904   -39.64517 1.000 99.43611  ? 103 SER   B CA  1 
ATOM   2455 C C   . SER   B 2 10  ? 24.73659 3.72746   -39.74993 1.000 101.69037 ? 103 SER   B C   1 
ATOM   2456 O O   . SER   B 2 10  ? 24.04567 4.27363   -40.62782 1.000 103.66116 ? 103 SER   B O   1 
ATOM   2457 C CB  . SER   B 2 10  ? 26.41346 5.54220   -39.32320 1.000 106.65701 ? 103 SER   B CB  1 
ATOM   2458 O OG  . SER   B 2 10  ? 25.73499 5.89739   -38.13090 1.000 101.67806 ? 103 SER   B OG  1 
ATOM   2459 N N   . PRO   B 2 11  ? 24.20495 2.84913   -38.90076 1.000 99.14029  ? 104 PRO   B N   1 
ATOM   2460 C CA  . PRO   B 2 11  ? 22.78233 2.49382   -38.96540 1.000 93.72281  ? 104 PRO   B CA  1 
ATOM   2461 C C   . PRO   B 2 11  ? 21.86569 3.34215   -38.09674 1.000 94.03932  ? 104 PRO   B C   1 
ATOM   2462 O O   . PRO   B 2 11  ? 20.65725 3.08250   -38.07753 1.000 96.51785  ? 104 PRO   B O   1 
ATOM   2463 C CB  . PRO   B 2 11  ? 22.79565 1.04327   -38.46932 1.000 88.32667  ? 104 PRO   B CB  1 
ATOM   2464 C CG  . PRO   B 2 11  ? 23.88776 1.03356   -37.45364 1.000 96.79198  ? 104 PRO   B CG  1 
ATOM   2465 C CD  . PRO   B 2 11  ? 24.93930 2.00373   -37.94360 1.000 94.75631  ? 104 PRO   B CD  1 
ATOM   2466 N N   . LEU   B 2 12  ? 22.39507 4.33274   -37.38124 1.000 95.72060  ? 105 LEU   B N   1 
ATOM   2467 C CA  . LEU   B 2 12  ? 21.55598 5.15058   -36.51575 1.000 94.96251  ? 105 LEU   B CA  1 
ATOM   2468 C C   . LEU   B 2 12  ? 20.75095 6.14944   -37.34550 1.000 95.00419  ? 105 LEU   B C   1 
ATOM   2469 O O   . LEU   B 2 12  ? 21.26592 6.70781   -38.31781 1.000 99.19117  ? 105 LEU   B O   1 
ATOM   2470 C CB  . LEU   B 2 12  ? 22.40620 5.89946   -35.49154 1.000 94.92765  ? 105 LEU   B CB  1 
ATOM   2471 C CG  . LEU   B 2 12  ? 23.12418 5.06070   -34.43350 1.000 80.43683  ? 105 LEU   B CG  1 
ATOM   2472 C CD1 . LEU   B 2 12  ? 24.06242 5.93262   -33.61543 1.000 75.67749  ? 105 LEU   B CD1 1 
ATOM   2473 C CD2 . LEU   B 2 12  ? 22.11940 4.36227   -33.53151 1.000 90.27692  ? 105 LEU   B CD2 1 
ATOM   2474 N N   . PRO   B 2 13  ? 19.48916 6.39273   -36.98512 1.000 93.17276  ? 106 PRO   B N   1 
ATOM   2475 C CA  . PRO   B 2 13  ? 18.70394 7.40830   -37.69772 1.000 96.66860  ? 106 PRO   B CA  1 
ATOM   2476 C C   . PRO   B 2 13  ? 19.11971 8.81659   -37.30788 1.000 96.74019  ? 106 PRO   B C   1 
ATOM   2477 O O   . PRO   B 2 13  ? 20.07779 8.99642   -36.54937 1.000 100.31334 ? 106 PRO   B O   1 
ATOM   2478 C CB  . PRO   B 2 13  ? 17.26716 7.10387   -37.26113 1.000 108.60835 ? 106 PRO   B CB  1 
ATOM   2479 C CG  . PRO   B 2 13  ? 17.42574 6.53253   -35.89408 1.000 106.41271 ? 106 PRO   B CG  1 
ATOM   2480 C CD  . PRO   B 2 13  ? 18.70746 5.73515   -35.92313 1.000 100.58568 ? 106 PRO   B CD  1 
ATOM   2481 N N   . VAL   B 2 14  ? 18.40711 9.82379   -37.81727 1.000 100.85551 ? 107 VAL   B N   1 
ATOM   2482 C CA  . VAL   B 2 14  ? 18.70529 11.19981  -37.44228 1.000 96.80591  ? 107 VAL   B CA  1 
ATOM   2483 C C   . VAL   B 2 14  ? 18.41608 11.39247  -35.96130 1.000 95.87894  ? 107 VAL   B C   1 
ATOM   2484 O O   . VAL   B 2 14  ? 17.32118 11.08251  -35.47403 1.000 92.25168  ? 107 VAL   B O   1 
ATOM   2485 C CB  . VAL   B 2 14  ? 17.90784 12.18164  -38.31410 1.000 93.34697  ? 107 VAL   B CB  1 
ATOM   2486 C CG1 . VAL   B 2 14  ? 18.52274 12.27010  -39.70334 1.000 95.44019  ? 107 VAL   B CG1 1 
ATOM   2487 C CG2 . VAL   B 2 14  ? 16.44920 11.75601  -38.40584 1.000 103.60226 ? 107 VAL   B CG2 1 
ATOM   2488 N N   . LEU   B 2 15  ? 19.40898 11.89045  -35.23285 1.000 90.40594  ? 108 LEU   B N   1 
ATOM   2489 C CA  . LEU   B 2 15  ? 19.29993 12.09593  -33.79627 1.000 94.44112  ? 108 LEU   B CA  1 
ATOM   2490 C C   . LEU   B 2 15  ? 19.03482 13.56784  -33.51384 1.000 92.21511  ? 108 LEU   B C   1 
ATOM   2491 O O   . LEU   B 2 15  ? 19.76070 14.44009  -34.00230 1.000 97.74286  ? 108 LEU   B O   1 
ATOM   2492 C CB  . LEU   B 2 15  ? 20.57208 11.63547  -33.08323 1.000 92.32053  ? 108 LEU   B CB  1 
ATOM   2493 C CG  . LEU   B 2 15  ? 21.01687 10.20021  -33.37232 1.000 96.59230  ? 108 LEU   B CG  1 
ATOM   2494 C CD1 . LEU   B 2 15  ? 22.27005 9.85509   -32.58279 1.000 86.02202  ? 108 LEU   B CD1 1 
ATOM   2495 C CD2 . LEU   B 2 15  ? 19.89733 9.21921   -33.06592 1.000 94.36452  ? 108 LEU   B CD2 1 
ATOM   2496 N N   . SER   B 2 16  ? 17.98982 13.83963  -32.73028 1.000 89.80996  ? 109 SER   B N   1 
ATOM   2497 C CA  . SER   B 2 16  ? 17.66069 15.22159  -32.40314 1.000 95.32212  ? 109 SER   B CA  1 
ATOM   2498 C C   . SER   B 2 16  ? 18.65429 15.81922  -31.41664 1.000 97.42910  ? 109 SER   B C   1 
ATOM   2499 O O   . SER   B 2 16  ? 18.84557 17.04007  -31.39836 1.000 98.62466  ? 109 SER   B O   1 
ATOM   2500 C CB  . SER   B 2 16  ? 16.24317 15.30623  -31.83761 1.000 96.59436  ? 109 SER   B CB  1 
ATOM   2501 O OG  . SER   B 2 16  ? 16.14555 14.61403  -30.60496 1.000 100.99183 ? 109 SER   B OG  1 
ATOM   2502 N N   . TRP   B 2 17  ? 19.30088 14.98449  -30.60343 1.000 92.44315  ? 110 TRP   B N   1 
ATOM   2503 C CA  . TRP   B 2 17  ? 20.15759 15.46641  -29.52883 1.000 86.03927  ? 110 TRP   B CA  1 
ATOM   2504 C C   . TRP   B 2 17  ? 21.61975 15.61684  -29.93069 1.000 85.82676  ? 110 TRP   B C   1 
ATOM   2505 O O   . TRP   B 2 17  ? 22.38210 16.24622  -29.18921 1.000 92.07896  ? 110 TRP   B O   1 
ATOM   2506 C CB  . TRP   B 2 17  ? 20.04790 14.54148  -28.30782 1.000 81.29884  ? 110 TRP   B CB  1 
ATOM   2507 C CG  . TRP   B 2 17  ? 19.88666 13.08306  -28.63330 1.000 88.05070  ? 110 TRP   B CG  1 
ATOM   2508 C CD1 . TRP   B 2 17  ? 18.74888 12.45696  -29.05782 1.000 91.71120  ? 110 TRP   B CD1 1 
ATOM   2509 C CD2 . TRP   B 2 17  ? 20.88884 12.06357  -28.52996 1.000 85.48408  ? 110 TRP   B CD2 1 
ATOM   2510 N NE1 . TRP   B 2 17  ? 18.98564 11.11598  -29.23981 1.000 83.88845  ? 110 TRP   B NE1 1 
ATOM   2511 C CE2 . TRP   B 2 17  ? 20.29103 10.84852  -28.92095 1.000 83.11041  ? 110 TRP   B CE2 1 
ATOM   2512 C CE3 . TRP   B 2 17  ? 22.23493 12.06133  -28.15139 1.000 76.90422  ? 110 TRP   B CE3 1 
ATOM   2513 C CZ2 . TRP   B 2 17  ? 20.99294 9.64441   -28.94403 1.000 77.39381  ? 110 TRP   B CZ2 1 
ATOM   2514 C CZ3 . TRP   B 2 17  ? 22.92988 10.86400  -28.17483 1.000 75.10373  ? 110 TRP   B CZ3 1 
ATOM   2515 C CH2 . TRP   B 2 17  ? 22.30801 9.67323   -28.56821 1.000 72.84581  ? 110 TRP   B CH2 1 
ATOM   2516 N N   . ALA   B 2 18  ? 22.02796 15.07503  -31.07445 1.000 89.94124  ? 111 ALA   B N   1 
ATOM   2517 C CA  . ALA   B 2 18  ? 23.40309 15.21253  -31.53996 1.000 93.16796  ? 111 ALA   B CA  1 
ATOM   2518 C C   . ALA   B 2 18  ? 23.46465 14.77101  -32.99448 1.000 101.37456 ? 111 ALA   B C   1 
ATOM   2519 O O   . ALA   B 2 18  ? 22.52451 14.17148  -33.52229 1.000 100.76366 ? 111 ALA   B O   1 
ATOM   2520 C CB  . ALA   B 2 18  ? 24.37800 14.39812  -30.68479 1.000 92.75666  ? 111 ALA   B CB  1 
ATOM   2521 N N   . ASN   B 2 19  ? 24.58745 15.08157  -33.63798 1.000 108.98367 ? 112 ASN   B N   1 
ATOM   2522 C CA  . ASN   B 2 19  ? 24.82924 14.60279  -34.99182 1.000 114.30192 ? 112 ASN   B CA  1 
ATOM   2523 C C   . ASN   B 2 19  ? 24.89757 13.08176  -34.98765 1.000 116.34346 ? 112 ASN   B C   1 
ATOM   2524 O O   . ASN   B 2 19  ? 25.69122 12.49059  -34.24868 1.000 113.62979 ? 112 ASN   B O   1 
ATOM   2525 C CB  . ASN   B 2 19  ? 26.12347 15.20296  -35.54083 1.000 118.29688 ? 112 ASN   B CB  1 
ATOM   2526 C CG  . ASN   B 2 19  ? 26.38330 14.81242  -36.98368 1.000 130.24769 ? 112 ASN   B CG  1 
ATOM   2527 O OD1 . ASN   B 2 19  ? 25.45971 14.47307  -37.72302 1.000 135.33479 ? 112 ASN   B OD1 1 
ATOM   2528 N ND2 . ASN   B 2 19  ? 27.64672 14.85958  -37.39162 1.000 132.94295 ? 112 ASN   B ND2 1 
ATOM   2529 N N   . ARG   B 2 20  ? 24.05040 12.45162  -35.80566 1.000 114.02456 ? 113 ARG   B N   1 
ATOM   2530 C CA  . ARG   B 2 20  ? 23.95518 10.99456  -35.80499 1.000 104.90436 ? 113 ARG   B CA  1 
ATOM   2531 C C   . ARG   B 2 20  ? 25.29770 10.34361  -36.11705 1.000 106.86024 ? 113 ARG   B C   1 
ATOM   2532 O O   . ARG   B 2 20  ? 25.66260 9.33313   -35.50432 1.000 95.26841  ? 113 ARG   B O   1 
ATOM   2533 C CB  . ARG   B 2 20  ? 22.89044 10.54458  -36.80399 1.000 108.04881 ? 113 ARG   B CB  1 
ATOM   2534 C CG  . ARG   B 2 20  ? 22.91587 11.30884  -38.11701 1.000 107.86329 ? 113 ARG   B CG  1 
ATOM   2535 C CD  . ARG   B 2 20  ? 21.95112 10.71006  -39.12367 1.000 107.94816 ? 113 ARG   B CD  1 
ATOM   2536 N NE  . ARG   B 2 20  ? 22.30246 9.33429   -39.45260 1.000 110.58251 ? 113 ARG   B NE  1 
ATOM   2537 C CZ  . ARG   B 2 20  ? 23.17578 8.98921   -40.38853 1.000 118.18735 ? 113 ARG   B CZ  1 
ATOM   2538 N NH1 . ARG   B 2 20  ? 23.80739 9.89826   -41.11312 1.000 122.93422 ? 113 ARG   B NH1 1 
ATOM   2539 N NH2 . ARG   B 2 20  ? 23.42278 7.69992   -40.60179 1.000 117.83917 ? 113 ARG   B NH2 1 
ATOM   2540 N N   . GLU   B 2 21  ? 26.04974 10.90728  -37.06430 1.000 128.13485 ? 114 GLU   B N   1 
ATOM   2541 C CA  . GLU   B 2 21  ? 27.37046 10.37130  -37.36756 1.000 127.59960 ? 114 GLU   B CA  1 
ATOM   2542 C C   . GLU   B 2 21  ? 28.37714 10.66517  -36.26464 1.000 120.12890 ? 114 GLU   B C   1 
ATOM   2543 O O   . GLU   B 2 21  ? 29.36602 9.93660   -36.13469 1.000 115.57763 ? 114 GLU   B O   1 
ATOM   2544 C CB  . GLU   B 2 21  ? 27.87372 10.92993  -38.69921 1.000 128.20059 ? 114 GLU   B CB  1 
ATOM   2545 C CG  . GLU   B 2 21  ? 27.08076 10.46171  -39.90953 1.000 136.97751 ? 114 GLU   B CG  1 
ATOM   2546 C CD  . GLU   B 2 21  ? 27.28578 8.98888   -40.21334 1.000 141.83778 ? 114 GLU   B CD  1 
ATOM   2547 O OE1 . GLU   B 2 21  ? 28.27019 8.40342   -39.71365 1.000 137.52518 ? 114 GLU   B OE1 1 
ATOM   2548 O OE2 . GLU   B 2 21  ? 26.46083 8.41656   -40.95583 1.000 143.66599 ? 114 GLU   B OE2 1 
ATOM   2549 N N   . GLU   B 2 22  ? 28.14643 11.70942  -35.46708 1.000 110.56603 ? 115 GLU   B N   1 
ATOM   2550 C CA  . GLU   B 2 22  ? 29.06971 12.02782  -34.38374 1.000 102.77945 ? 115 GLU   B CA  1 
ATOM   2551 C C   . GLU   B 2 22  ? 28.93557 11.03315  -33.23736 1.000 93.34555  ? 115 GLU   B C   1 
ATOM   2552 O O   . GLU   B 2 22  ? 29.94135 10.59961  -32.66311 1.000 88.43720  ? 115 GLU   B O   1 
ATOM   2553 C CB  . GLU   B 2 22  ? 28.82497 13.45439  -33.89259 1.000 107.50084 ? 115 GLU   B CB  1 
ATOM   2554 C CG  . GLU   B 2 22  ? 29.86739 13.97010  -32.91530 1.000 105.09929 ? 115 GLU   B CG  1 
ATOM   2555 C CD  . GLU   B 2 22  ? 29.55068 15.36555  -32.41238 1.000 107.50971 ? 115 GLU   B CD  1 
ATOM   2556 O OE1 . GLU   B 2 22  ? 28.37105 15.77135  -32.48119 1.000 102.38450 ? 115 GLU   B OE1 1 
ATOM   2557 O OE2 . GLU   B 2 22  ? 30.48193 16.05800  -31.95110 1.000 103.54942 ? 115 GLU   B OE2 1 
ATOM   2558 N N   . VAL   B 2 23  ? 27.70088 10.66095  -32.89100 1.000 82.51367  ? 116 VAL   B N   1 
ATOM   2559 C CA  . VAL   B 2 23  ? 27.48729 9.68580   -31.82623 1.000 82.66619  ? 116 VAL   B CA  1 
ATOM   2560 C C   . VAL   B 2 23  ? 28.03389 8.32389   -32.23368 1.000 83.79330  ? 116 VAL   B C   1 
ATOM   2561 O O   . VAL   B 2 23  ? 28.66972 7.62829   -31.43255 1.000 69.73102  ? 116 VAL   B O   1 
ATOM   2562 C CB  . VAL   B 2 23  ? 25.99244 9.61254   -31.46313 1.000 76.12582  ? 116 VAL   B CB  1 
ATOM   2563 C CG1 . VAL   B 2 23  ? 25.74929 8.54928   -30.40361 1.000 74.62175  ? 116 VAL   B CG1 1 
ATOM   2564 C CG2 . VAL   B 2 23  ? 25.50325 10.96482  -30.98361 1.000 70.11670  ? 116 VAL   B CG2 1 
ATOM   2565 N N   . TRP   B 2 24  ? 27.80643 7.92651   -33.48661 1.000 83.79518  ? 117 TRP   B N   1 
ATOM   2566 C CA  . TRP   B 2 24  ? 28.28343 6.62829   -33.95078 1.000 80.34216  ? 117 TRP   B CA  1 
ATOM   2567 C C   . TRP   B 2 24  ? 29.80522 6.59621   -34.03881 1.000 83.99826  ? 117 TRP   B C   1 
ATOM   2568 O O   . TRP   B 2 24  ? 30.42789 5.57262   -33.73166 1.000 73.99282  ? 117 TRP   B O   1 
ATOM   2569 C CB  . TRP   B 2 24  ? 27.65049 6.29737   -35.30352 1.000 86.12111  ? 117 TRP   B CB  1 
ATOM   2570 C CG  . TRP   B 2 24  ? 27.98188 4.92906   -35.81844 1.000 80.81054  ? 117 TRP   B CG  1 
ATOM   2571 C CD1 . TRP   B 2 24  ? 28.86860 4.61746   -36.80772 1.000 96.76772  ? 117 TRP   B CD1 1 
ATOM   2572 C CD2 . TRP   B 2 24  ? 27.42577 3.68638   -35.37237 1.000 78.24629  ? 117 TRP   B CD2 1 
ATOM   2573 N NE1 . TRP   B 2 24  ? 28.89828 3.25766   -37.00597 1.000 88.92655  ? 117 TRP   B NE1 1 
ATOM   2574 C CE2 . TRP   B 2 24  ? 28.02306 2.66329   -36.13542 1.000 85.46793  ? 117 TRP   B CE2 1 
ATOM   2575 C CE3 . TRP   B 2 24  ? 26.48227 3.33945   -34.40077 1.000 76.78609  ? 117 TRP   B CE3 1 
ATOM   2576 C CZ2 . TRP   B 2 24  ? 27.70800 1.31763   -35.95609 1.000 84.19580  ? 117 TRP   B CZ2 1 
ATOM   2577 C CZ3 . TRP   B 2 24  ? 26.17062 2.00388   -34.22594 1.000 81.89710  ? 117 TRP   B CZ3 1 
ATOM   2578 C CH2 . TRP   B 2 24  ? 26.78048 1.01004   -34.99953 1.000 73.84018  ? 117 TRP   B CH2 1 
ATOM   2579 N N   . LYS   B 2 25  ? 30.42003 7.70813   -34.45328 1.000 92.05933  ? 118 LYS   B N   1 
ATOM   2580 C CA  . LYS   B 2 25  ? 31.87685 7.77000   -34.53077 1.000 83.00740  ? 118 LYS   B CA  1 
ATOM   2581 C C   . LYS   B 2 25  ? 32.50786 7.58978   -33.15601 1.000 77.27788  ? 118 LYS   B C   1 
ATOM   2582 O O   . LYS   B 2 25  ? 33.50393 6.87143   -33.00966 1.000 77.12387  ? 118 LYS   B O   1 
ATOM   2583 C CB  . LYS   B 2 25  ? 32.31318 9.10086   -35.14582 1.000 87.81439  ? 118 LYS   B CB  1 
ATOM   2584 C CG  . LYS   B 2 25  ? 33.28050 8.97491   -36.31193 1.000 103.55455 ? 118 LYS   B CG  1 
ATOM   2585 C CD  . LYS   B 2 25  ? 32.56239 8.55937   -37.58416 1.000 106.10527 ? 118 LYS   B CD  1 
ATOM   2586 C CE  . LYS   B 2 25  ? 33.49869 8.59674   -38.78022 1.000 112.04815 ? 118 LYS   B CE  1 
ATOM   2587 N NZ  . LYS   B 2 25  ? 32.78217 8.31645   -40.05480 1.000 107.05525 ? 118 LYS   B NZ  1 
ATOM   2588 N N   . ILE   B 2 26  ? 31.93623 8.23420   -32.13569 1.000 70.07908  ? 119 ILE   B N   1 
ATOM   2589 C CA  . ILE   B 2 26  ? 32.46621 8.12164   -30.77913 1.000 78.12785  ? 119 ILE   B CA  1 
ATOM   2590 C C   . ILE   B 2 26  ? 32.37334 6.68315   -30.28579 1.000 70.81783  ? 119 ILE   B C   1 
ATOM   2591 O O   . ILE   B 2 26  ? 33.30245 6.16603   -29.65316 1.000 71.41855  ? 119 ILE   B O   1 
ATOM   2592 C CB  . ILE   B 2 26  ? 31.72693 9.09428   -29.84086 1.000 78.67882  ? 119 ILE   B CB  1 
ATOM   2593 C CG1 . ILE   B 2 26  ? 32.01880 10.54240  -30.23902 1.000 78.80446  ? 119 ILE   B CG1 1 
ATOM   2594 C CG2 . ILE   B 2 26  ? 32.10912 8.84130   -28.38844 1.000 69.53935  ? 119 ILE   B CG2 1 
ATOM   2595 C CD1 . ILE   B 2 26  ? 31.07361 11.54509  -29.61931 1.000 79.29486  ? 119 ILE   B CD1 1 
ATOM   2596 N N   . MET   B 2 27  ? 31.25480 6.01229   -30.57098 1.000 62.50179  ? 120 MET   B N   1 
ATOM   2597 C CA  . MET   B 2 27  ? 31.10060 4.62144   -30.15604 1.000 71.94783  ? 120 MET   B CA  1 
ATOM   2598 C C   . MET   B 2 27  ? 32.11970 3.72433   -30.84743 1.000 71.44394  ? 120 MET   B C   1 
ATOM   2599 O O   . MET   B 2 27  ? 32.66542 2.80142   -30.23097 1.000 67.41920  ? 120 MET   B O   1 
ATOM   2600 C CB  . MET   B 2 27  ? 29.67627 4.14422   -30.44299 1.000 72.26613  ? 120 MET   B CB  1 
ATOM   2601 C CG  . MET   B 2 27  ? 28.60319 4.90673   -29.68118 1.000 67.45103  ? 120 MET   B CG  1 
ATOM   2602 S SD  . MET   B 2 27  ? 26.92821 4.39915   -30.11793 1.000 72.17429  ? 120 MET   B SD  1 
ATOM   2603 C CE  . MET   B 2 27  ? 26.93668 2.69805   -29.56096 1.000 79.98048  ? 120 MET   B CE  1 
ATOM   2604 N N   . LEU   B 2 28  ? 32.39268 3.98201   -32.12880 1.000 68.37375  ? 121 LEU   B N   1 
ATOM   2605 C CA  . LEU   B 2 28  ? 33.40726 3.20663   -32.83470 1.000 76.45198  ? 121 LEU   B CA  1 
ATOM   2606 C C   . LEU   B 2 28  ? 34.80808 3.58456   -32.37311 1.000 75.00321  ? 121 LEU   B C   1 
ATOM   2607 O O   . LEU   B 2 28  ? 35.67329 2.71425   -32.21981 1.000 81.71437  ? 121 LEU   B O   1 
ATOM   2608 C CB  . LEU   B 2 28  ? 33.27457 3.40870   -34.34410 1.000 72.07914  ? 121 LEU   B CB  1 
ATOM   2609 C CG  . LEU   B 2 28  ? 31.98379 2.94745   -35.02072 1.000 79.44929  ? 121 LEU   B CG  1 
ATOM   2610 C CD1 . LEU   B 2 28  ? 32.10895 3.09361   -36.52931 1.000 82.15092  ? 121 LEU   B CD1 1 
ATOM   2611 C CD2 . LEU   B 2 28  ? 31.65347 1.51336   -34.63965 1.000 77.09896  ? 121 LEU   B CD2 1 
ATOM   2612 N N   . ASN   B 2 29  ? 35.04874 4.87914   -32.14687 1.000 78.32634  ? 122 ASN   B N   1 
ATOM   2613 C CA  . ASN   B 2 29  ? 36.37233 5.32619   -31.72740 1.000 92.15040  ? 122 ASN   B CA  1 
ATOM   2614 C C   . ASN   B 2 29  ? 36.73576 4.78167   -30.35239 1.000 87.03723  ? 122 ASN   B C   1 
ATOM   2615 O O   . ASN   B 2 29  ? 37.92088 4.60191   -30.04947 1.000 91.15655  ? 122 ASN   B O   1 
ATOM   2616 C CB  . ASN   B 2 29  ? 36.43373 6.85466   -31.73255 1.000 95.37287  ? 122 ASN   B CB  1 
ATOM   2617 C CG  . ASN   B 2 29  ? 37.84087 7.38200   -31.93468 1.000 109.21690 ? 122 ASN   B CG  1 
ATOM   2618 O OD1 . ASN   B 2 29  ? 38.26822 7.62516   -33.06340 1.000 115.36933 ? 122 ASN   B OD1 1 
ATOM   2619 N ND2 . ASN   B 2 29  ? 38.56878 7.56275   -30.83972 1.000 96.27973  ? 122 ASN   B ND2 1 
ATOM   2620 N N   . LYS   B 2 30  ? 35.73512 4.50974   -29.51092 1.000 92.35130  ? 123 LYS   B N   1 
ATOM   2621 C CA  . LYS   B 2 30  ? 36.00722 3.92774   -28.20076 1.000 91.94863  ? 123 LYS   B CA  1 
ATOM   2622 C C   . LYS   B 2 30  ? 36.50392 2.49316   -28.32678 1.000 94.72116  ? 123 LYS   B C   1 
ATOM   2623 O O   . LYS   B 2 30  ? 37.38509 2.06576   -27.57124 1.000 96.72889  ? 123 LYS   B O   1 
ATOM   2624 C CB  . LYS   B 2 30  ? 34.75170 3.98641   -27.32934 1.000 93.59742  ? 123 LYS   B CB  1 
ATOM   2625 C CG  . LYS   B 2 30  ? 34.83876 3.14908   -26.06156 1.000 92.14377  ? 123 LYS   B CG  1 
ATOM   2626 C CD  . LYS   B 2 30  ? 33.57218 3.24761   -25.22856 1.000 89.39993  ? 123 LYS   B CD  1 
ATOM   2627 C CE  . LYS   B 2 30  ? 33.36692 4.65853   -24.71041 1.000 83.79816  ? 123 LYS   B CE  1 
ATOM   2628 N NZ  . LYS   B 2 30  ? 32.23360 4.73798   -23.74906 1.000 88.83362  ? 123 LYS   B NZ  1 
ATOM   2629 N N   . GLU   B 2 31  ? 35.95820 1.73810   -29.28318 1.000 96.42165  ? 124 GLU   B N   1 
ATOM   2630 C CA  . GLU   B 2 31  ? 36.34212 0.34078   -29.44494 1.000 101.25365 ? 124 GLU   B CA  1 
ATOM   2631 C C   . GLU   B 2 31  ? 37.81350 0.18507   -29.80726 1.000 104.31863 ? 124 GLU   B C   1 
ATOM   2632 O O   . GLU   B 2 31  ? 38.36950 -0.90633  -29.64221 1.000 107.43899 ? 124 GLU   B O   1 
ATOM   2633 C CB  . GLU   B 2 31  ? 35.45916 -0.31687  -30.50579 1.000 109.13516 ? 124 GLU   B CB  1 
ATOM   2634 C CG  . GLU   B 2 31  ? 35.30629 -1.82134  -30.35460 1.000 115.44034 ? 124 GLU   B CG  1 
ATOM   2635 C CD  . GLU   B 2 31  ? 33.86414 -2.27112  -30.49708 1.000 108.06023 ? 124 GLU   B CD  1 
ATOM   2636 O OE1 . GLU   B 2 31  ? 32.97321 -1.58971  -29.94765 1.000 93.22557  ? 124 GLU   B OE1 1 
ATOM   2637 O OE2 . GLU   B 2 31  ? 33.61971 -3.29975  -31.16188 1.000 102.22392 ? 124 GLU   B OE2 1 
ATOM   2638 N N   . LYS   B 2 32  ? 38.45303 1.24735   -30.30103 1.000 117.49984 ? 125 LYS   B N   1 
ATOM   2639 C CA  . LYS   B 2 32  ? 39.89221 1.23175   -30.52383 1.000 109.32662 ? 125 LYS   B CA  1 
ATOM   2640 C C   . LYS   B 2 32  ? 40.67652 1.54706   -29.25772 1.000 105.84920 ? 125 LYS   B C   1 
ATOM   2641 O O   . LYS   B 2 32  ? 41.84092 1.14773   -29.14987 1.000 111.97288 ? 125 LYS   B O   1 
ATOM   2642 C CB  . LYS   B 2 32  ? 40.26475 2.22539   -31.62643 1.000 113.27723 ? 125 LYS   B CB  1 
ATOM   2643 C CG  . LYS   B 2 32  ? 39.59985 1.93722   -32.96197 1.000 119.38025 ? 125 LYS   B CG  1 
ATOM   2644 C CD  . LYS   B 2 32  ? 40.00867 2.94968   -34.01842 1.000 127.73972 ? 125 LYS   B CD  1 
ATOM   2645 C CE  . LYS   B 2 32  ? 39.35932 2.63678   -35.35683 1.000 131.46681 ? 125 LYS   B CE  1 
ATOM   2646 N NZ  . LYS   B 2 32  ? 39.75707 3.60955   -36.41166 1.000 140.43543 ? 125 LYS   B NZ  1 
ATOM   2647 N N   . THR   B 2 33  ? 40.06633 2.25226   -28.30163 1.000 104.63364 ? 126 THR   B N   1 
ATOM   2648 C CA  . THR   B 2 33  ? 40.73173 2.50551   -27.02771 1.000 98.93569  ? 126 THR   B CA  1 
ATOM   2649 C C   . THR   B 2 33  ? 40.78183 1.24422   -26.17490 1.000 93.80370  ? 126 THR   B C   1 
ATOM   2650 O O   . THR   B 2 33  ? 41.79814 0.96344   -25.52862 1.000 98.61668  ? 126 THR   B O   1 
ATOM   2651 C CB  . THR   B 2 33  ? 40.01843 3.63004   -26.27439 1.000 97.10180  ? 126 THR   B CB  1 
ATOM   2652 O OG1 . THR   B 2 33  ? 40.03303 4.82506   -27.06509 1.000 99.82550  ? 126 THR   B OG1 1 
ATOM   2653 C CG2 . THR   B 2 33  ? 40.69928 3.90140   -24.93559 1.000 102.80258 ? 126 THR   B CG2 1 
ATOM   2654 N N   . TYR   B 2 34  ? 39.69683 0.47365   -26.16151 1.000 95.28565  ? 127 TYR   B N   1 
ATOM   2655 C CA  . TYR   B 2 34  ? 39.61908 -0.75980  -25.38611 1.000 89.06764  ? 127 TYR   B CA  1 
ATOM   2656 C C   . TYR   B 2 34  ? 40.11735 -1.91091  -26.25122 1.000 96.16954  ? 127 TYR   B C   1 
ATOM   2657 O O   . TYR   B 2 34  ? 39.45947 -2.29830  -27.22245 1.000 101.62184 ? 127 TYR   B O   1 
ATOM   2658 C CB  . TYR   B 2 34  ? 38.19124 -1.00407  -24.90609 1.000 88.39307  ? 127 TYR   B CB  1 
ATOM   2659 C CG  . TYR   B 2 34  ? 37.72946 -0.01784  -23.85835 1.000 87.28682  ? 127 TYR   B CG  1 
ATOM   2660 C CD1 . TYR   B 2 34  ? 37.30311 1.25462   -24.21381 1.000 79.76022  ? 127 TYR   B CD1 1 
ATOM   2661 C CD2 . TYR   B 2 34  ? 37.72223 -0.35889  -22.51268 1.000 77.72908  ? 127 TYR   B CD2 1 
ATOM   2662 C CE1 . TYR   B 2 34  ? 36.88274 2.16040   -23.25817 1.000 84.96137  ? 127 TYR   B CE1 1 
ATOM   2663 C CE2 . TYR   B 2 34  ? 37.30277 0.53980   -21.54893 1.000 79.57291  ? 127 TYR   B CE2 1 
ATOM   2664 C CZ  . TYR   B 2 34  ? 36.88418 1.79816   -21.92713 1.000 78.73032  ? 127 TYR   B CZ  1 
ATOM   2665 O OH  . TYR   B 2 34  ? 36.46597 2.69734   -20.97239 1.000 68.83052  ? 127 TYR   B OH  1 
ATOM   2666 N N   . LEU   B 2 35  ? 41.27556 -2.45723  -25.89615 1.000 94.41084  ? 128 LEU   B N   1 
ATOM   2667 C CA  . LEU   B 2 35  ? 41.91253 -3.50597  -26.67697 1.000 96.96517  ? 128 LEU   B CA  1 
ATOM   2668 C C   . LEU   B 2 35  ? 41.51429 -4.88615  -26.16990 1.000 99.56231  ? 128 LEU   B C   1 
ATOM   2669 O O   . LEU   B 2 35  ? 41.26456 -5.08795  -24.97836 1.000 105.30111 ? 128 LEU   B O   1 
ATOM   2670 C CB  . LEU   B 2 35  ? 43.43629 -3.36735  -26.63389 1.000 102.43518 ? 128 LEU   B CB  1 
ATOM   2671 C CG  . LEU   B 2 35  ? 44.11425 -2.38758  -27.59587 1.000 99.78913  ? 128 LEU   B CG  1 
ATOM   2672 C CD1 . LEU   B 2 35  ? 43.77918 -0.94352  -27.25837 1.000 101.65496 ? 128 LEU   B CD1 1 
ATOM   2673 C CD2 . LEU   B 2 35  ? 45.62067 -2.60433  -27.59306 1.000 92.84509  ? 128 LEU   B CD2 1 
ATOM   2674 N N   . ARG   B 2 36  ? 41.45821 -5.83916  -27.09596 1.000 111.60911 ? 129 ARG   B N   1 
ATOM   2675 C CA  . ARG   B 2 36  ? 41.23744 -7.24037  -26.77750 1.000 114.03013 ? 129 ARG   B CA  1 
ATOM   2676 C C   . ARG   B 2 36  ? 42.41046 -8.06628  -27.28426 1.000 119.41797 ? 129 ARG   B C   1 
ATOM   2677 O O   . ARG   B 2 36  ? 43.10043 -7.68023  -28.23254 1.000 126.32114 ? 129 ARG   B O   1 
ATOM   2678 C CB  . ARG   B 2 36  ? 39.92955 -7.76663  -27.38581 1.000 113.97909 ? 129 ARG   B CB  1 
ATOM   2679 C CG  . ARG   B 2 36  ? 38.69237 -7.45602  -26.55981 1.000 111.89563 ? 129 ARG   B CG  1 
ATOM   2680 C CD  . ARG   B 2 36  ? 38.21659 -6.02966  -26.77259 1.000 115.78215 ? 129 ARG   B CD  1 
ATOM   2681 N NE  . ARG   B 2 36  ? 37.57384 -5.48955  -25.58088 1.000 108.31965 ? 129 ARG   B NE  1 
ATOM   2682 C CZ  . ARG   B 2 36  ? 36.90848 -4.34356  -25.54153 1.000 107.62194 ? 129 ARG   B CZ  1 
ATOM   2683 N NH1 . ARG   B 2 36  ? 36.74631 -3.60096  -26.62442 1.000 109.74913 ? 129 ARG   B NH1 1 
ATOM   2684 N NH2 . ARG   B 2 36  ? 36.39030 -3.93395  -24.38710 1.000 104.29822 ? 129 ARG   B NH2 1 
ATOM   2685 N N   . ASP   B 2 37  ? 42.63205 -9.20871  -26.63848 1.000 108.92935 ? 130 ASP   B N   1 
ATOM   2686 C CA  . ASP   B 2 37  ? 43.72964 -10.10789 -26.99157 1.000 117.99591 ? 130 ASP   B CA  1 
ATOM   2687 C C   . ASP   B 2 37  ? 43.22887 -11.53133 -26.77140 1.000 115.16979 ? 130 ASP   B C   1 
ATOM   2688 O O   . ASP   B 2 37  ? 43.14682 -11.99277 -25.63023 1.000 108.47915 ? 130 ASP   B O   1 
ATOM   2689 C CB  . ASP   B 2 37  ? 44.97158 -9.81364  -26.15768 1.000 109.61146 ? 130 ASP   B CB  1 
ATOM   2690 C CG  . ASP   B 2 37  ? 46.24351 -10.33543 -26.79683 1.000 122.15661 ? 130 ASP   B CG  1 
ATOM   2691 O OD1 . ASP   B 2 37  ? 46.16550 -11.29527 -27.59201 1.000 121.39740 ? 130 ASP   B OD1 1 
ATOM   2692 O OD2 . ASP   B 2 37  ? 47.32421 -9.78273  -26.50173 1.000 115.39681 ? 130 ASP   B OD2 1 
ATOM   2693 N N   . GLN   B 2 38  ? 42.89543 -12.22436 -27.86282 1.000 105.16053 ? 131 GLN   B N   1 
ATOM   2694 C CA  . GLN   B 2 38  ? 42.35652 -13.57459 -27.74682 1.000 108.93044 ? 131 GLN   B CA  1 
ATOM   2695 C C   . GLN   B 2 38  ? 43.38166 -14.58146 -27.24341 1.000 112.63203 ? 131 GLN   B C   1 
ATOM   2696 O O   . GLN   B 2 38  ? 43.01300 -15.72996 -26.97455 1.000 108.72705 ? 131 GLN   B O   1 
ATOM   2697 C CB  . GLN   B 2 38  ? 41.79720 -14.04471 -29.09229 1.000 110.93124 ? 131 GLN   B CB  1 
ATOM   2698 C CG  . GLN   B 2 38  ? 42.84876 -14.32213 -30.15763 1.000 114.58692 ? 131 GLN   B CG  1 
ATOM   2699 C CD  . GLN   B 2 38  ? 43.08495 -13.13724 -31.07365 1.000 116.37466 ? 131 GLN   B CD  1 
ATOM   2700 O OE1 . GLN   B 2 38  ? 42.85423 -11.98888 -30.69595 1.000 116.92699 ? 131 GLN   B OE1 1 
ATOM   2701 N NE2 . GLN   B 2 38  ? 43.53980 -13.41293 -32.29096 1.000 110.90898 ? 131 GLN   B NE2 1 
ATOM   2702 N N   . HIS   B 2 39  ? 44.64641 -14.18487 -27.10672 1.000 113.72065 ? 132 HIS   B N   1 
ATOM   2703 C CA  . HIS   B 2 39  ? 45.70599 -15.06856 -26.63856 1.000 118.05614 ? 132 HIS   B CA  1 
ATOM   2704 C C   . HIS   B 2 39  ? 46.39587 -14.51008 -25.39854 1.000 118.59144 ? 132 HIS   B C   1 
ATOM   2705 O O   . HIS   B 2 39  ? 47.59720 -14.71081 -25.20854 1.000 122.32041 ? 132 HIS   B O   1 
ATOM   2706 C CB  . HIS   B 2 39  ? 46.72730 -15.31923 -27.74710 1.000 123.28859 ? 132 HIS   B CB  1 
ATOM   2707 C CG  . HIS   B 2 39  ? 46.15769 -16.00399 -28.94973 1.000 117.87548 ? 132 HIS   B CG  1 
ATOM   2708 N ND1 . HIS   B 2 39  ? 46.66950 -15.82965 -30.21748 1.000 122.88811 ? 132 HIS   B ND1 1 
ATOM   2709 C CD2 . HIS   B 2 39  ? 45.12314 -16.86815 -29.07722 1.000 121.96439 ? 132 HIS   B CD2 1 
ATOM   2710 C CE1 . HIS   B 2 39  ? 45.97263 -16.55399 -31.07472 1.000 121.35666 ? 132 HIS   B CE1 1 
ATOM   2711 N NE2 . HIS   B 2 39  ? 45.02865 -17.19396 -30.40840 1.000 120.96073 ? 132 HIS   B NE2 1 
ATOM   2712 N N   . PHE   B 2 40  ? 45.65062 -13.80268 -24.54386 1.000 115.05009 ? 133 PHE   B N   1 
ATOM   2713 C CA  . PHE   B 2 40  ? 46.25318 -13.26245 -23.33059 1.000 112.36669 ? 133 PHE   B CA  1 
ATOM   2714 C C   . PHE   B 2 40  ? 46.60620 -14.35432 -22.33038 1.000 113.23280 ? 133 PHE   B C   1 
ATOM   2715 O O   . PHE   B 2 40  ? 47.42592 -14.11631 -21.43711 1.000 115.26234 ? 133 PHE   B O   1 
ATOM   2716 C CB  . PHE   B 2 40  ? 45.32754 -12.22648 -22.67787 1.000 102.99126 ? 133 PHE   B CB  1 
ATOM   2717 C CG  . PHE   B 2 40  ? 44.08182 -12.80946 -22.05810 1.000 99.50764  ? 133 PHE   B CG  1 
ATOM   2718 C CD1 . PHE   B 2 40  ? 44.09272 -13.29070 -20.75845 1.000 99.15015  ? 133 PHE   B CD1 1 
ATOM   2719 C CD2 . PHE   B 2 40  ? 42.89266 -12.84725 -22.76518 1.000 111.50812 ? 133 PHE   B CD2 1 
ATOM   2720 C CE1 . PHE   B 2 40  ? 42.95089 -13.81948 -20.18932 1.000 98.81223  ? 133 PHE   B CE1 1 
ATOM   2721 C CE2 . PHE   B 2 40  ? 41.74645 -13.37199 -22.19868 1.000 105.17662 ? 133 PHE   B CE2 1 
ATOM   2722 C CZ  . PHE   B 2 40  ? 41.77645 -13.85777 -20.90897 1.000 99.44435  ? 133 PHE   B CZ  1 
ATOM   2723 N N   . LEU   B 2 41  ? 46.00726 -15.54062 -22.45649 1.000 108.88192 ? 134 LEU   B N   1 
ATOM   2724 C CA  . LEU   B 2 41  ? 46.32029 -16.64062 -21.55343 1.000 119.56658 ? 134 LEU   B CA  1 
ATOM   2725 C C   . LEU   B 2 41  ? 47.69801 -17.23680 -21.80441 1.000 121.16885 ? 134 LEU   B C   1 
ATOM   2726 O O   . LEU   B 2 41  ? 48.15733 -18.04783 -20.99353 1.000 118.12521 ? 134 LEU   B O   1 
ATOM   2727 C CB  . LEU   B 2 41  ? 45.25119 -17.72867 -21.65875 1.000 112.04577 ? 134 LEU   B CB  1 
ATOM   2728 C CG  . LEU   B 2 41  ? 43.93432 -17.39070 -20.95807 1.000 111.15391 ? 134 LEU   B CG  1 
ATOM   2729 C CD1 . LEU   B 2 41  ? 42.92015 -18.50277 -21.14563 1.000 118.73996 ? 134 LEU   B CD1 1 
ATOM   2730 C CD2 . LEU   B 2 41  ? 44.17552 -17.12745 -19.47903 1.000 113.37739 ? 134 LEU   B CD2 1 
ATOM   2731 N N   . GLU   B 2 42  ? 48.36303 -16.86504 -22.90058 1.000 119.82289 ? 135 GLU   B N   1 
ATOM   2732 C CA  . GLU   B 2 42  ? 49.76096 -17.23704 -23.07369 1.000 119.47950 ? 135 GLU   B CA  1 
ATOM   2733 C C   . GLU   B 2 42  ? 50.66408 -16.50804 -22.08885 1.000 126.42157 ? 135 GLU   B C   1 
ATOM   2734 O O   . GLU   B 2 42  ? 51.77567 -16.97597 -21.81975 1.000 127.01801 ? 135 GLU   B O   1 
ATOM   2735 C CB  . GLU   B 2 42  ? 50.20860 -16.95842 -24.50896 1.000 124.67529 ? 135 GLU   B CB  1 
ATOM   2736 C CG  . GLU   B 2 42  ? 49.44105 -17.74934 -25.55605 1.000 128.82215 ? 135 GLU   B CG  1 
ATOM   2737 C CD  . GLU   B 2 42  ? 49.88250 -17.42872 -26.96945 1.000 130.03608 ? 135 GLU   B CD  1 
ATOM   2738 O OE1 . GLU   B 2 42  ? 50.83406 -16.63629 -27.13031 1.000 133.68760 ? 135 GLU   B OE1 1 
ATOM   2739 O OE2 . GLU   B 2 42  ? 49.27710 -17.96781 -27.91955 1.000 142.13122 ? 135 GLU   B OE2 1 
ATOM   2740 N N   . GLN   B 2 43  ? 50.21005 -15.37411 -21.54845 1.000 118.18894 ? 136 GLN   B N   1 
ATOM   2741 C CA  . GLN   B 2 43  ? 50.94229 -14.70058 -20.48389 1.000 119.86169 ? 136 GLN   B CA  1 
ATOM   2742 C C   . GLN   B 2 43  ? 50.80993 -15.42816 -19.15295 1.000 114.87959 ? 136 GLN   B C   1 
ATOM   2743 O O   . GLN   B 2 43  ? 51.59398 -15.16569 -18.23478 1.000 118.11875 ? 136 GLN   B O   1 
ATOM   2744 C CB  . GLN   B 2 43  ? 50.45179 -13.25814 -20.34070 1.000 116.55754 ? 136 GLN   B CB  1 
ATOM   2745 C CG  . GLN   B 2 43  ? 50.49179 -12.45735 -21.63342 1.000 118.92491 ? 136 GLN   B CG  1 
ATOM   2746 C CD  . GLN   B 2 43  ? 49.84867 -11.09061 -21.49457 1.000 118.31365 ? 136 GLN   B CD  1 
ATOM   2747 O OE1 . GLN   B 2 43  ? 49.85032 -10.29283 -22.43203 1.000 115.64326 ? 136 GLN   B OE1 1 
ATOM   2748 N NE2 . GLN   B 2 43  ? 49.29159 -10.81494 -20.32117 1.000 115.45850 ? 136 GLN   B NE2 1 
ATOM   2749 N N   . HIS   B 2 44  ? 49.83538 -16.33305 -19.03009 1.000 115.57219 ? 137 HIS   B N   1 
ATOM   2750 C CA  . HIS   B 2 44  ? 49.61519 -17.13357 -17.82783 1.000 114.44131 ? 137 HIS   B CA  1 
ATOM   2751 C C   . HIS   B 2 44  ? 49.70656 -18.60003 -18.23491 1.000 122.49927 ? 137 HIS   B C   1 
ATOM   2752 O O   . HIS   B 2 44  ? 48.67972 -19.25496 -18.47194 1.000 123.88495 ? 137 HIS   B O   1 
ATOM   2753 C CB  . HIS   B 2 44  ? 48.26656 -16.81362 -17.18552 1.000 116.91115 ? 137 HIS   B CB  1 
ATOM   2754 C CG  . HIS   B 2 44  ? 47.96371 -15.34867 -17.11656 1.000 113.86812 ? 137 HIS   B CG  1 
ATOM   2755 N ND1 . HIS   B 2 44  ? 48.29583 -14.56900 -16.02950 1.000 106.98777 ? 137 HIS   B ND1 1 
ATOM   2756 C CD2 . HIS   B 2 44  ? 47.36241 -14.52045 -18.00337 1.000 110.32378 ? 137 HIS   B CD2 1 
ATOM   2757 C CE1 . HIS   B 2 44  ? 47.91102 -13.32431 -16.24892 1.000 108.60478 ? 137 HIS   B CE1 1 
ATOM   2758 N NE2 . HIS   B 2 44  ? 47.34173 -13.26800 -17.43939 1.000 112.63896 ? 137 HIS   B NE2 1 
ATOM   2759 N N   . PRO   B 2 45  ? 50.92142 -19.14811 -18.32992 1.000 132.01081 ? 138 PRO   B N   1 
ATOM   2760 C CA  . PRO   B 2 45  ? 51.07116 -20.51171 -18.86754 1.000 129.35083 ? 138 PRO   B CA  1 
ATOM   2761 C C   . PRO   B 2 45  ? 50.39863 -21.58441 -18.02914 1.000 129.41097 ? 138 PRO   B C   1 
ATOM   2762 O O   . PRO   B 2 45  ? 50.03494 -22.63723 -18.56788 1.000 138.13954 ? 138 PRO   B O   1 
ATOM   2763 C CB  . PRO   B 2 45  ? 52.59491 -20.70436 -18.90833 1.000 132.30182 ? 138 PRO   B CB  1 
ATOM   2764 C CG  . PRO   B 2 45  ? 53.16161 -19.31768 -18.90364 1.000 131.18396 ? 138 PRO   B CG  1 
ATOM   2765 C CD  . PRO   B 2 45  ? 52.22178 -18.51310 -18.06082 1.000 128.47485 ? 138 PRO   B CD  1 
ATOM   2766 N N   . LEU   B 2 46  ? 50.22016 -21.35665 -16.72784 1.000 128.90278 ? 139 LEU   B N   1 
ATOM   2767 C CA  . LEU   B 2 46  ? 49.60535 -22.36471 -15.87387 1.000 133.04617 ? 139 LEU   B CA  1 
ATOM   2768 C C   . LEU   B 2 46  ? 48.09323 -22.44038 -16.04846 1.000 134.26294 ? 139 LEU   B C   1 
ATOM   2769 O O   . LEU   B 2 46  ? 47.48888 -23.45195 -15.67505 1.000 136.85805 ? 139 LEU   B O   1 
ATOM   2770 C CB  . LEU   B 2 46  ? 49.95132 -22.08807 -14.40767 1.000 139.23243 ? 139 LEU   B CB  1 
ATOM   2771 C CG  . LEU   B 2 46  ? 49.67478 -23.20853 -13.40189 1.000 145.18513 ? 139 LEU   B CG  1 
ATOM   2772 C CD1 . LEU   B 2 46  ? 50.34593 -24.50141 -13.84060 1.000 144.94083 ? 139 LEU   B CD1 1 
ATOM   2773 C CD2 . LEU   B 2 46  ? 50.13651 -22.80837 -12.00939 1.000 133.49128 ? 139 LEU   B CD2 1 
ATOM   2774 N N   . LEU   B 2 47  ? 47.47377 -21.40956 -16.61396 1.000 130.34035 ? 140 LEU   B N   1 
ATOM   2775 C CA  . LEU   B 2 47  ? 46.03166 -21.38559 -16.80201 1.000 126.01317 ? 140 LEU   B CA  1 
ATOM   2776 C C   . LEU   B 2 47  ? 45.64696 -22.01586 -18.13475 1.000 130.58680 ? 140 LEU   B C   1 
ATOM   2777 O O   . LEU   B 2 47  ? 46.43480 -22.04509 -19.08403 1.000 125.95784 ? 140 LEU   B O   1 
ATOM   2778 C CB  . LEU   B 2 47  ? 45.50166 -19.95265 -16.73668 1.000 119.04274 ? 140 LEU   B CB  1 
ATOM   2779 C CG  . LEU   B 2 47  ? 45.74138 -19.20099 -15.42742 1.000 121.44399 ? 140 LEU   B CG  1 
ATOM   2780 C CD1 . LEU   B 2 47  ? 45.12050 -17.81603 -15.48756 1.000 113.62074 ? 140 LEU   B CD1 1 
ATOM   2781 C CD2 . LEU   B 2 47  ? 45.19341 -19.98873 -14.24757 1.000 120.65705 ? 140 LEU   B CD2 1 
ATOM   2782 N N   . GLN   B 2 48  ? 44.41607 -22.52037 -18.19467 1.000 130.02109 ? 141 GLN   B N   1 
ATOM   2783 C CA  . GLN   B 2 48  ? 43.86072 -23.12163 -19.39408 1.000 127.18402 ? 141 GLN   B CA  1 
ATOM   2784 C C   . GLN   B 2 48  ? 42.61157 -22.36427 -19.83266 1.000 124.23427 ? 141 GLN   B C   1 
ATOM   2785 O O   . GLN   B 2 48  ? 41.93759 -21.74170 -19.00557 1.000 123.89080 ? 141 GLN   B O   1 
ATOM   2786 C CB  . GLN   B 2 48  ? 43.51371 -24.59885 -19.16376 1.000 128.45056 ? 141 GLN   B CB  1 
ATOM   2787 C CG  . GLN   B 2 48  ? 44.70046 -25.45760 -18.74721 1.000 137.41516 ? 141 GLN   B CG  1 
ATOM   2788 C CD  . GLN   B 2 48  ? 45.81259 -25.46906 -19.78128 1.000 137.24076 ? 141 GLN   B CD  1 
ATOM   2789 O OE1 . GLN   B 2 48  ? 45.56581 -25.33498 -20.98009 1.000 139.38442 ? 141 GLN   B OE1 1 
ATOM   2790 N NE2 . GLN   B 2 48  ? 47.04730 -25.62763 -19.31859 1.000 133.12836 ? 141 GLN   B NE2 1 
ATOM   2791 N N   . PRO   B 2 49  ? 42.28365 -22.38879 -21.12818 1.000 125.05180 ? 142 PRO   B N   1 
ATOM   2792 C CA  . PRO   B 2 49  ? 41.11308 -21.62764 -21.59858 1.000 118.38100 ? 142 PRO   B CA  1 
ATOM   2793 C C   . PRO   B 2 49  ? 39.79730 -22.07587 -20.98620 1.000 112.58850 ? 142 PRO   B C   1 
ATOM   2794 O O   . PRO   B 2 49  ? 38.87253 -21.26119 -20.87423 1.000 110.26774 ? 142 PRO   B O   1 
ATOM   2795 C CB  . PRO   B 2 49  ? 41.13488 -21.85921 -23.11637 1.000 115.01472 ? 142 PRO   B CB  1 
ATOM   2796 C CG  . PRO   B 2 49  ? 42.55529 -22.18746 -23.42822 1.000 113.78777 ? 142 PRO   B CG  1 
ATOM   2797 C CD  . PRO   B 2 49  ? 43.05678 -22.95849 -22.24512 1.000 122.50885 ? 142 PRO   B CD  1 
ATOM   2798 N N   . LYS   B 2 50  ? 39.67870 -23.34390 -20.58467 1.000 111.80569 ? 143 LYS   B N   1 
ATOM   2799 C CA  . LYS   B 2 50  ? 38.42190 -23.81241 -20.00916 1.000 108.59817 ? 143 LYS   B CA  1 
ATOM   2800 C C   . LYS   B 2 50  ? 38.16699 -23.20150 -18.63624 1.000 112.99904 ? 143 LYS   B C   1 
ATOM   2801 O O   . LYS   B 2 50  ? 37.00723 -22.99854 -18.25721 1.000 105.79893 ? 143 LYS   B O   1 
ATOM   2802 C CB  . LYS   B 2 50  ? 38.41518 -25.34017 -19.92953 1.000 117.49902 ? 143 LYS   B CB  1 
ATOM   2803 C CG  . LYS   B 2 50  ? 37.16369 -25.92465 -19.28996 1.000 119.35971 ? 143 LYS   B CG  1 
ATOM   2804 C CD  . LYS   B 2 50  ? 36.97650 -27.38712 -19.65200 1.000 117.67456 ? 143 LYS   B CD  1 
ATOM   2805 C CE  . LYS   B 2 50  ? 36.59961 -27.54480 -21.11596 1.000 127.39499 ? 143 LYS   B CE  1 
ATOM   2806 N NZ  . LYS   B 2 50  ? 36.30846 -28.96173 -21.46495 1.000 122.75860 ? 143 LYS   B NZ  1 
ATOM   2807 N N   . MET   B 2 51  ? 39.22864 -22.89482 -17.88489 1.000 109.98574 ? 144 MET   B N   1 
ATOM   2808 C CA  . MET   B 2 51  ? 39.05478 -22.26777 -16.57762 1.000 111.73149 ? 144 MET   B CA  1 
ATOM   2809 C C   . MET   B 2 51  ? 38.33326 -20.93152 -16.69826 1.000 99.51496  ? 144 MET   B C   1 
ATOM   2810 O O   . MET   B 2 51  ? 37.54337 -20.56170 -15.82092 1.000 97.83735  ? 144 MET   B O   1 
ATOM   2811 C CB  . MET   B 2 51  ? 40.41124 -22.08156 -15.89810 1.000 111.36135 ? 144 MET   B CB  1 
ATOM   2812 C CG  . MET   B 2 51  ? 41.24198 -23.34786 -15.80073 1.000 123.84632 ? 144 MET   B CG  1 
ATOM   2813 S SD  . MET   B 2 51  ? 42.84332 -23.05566 -15.02567 1.000 128.88321 ? 144 MET   B SD  1 
ATOM   2814 C CE  . MET   B 2 51  ? 43.60224 -24.66753 -15.20383 1.000 128.35190 ? 144 MET   B CE  1 
ATOM   2815 N N   . ARG   B 2 52  ? 38.59275 -20.19335 -17.78029 1.000 105.27022 ? 145 ARG   B N   1 
ATOM   2816 C CA  . ARG   B 2 52  ? 37.89253 -18.93276 -18.00108 1.000 99.34544  ? 145 ARG   B CA  1 
ATOM   2817 C C   . ARG   B 2 52  ? 36.40586 -19.16498 -18.24246 1.000 96.07364  ? 145 ARG   B C   1 
ATOM   2818 O O   . ARG   B 2 52  ? 35.56451 -18.38365 -17.78325 1.000 98.58103  ? 145 ARG   B O   1 
ATOM   2819 C CB  . ARG   B 2 52  ? 38.52098 -18.18706 -19.17795 1.000 99.44749  ? 145 ARG   B CB  1 
ATOM   2820 C CG  . ARG   B 2 52  ? 37.82027 -16.88986 -19.54668 1.000 97.38188  ? 145 ARG   B CG  1 
ATOM   2821 C CD  . ARG   B 2 52  ? 38.50342 -16.21748 -20.72290 1.000 93.56055  ? 145 ARG   B CD  1 
ATOM   2822 N NE  . ARG   B 2 52  ? 37.78144 -15.03447 -21.17405 1.000 92.34914  ? 145 ARG   B NE  1 
ATOM   2823 C CZ  . ARG   B 2 52  ? 36.80310 -15.05329 -22.06870 1.000 95.71584  ? 145 ARG   B CZ  1 
ATOM   2824 N NH1 . ARG   B 2 52  ? 36.39986 -16.18260 -22.62760 1.000 92.14128  ? 145 ARG   B NH1 1 
ATOM   2825 N NH2 . ARG   B 2 52  ? 36.21333 -13.91098 -22.40997 1.000 87.77473  ? 145 ARG   B NH2 1 
ATOM   2826 N N   . ALA   B 2 53  ? 36.06253 -20.24078 -18.95583 1.000 103.60020 ? 146 ALA   B N   1 
ATOM   2827 C CA  . ALA   B 2 53  ? 34.65786 -20.55249 -19.19848 1.000 95.37309  ? 146 ALA   B CA  1 
ATOM   2828 C C   . ALA   B 2 53  ? 33.94533 -20.93412 -17.90761 1.000 102.53380 ? 146 ALA   B C   1 
ATOM   2829 O O   . ALA   B 2 53  ? 32.80510 -20.51697 -17.67601 1.000 90.82159  ? 146 ALA   B O   1 
ATOM   2830 C CB  . ALA   B 2 53  ? 34.54225 -21.67359 -20.22989 1.000 98.66975  ? 146 ALA   B CB  1 
ATOM   2831 N N   . ILE   B 2 54  ? 34.60075 -21.72678 -17.05593 1.000 105.16343 ? 147 ILE   B N   1 
ATOM   2832 C CA  . ILE   B 2 54  ? 33.99865 -22.10817 -15.78273 1.000 98.09184  ? 147 ILE   B CA  1 
ATOM   2833 C C   . ILE   B 2 54  ? 33.83408 -20.89223 -14.88022 1.000 104.38140 ? 147 ILE   B C   1 
ATOM   2834 O O   . ILE   B 2 54  ? 32.86535 -20.80313 -14.11538 1.000 100.79151 ? 147 ILE   B O   1 
ATOM   2835 C CB  . ILE   B 2 54  ? 34.83967 -23.20765 -15.10689 1.000 107.16319 ? 147 ILE   B CB  1 
ATOM   2836 C CG1 . ILE   B 2 54  ? 35.04689 -24.38258 -16.06458 1.000 109.41845 ? 147 ILE   B CG1 1 
ATOM   2837 C CG2 . ILE   B 2 54  ? 34.17333 -23.68339 -13.82464 1.000 120.51528 ? 147 ILE   B CG2 1 
ATOM   2838 C CD1 . ILE   B 2 54  ? 35.93976 -25.46960 -15.51078 1.000 122.69598 ? 147 ILE   B CD1 1 
ATOM   2839 N N   . LEU   B 2 55  ? 34.76020 -19.93446 -14.95748 1.000 102.78552 ? 148 LEU   B N   1 
ATOM   2840 C CA  . LEU   B 2 55  ? 34.66055 -18.73840 -14.12722 1.000 99.36639  ? 148 LEU   B CA  1 
ATOM   2841 C C   . LEU   B 2 55  ? 33.53054 -17.83207 -14.60040 1.000 95.69133  ? 148 LEU   B C   1 
ATOM   2842 O O   . LEU   B 2 55  ? 32.70349 -17.38425 -13.79751 1.000 96.36090  ? 148 LEU   B O   1 
ATOM   2843 C CB  . LEU   B 2 55  ? 35.99037 -17.98389 -14.13034 1.000 99.17735  ? 148 LEU   B CB  1 
ATOM   2844 C CG  . LEU   B 2 55  ? 36.01632 -16.67820 -13.33211 1.000 100.74557 ? 148 LEU   B CG  1 
ATOM   2845 C CD1 . LEU   B 2 55  ? 35.92967 -16.95636 -11.83783 1.000 90.97208  ? 148 LEU   B CD1 1 
ATOM   2846 C CD2 . LEU   B 2 55  ? 37.25557 -15.86015 -13.66504 1.000 104.54191 ? 148 LEU   B CD2 1 
ATOM   2847 N N   . LEU   B 2 56  ? 33.48240 -17.54728 -15.90484 1.000 96.67009  ? 149 LEU   B N   1 
ATOM   2848 C CA  . LEU   B 2 56  ? 32.44920 -16.66085 -16.43247 1.000 89.73295  ? 149 LEU   B CA  1 
ATOM   2849 C C   . LEU   B 2 56  ? 31.06195 -17.26788 -16.26817 1.000 93.56828  ? 149 LEU   B C   1 
ATOM   2850 O O   . LEU   B 2 56  ? 30.09258 -16.55264 -15.98868 1.000 90.36045  ? 149 LEU   B O   1 
ATOM   2851 C CB  . LEU   B 2 56  ? 32.72656 -16.34619 -17.90271 1.000 85.90376  ? 149 LEU   B CB  1 
ATOM   2852 C CG  . LEU   B 2 56  ? 34.00748 -15.56613 -18.20542 1.000 85.21207  ? 149 LEU   B CG  1 
ATOM   2853 C CD1 . LEU   B 2 56  ? 34.19528 -15.40194 -19.70433 1.000 92.23036  ? 149 LEU   B CD1 1 
ATOM   2854 C CD2 . LEU   B 2 56  ? 33.98597 -14.21199 -17.51352 1.000 84.99353  ? 149 LEU   B CD2 1 
ATOM   2855 N N   . ASP   B 2 57  ? 30.94612 -18.58672 -16.43945 1.000 93.94912  ? 150 ASP   B N   1 
ATOM   2856 C CA  . ASP   B 2 57  ? 29.65909 -19.24415 -16.23917 1.000 92.70362  ? 150 ASP   B CA  1 
ATOM   2857 C C   . ASP   B 2 57  ? 29.21787 -19.15588 -14.78416 1.000 97.96114  ? 150 ASP   B C   1 
ATOM   2858 O O   . ASP   B 2 57  ? 28.02345 -19.00993 -14.49946 1.000 95.29381  ? 150 ASP   B O   1 
ATOM   2859 C CB  . ASP   B 2 57  ? 29.73708 -20.70182 -16.68943 1.000 99.86444  ? 150 ASP   B CB  1 
ATOM   2860 C CG  . ASP   B 2 57  ? 28.43120 -21.44244 -16.48995 1.000 106.66297 ? 150 ASP   B CG  1 
ATOM   2861 O OD1 . ASP   B 2 57  ? 27.47334 -21.18088 -17.24838 1.000 119.50320 ? 150 ASP   B OD1 1 
ATOM   2862 O OD2 . ASP   B 2 57  ? 28.36236 -22.28551 -15.57112 1.000 104.69202 ? 150 ASP   B OD2 1 
ATOM   2863 N N   . TRP   B 2 58  ? 30.16754 -19.24693 -13.84984 1.000 102.20439 ? 151 TRP   B N   1 
ATOM   2864 C CA  . TRP   B 2 58  ? 29.83722 -19.06635 -12.44032 1.000 98.06184  ? 151 TRP   B CA  1 
ATOM   2865 C C   . TRP   B 2 58  ? 29.34723 -17.64979 -12.17185 1.000 95.28000  ? 151 TRP   B C   1 
ATOM   2866 O O   . TRP   B 2 58  ? 28.41326 -17.44522 -11.38780 1.000 93.90988  ? 151 TRP   B O   1 
ATOM   2867 C CB  . TRP   B 2 58  ? 31.05263 -19.39510 -11.57159 1.000 108.16437 ? 151 TRP   B CB  1 
ATOM   2868 C CG  . TRP   B 2 58  ? 30.88329 -19.03682 -10.12480 1.000 107.73824 ? 151 TRP   B CG  1 
ATOM   2869 C CD1 . TRP   B 2 58  ? 29.99358 -19.58001 -9.24424  1.000 114.37963 ? 151 TRP   B CD1 1 
ATOM   2870 C CD2 . TRP   B 2 58  ? 31.63588 -18.06552 -9.38650  1.000 106.56179 ? 151 TRP   B CD2 1 
ATOM   2871 N NE1 . TRP   B 2 58  ? 30.13900 -19.00126 -8.00616  1.000 119.45236 ? 151 TRP   B NE1 1 
ATOM   2872 C CE2 . TRP   B 2 58  ? 31.14145 -18.06914 -8.06686  1.000 114.86261 ? 151 TRP   B CE2 1 
ATOM   2873 C CE3 . TRP   B 2 58  ? 32.67689 -17.19106 -9.71423  1.000 105.40106 ? 151 TRP   B CE3 1 
ATOM   2874 C CZ2 . TRP   B 2 58  ? 31.65222 -17.23253 -7.07567  1.000 115.11728 ? 151 TRP   B CZ2 1 
ATOM   2875 C CZ3 . TRP   B 2 58  ? 33.18243 -16.36105 -8.72877  1.000 107.31619 ? 151 TRP   B CZ3 1 
ATOM   2876 C CH2 . TRP   B 2 58  ? 32.66999 -16.38799 -7.42573  1.000 108.33571 ? 151 TRP   B CH2 1 
ATOM   2877 N N   . LEU   B 2 59  ? 29.96078 -16.65809 -12.82224 1.000 97.99127  ? 152 LEU   B N   1 
ATOM   2878 C CA  . LEU   B 2 59  ? 29.51114 -15.27992 -12.66325 1.000 87.95279  ? 152 LEU   B CA  1 
ATOM   2879 C C   . LEU   B 2 59  ? 28.12085 -15.07161 -13.25020 1.000 90.03003  ? 152 LEU   B C   1 
ATOM   2880 O O   . LEU   B 2 59  ? 27.35229 -14.24994 -12.73728 1.000 89.09357  ? 152 LEU   B O   1 
ATOM   2881 C CB  . LEU   B 2 59  ? 30.51388 -14.32363 -13.30826 1.000 83.31669  ? 152 LEU   B CB  1 
ATOM   2882 C CG  . LEU   B 2 59  ? 31.93005 -14.34950 -12.72825 1.000 86.65506  ? 152 LEU   B CG  1 
ATOM   2883 C CD1 . LEU   B 2 59  ? 32.84749 -13.40894 -13.49499 1.000 84.60377  ? 152 LEU   B CD1 1 
ATOM   2884 C CD2 . LEU   B 2 59  ? 31.90999 -13.99508 -11.24942 1.000 84.58269  ? 152 LEU   B CD2 1 
ATOM   2885 N N   . MET   B 2 60  ? 27.78182 -15.79738 -14.31972 1.000 86.23423  ? 153 MET   B N   1 
ATOM   2886 C CA  . MET   B 2 60  ? 26.42374 -15.74121 -14.85283 1.000 87.12200  ? 153 MET   B CA  1 
ATOM   2887 C C   . MET   B 2 60  ? 25.41619 -16.21989 -13.81725 1.000 84.01153  ? 153 MET   B C   1 
ATOM   2888 O O   . MET   B 2 60  ? 24.38044 -15.58179 -13.59602 1.000 88.32770  ? 153 MET   B O   1 
ATOM   2889 C CB  . MET   B 2 60  ? 26.31117 -16.58804 -16.12185 1.000 91.58710  ? 153 MET   B CB  1 
ATOM   2890 C CG  . MET   B 2 60  ? 27.11524 -16.09983 -17.30881 1.000 91.33205  ? 153 MET   B CG  1 
ATOM   2891 S SD  . MET   B 2 60  ? 26.66383 -17.01264 -18.79924 1.000 92.60427  ? 153 MET   B SD  1 
ATOM   2892 C CE  . MET   B 2 60  ? 27.93564 -16.48263 -19.93998 1.000 87.63868  ? 153 MET   B CE  1 
ATOM   2893 N N   . GLU   B 2 61  ? 25.70391 -17.35551 -13.17743 1.000 90.89488  ? 154 GLU   B N   1 
ATOM   2894 C CA  . GLU   B 2 61  ? 24.79189 -17.89515 -12.17563 1.000 100.35341 ? 154 GLU   B CA  1 
ATOM   2895 C C   . GLU   B 2 61  ? 24.68484 -16.96705 -10.97262 1.000 92.17126  ? 154 GLU   B C   1 
ATOM   2896 O O   . GLU   B 2 61  ? 23.59770 -16.79108 -10.41064 1.000 89.42978  ? 154 GLU   B O   1 
ATOM   2897 C CB  . GLU   B 2 61  ? 25.25570 -19.28725 -11.74851 1.000 105.59821 ? 154 GLU   B CB  1 
ATOM   2898 C CG  . GLU   B 2 61  ? 24.27770 -20.02913 -10.85610 1.000 110.49243 ? 154 GLU   B CG  1 
ATOM   2899 C CD  . GLU   B 2 61  ? 24.68618 -21.47047 -10.62603 1.000 116.75587 ? 154 GLU   B CD  1 
ATOM   2900 O OE1 . GLU   B 2 61  ? 25.69807 -21.90407 -11.21642 1.000 120.51096 ? 154 GLU   B OE1 1 
ATOM   2901 O OE2 . GLU   B 2 61  ? 23.99569 -22.17024 -9.85644  1.000 121.53994 ? 154 GLU   B OE2 1 
ATOM   2902 N N   . VAL   B 2 62  ? 25.80351 -16.36190 -10.56485 1.000 88.93595  ? 155 VAL   B N   1 
ATOM   2903 C CA  . VAL   B 2 62  ? 25.77190 -15.39429 -9.47085  1.000 81.69007  ? 155 VAL   B CA  1 
ATOM   2904 C C   . VAL   B 2 62  ? 24.90593 -14.19862 -9.84486  1.000 91.70828  ? 155 VAL   B C   1 
ATOM   2905 O O   . VAL   B 2 62  ? 24.16465 -13.66355 -9.01071  1.000 86.21974  ? 155 VAL   B O   1 
ATOM   2906 C CB  . VAL   B 2 62  ? 27.20306 -14.96365 -9.09525  1.000 93.91642  ? 155 VAL   B CB  1 
ATOM   2907 C CG1 . VAL   B 2 62  ? 27.17609 -13.80332 -8.11095  1.000 85.05203  ? 155 VAL   B CG1 1 
ATOM   2908 C CG2 . VAL   B 2 62  ? 27.97337 -16.13426 -8.51045  1.000 100.30565 ? 155 VAL   B CG2 1 
ATOM   2909 N N   . CYS   B 2 63  ? 24.97517 -13.76863 -11.10755 1.000 87.16640  ? 156 CYS   B N   1 
ATOM   2910 C CA  . CYS   B 2 63  ? 24.17774 -12.62709 -11.54377 1.000 84.86884  ? 156 CYS   B CA  1 
ATOM   2911 C C   . CYS   B 2 63  ? 22.68689 -12.93705 -11.49218 1.000 86.36743  ? 156 CYS   B C   1 
ATOM   2912 O O   . CYS   B 2 63  ? 21.88134 -12.07550 -11.12317 1.000 83.56814  ? 156 CYS   B O   1 
ATOM   2913 C CB  . CYS   B 2 63  ? 24.59010 -12.20378 -12.95396 1.000 81.20856  ? 156 CYS   B CB  1 
ATOM   2914 S SG  . CYS   B 2 63  ? 26.17394 -11.33550 -13.04253 1.000 79.70901  ? 156 CYS   B SG  1 
ATOM   2915 N N   . GLU   B 2 64  ? 22.29882 -14.16396 -11.84971 1.000 85.08940  ? 157 GLU   B N   1 
ATOM   2916 C CA  . GLU   B 2 64  ? 20.88030 -14.50853 -11.86156 1.000 92.25559  ? 157 GLU   B CA  1 
ATOM   2917 C C   . GLU   B 2 64  ? 20.32778 -14.63645 -10.44724 1.000 91.49420  ? 157 GLU   B C   1 
ATOM   2918 O O   . GLU   B 2 64  ? 19.17462 -14.26997 -10.19181 1.000 95.02754  ? 157 GLU   B O   1 
ATOM   2919 C CB  . GLU   B 2 64  ? 20.65699 -15.80311 -12.64267 1.000 90.19365  ? 157 GLU   B CB  1 
ATOM   2920 C CG  . GLU   B 2 64  ? 19.18987 -16.12611 -12.88112 1.000 91.72429  ? 157 GLU   B CG  1 
ATOM   2921 C CD  . GLU   B 2 64  ? 18.99163 -17.44099 -13.60486 1.000 104.53250 ? 157 GLU   B CD  1 
ATOM   2922 O OE1 . GLU   B 2 64  ? 19.95679 -18.22885 -13.68200 1.000 102.46197 ? 157 GLU   B OE1 1 
ATOM   2923 O OE2 . GLU   B 2 64  ? 17.87089 -17.68666 -14.09725 1.000 110.48183 ? 157 GLU   B OE2 1 
ATOM   2924 N N   . VAL   B 2 65  ? 21.13181 -15.15933 -9.51735  1.000 92.76594  ? 158 VAL   B N   1 
ATOM   2925 C CA  . VAL   B 2 65  ? 20.67550 -15.31032 -8.13737  1.000 98.25246  ? 158 VAL   B CA  1 
ATOM   2926 C C   . VAL   B 2 65  ? 20.35937 -13.95034 -7.52896  1.000 93.12565  ? 158 VAL   B C   1 
ATOM   2927 O O   . VAL   B 2 65  ? 19.33996 -13.77849 -6.84919  1.000 94.07602  ? 158 VAL   B O   1 
ATOM   2928 C CB  . VAL   B 2 65  ? 21.72273 -16.07536 -7.30611  1.000 92.01997  ? 158 VAL   B CB  1 
ATOM   2929 C CG1 . VAL   B 2 65  ? 21.32924 -16.09072 -5.83646  1.000 101.63165 ? 158 VAL   B CG1 1 
ATOM   2930 C CG2 . VAL   B 2 65  ? 21.87889 -17.49496 -7.82836  1.000 91.20725  ? 158 VAL   B CG2 1 
ATOM   2931 N N   . TYR   B 2 66  ? 21.21741 -12.96274 -7.76961  1.000 92.18845  ? 159 TYR   B N   1 
ATOM   2932 C CA  . TYR   B 2 66  ? 20.99346 -11.60500 -7.29490  1.000 90.81115  ? 159 TYR   B CA  1 
ATOM   2933 C C   . TYR   B 2 66  ? 20.32044 -10.72360 -8.33867  1.000 83.22361  ? 159 TYR   B C   1 
ATOM   2934 O O   . TYR   B 2 66  ? 20.19163 -9.51408  -8.12045  1.000 81.78303  ? 159 TYR   B O   1 
ATOM   2935 C CB  . TYR   B 2 66  ? 22.31595 -10.98115 -6.84420  1.000 86.26984  ? 159 TYR   B CB  1 
ATOM   2936 C CG  . TYR   B 2 66  ? 22.86720 -11.61017 -5.58542  1.000 87.94999  ? 159 TYR   B CG  1 
ATOM   2937 C CD1 . TYR   B 2 66  ? 23.60275 -12.78660 -5.63872  1.000 97.88966  ? 159 TYR   B CD1 1 
ATOM   2938 C CD2 . TYR   B 2 66  ? 22.64311 -11.03367 -4.34190  1.000 84.42995  ? 159 TYR   B CD2 1 
ATOM   2939 C CE1 . TYR   B 2 66  ? 24.10345 -13.36911 -4.48993  1.000 96.89874  ? 159 TYR   B CE1 1 
ATOM   2940 C CE2 . TYR   B 2 66  ? 23.14183 -11.60911 -3.18660  1.000 94.43108  ? 159 TYR   B CE2 1 
ATOM   2941 C CZ  . TYR   B 2 66  ? 23.87160 -12.77673 -3.26681  1.000 95.46830  ? 159 TYR   B CZ  1 
ATOM   2942 O OH  . TYR   B 2 66  ? 24.37074 -13.35535 -2.12136  1.000 104.18957 ? 159 TYR   B OH  1 
ATOM   2943 N N   . LYS   B 2 67  ? 19.89691 -11.30611 -9.46307  1.000 92.65104  ? 160 LYS   B N   1 
ATOM   2944 C CA  . LYS   B 2 67  ? 19.11108 -10.60889 -10.48304 1.000 88.43378  ? 160 LYS   B CA  1 
ATOM   2945 C C   . LYS   B 2 67  ? 19.85244 -9.39009  -11.02762 1.000 79.56367  ? 160 LYS   B C   1 
ATOM   2946 O O   . LYS   B 2 67  ? 19.27293 -8.32015  -11.22427 1.000 75.97384  ? 160 LYS   B O   1 
ATOM   2947 C CB  . LYS   B 2 67  ? 17.73296 -10.22653 -9.93993  1.000 92.85606  ? 160 LYS   B CB  1 
ATOM   2948 C CG  . LYS   B 2 67  ? 16.97725 -11.41921 -9.37264  1.000 96.84416  ? 160 LYS   B CG  1 
ATOM   2949 C CD  . LYS   B 2 67  ? 15.61229 -11.03781 -8.83432  1.000 105.91535 ? 160 LYS   B CD  1 
ATOM   2950 C CE  . LYS   B 2 67  ? 14.89848 -12.25826 -8.27549  1.000 108.71838 ? 160 LYS   B CE  1 
ATOM   2951 N NZ  . LYS   B 2 67  ? 13.54508 -11.92992 -7.75589  1.000 110.45386 ? 160 LYS   B NZ  1 
ATOM   2952 N N   . LEU   B 2 68  ? 21.14678 -9.55751  -11.27652 1.000 84.37254  ? 161 LEU   B N   1 
ATOM   2953 C CA  . LEU   B 2 68  ? 21.95252 -8.49804  -11.86063 1.000 75.86232  ? 161 LEU   B CA  1 
ATOM   2954 C C   . LEU   B 2 68  ? 21.74382 -8.44996  -13.36962 1.000 72.98607  ? 161 LEU   B C   1 
ATOM   2955 O O   . LEU   B 2 68  ? 21.46258 -9.46568  -14.01205 1.000 74.94893  ? 161 LEU   B O   1 
ATOM   2956 C CB  . LEU   B 2 68  ? 23.43255 -8.71066  -11.53724 1.000 74.78811  ? 161 LEU   B CB  1 
ATOM   2957 C CG  . LEU   B 2 68  ? 24.00207 -8.05135  -10.27573 1.000 81.77659  ? 161 LEU   B CG  1 
ATOM   2958 C CD1 . LEU   B 2 68  ? 23.00711 -8.06248  -9.12279  1.000 68.80871  ? 161 LEU   B CD1 1 
ATOM   2959 C CD2 . LEU   B 2 68  ? 25.29397 -8.74111  -9.86516  1.000 70.21396  ? 161 LEU   B CD2 1 
ATOM   2960 N N   . HIS   B 2 69  ? 21.88306 -7.25277  -13.93284 1.000 70.05990  ? 162 HIS   B N   1 
ATOM   2961 C CA  . HIS   B 2 69  ? 21.63621 -7.05977  -15.35320 1.000 76.21066  ? 162 HIS   B CA  1 
ATOM   2962 C C   . HIS   B 2 69  ? 22.70642 -7.74992  -16.19715 1.000 69.99090  ? 162 HIS   B C   1 
ATOM   2963 O O   . HIS   B 2 69  ? 23.82341 -8.01794  -15.74402 1.000 70.11173  ? 162 HIS   B O   1 
ATOM   2964 C CB  . HIS   B 2 69  ? 21.58276 -5.56956  -15.69271 1.000 65.69416  ? 162 HIS   B CB  1 
ATOM   2965 C CG  . HIS   B 2 69  ? 20.34761 -4.88193  -15.19974 1.000 80.50891  ? 162 HIS   B CG  1 
ATOM   2966 N ND1 . HIS   B 2 69  ? 20.17041 -4.52247  -13.88092 1.000 81.18020  ? 162 HIS   B ND1 1 
ATOM   2967 C CD2 . HIS   B 2 69  ? 19.22564 -4.49160  -15.84975 1.000 83.35637  ? 162 HIS   B CD2 1 
ATOM   2968 C CE1 . HIS   B 2 69  ? 18.99378 -3.93846  -13.74013 1.000 80.94237  ? 162 HIS   B CE1 1 
ATOM   2969 N NE2 . HIS   B 2 69  ? 18.40027 -3.90767  -14.91974 1.000 81.54695  ? 162 HIS   B NE2 1 
ATOM   2970 N N   . ARG   B 2 70  ? 22.33915 -8.04359  -17.44902 1.000 78.60213  ? 163 ARG   B N   1 
ATOM   2971 C CA  . ARG   B 2 70  ? 23.28779 -8.64031  -18.38510 1.000 75.46939  ? 163 ARG   B CA  1 
ATOM   2972 C C   . ARG   B 2 70  ? 24.47170 -7.71518  -18.63028 1.000 64.03693  ? 163 ARG   B C   1 
ATOM   2973 O O   . ARG   B 2 70  ? 25.60777 -8.17640  -18.79174 1.000 68.92573  ? 163 ARG   B O   1 
ATOM   2974 C CB  . ARG   B 2 70  ? 22.59140 -8.96834  -19.70625 1.000 65.45872  ? 163 ARG   B CB  1 
ATOM   2975 C CG  . ARG   B 2 70  ? 21.37768 -9.87153  -19.57867 1.000 67.77987  ? 163 ARG   B CG  1 
ATOM   2976 C CD  . ARG   B 2 70  ? 20.78463 -10.17516 -20.94486 1.000 75.41804  ? 163 ARG   B CD  1 
ATOM   2977 N NE  . ARG   B 2 70  ? 19.63963 -11.07196 -20.85505 1.000 73.69963  ? 163 ARG   B NE  1 
ATOM   2978 C CZ  . ARG   B 2 70  ? 19.72902 -12.39400 -20.81517 1.000 74.96035  ? 163 ARG   B CZ  1 
ATOM   2979 N NH1 . ARG   B 2 70  ? 20.90002 -13.00872 -20.85585 1.000 74.31393  ? 163 ARG   B NH1 1 
ATOM   2980 N NH2 . ARG   B 2 70  ? 18.61618 -13.11739 -20.73024 1.000 82.44597  ? 163 ARG   B NH2 1 
ATOM   2981 N N   . GLU   B 2 71  ? 24.22119 -6.40382  -18.66643 1.000 65.73415  ? 164 GLU   B N   1 
ATOM   2982 C CA  . GLU   B 2 71  ? 25.30448 -5.43963  -18.82780 1.000 67.83022  ? 164 GLU   B CA  1 
ATOM   2983 C C   . GLU   B 2 71  ? 26.32830 -5.56786  -17.70736 1.000 69.11810  ? 164 GLU   B C   1 
ATOM   2984 O O   . GLU   B 2 71  ? 27.53304 -5.40726  -17.93532 1.000 66.06182  ? 164 GLU   B O   1 
ATOM   2985 C CB  . GLU   B 2 71  ? 24.73360 -4.02095  -18.87821 1.000 72.17044  ? 164 GLU   B CB  1 
ATOM   2986 C CG  . GLU   B 2 71  ? 25.77442 -2.91132  -18.80570 1.000 78.63221  ? 164 GLU   B CG  1 
ATOM   2987 C CD  . GLU   B 2 71  ? 26.57777 -2.76749  -20.08357 1.000 67.51469  ? 164 GLU   B CD  1 
ATOM   2988 O OE1 . GLU   B 2 71  ? 26.19636 -3.37813  -21.10413 1.000 70.87569  ? 164 GLU   B OE1 1 
ATOM   2989 O OE2 . GLU   B 2 71  ? 27.59123 -2.03747  -20.06854 1.000 70.83910  ? 164 GLU   B OE2 1 
ATOM   2990 N N   . THR   B 2 72  ? 25.86827 -5.87145  -16.49117 1.000 72.48662  ? 165 THR   B N   1 
ATOM   2991 C CA  . THR   B 2 72  ? 26.78543 -6.00642  -15.36436 1.000 69.55978  ? 165 THR   B CA  1 
ATOM   2992 C C   . THR   B 2 72  ? 27.72198 -7.19493  -15.55016 1.000 67.13676  ? 165 THR   B C   1 
ATOM   2993 O O   . THR   B 2 72  ? 28.91665 -7.10737  -15.24172 1.000 63.98120  ? 165 THR   B O   1 
ATOM   2994 C CB  . THR   B 2 72  ? 25.99734 -6.14167  -14.06133 1.000 71.04415  ? 165 THR   B CB  1 
ATOM   2995 O OG1 . THR   B 2 72  ? 25.15441 -4.99495  -13.89007 1.000 70.66768  ? 165 THR   B OG1 1 
ATOM   2996 C CG2 . THR   B 2 72  ? 26.94403 -6.24835  -12.87809 1.000 65.26966  ? 165 THR   B CG2 1 
ATOM   2997 N N   . PHE   B 2 73  ? 27.20037 -8.31583  -16.05417 1.000 73.60127  ? 166 PHE   B N   1 
ATOM   2998 C CA  . PHE   B 2 73  ? 28.04667 -9.48353  -16.27922 1.000 73.64795  ? 166 PHE   B CA  1 
ATOM   2999 C C   . PHE   B 2 73  ? 29.10198 -9.20315  -17.34169 1.000 72.47079  ? 166 PHE   B C   1 
ATOM   3000 O O   . PHE   B 2 73  ? 30.28449 -9.51513  -17.15752 1.000 72.64616  ? 166 PHE   B O   1 
ATOM   3001 C CB  . PHE   B 2 73  ? 27.20021 -10.68923 -16.68516 1.000 71.01264  ? 166 PHE   B CB  1 
ATOM   3002 C CG  . PHE   B 2 73  ? 28.00148 -11.78978 -17.31703 1.000 70.63427  ? 166 PHE   B CG  1 
ATOM   3003 C CD1 . PHE   B 2 73  ? 28.84325 -12.57375 -16.54745 1.000 74.30116  ? 166 PHE   B CD1 1 
ATOM   3004 C CD2 . PHE   B 2 73  ? 27.93381 -12.02576 -18.68103 1.000 75.42136  ? 166 PHE   B CD2 1 
ATOM   3005 C CE1 . PHE   B 2 73  ? 29.59491 -13.57767 -17.12026 1.000 80.11105  ? 166 PHE   B CE1 1 
ATOM   3006 C CE2 . PHE   B 2 73  ? 28.68406 -13.03108 -19.26065 1.000 73.95191  ? 166 PHE   B CE2 1 
ATOM   3007 C CZ  . PHE   B 2 73  ? 29.51726 -13.80595 -18.47812 1.000 81.09712  ? 166 PHE   B CZ  1 
ATOM   3008 N N   . TYR   B 2 74  ? 28.68910 -8.62523  -18.47218 1.000 62.87642  ? 167 TYR   B N   1 
ATOM   3009 C CA  . TYR   B 2 74  ? 29.62969 -8.38844  -19.55934 1.000 72.21681  ? 167 TYR   B CA  1 
ATOM   3010 C C   . TYR   B 2 74  ? 30.63739 -7.29997  -19.21842 1.000 67.26304  ? 167 TYR   B C   1 
ATOM   3011 O O   . TYR   B 2 74  ? 31.73161 -7.28236  -19.79349 1.000 69.59625  ? 167 TYR   B O   1 
ATOM   3012 C CB  . TYR   B 2 74  ? 28.87520 -8.04318  -20.84308 1.000 61.52535  ? 167 TYR   B CB  1 
ATOM   3013 C CG  . TYR   B 2 74  ? 28.37443 -9.26203  -21.58399 1.000 67.12362  ? 167 TYR   B CG  1 
ATOM   3014 C CD1 . TYR   B 2 74  ? 29.20055 -9.94581  -22.46663 1.000 73.33347  ? 167 TYR   B CD1 1 
ATOM   3015 C CD2 . TYR   B 2 74  ? 27.08326 -9.73791  -21.39349 1.000 67.00043  ? 167 TYR   B CD2 1 
ATOM   3016 C CE1 . TYR   B 2 74  ? 28.75425 -11.06315 -23.14355 1.000 69.01503  ? 167 TYR   B CE1 1 
ATOM   3017 C CE2 . TYR   B 2 74  ? 26.62727 -10.85597 -22.06763 1.000 67.70841  ? 167 TYR   B CE2 1 
ATOM   3018 C CZ  . TYR   B 2 74  ? 27.46759 -11.51394 -22.94164 1.000 70.22267  ? 167 TYR   B CZ  1 
ATOM   3019 O OH  . TYR   B 2 74  ? 27.02149 -12.62782 -23.61658 1.000 73.57295  ? 167 TYR   B OH  1 
ATOM   3020 N N   . LEU   B 2 75  ? 30.29982 -6.39739  -18.29532 1.000 67.00871  ? 168 LEU   B N   1 
ATOM   3021 C CA  . LEU   B 2 75  ? 31.31033 -5.49780  -17.75126 1.000 65.91831  ? 168 LEU   B CA  1 
ATOM   3022 C C   . LEU   B 2 75  ? 32.35614 -6.28021  -16.96893 1.000 67.34155  ? 168 LEU   B C   1 
ATOM   3023 O O   . LEU   B 2 75  ? 33.56092 -6.04444  -17.11056 1.000 70.19693  ? 168 LEU   B O   1 
ATOM   3024 C CB  . LEU   B 2 75  ? 30.65648 -4.43827  -16.86375 1.000 68.47272  ? 168 LEU   B CB  1 
ATOM   3025 C CG  . LEU   B 2 75  ? 29.92674 -3.27662  -17.53858 1.000 65.34764  ? 168 LEU   B CG  1 
ATOM   3026 C CD1 . LEU   B 2 75  ? 29.23053 -2.40859  -16.50156 1.000 67.35740  ? 168 LEU   B CD1 1 
ATOM   3027 C CD2 . LEU   B 2 75  ? 30.89540 -2.44898  -18.36029 1.000 71.95347  ? 168 LEU   B CD2 1 
ATOM   3028 N N   . ALA   B 2 76  ? 31.90758 -7.22261  -16.13482 1.000 67.85327  ? 169 ALA   B N   1 
ATOM   3029 C CA  . ALA   B 2 76  ? 32.83899 -8.04332  -15.36711 1.000 74.33633  ? 169 ALA   B CA  1 
ATOM   3030 C C   . ALA   B 2 76  ? 33.69505 -8.91025  -16.28078 1.000 70.41131  ? 169 ALA   B C   1 
ATOM   3031 O O   . ALA   B 2 76  ? 34.89174 -9.09612  -16.02928 1.000 77.65015  ? 169 ALA   B O   1 
ATOM   3032 C CB  . ALA   B 2 76  ? 32.07493 -8.91256  -14.36865 1.000 71.29805  ? 169 ALA   B CB  1 
ATOM   3033 N N   . GLN   B 2 77  ? 33.09755 -9.45732  -17.34220 1.000 71.42017  ? 170 GLN   B N   1 
ATOM   3034 C CA  . GLN   B 2 77  ? 33.86670 -10.24275 -18.30231 1.000 72.50729  ? 170 GLN   B CA  1 
ATOM   3035 C C   . GLN   B 2 77  ? 34.93107 -9.38834  -18.97913 1.000 77.19676  ? 170 GLN   B C   1 
ATOM   3036 O O   . GLN   B 2 77  ? 36.08250 -9.81322  -19.13025 1.000 80.44759  ? 170 GLN   B O   1 
ATOM   3037 C CB  . GLN   B 2 77  ? 32.93070 -10.86639 -19.33933 1.000 77.44991  ? 170 GLN   B CB  1 
ATOM   3038 C CG  . GLN   B 2 77  ? 33.63688 -11.45817 -20.55451 1.000 78.52190  ? 170 GLN   B CG  1 
ATOM   3039 C CD  . GLN   B 2 77  ? 33.73710 -10.47851 -21.71217 1.000 74.57628  ? 170 GLN   B CD  1 
ATOM   3040 O OE1 . GLN   B 2 77  ? 32.79956 -9.72954  -21.98993 1.000 75.67745  ? 170 GLN   B OE1 1 
ATOM   3041 N NE2 . GLN   B 2 77  ? 34.87961 -10.47778 -22.39049 1.000 82.57925  ? 170 GLN   B NE2 1 
ATOM   3042 N N   . ASP   B 2 78  ? 34.56176 -8.17440  -19.39500 1.000 75.04541  ? 171 ASP   B N   1 
ATOM   3043 C CA  . ASP   B 2 78  ? 35.52291 -7.29912  -20.05836 1.000 73.94826  ? 171 ASP   B CA  1 
ATOM   3044 C C   . ASP   B 2 78  ? 36.60091 -6.82625  -19.09074 1.000 76.01763  ? 171 ASP   B C   1 
ATOM   3045 O O   . ASP   B 2 78  ? 37.77358 -6.71362  -19.46735 1.000 71.85477  ? 171 ASP   B O   1 
ATOM   3046 C CB  . ASP   B 2 78  ? 34.80498 -6.10525  -20.68669 1.000 73.53913  ? 171 ASP   B CB  1 
ATOM   3047 C CG  . ASP   B 2 78  ? 35.74279 -5.21528  -21.47768 1.000 74.85126  ? 171 ASP   B CG  1 
ATOM   3048 O OD1 . ASP   B 2 78  ? 36.20678 -5.64566  -22.55450 1.000 86.45409  ? 171 ASP   B OD1 1 
ATOM   3049 O OD2 . ASP   B 2 78  ? 36.02093 -4.08722  -21.02130 1.000 82.94160  ? 171 ASP   B OD2 1 
ATOM   3050 N N   . PHE   B 2 79  ? 36.22374 -6.53829  -17.84212 1.000 69.62240  ? 172 PHE   B N   1 
ATOM   3051 C CA  . PHE   B 2 79  ? 37.21782 -6.16100  -16.84187 1.000 76.38183  ? 172 PHE   B CA  1 
ATOM   3052 C C   . PHE   B 2 79  ? 38.18833 -7.30385  -16.57753 1.000 77.23150  ? 172 PHE   B C   1 
ATOM   3053 O O   . PHE   B 2 79  ? 39.38964 -7.07920  -16.39233 1.000 77.42624  ? 172 PHE   B O   1 
ATOM   3054 C CB  . PHE   B 2 79  ? 36.53237 -5.73941  -15.54160 1.000 69.15313  ? 172 PHE   B CB  1 
ATOM   3055 C CG  . PHE   B 2 79  ? 35.70873 -4.48805  -15.66026 1.000 72.05405  ? 172 PHE   B CG  1 
ATOM   3056 C CD1 . PHE   B 2 79  ? 35.87621 -3.62306  -16.72974 1.000 67.10529  ? 172 PHE   B CD1 1 
ATOM   3057 C CD2 . PHE   B 2 79  ? 34.76729 -4.17561  -14.69372 1.000 67.54736  ? 172 PHE   B CD2 1 
ATOM   3058 C CE1 . PHE   B 2 79  ? 35.11614 -2.47308  -16.83440 1.000 64.16389  ? 172 PHE   B CE1 1 
ATOM   3059 C CE2 . PHE   B 2 79  ? 34.00594 -3.02750  -14.79139 1.000 62.91051  ? 172 PHE   B CE2 1 
ATOM   3060 C CZ  . PHE   B 2 79  ? 34.18019 -2.17479  -15.86315 1.000 67.75294  ? 172 PHE   B CZ  1 
ATOM   3061 N N   . PHE   B 2 80  ? 37.68372 -8.53851  -16.55805 1.000 74.27733  ? 173 PHE   B N   1 
ATOM   3062 C CA  . PHE   B 2 80  ? 38.54230 -9.69159  -16.31108 1.000 85.40245  ? 173 PHE   B CA  1 
ATOM   3063 C C   . PHE   B 2 80  ? 39.52507 -9.90251  -17.45702 1.000 83.89722  ? 173 PHE   B C   1 
ATOM   3064 O O   . PHE   B 2 80  ? 40.72248 -10.10846 -17.23062 1.000 83.68107  ? 173 PHE   B O   1 
ATOM   3065 C CB  . PHE   B 2 80  ? 37.68465 -10.93942 -16.09329 1.000 84.53947  ? 173 PHE   B CB  1 
ATOM   3066 C CG  . PHE   B 2 80  ? 38.47858 -12.20734 -15.96039 1.000 87.94939  ? 173 PHE   B CG  1 
ATOM   3067 C CD1 . PHE   B 2 80  ? 39.15432 -12.49765 -14.78648 1.000 96.38712  ? 173 PHE   B CD1 1 
ATOM   3068 C CD2 . PHE   B 2 80  ? 38.54252 -13.11335 -17.00629 1.000 90.77682  ? 173 PHE   B CD2 1 
ATOM   3069 C CE1 . PHE   B 2 80  ? 39.88593 -13.66509 -14.65966 1.000 92.43067  ? 173 PHE   B CE1 1 
ATOM   3070 C CE2 . PHE   B 2 80  ? 39.27129 -14.28325 -16.88607 1.000 96.07465  ? 173 PHE   B CE2 1 
ATOM   3071 C CZ  . PHE   B 2 80  ? 39.94363 -14.55937 -15.71098 1.000 88.53974  ? 173 PHE   B CZ  1 
ATOM   3072 N N   . ASP   B 2 81  ? 39.03825 -9.84379  -18.69869 1.000 83.33588  ? 174 ASP   B N   1 
ATOM   3073 C CA  . ASP   B 2 81  ? 39.90014 -10.12751 -19.84258 1.000 86.72296  ? 174 ASP   B CA  1 
ATOM   3074 C C   . ASP   B 2 81  ? 40.96185 -9.04941  -20.02732 1.000 88.68973  ? 174 ASP   B C   1 
ATOM   3075 O O   . ASP   B 2 81  ? 42.12539 -9.36094  -20.30730 1.000 94.71008  ? 174 ASP   B O   1 
ATOM   3076 C CB  . ASP   B 2 81  ? 39.05989 -10.27632 -21.11086 1.000 83.09705  ? 174 ASP   B CB  1 
ATOM   3077 C CG  . ASP   B 2 81  ? 38.23442 -11.55036 -21.11904 1.000 88.44097  ? 174 ASP   B CG  1 
ATOM   3078 O OD1 . ASP   B 2 81  ? 38.67400 -12.55010 -20.51376 1.000 95.04809  ? 174 ASP   B OD1 1 
ATOM   3079 O OD2 . ASP   B 2 81  ? 37.14685 -11.55342 -21.73441 1.000 91.75038  ? 174 ASP   B OD2 1 
ATOM   3080 N N   . ARG   B 2 82  ? 40.58527 -7.77669  -19.87792 1.000 78.26110  ? 175 ARG   B N   1 
ATOM   3081 C CA  . ARG   B 2 82  ? 41.55628 -6.70369  -20.06819 1.000 82.70671  ? 175 ARG   B CA  1 
ATOM   3082 C C   . ARG   B 2 82  ? 42.54761 -6.62572  -18.91419 1.000 90.72916  ? 175 ARG   B C   1 
ATOM   3083 O O   . ARG   B 2 82  ? 43.68026 -6.16960  -19.10578 1.000 97.99858  ? 175 ARG   B O   1 
ATOM   3084 C CB  . ARG   B 2 82  ? 40.84208 -5.36268  -20.25118 1.000 79.08524  ? 175 ARG   B CB  1 
ATOM   3085 C CG  . ARG   B 2 82  ? 40.19085 -5.19536  -21.61630 1.000 76.55657  ? 175 ARG   B CG  1 
ATOM   3086 C CD  . ARG   B 2 82  ? 39.75706 -3.75815  -21.87999 1.000 72.43794  ? 175 ARG   B CD  1 
ATOM   3087 N NE  . ARG   B 2 82  ? 38.70471 -3.31736  -20.97211 1.000 78.34869  ? 175 ARG   B NE  1 
ATOM   3088 C CZ  . ARG   B 2 82  ? 38.84668 -2.36375  -20.06132 1.000 69.68608  ? 175 ARG   B CZ  1 
ATOM   3089 N NH1 . ARG   B 2 82  ? 39.98772 -1.70941  -19.91607 1.000 81.25909  ? 175 ARG   B NH1 1 
ATOM   3090 N NH2 . ARG   B 2 82  ? 37.81382 -2.05080  -19.28408 1.000 70.76583  ? 175 ARG   B NH2 1 
ATOM   3091 N N   . TYR   B 2 83  ? 42.14951 -7.06337  -17.71692 1.000 87.80008  ? 176 TYR   B N   1 
ATOM   3092 C CA  . TYR   B 2 83  ? 43.07612 -7.05431  -16.58892 1.000 82.93411  ? 176 TYR   B CA  1 
ATOM   3093 C C   . TYR   B 2 83  ? 44.13133 -8.14261  -16.73207 1.000 93.09773  ? 176 TYR   B C   1 
ATOM   3094 O O   . TYR   B 2 83  ? 45.31461 -7.90540  -16.46257 1.000 98.00302  ? 176 TYR   B O   1 
ATOM   3095 C CB  . TYR   B 2 83  ? 42.31406 -7.21722  -15.27387 1.000 85.36247  ? 176 TYR   B CB  1 
ATOM   3096 C CG  . TYR   B 2 83  ? 43.20510 -7.42781  -14.06822 1.000 87.42097  ? 176 TYR   B CG  1 
ATOM   3097 C CD1 . TYR   B 2 83  ? 43.85489 -6.35908  -13.46530 1.000 89.51607  ? 176 TYR   B CD1 1 
ATOM   3098 C CD2 . TYR   B 2 83  ? 43.38949 -8.69509  -13.52858 1.000 90.08526  ? 176 TYR   B CD2 1 
ATOM   3099 C CE1 . TYR   B 2 83  ? 44.66843 -6.54634  -12.36200 1.000 91.75535  ? 176 TYR   B CE1 1 
ATOM   3100 C CE2 . TYR   B 2 83  ? 44.20111 -8.89215  -12.42527 1.000 95.78040  ? 176 TYR   B CE2 1 
ATOM   3101 C CZ  . TYR   B 2 83  ? 44.83747 -7.81420  -11.84598 1.000 97.70786  ? 176 TYR   B CZ  1 
ATOM   3102 O OH  . TYR   B 2 83  ? 45.64617 -8.00471  -10.74891 1.000 93.12159  ? 176 TYR   B OH  1 
ATOM   3103 N N   . MET   B 2 84  ? 43.72332 -9.34392  -17.14895 1.000 93.10150  ? 177 MET   B N   1 
ATOM   3104 C CA  . MET   B 2 84  ? 44.68792 -10.42257 -17.33224 1.000 93.84126  ? 177 MET   B CA  1 
ATOM   3105 C C   . MET   B 2 84  ? 45.65990 -10.11477 -18.46259 1.000 100.82474 ? 177 MET   B C   1 
ATOM   3106 O O   . MET   B 2 84  ? 46.79428 -10.60594 -18.45547 1.000 106.16970 ? 177 MET   B O   1 
ATOM   3107 C CB  . MET   B 2 84  ? 43.96152 -11.74015 -17.59969 1.000 93.91163  ? 177 MET   B CB  1 
ATOM   3108 C CG  . MET   B 2 84  ? 42.96709 -12.13280 -16.52171 1.000 92.69078  ? 177 MET   B CG  1 
ATOM   3109 S SD  . MET   B 2 84  ? 43.74136 -12.60252 -14.96483 1.000 101.45781 ? 177 MET   B SD  1 
ATOM   3110 C CE  . MET   B 2 84  ? 44.30156 -14.25942 -15.35007 1.000 103.32682 ? 177 MET   B CE  1 
ATOM   3111 N N   . ALA   B 2 85  ? 45.23822 -9.30703  -19.43994 1.000 96.96233  ? 178 ALA   B N   1 
ATOM   3112 C CA  . ALA   B 2 85  ? 46.14620 -8.87560  -20.49568 1.000 91.68056  ? 178 ALA   B CA  1 
ATOM   3113 C C   . ALA   B 2 85  ? 47.24575 -7.96255  -19.97070 1.000 102.61236 ? 178 ALA   B C   1 
ATOM   3114 O O   . ALA   B 2 85  ? 48.27151 -7.79973  -20.63982 1.000 102.80182 ? 178 ALA   B O   1 
ATOM   3115 C CB  . ALA   B 2 85  ? 45.36719 -8.16958  -21.60698 1.000 94.17868  ? 178 ALA   B CB  1 
ATOM   3116 N N   . THR   B 2 86  ? 47.05622 -7.36688  -18.79492 1.000 95.68926  ? 179 THR   B N   1 
ATOM   3117 C CA  . THR   B 2 86  ? 48.06826 -6.52066  -18.18003 1.000 97.60897  ? 179 THR   B CA  1 
ATOM   3118 C C   . THR   B 2 86  ? 48.93191 -7.26447  -17.17011 1.000 99.13840  ? 179 THR   B C   1 
ATOM   3119 O O   . THR   B 2 86  ? 49.97323 -6.73788  -16.76286 1.000 103.17559 ? 179 THR   B O   1 
ATOM   3120 C CB  . THR   B 2 86  ? 47.40898 -5.32249  -17.48753 1.000 98.08390  ? 179 THR   B CB  1 
ATOM   3121 O OG1 . THR   B 2 86  ? 46.64767 -5.77678  -16.36108 1.000 94.85038  ? 179 THR   B OG1 1 
ATOM   3122 C CG2 . THR   B 2 86  ? 46.48726 -4.59487  -18.45196 1.000 92.06819  ? 179 THR   B CG2 1 
ATOM   3123 N N   . GLN   B 2 87  ? 48.53317 -8.46434  -16.76142 1.000 95.98016  ? 180 GLN   B N   1 
ATOM   3124 C CA  . GLN   B 2 87  ? 49.23393 -9.22723  -15.74030 1.000 100.32802 ? 180 GLN   B CA  1 
ATOM   3125 C C   . GLN   B 2 87  ? 49.89442 -10.45588 -16.35192 1.000 106.76395 ? 180 GLN   B C   1 
ATOM   3126 O O   . GLN   B 2 87  ? 49.63452 -10.83254 -17.49781 1.000 112.15725 ? 180 GLN   B O   1 
ATOM   3127 C CB  . GLN   B 2 87  ? 48.27330 -9.63850  -14.61858 1.000 97.19801  ? 180 GLN   B CB  1 
ATOM   3128 C CG  . GLN   B 2 87  ? 47.61881 -8.46500  -13.91346 1.000 96.22051  ? 180 GLN   B CG  1 
ATOM   3129 C CD  . GLN   B 2 87  ? 48.63302 -7.51794  -13.30537 1.000 96.84265  ? 180 GLN   B CD  1 
ATOM   3130 O OE1 . GLN   B 2 87  ? 49.58800 -7.94555  -12.65732 1.000 106.39663 ? 180 GLN   B OE1 1 
ATOM   3131 N NE2 . GLN   B 2 87  ? 48.43569 -6.22276  -13.51943 1.000 97.50317  ? 180 GLN   B NE2 1 
ATOM   3132 N N   . GLU   B 2 88  ? 50.76551 -11.07881 -15.56030 1.000 109.64770 ? 181 GLU   B N   1 
ATOM   3133 C CA  . GLU   B 2 88  ? 51.50292 -12.26092 -15.97771 1.000 119.04638 ? 181 GLU   B CA  1 
ATOM   3134 C C   . GLU   B 2 88  ? 51.52820 -13.26716 -14.83719 1.000 118.38526 ? 181 GLU   B C   1 
ATOM   3135 O O   . GLU   B 2 88  ? 51.60215 -12.89322 -13.66366 1.000 123.22354 ? 181 GLU   B O   1 
ATOM   3136 C CB  . GLU   B 2 88  ? 52.94291 -11.91944 -16.39096 1.000 124.25711 ? 181 GLU   B CB  1 
ATOM   3137 C CG  . GLU   B 2 88  ? 53.05892 -10.87949 -17.49323 1.000 126.89449 ? 181 GLU   B CG  1 
ATOM   3138 C CD  . GLU   B 2 88  ? 54.49412 -10.46223 -17.74670 1.000 131.12174 ? 181 GLU   B CD  1 
ATOM   3139 O OE1 . GLU   B 2 88  ? 55.40066 -11.02135 -17.09378 1.000 123.05323 ? 181 GLU   B OE1 1 
ATOM   3140 O OE2 . GLU   B 2 88  ? 54.71615 -9.57421  -18.59634 1.000 138.59092 ? 181 GLU   B OE2 1 
ATOM   3141 N N   . ASN   B 2 89  ? 51.46445 -14.55038 -15.20026 1.000 120.33473 ? 182 ASN   B N   1 
ATOM   3142 C CA  . ASN   B 2 89  ? 51.59827 -15.65878 -14.25856 1.000 121.57920 ? 182 ASN   B CA  1 
ATOM   3143 C C   . ASN   B 2 89  ? 50.57756 -15.58358 -13.12786 1.000 122.30494 ? 182 ASN   B C   1 
ATOM   3144 O O   . ASN   B 2 89  ? 50.87221 -15.05271 -12.05209 1.000 131.82357 ? 182 ASN   B O   1 
ATOM   3145 C CB  . ASN   B 2 89  ? 53.01742 -15.69906 -13.68337 1.000 126.46707 ? 182 ASN   B CB  1 
ATOM   3146 C CG  . ASN   B 2 89  ? 54.08522 -15.66711 -14.76082 1.000 134.39931 ? 182 ASN   B CG  1 
ATOM   3147 O OD1 . ASN   B 2 89  ? 54.36100 -16.67674 -15.40902 1.000 129.61348 ? 182 ASN   B OD1 1 
ATOM   3148 N ND2 . ASN   B 2 89  ? 54.69744 -14.50406 -14.95228 1.000 135.62260 ? 182 ASN   B ND2 1 
ATOM   3149 N N   . VAL   B 2 90  ? 49.38245 -16.12366 -13.35585 1.000 115.87815 ? 183 VAL   B N   1 
ATOM   3150 C CA  . VAL   B 2 90  ? 48.31293 -16.14029 -12.36519 1.000 113.87121 ? 183 VAL   B CA  1 
ATOM   3151 C C   . VAL   B 2 90  ? 47.90652 -17.58618 -12.11258 1.000 108.00529 ? 183 VAL   B C   1 
ATOM   3152 O O   . VAL   B 2 90  ? 47.84217 -18.39518 -13.04473 1.000 125.50822 ? 183 VAL   B O   1 
ATOM   3153 C CB  . VAL   B 2 90  ? 47.10600 -15.29141 -12.82140 1.000 118.22783 ? 183 VAL   B CB  1 
ATOM   3154 C CG1 . VAL   B 2 90  ? 45.91704 -15.49051 -11.89392 1.000 112.40498 ? 183 VAL   B CG1 1 
ATOM   3155 C CG2 . VAL   B 2 90  ? 47.48900 -13.82054 -12.87306 1.000 113.48258 ? 183 VAL   B CG2 1 
ATOM   3156 N N   . VAL   B 2 91  ? 47.64295 -17.90943 -10.84614 1.000 123.78754 ? 184 VAL   B N   1 
ATOM   3157 C CA  . VAL   B 2 91  ? 47.29886 -19.26666 -10.43604 1.000 131.70539 ? 184 VAL   B CA  1 
ATOM   3158 C C   . VAL   B 2 91  ? 45.78859 -19.45906 -10.52950 1.000 127.06822 ? 184 VAL   B C   1 
ATOM   3159 O O   . VAL   B 2 91  ? 45.04403 -18.50411 -10.77843 1.000 125.46503 ? 184 VAL   B O   1 
ATOM   3160 C CB  . VAL   B 2 91  ? 47.81836 -19.55171 -9.01298  1.000 127.20979 ? 184 VAL   B CB  1 
ATOM   3161 C CG1 . VAL   B 2 91  ? 46.87584 -18.96680 -7.96882  1.000 131.07775 ? 184 VAL   B CG1 1 
ATOM   3162 C CG2 . VAL   B 2 91  ? 48.04306 -21.04650 -8.79472  1.000 129.21061 ? 184 VAL   B CG2 1 
ATOM   3163 N N   . LYS   B 2 92  ? 45.32819 -20.69830 -10.33363 1.000 134.24837 ? 185 LYS   B N   1 
ATOM   3164 C CA  . LYS   B 2 92  ? 43.90194 -20.99395 -10.43255 1.000 134.17669 ? 185 LYS   B CA  1 
ATOM   3165 C C   . LYS   B 2 92  ? 43.12489 -20.41119 -9.25746  1.000 128.04503 ? 185 LYS   B C   1 
ATOM   3166 O O   . LYS   B 2 92  ? 42.03162 -19.86329 -9.44117  1.000 126.11642 ? 185 LYS   B O   1 
ATOM   3167 C CB  . LYS   B 2 92  ? 43.68924 -22.50528 -10.51138 1.000 137.52657 ? 185 LYS   B CB  1 
ATOM   3168 C CG  . LYS   B 2 92  ? 44.40200 -23.17787 -11.67139 1.000 139.18497 ? 185 LYS   B CG  1 
ATOM   3169 C CD  . LYS   B 2 92  ? 44.56064 -24.66993 -11.42342 1.000 145.16041 ? 185 LYS   B CD  1 
ATOM   3170 C CE  . LYS   B 2 92  ? 43.22720 -25.32969 -11.10972 1.000 148.45636 ? 185 LYS   B CE  1 
ATOM   3171 N NZ  . LYS   B 2 92  ? 43.38676 -26.77983 -10.80872 1.000 153.13374 ? 185 LYS   B NZ  1 
ATOM   3172 N N   . THR   B 2 93  ? 43.66758 -20.52425 -8.04162  1.000 129.32084 ? 186 THR   B N   1 
ATOM   3173 C CA  . THR   B 2 93  ? 42.95443 -20.05533 -6.85778  1.000 129.96439 ? 186 THR   B CA  1 
ATOM   3174 C C   . THR   B 2 93  ? 42.81168 -18.53914 -6.82332  1.000 128.57844 ? 186 THR   B C   1 
ATOM   3175 O O   . THR   B 2 93  ? 41.98586 -18.02491 -6.06131  1.000 121.60598 ? 186 THR   B O   1 
ATOM   3176 C CB  . THR   B 2 93  ? 43.65854 -20.53772 -5.58785  1.000 134.00644 ? 186 THR   B CB  1 
ATOM   3177 O OG1 . THR   B 2 93  ? 45.00411 -20.04579 -5.56593  1.000 136.01302 ? 186 THR   B OG1 1 
ATOM   3178 C CG2 . THR   B 2 93  ? 43.67787 -22.05936 -5.53512  1.000 131.30889 ? 186 THR   B CG2 1 
ATOM   3179 N N   . LEU   B 2 94  ? 43.59409 -17.81535 -7.62342  1.000 127.38937 ? 187 LEU   B N   1 
ATOM   3180 C CA  . LEU   B 2 94  ? 43.45588 -16.36909 -7.72425  1.000 123.39049 ? 187 LEU   B CA  1 
ATOM   3181 C C   . LEU   B 2 94  ? 42.36987 -15.95164 -8.70853  1.000 120.35925 ? 187 LEU   B C   1 
ATOM   3182 O O   . LEU   B 2 94  ? 41.98776 -14.77666 -8.72436  1.000 119.22567 ? 187 LEU   B O   1 
ATOM   3183 C CB  . LEU   B 2 94  ? 44.79859 -15.74722 -8.12686  1.000 124.41299 ? 187 LEU   B CB  1 
ATOM   3184 C CG  . LEU   B 2 94  ? 44.97737 -14.23346 -7.98190  1.000 123.95292 ? 187 LEU   B CG  1 
ATOM   3185 C CD1 . LEU   B 2 94  ? 44.67838 -13.79188 -6.55799  1.000 117.76378 ? 187 LEU   B CD1 1 
ATOM   3186 C CD2 . LEU   B 2 94  ? 46.38264 -13.81757 -8.39040  1.000 120.54793 ? 187 LEU   B CD2 1 
ATOM   3187 N N   . LEU   B 2 95  ? 41.85274 -16.88569 -9.51116  1.000 119.25744 ? 188 LEU   B N   1 
ATOM   3188 C CA  . LEU   B 2 95  ? 40.85379 -16.53605 -10.51686 1.000 108.74203 ? 188 LEU   B CA  1 
ATOM   3189 C C   . LEU   B 2 95  ? 39.52651 -16.14340 -9.87939  1.000 101.03148 ? 188 LEU   B C   1 
ATOM   3190 O O   . LEU   B 2 95  ? 38.87347 -15.19567 -10.33174 1.000 103.55059 ? 188 LEU   B O   1 
ATOM   3191 C CB  . LEU   B 2 95  ? 40.65311 -17.70238 -11.48410 1.000 117.75475 ? 188 LEU   B CB  1 
ATOM   3192 C CG  . LEU   B 2 95  ? 41.82994 -18.05124 -12.39394 1.000 113.01889 ? 188 LEU   B CG  1 
ATOM   3193 C CD1 . LEU   B 2 95  ? 41.50475 -19.28118 -13.22576 1.000 109.61761 ? 188 LEU   B CD1 1 
ATOM   3194 C CD2 . LEU   B 2 95  ? 42.17511 -16.87059 -13.28772 1.000 99.04256  ? 188 LEU   B CD2 1 
ATOM   3195 N N   . GLN   B 2 96  ? 39.10661 -16.86123 -8.83407  1.000 102.77515 ? 189 GLN   B N   1 
ATOM   3196 C CA  . GLN   B 2 96  ? 37.80926 -16.58265 -8.22481  1.000 104.99768 ? 189 GLN   B CA  1 
ATOM   3197 C C   . GLN   B 2 96  ? 37.77329 -15.18870 -7.61052  1.000 107.72032 ? 189 GLN   B C   1 
ATOM   3198 O O   . GLN   B 2 96  ? 36.73589 -14.51627 -7.63904  1.000 98.90364  ? 189 GLN   B O   1 
ATOM   3199 C CB  . GLN   B 2 96  ? 37.48188 -17.64184 -7.17207  1.000 99.14669  ? 189 GLN   B CB  1 
ATOM   3200 C CG  . GLN   B 2 96  ? 36.06521 -17.54626 -6.62119  1.000 103.98182 ? 189 GLN   B CG  1 
ATOM   3201 C CD  . GLN   B 2 96  ? 35.78844 -18.56312 -5.52946  1.000 115.52023 ? 189 GLN   B CD  1 
ATOM   3202 O OE1 . GLN   B 2 96  ? 36.70381 -19.02725 -4.84970  1.000 126.28554 ? 189 GLN   B OE1 1 
ATOM   3203 N NE2 . GLN   B 2 96  ? 34.51952 -18.91603 -5.35796  1.000 106.95663 ? 189 GLN   B NE2 1 
ATOM   3204 N N   . LEU   B 2 97  ? 38.89896 -14.73425 -7.05564  1.000 98.21493  ? 190 LEU   B N   1 
ATOM   3205 C CA  . LEU   B 2 97  ? 38.94212 -13.40070 -6.46478  1.000 104.44508 ? 190 LEU   B CA  1 
ATOM   3206 C C   . LEU   B 2 97  ? 38.89476 -12.31886 -7.53711  1.000 99.39974  ? 190 LEU   B C   1 
ATOM   3207 O O   . LEU   B 2 97  ? 38.21421 -11.30038 -7.36910  1.000 94.69042  ? 190 LEU   B O   1 
ATOM   3208 C CB  . LEU   B 2 97  ? 40.19461 -13.25009 -5.60149  1.000 97.98830  ? 190 LEU   B CB  1 
ATOM   3209 C CG  . LEU   B 2 97  ? 40.41172 -11.87695 -4.96311  1.000 90.41561  ? 190 LEU   B CG  1 
ATOM   3210 C CD1 . LEU   B 2 97  ? 39.23312 -11.50093 -4.07845  1.000 96.44740  ? 190 LEU   B CD1 1 
ATOM   3211 C CD2 . LEU   B 2 97  ? 41.71033 -11.85237 -4.17218  1.000 103.54304 ? 190 LEU   B CD2 1 
ATOM   3212 N N   . ILE   B 2 98  ? 39.60770 -12.52211 -8.64683  1.000 89.17053  ? 191 ILE   B N   1 
ATOM   3213 C CA  . ILE   B 2 98  ? 39.60213 -11.53595 -9.72299  1.000 101.25969 ? 191 ILE   B CA  1 
ATOM   3214 C C   . ILE   B 2 98  ? 38.22304 -11.45403 -10.36548 1.000 96.91628  ? 191 ILE   B C   1 
ATOM   3215 O O   . ILE   B 2 98  ? 37.75310 -10.36754 -10.72437 1.000 85.37978  ? 191 ILE   B O   1 
ATOM   3216 C CB  . ILE   B 2 98  ? 40.69175 -11.87038 -10.75841 1.000 104.26631 ? 191 ILE   B CB  1 
ATOM   3217 C CG1 . ILE   B 2 98  ? 42.07220 -11.87025 -10.10083 1.000 98.30777  ? 191 ILE   B CG1 1 
ATOM   3218 C CG2 . ILE   B 2 98  ? 40.65638 -10.88290 -11.91481 1.000 93.77855  ? 191 ILE   B CG2 1 
ATOM   3219 C CD1 . ILE   B 2 98  ? 43.19823 -12.21601 -11.04987 1.000 98.87319  ? 191 ILE   B CD1 1 
ATOM   3220 N N   . GLY   B 2 99  ? 37.54851 -12.59555 -10.51065 1.000 94.25725  ? 192 GLY   B N   1 
ATOM   3221 C CA  . GLY   B 2 99  ? 36.23975 -12.59247 -11.14506 1.000 90.02454  ? 192 GLY   B CA  1 
ATOM   3222 C C   . GLY   B 2 99  ? 35.17310 -11.93977 -10.28561 1.000 92.18096  ? 192 GLY   B C   1 
ATOM   3223 O O   . GLY   B 2 99  ? 34.38697 -11.11954 -10.76767 1.000 91.95528  ? 192 GLY   B O   1 
ATOM   3224 N N   . ILE   B 2 100 ? 35.13121 -12.29317 -8.99856  1.000 84.48659  ? 193 ILE   B N   1 
ATOM   3225 C CA  . ILE   B 2 100 ? 34.09963 -11.74521 -8.12299  1.000 92.35417  ? 193 ILE   B CA  1 
ATOM   3226 C C   . ILE   B 2 100 ? 34.33858 -10.26229 -7.86120  1.000 88.46911  ? 193 ILE   B C   1 
ATOM   3227 O O   . ILE   B 2 100 ? 33.38695 -9.50474  -7.63316  1.000 79.13409  ? 193 ILE   B O   1 
ATOM   3228 C CB  . ILE   B 2 100 ? 34.02283 -12.55127 -6.81125  1.000 99.57190  ? 193 ILE   B CB  1 
ATOM   3229 C CG1 . ILE   B 2 100 ? 32.72245 -12.23898 -6.06837  1.000 91.05759  ? 193 ILE   B CG1 1 
ATOM   3230 C CG2 . ILE   B 2 100 ? 35.22623 -12.26731 -5.92071  1.000 90.06736  ? 193 ILE   B CG2 1 
ATOM   3231 C CD1 . ILE   B 2 100 ? 31.47746 -12.63345 -6.82963  1.000 90.70066  ? 193 ILE   B CD1 1 
ATOM   3232 N N   . SER   B 2 101 ? 35.59714 -9.81757  -7.89419  1.000 90.17687  ? 194 SER   B N   1 
ATOM   3233 C CA  . SER   B 2 101 ? 35.88163 -8.39937  -7.71447  1.000 83.07951  ? 194 SER   B CA  1 
ATOM   3234 C C   . SER   B 2 101 ? 35.57761 -7.60250  -8.97424  1.000 77.72665  ? 194 SER   B C   1 
ATOM   3235 O O   . SER   B 2 101 ? 35.15691 -6.44395  -8.88294  1.000 71.12306  ? 194 SER   B O   1 
ATOM   3236 C CB  . SER   B 2 101 ? 37.33876 -8.20058  -7.29935  1.000 80.67674  ? 194 SER   B CB  1 
ATOM   3237 O OG  . SER   B 2 101 ? 37.61482 -8.89419  -6.09571  1.000 89.23179  ? 194 SER   B OG  1 
ATOM   3238 N N   . SER   B 2 102 ? 35.78365 -8.20084  -10.14989 1.000 79.88871  ? 195 SER   B N   1 
ATOM   3239 C CA  . SER   B 2 102 ? 35.35170 -7.56108  -11.38743 1.000 74.36608  ? 195 SER   B CA  1 
ATOM   3240 C C   . SER   B 2 102 ? 33.84015 -7.37587  -11.40195 1.000 72.37268  ? 195 SER   B C   1 
ATOM   3241 O O   . SER   B 2 102 ? 33.33534 -6.34268  -11.85725 1.000 67.57041  ? 195 SER   B O   1 
ATOM   3242 C CB  . SER   B 2 102 ? 35.80429 -8.38799  -12.59092 1.000 73.85650  ? 195 SER   B CB  1 
ATOM   3243 O OG  . SER   B 2 102 ? 37.20955 -8.56860  -12.58875 1.000 83.06609  ? 195 SER   B OG  1 
ATOM   3244 N N   . LEU   B 2 103 ? 33.10128 -8.36913  -10.90161 1.000 73.15572  ? 196 LEU   B N   1 
ATOM   3245 C CA  . LEU   B 2 103 ? 31.65375 -8.23502  -10.79041 1.000 71.39732  ? 196 LEU   B CA  1 
ATOM   3246 C C   . LEU   B 2 103 ? 31.26887 -7.21034  -9.73159  1.000 72.61060  ? 196 LEU   B C   1 
ATOM   3247 O O   . LEU   B 2 103 ? 30.23976 -6.53820  -9.86591  1.000 69.63311  ? 196 LEU   B O   1 
ATOM   3248 C CB  . LEU   B 2 103 ? 31.02782 -9.59434  -10.47608 1.000 72.37456  ? 196 LEU   B CB  1 
ATOM   3249 C CG  . LEU   B 2 103 ? 29.50136 -9.66692  -10.42976 1.000 75.38223  ? 196 LEU   B CG  1 
ATOM   3250 C CD1 . LEU   B 2 103 ? 28.90637 -9.21620  -11.75502 1.000 72.32264  ? 196 LEU   B CD1 1 
ATOM   3251 C CD2 . LEU   B 2 103 ? 29.04885 -11.07622 -10.08591 1.000 76.83883  ? 196 LEU   B CD2 1 
ATOM   3252 N N   . PHE   B 2 104 ? 32.08090 -7.07370  -8.68070  1.000 74.64592  ? 197 PHE   B N   1 
ATOM   3253 C CA  . PHE   B 2 104 ? 31.81044 -6.07056  -7.65567  1.000 73.65484  ? 197 PHE   B CA  1 
ATOM   3254 C C   . PHE   B 2 104 ? 31.96033 -4.66264  -8.21841  1.000 69.20440  ? 197 PHE   B C   1 
ATOM   3255 O O   . PHE   B 2 104 ? 31.12870 -3.78533  -7.95533  1.000 71.34502  ? 197 PHE   B O   1 
ATOM   3256 C CB  . PHE   B 2 104 ? 32.74082 -6.28239  -6.46048  1.000 78.95042  ? 197 PHE   B CB  1 
ATOM   3257 C CG  . PHE   B 2 104 ? 32.48577 -5.34379  -5.31524  1.000 83.07134  ? 197 PHE   B CG  1 
ATOM   3258 C CD1 . PHE   B 2 104 ? 31.22811 -5.25570  -4.74105  1.000 82.03240  ? 197 PHE   B CD1 1 
ATOM   3259 C CD2 . PHE   B 2 104 ? 33.50960 -4.56541  -4.79856  1.000 82.23607  ? 197 PHE   B CD2 1 
ATOM   3260 C CE1 . PHE   B 2 104 ? 30.99106 -4.39753  -3.68207  1.000 86.08233  ? 197 PHE   B CE1 1 
ATOM   3261 C CE2 . PHE   B 2 104 ? 33.27988 -3.70653  -3.73908  1.000 83.19164  ? 197 PHE   B CE2 1 
ATOM   3262 C CZ  . PHE   B 2 104 ? 32.01872 -3.62215  -3.18065  1.000 81.31808  ? 197 PHE   B CZ  1 
ATOM   3263 N N   . ILE   B 2 105 ? 33.02064 -4.42921  -8.99614  1.000 71.60363  ? 198 ILE   B N   1 
ATOM   3264 C CA  . ILE   B 2 105 ? 33.18742 -3.14195  -9.66512  1.000 69.67770  ? 198 ILE   B CA  1 
ATOM   3265 C C   . ILE   B 2 105 ? 32.04877 -2.90454  -10.64709 1.000 67.37729  ? 198 ILE   B C   1 
ATOM   3266 O O   . ILE   B 2 105 ? 31.50658 -1.79599  -10.73859 1.000 63.43411  ? 198 ILE   B O   1 
ATOM   3267 C CB  . ILE   B 2 105 ? 34.55532 -3.07836  -10.36952 1.000 69.61188  ? 198 ILE   B CB  1 
ATOM   3268 C CG1 . ILE   B 2 105 ? 35.68771 -3.32823  -9.37359  1.000 66.60102  ? 198 ILE   B CG1 1 
ATOM   3269 C CG2 . ILE   B 2 105 ? 34.73725 -1.73771  -11.06732 1.000 60.70198  ? 198 ILE   B CG2 1 
ATOM   3270 C CD1 . ILE   B 2 105 ? 37.02313 -3.57717  -10.03284 1.000 68.98526  ? 198 ILE   B CD1 1 
ATOM   3271 N N   . ALA   B 2 106 ? 31.66497 -3.94420  -11.39237 1.000 66.83256  ? 199 ALA   B N   1 
ATOM   3272 C CA  . ALA   B 2 106 ? 30.61776 -3.79483  -12.39693 1.000 69.35476  ? 199 ALA   B CA  1 
ATOM   3273 C C   . ALA   B 2 106 ? 29.25945 -3.54291  -11.75449 1.000 62.62033  ? 199 ALA   B C   1 
ATOM   3274 O O   . ALA   B 2 106 ? 28.47309 -2.73031  -12.25483 1.000 61.45520  ? 199 ALA   B O   1 
ATOM   3275 C CB  . ALA   B 2 106 ? 30.56681 -5.03577  -13.28793 1.000 65.23689  ? 199 ALA   B CB  1 
ATOM   3276 N N   . ALA   B 2 107 ? 28.96485 -4.22909  -10.64676 1.000 61.83377  ? 200 ALA   B N   1 
ATOM   3277 C CA  . ALA   B 2 107 ? 27.66693 -4.06410  -9.99870  1.000 68.51930  ? 200 ALA   B CA  1 
ATOM   3278 C C   . ALA   B 2 107 ? 27.50733 -2.66384  -9.42045  1.000 66.70895  ? 200 ALA   B C   1 
ATOM   3279 O O   . ALA   B 2 107 ? 26.42529 -2.07113  -9.50759  1.000 68.68089  ? 200 ALA   B O   1 
ATOM   3280 C CB  . ALA   B 2 107 ? 27.48317 -5.11882  -8.90874  1.000 69.86447  ? 200 ALA   B CB  1 
ATOM   3281 N N   . LYS   B 2 108 ? 28.57156 -2.11855  -8.82477  1.000 73.11564  ? 201 LYS   B N   1 
ATOM   3282 C CA  . LYS   B 2 108 ? 28.50024 -0.76235  -8.29126  1.000 72.87761  ? 201 LYS   B CA  1 
ATOM   3283 C C   . LYS   B 2 108 ? 28.35206 0.27106   -9.39978  1.000 68.44044  ? 201 LYS   B C   1 
ATOM   3284 O O   . LYS   B 2 108 ? 27.78776 1.34671   -9.16991  1.000 70.76193  ? 201 LYS   B O   1 
ATOM   3285 C CB  . LYS   B 2 108 ? 29.73822 -0.45662  -7.44617  1.000 70.80166  ? 201 LYS   B CB  1 
ATOM   3286 C CG  . LYS   B 2 108 ? 29.75899 -1.16417  -6.10171  1.000 68.76214  ? 201 LYS   B CG  1 
ATOM   3287 C CD  . LYS   B 2 108 ? 30.86215 -0.62971  -5.20022  1.000 72.90728  ? 201 LYS   B CD  1 
ATOM   3288 C CE  . LYS   B 2 108 ? 32.24228 -0.96348  -5.74116  1.000 72.76742  ? 201 LYS   B CE  1 
ATOM   3289 N NZ  . LYS   B 2 108 ? 33.31916 -0.53068  -4.80656  1.000 74.20319  ? 201 LYS   B NZ  1 
ATOM   3290 N N   . LEU   B 2 109 ? 28.84375 -0.03485  -10.60223 1.000 70.99794  ? 202 LEU   B N   1 
ATOM   3291 C CA  . LEU   B 2 109 ? 28.75174 0.90860   -11.71129 1.000 72.33419  ? 202 LEU   B CA  1 
ATOM   3292 C C   . LEU   B 2 109 ? 27.37042 0.90221   -12.35475 1.000 71.17190  ? 202 LEU   B C   1 
ATOM   3293 O O   . LEU   B 2 109 ? 26.86022 1.95933   -12.74195 1.000 72.71414  ? 202 LEU   B O   1 
ATOM   3294 C CB  . LEU   B 2 109 ? 29.81431 0.58902   -12.76428 1.000 66.26999  ? 202 LEU   B CB  1 
ATOM   3295 C CG  . LEU   B 2 109 ? 31.24609 1.03961   -12.48011 1.000 73.37266  ? 202 LEU   B CG  1 
ATOM   3296 C CD1 . LEU   B 2 109 ? 32.20043 0.44222   -13.50224 1.000 64.39984  ? 202 LEU   B CD1 1 
ATOM   3297 C CD2 . LEU   B 2 109 ? 31.32608 2.55528   -12.49773 1.000 77.88336  ? 202 LEU   B CD2 1 
ATOM   3298 N N   . GLU   B 2 110 ? 26.75140 -0.27037  -12.47768 1.000 69.71448  ? 203 GLU   B N   1 
ATOM   3299 C CA  . GLU   B 2 110 ? 25.55326 -0.43055  -13.29295 1.000 72.04771  ? 203 GLU   B CA  1 
ATOM   3300 C C   . GLU   B 2 110 ? 24.25831 -0.43620  -12.49116 1.000 74.99997  ? 203 GLU   B C   1 
ATOM   3301 O O   . GLU   B 2 110 ? 23.27095 0.16695   -12.92226 1.000 67.19340  ? 203 GLU   B O   1 
ATOM   3302 C CB  . GLU   B 2 110 ? 25.64907 -1.72449  -14.10743 1.000 67.07790  ? 203 GLU   B CB  1 
ATOM   3303 C CG  . GLU   B 2 110 ? 24.53277 -1.90302  -15.11853 1.000 71.16545  ? 203 GLU   B CG  1 
ATOM   3304 C CD  . GLU   B 2 110 ? 24.55362 -0.84093  -16.20119 1.000 81.17132  ? 203 GLU   B CD  1 
ATOM   3305 O OE1 . GLU   B 2 110 ? 25.64677 -0.31953  -16.50784 1.000 84.16475  ? 203 GLU   B OE1 1 
ATOM   3306 O OE2 . GLU   B 2 110 ? 23.47534 -0.52485  -16.74446 1.000 88.56277  ? 203 GLU   B OE2 1 
ATOM   3307 N N   . GLU   B 2 111 ? 24.23102 -1.10202  -11.34128 1.000 68.79677  ? 204 GLU   B N   1 
ATOM   3308 C CA  . GLU   B 2 111 ? 22.98893 -1.27753  -10.60430 1.000 76.97181  ? 204 GLU   B CA  1 
ATOM   3309 C C   . GLU   B 2 111 ? 22.63960 -0.02810  -9.80408  1.000 80.42355  ? 204 GLU   B C   1 
ATOM   3310 O O   . GLU   B 2 111 ? 23.51517 0.71228   -9.34742  1.000 79.79039  ? 204 GLU   B O   1 
ATOM   3311 C CB  . GLU   B 2 111 ? 23.08646 -2.48345  -9.66784  1.000 67.22292  ? 204 GLU   B CB  1 
ATOM   3312 C CG  . GLU   B 2 111 ? 23.49741 -3.78005  -10.35332 1.000 70.06847  ? 204 GLU   B CG  1 
ATOM   3313 C CD  . GLU   B 2 111 ? 22.46368 -4.28292  -11.34559 1.000 80.00600  ? 204 GLU   B CD  1 
ATOM   3314 O OE1 . GLU   B 2 111 ? 21.29012 -3.86350  -11.25923 1.000 80.31760  ? 204 GLU   B OE1 1 
ATOM   3315 O OE2 . GLU   B 2 111 ? 22.82712 -5.10315  -12.21433 1.000 74.68919  ? 204 GLU   B OE2 1 
ATOM   3316 N N   . ILE   B 2 112 ? 21.33497 0.20088   -9.64059  1.000 74.97916  ? 205 ILE   B N   1 
ATOM   3317 C CA  . ILE   B 2 112 ? 20.87096 1.30715   -8.80865  1.000 82.67342  ? 205 ILE   B CA  1 
ATOM   3318 C C   . ILE   B 2 112 ? 21.08711 0.98544   -7.33532  1.000 81.64067  ? 205 ILE   B C   1 
ATOM   3319 O O   . ILE   B 2 112 ? 21.63033 1.79732   -6.57723  1.000 78.80142  ? 205 ILE   B O   1 
ATOM   3320 C CB  . ILE   B 2 112 ? 19.39380 1.62224   -9.10656  1.000 80.24618  ? 205 ILE   B CB  1 
ATOM   3321 C CG1 . ILE   B 2 112 ? 19.21453 2.01997   -10.57343 1.000 73.66186  ? 205 ILE   B CG1 1 
ATOM   3322 C CG2 . ILE   B 2 112 ? 18.88606 2.72228   -8.18611  1.000 73.96550  ? 205 ILE   B CG2 1 
ATOM   3323 C CD1 . ILE   B 2 112 ? 17.79395 2.40593   -10.93413 1.000 63.50360  ? 205 ILE   B CD1 1 
ATOM   3324 N N   . TYR   B 2 113 ? 20.66287 -0.20647  -6.90778  1.000 75.26947  ? 206 TYR   B N   1 
ATOM   3325 C CA  . TYR   B 2 113 ? 20.86966 -0.69952  -5.54760  1.000 81.75386  ? 206 TYR   B CA  1 
ATOM   3326 C C   . TYR   B 2 113 ? 21.69368 -1.97882  -5.63935  1.000 79.55745  ? 206 TYR   B C   1 
ATOM   3327 O O   . TYR   B 2 113 ? 21.14341 -3.09030  -5.59944  1.000 82.42292  ? 206 TYR   B O   1 
ATOM   3328 C CB  . TYR   B 2 113 ? 19.54461 -0.94571  -4.82801  1.000 82.90328  ? 206 TYR   B CB  1 
ATOM   3329 C CG  . TYR   B 2 113 ? 18.65678 0.27493   -4.73916  1.000 86.79493  ? 206 TYR   B CG  1 
ATOM   3330 C CD1 . TYR   B 2 113 ? 18.87560 1.24840   -3.77330  1.000 81.41298  ? 206 TYR   B CD1 1 
ATOM   3331 C CD2 . TYR   B 2 113 ? 17.59529 0.45092   -5.61812  1.000 93.61876  ? 206 TYR   B CD2 1 
ATOM   3332 C CE1 . TYR   B 2 113 ? 18.06522 2.36682   -3.68797  1.000 90.82713  ? 206 TYR   B CE1 1 
ATOM   3333 C CE2 . TYR   B 2 113 ? 16.77858 1.56529   -5.54047  1.000 89.35845  ? 206 TYR   B CE2 1 
ATOM   3334 C CZ  . TYR   B 2 113 ? 17.01828 2.51996   -4.57412  1.000 101.30799 ? 206 TYR   B CZ  1 
ATOM   3335 O OH  . TYR   B 2 113 ? 16.20873 3.63060   -4.49340  1.000 101.04526 ? 206 TYR   B OH  1 
ATOM   3336 N N   . PRO   B 2 114 ? 23.01210 -1.86252  -5.76574  1.000 80.22546  ? 207 PRO   B N   1 
ATOM   3337 C CA  . PRO   B 2 114 ? 23.85543 -3.05072  -5.91467  1.000 78.21332  ? 207 PRO   B CA  1 
ATOM   3338 C C   . PRO   B 2 114 ? 23.93121 -3.83120  -4.61603  1.000 79.12581  ? 207 PRO   B C   1 
ATOM   3339 O O   . PRO   B 2 114 ? 23.59083 -3.30628  -3.54521  1.000 91.68390  ? 207 PRO   B O   1 
ATOM   3340 C CB  . PRO   B 2 114 ? 25.22291 -2.46318  -6.29320  1.000 76.54792  ? 207 PRO   B CB  1 
ATOM   3341 C CG  . PRO   B 2 114 ? 25.22071 -1.10943  -5.68452  1.000 75.21804  ? 207 PRO   B CG  1 
ATOM   3342 C CD  . PRO   B 2 114 ? 23.80129 -0.61850  -5.77853  1.000 79.02717  ? 207 PRO   B CD  1 
ATOM   3343 N N   . PRO   B 2 115 ? 24.35896 -5.08989  -4.66743  1.000 90.46474  ? 208 PRO   B N   1 
ATOM   3344 C CA  . PRO   B 2 115 ? 24.53480 -5.85704  -3.43132  1.000 78.81895  ? 208 PRO   B CA  1 
ATOM   3345 C C   . PRO   B 2 115 ? 25.69915 -5.32296  -2.61203  1.000 89.48068  ? 208 PRO   B C   1 
ATOM   3346 O O   . PRO   B 2 115 ? 26.59132 -4.63565  -3.11406  1.000 78.45736  ? 208 PRO   B O   1 
ATOM   3347 C CB  . PRO   B 2 115 ? 24.81405 -7.28151  -3.92653  1.000 82.37046  ? 208 PRO   B CB  1 
ATOM   3348 C CG  . PRO   B 2 115 ? 24.34178 -7.30370  -5.34422  1.000 85.06994  ? 208 PRO   B CG  1 
ATOM   3349 C CD  . PRO   B 2 115 ? 24.56815 -5.92076  -5.86372  1.000 84.78845  ? 208 PRO   B CD  1 
ATOM   3350 N N   . LYS   B 2 116 ? 25.67793 -5.65303  -1.32406  1.000 90.63936  ? 209 LYS   B N   1 
ATOM   3351 C CA  . LYS   B 2 116 ? 26.72413 -5.20298  -0.42213  1.000 91.31342  ? 209 LYS   B CA  1 
ATOM   3352 C C   . LYS   B 2 116 ? 27.98751 -6.04155  -0.60681  1.000 88.25790  ? 209 LYS   B C   1 
ATOM   3353 O O   . LYS   B 2 116 ? 27.99147 -7.07513  -1.28062  1.000 91.89144  ? 209 LYS   B O   1 
ATOM   3354 C CB  . LYS   B 2 116 ? 26.24298 -5.25904  1.02750   1.000 98.21468  ? 209 LYS   B CB  1 
ATOM   3355 C CG  . LYS   B 2 116 ? 25.18140 -4.22366  1.36418   1.000 92.58079  ? 209 LYS   B CG  1 
ATOM   3356 C CD  . LYS   B 2 116 ? 25.71220 -2.81132  1.16452   1.000 95.71204  ? 209 LYS   B CD  1 
ATOM   3357 C CE  . LYS   B 2 116 ? 24.67867 -1.76426  1.54727   1.000 96.62694  ? 209 LYS   B CE  1 
ATOM   3358 N NZ  . LYS   B 2 116 ? 23.45459 -1.85189  0.70448   1.000 80.88417  ? 209 LYS   B NZ  1 
ATOM   3359 N N   . LEU   B 2 117 ? 29.07755 -5.57370  0.00646   1.000 91.36423  ? 210 LEU   B N   1 
ATOM   3360 C CA  . LEU   B 2 117 ? 30.36554 -6.24150  -0.15429  1.000 90.97150  ? 210 LEU   B CA  1 
ATOM   3361 C C   . LEU   B 2 117 ? 30.34436 -7.64772  0.43169   1.000 97.27844  ? 210 LEU   B C   1 
ATOM   3362 O O   . LEU   B 2 117 ? 30.91723 -8.57802  -0.14870  1.000 101.02067 ? 210 LEU   B O   1 
ATOM   3363 C CB  . LEU   B 2 117 ? 31.46978 -5.41062  0.49757   1.000 91.06052  ? 210 LEU   B CB  1 
ATOM   3364 C CG  . LEU   B 2 117 ? 32.82116 -6.10910  0.66091   1.000 91.15530  ? 210 LEU   B CG  1 
ATOM   3365 C CD1 . LEU   B 2 117 ? 33.46176 -6.37942  -0.69360  1.000 90.27228  ? 210 LEU   B CD1 1 
ATOM   3366 C CD2 . LEU   B 2 117 ? 33.74399 -5.29512  1.55171   1.000 87.34246  ? 210 LEU   B CD2 1 
ATOM   3367 N N   . HIS   B 2 118 ? 29.68949 -7.82402  1.58261   1.000 100.08532 ? 211 HIS   B N   1 
ATOM   3368 C CA  . HIS   B 2 118 ? 29.69975 -9.12675  2.24006   1.000 107.43879 ? 211 HIS   B CA  1 
ATOM   3369 C C   . HIS   B 2 118 ? 28.95233 -10.17624 1.42679   1.000 99.81663  ? 211 HIS   B C   1 
ATOM   3370 O O   . HIS   B 2 118 ? 29.28695 -11.36421 1.49886   1.000 101.35317 ? 211 HIS   B O   1 
ATOM   3371 C CB  . HIS   B 2 118 ? 29.10587 -9.01510  3.64487   1.000 107.94950 ? 211 HIS   B CB  1 
ATOM   3372 C CG  . HIS   B 2 118 ? 27.61936 -8.84036  3.66258   1.000 111.91152 ? 211 HIS   B CG  1 
ATOM   3373 N ND1 . HIS   B 2 118 ? 27.00362 -7.65716  3.31501   1.000 116.15766 ? 211 HIS   B ND1 1 
ATOM   3374 C CD2 . HIS   B 2 118 ? 26.62559 -9.69850  3.99375   1.000 111.14797 ? 211 HIS   B CD2 1 
ATOM   3375 C CE1 . HIS   B 2 118 ? 25.69450 -7.79533  3.42703   1.000 112.71555 ? 211 HIS   B CE1 1 
ATOM   3376 N NE2 . HIS   B 2 118 ? 25.43887 -9.02445  3.83775   1.000 115.58361 ? 211 HIS   B NE2 1 
ATOM   3377 N N   . GLN   B 2 119 ? 27.94699 -9.76383  0.64949   1.000 97.36999  ? 212 GLN   B N   1 
ATOM   3378 C CA  . GLN   B 2 119 ? 27.24732 -10.71232 -0.21207  1.000 109.27934 ? 212 GLN   B CA  1 
ATOM   3379 C C   . GLN   B 2 119 ? 28.15551 -11.22143 -1.32451  1.000 96.29825  ? 212 GLN   B C   1 
ATOM   3380 O O   . GLN   B 2 119 ? 28.06581 -12.38936 -1.72024  1.000 93.05054  ? 212 GLN   B O   1 
ATOM   3381 C CB  . GLN   B 2 119 ? 25.99085 -10.06943 -0.79811  1.000 93.45685  ? 212 GLN   B CB  1 
ATOM   3382 C CG  . GLN   B 2 119 ? 24.88844 -9.82144  0.21717   1.000 106.88625 ? 212 GLN   B CG  1 
ATOM   3383 C CD  . GLN   B 2 119 ? 23.67308 -9.15110  -0.39389  1.000 102.08002 ? 212 GLN   B CD  1 
ATOM   3384 O OE1 . GLN   B 2 119 ? 23.73912 -8.00570  -0.83970  1.000 99.63015  ? 212 GLN   B OE1 1 
ATOM   3385 N NE2 . GLN   B 2 119 ? 22.55380 -9.86439  -0.41707  1.000 101.40251 ? 212 GLN   B NE2 1 
ATOM   3386 N N   . PHE   B 2 120 ? 29.03417 -10.36069 -1.84396  1.000 92.09015  ? 213 PHE   B N   1 
ATOM   3387 C CA  . PHE   B 2 120 ? 30.01221 -10.81305 -2.82840  1.000 94.16837  ? 213 PHE   B CA  1 
ATOM   3388 C C   . PHE   B 2 120 ? 31.02847 -11.75883 -2.20014  1.000 94.18707  ? 213 PHE   B C   1 
ATOM   3389 O O   . PHE   B 2 120 ? 31.50015 -12.69587 -2.85436  1.000 94.47691  ? 213 PHE   B O   1 
ATOM   3390 C CB  . PHE   B 2 120 ? 30.70953 -9.61278  -3.46730  1.000 96.12226  ? 213 PHE   B CB  1 
ATOM   3391 C CG  . PHE   B 2 120 ? 29.88647 -8.92678  -4.51890  1.000 85.86980  ? 213 PHE   B CG  1 
ATOM   3392 C CD1 . PHE   B 2 120 ? 28.92063 -7.99943  -4.16712  1.000 86.08463  ? 213 PHE   B CD1 1 
ATOM   3393 C CD2 . PHE   B 2 120 ? 30.07639 -9.21442  -5.86020  1.000 87.99615  ? 213 PHE   B CD2 1 
ATOM   3394 C CE1 . PHE   B 2 120 ? 28.16102 -7.36971  -5.13354  1.000 90.80036  ? 213 PHE   B CE1 1 
ATOM   3395 C CE2 . PHE   B 2 120 ? 29.32002 -8.58874  -6.83207  1.000 81.34179  ? 213 PHE   B CE2 1 
ATOM   3396 C CZ  . PHE   B 2 120 ? 28.36043 -7.66492  -6.46823  1.000 81.93365  ? 213 PHE   B CZ  1 
ATOM   3397 N N   . ALA   B 2 121 ? 31.38100 -11.52847 -0.93343  1.000 100.52814 ? 214 ALA   B N   1 
ATOM   3398 C CA  . ALA   B 2 121 ? 32.22722 -12.47148 -0.21316  1.000 104.27267 ? 214 ALA   B CA  1 
ATOM   3399 C C   . ALA   B 2 121 ? 31.45682 -13.71102 0.22149   1.000 100.28633 ? 214 ALA   B C   1 
ATOM   3400 O O   . ALA   B 2 121 ? 32.07002 -14.75272 0.47912   1.000 101.86823 ? 214 ALA   B O   1 
ATOM   3401 C CB  . ALA   B 2 121 ? 32.85622 -11.78927 1.00379   1.000 95.02813  ? 214 ALA   B CB  1 
ATOM   3402 N N   . TYR   B 2 122 ? 30.12766 -13.62161 0.29580   1.000 99.47840  ? 215 TYR   B N   1 
ATOM   3403 C CA  . TYR   B 2 122 ? 29.32687 -14.74899 0.75993   1.000 99.10528  ? 215 TYR   B CA  1 
ATOM   3404 C C   . TYR   B 2 122 ? 29.23219 -15.84200 -0.29715  1.000 110.57461 ? 215 TYR   B C   1 
ATOM   3405 O O   . TYR   B 2 122 ? 29.33981 -17.03156 0.02225   1.000 106.32423 ? 215 TYR   B O   1 
ATOM   3406 C CB  . TYR   B 2 122 ? 27.93419 -14.26216 1.16038   1.000 98.00824  ? 215 TYR   B CB  1 
ATOM   3407 C CG  . TYR   B 2 122 ? 26.94575 -15.36691 1.44440   1.000 104.86437 ? 215 TYR   B CG  1 
ATOM   3408 C CD1 . TYR   B 2 122 ? 27.03687 -16.12584 2.60382   1.000 104.82644 ? 215 TYR   B CD1 1 
ATOM   3409 C CD2 . TYR   B 2 122 ? 25.91178 -15.64275 0.55958   1.000 101.89118 ? 215 TYR   B CD2 1 
ATOM   3410 C CE1 . TYR   B 2 122 ? 26.13141 -17.13501 2.86935   1.000 97.13411  ? 215 TYR   B CE1 1 
ATOM   3411 C CE2 . TYR   B 2 122 ? 25.00008 -16.64779 0.81780   1.000 110.24059 ? 215 TYR   B CE2 1 
ATOM   3412 C CZ  . TYR   B 2 122 ? 25.11551 -17.39177 1.97282   1.000 111.93830 ? 215 TYR   B CZ  1 
ATOM   3413 O OH  . TYR   B 2 122 ? 24.20995 -18.39455 2.23255   1.000 114.41798 ? 215 TYR   B OH  1 
ATOM   3414 N N   . VAL   B 2 123 ? 29.03461 -15.46220 -1.56197  1.000 111.43351 ? 216 VAL   B N   1 
ATOM   3415 C CA  . VAL   B 2 123 ? 28.86455 -16.44842 -2.62248  1.000 109.72712 ? 216 VAL   B CA  1 
ATOM   3416 C C   . VAL   B 2 123 ? 30.14145 -17.21189 -2.93259  1.000 113.99439 ? 216 VAL   B C   1 
ATOM   3417 O O   . VAL   B 2 123 ? 30.08401 -18.24616 -3.60774  1.000 122.13188 ? 216 VAL   B O   1 
ATOM   3418 C CB  . VAL   B 2 123 ? 28.34015 -15.77720 -3.90751  1.000 113.31402 ? 216 VAL   B CB  1 
ATOM   3419 C CG1 . VAL   B 2 123 ? 26.93999 -15.24052 -3.68377  1.000 110.07928 ? 216 VAL   B CG1 1 
ATOM   3420 C CG2 . VAL   B 2 123 ? 29.27869 -14.66715 -4.34947  1.000 109.18947 ? 216 VAL   B CG2 1 
ATOM   3421 N N   . THR   B 2 124 ? 31.29191 -16.73956 -2.45608  1.000 110.10395 ? 217 THR   B N   1 
ATOM   3422 C CA  . THR   B 2 124 ? 32.55684 -17.42485 -2.68902  1.000 112.72437 ? 217 THR   B CA  1 
ATOM   3423 C C   . THR   B 2 124 ? 32.75694 -18.62474 -1.77243  1.000 119.47884 ? 217 THR   B C   1 
ATOM   3424 O O   . THR   B 2 124 ? 33.84523 -19.21096 -1.77844  1.000 110.12828 ? 217 THR   B O   1 
ATOM   3425 C CB  . THR   B 2 124 ? 33.72424 -16.44897 -2.52247  1.000 114.60279 ? 217 THR   B CB  1 
ATOM   3426 O OG1 . THR   B 2 124 ? 33.75266 -15.95895 -1.17647  1.000 116.05288 ? 217 THR   B OG1 1 
ATOM   3427 C CG2 . THR   B 2 124 ? 33.57119 -15.27576 -3.47539  1.000 108.12523 ? 217 THR   B CG2 1 
ATOM   3428 N N   . ASP   B 2 125 ? 31.73636 -18.99432 -0.99480  1.000 134.59276 ? 218 ASP   B N   1 
ATOM   3429 C CA  . ASP   B 2 125 ? 31.80799 -20.10892 -0.04937  1.000 140.30438 ? 218 ASP   B CA  1 
ATOM   3430 C C   . ASP   B 2 125 ? 32.94878 -19.92780 0.94884   1.000 138.24626 ? 218 ASP   B C   1 
ATOM   3431 O O   . ASP   B 2 125 ? 33.57638 -20.89904 1.37817   1.000 139.08083 ? 218 ASP   B O   1 
ATOM   3432 C CB  . ASP   B 2 125 ? 31.93519 -21.45125 -0.77771  1.000 145.01756 ? 218 ASP   B CB  1 
ATOM   3433 C CG  . ASP   B 2 125 ? 31.51711 -22.62574 0.08657   1.000 150.35109 ? 218 ASP   B CG  1 
ATOM   3434 O OD1 . ASP   B 2 125 ? 30.30560 -22.76204 0.35843   1.000 155.30013 ? 218 ASP   B OD1 1 
ATOM   3435 O OD2 . ASP   B 2 125 ? 32.39891 -23.40985 0.49608   1.000 151.84090 ? 218 ASP   B OD2 1 
ATOM   3436 N N   . GLY   B 2 126 ? 33.22741 -18.68106 1.32228   1.000 128.23637 ? 219 GLY   B N   1 
ATOM   3437 C CA  . GLY   B 2 126 ? 34.26582 -18.39402 2.28912   1.000 133.78410 ? 219 GLY   B CA  1 
ATOM   3438 C C   . GLY   B 2 126 ? 35.67720 -18.40682 1.75029   1.000 131.37996 ? 219 GLY   B C   1 
ATOM   3439 O O   . GLY   B 2 126 ? 36.62394 -18.43319 2.54480   1.000 133.51532 ? 219 GLY   B O   1 
ATOM   3440 N N   . ALA   B 2 127 ? 35.85385 -18.38740 0.43051   1.000 122.86200 ? 220 ALA   B N   1 
ATOM   3441 C CA  . ALA   B 2 127 ? 37.18069 -18.38832 -0.16899  1.000 122.01676 ? 220 ALA   B CA  1 
ATOM   3442 C C   . ALA   B 2 127 ? 37.70610 -16.98969 -0.46297  1.000 123.39737 ? 220 ALA   B C   1 
ATOM   3443 O O   . ALA   B 2 127 ? 38.88122 -16.84934 -0.81896  1.000 121.95806 ? 220 ALA   B O   1 
ATOM   3444 C CB  . ALA   B 2 127 ? 37.17587 -19.21183 -1.46138  1.000 127.73581 ? 220 ALA   B CB  1 
ATOM   3445 N N   . CYS   B 2 128 ? 36.87442 -15.95918 -0.32424  1.000 119.16665 ? 221 CYS   B N   1 
ATOM   3446 C CA  . CYS   B 2 128 ? 37.28248 -14.58500 -0.59265  1.000 119.71337 ? 221 CYS   B CA  1 
ATOM   3447 C C   . CYS   B 2 128 ? 36.75794 -13.69553 0.52173   1.000 116.94518 ? 221 CYS   B C   1 
ATOM   3448 O O   . CYS   B 2 128 ? 35.54633 -13.63578 0.75082   1.000 117.48065 ? 221 CYS   B O   1 
ATOM   3449 C CB  . CYS   B 2 128 ? 36.76372 -14.10601 -1.95209  1.000 113.20101 ? 221 CYS   B CB  1 
ATOM   3450 S SG  . CYS   B 2 128 ? 37.36394 -15.06607 -3.36061  1.000 118.51969 ? 221 CYS   B SG  1 
ATOM   3451 N N   . SER   B 2 129 ? 37.66616 -13.01273 1.21201   1.000 114.00312 ? 222 SER   B N   1 
ATOM   3452 C CA  . SER   B 2 129 ? 37.26910 -12.10050 2.27060   1.000 107.66107 ? 222 SER   B CA  1 
ATOM   3453 C C   . SER   B 2 129 ? 36.67429 -10.82670 1.68000   1.000 110.76605 ? 222 SER   B C   1 
ATOM   3454 O O   . SER   B 2 129 ? 36.87688 -10.49705 0.50813   1.000 102.04054 ? 222 SER   B O   1 
ATOM   3455 C CB  . SER   B 2 129 ? 38.46449 -11.75151 3.15703   1.000 106.40238 ? 222 SER   B CB  1 
ATOM   3456 O OG  . SER   B 2 129 ? 39.10596 -12.92115 3.63215   1.000 134.02374 ? 222 SER   B OG  1 
ATOM   3457 N N   . GLY   B 2 130 ? 35.92113 -10.10746 2.51322   1.000 106.28896 ? 223 GLY   B N   1 
ATOM   3458 C CA  . GLY   B 2 130 ? 35.43972 -8.80052  2.10558   1.000 93.59481  ? 223 GLY   B CA  1 
ATOM   3459 C C   . GLY   B 2 130 ? 36.56757 -7.81775  1.86898   1.000 103.67140 ? 223 GLY   B C   1 
ATOM   3460 O O   . GLY   B 2 130 ? 36.47147 -6.95177  0.99501   1.000 90.75383  ? 223 GLY   B O   1 
ATOM   3461 N N   . ASP   B 2 131 ? 37.65421 -7.94241  2.63378   1.000 103.93758 ? 224 ASP   B N   1 
ATOM   3462 C CA  . ASP   B 2 131 ? 38.81736 -7.08861  2.42879   1.000 104.23923 ? 224 ASP   B CA  1 
ATOM   3463 C C   . ASP   B 2 131 ? 39.69243 -7.58764  1.28686   1.000 98.70329  ? 224 ASP   B C   1 
ATOM   3464 O O   . ASP   B 2 131 ? 40.40514 -6.79113  0.66633   1.000 98.10606  ? 224 ASP   B O   1 
ATOM   3465 C CB  . ASP   B 2 131 ? 39.63001 -6.99114  3.72043   1.000 116.96010 ? 224 ASP   B CB  1 
ATOM   3466 C CG  . ASP   B 2 131 ? 38.80568 -6.48262  4.88582   1.000 125.25425 ? 224 ASP   B CG  1 
ATOM   3467 O OD1 . ASP   B 2 131 ? 37.90378 -7.21812  5.33871   1.000 131.60629 ? 224 ASP   B OD1 1 
ATOM   3468 O OD2 . ASP   B 2 131 ? 39.05578 -5.34837  5.34599   1.000 129.84928 ? 224 ASP   B OD2 1 
ATOM   3469 N N   . GLU   B 2 132 ? 39.65671 -8.89112  0.99738   1.000 100.97322 ? 225 GLU   B N   1 
ATOM   3470 C CA  . GLU   B 2 132 ? 40.33977 -9.39902  -0.18826  1.000 103.91247 ? 225 GLU   B CA  1 
ATOM   3471 C C   . GLU   B 2 132 ? 39.71941 -8.83518  -1.46003  1.000 92.20681  ? 225 GLU   B C   1 
ATOM   3472 O O   . GLU   B 2 132 ? 40.42929 -8.53152  -2.42622  1.000 92.69854  ? 225 GLU   B O   1 
ATOM   3473 C CB  . GLU   B 2 132 ? 40.30123 -10.92730 -0.20978  1.000 102.12872 ? 225 GLU   B CB  1 
ATOM   3474 C CG  . GLU   B 2 132 ? 41.33323 -11.60006 0.67948   1.000 109.56294 ? 225 GLU   B CG  1 
ATOM   3475 C CD  . GLU   B 2 132 ? 41.38508 -13.10241 0.46743   1.000 112.40569 ? 225 GLU   B CD  1 
ATOM   3476 O OE1 . GLU   B 2 132 ? 40.34762 -13.68667 0.09260   1.000 112.42688 ? 225 GLU   B OE1 1 
ATOM   3477 O OE2 . GLU   B 2 132 ? 42.46363 -13.69993 0.66572   1.000 115.94159 ? 225 GLU   B OE2 1 
ATOM   3478 N N   . ILE   B 2 133 ? 38.39306 -8.69096  -1.47810  1.000 91.74607  ? 226 ILE   B N   1 
ATOM   3479 C CA  . ILE   B 2 133 ? 37.72060 -8.11232  -2.63620  1.000 89.93739  ? 226 ILE   B CA  1 
ATOM   3480 C C   . ILE   B 2 133 ? 38.06261 -6.63299  -2.76872  1.000 92.62145  ? 226 ILE   B C   1 
ATOM   3481 O O   . ILE   B 2 133 ? 38.26642 -6.12542  -3.87841  1.000 87.87593  ? 226 ILE   B O   1 
ATOM   3482 C CB  . ILE   B 2 133 ? 36.20136 -8.34117  -2.53206  1.000 85.89165  ? 226 ILE   B CB  1 
ATOM   3483 C CG1 . ILE   B 2 133 ? 35.88543 -9.83887  -2.54984  1.000 90.45430  ? 226 ILE   B CG1 1 
ATOM   3484 C CG2 . ILE   B 2 133 ? 35.47002 -7.62529  -3.65433  1.000 74.48537  ? 226 ILE   B CG2 1 
ATOM   3485 C CD1 . ILE   B 2 133 ? 34.41372 -10.15536 -2.39162  1.000 97.02858  ? 226 ILE   B CD1 1 
ATOM   3486 N N   . LEU   B 2 134 ? 38.13799 -5.91955  -1.64211  1.000 90.25634  ? 227 LEU   B N   1 
ATOM   3487 C CA  . LEU   B 2 134 ? 38.46910 -4.49809  -1.68382  1.000 88.26818  ? 227 LEU   B CA  1 
ATOM   3488 C C   . LEU   B 2 134 ? 39.88921 -4.27300  -2.18688  1.000 89.11927  ? 227 LEU   B C   1 
ATOM   3489 O O   . LEU   B 2 134 ? 40.15549 -3.29426  -2.89418  1.000 89.95982  ? 227 LEU   B O   1 
ATOM   3490 C CB  . LEU   B 2 134 ? 38.28154 -3.87744  -0.30000  1.000 85.58019  ? 227 LEU   B CB  1 
ATOM   3491 C CG  . LEU   B 2 134 ? 37.02507 -3.02928  -0.09724  1.000 95.78141  ? 227 LEU   B CG  1 
ATOM   3492 C CD1 . LEU   B 2 134 ? 35.85164 -3.59681  -0.88231  1.000 86.92831  ? 227 LEU   B CD1 1 
ATOM   3493 C CD2 . LEU   B 2 134 ? 36.68659 -2.93165  1.38327   1.000 95.16667  ? 227 LEU   B CD2 1 
ATOM   3494 N N   . THR   B 2 135 ? 40.81561 -5.16406  -1.82993  1.000 88.91617  ? 228 THR   B N   1 
ATOM   3495 C CA  . THR   B 2 135 ? 42.17186 -5.06178  -2.35719  1.000 91.47243  ? 228 THR   B CA  1 
ATOM   3496 C C   . THR   B 2 135 ? 42.20454 -5.37921  -3.84664  1.000 94.53340  ? 228 THR   B C   1 
ATOM   3497 O O   . THR   B 2 135 ? 42.93479 -4.73616  -4.61001  1.000 93.79296  ? 228 THR   B O   1 
ATOM   3498 C CB  . THR   B 2 135 ? 43.10723 -5.99629  -1.58807  1.000 97.78987  ? 228 THR   B CB  1 
ATOM   3499 O OG1 . THR   B 2 135 ? 43.09069 -5.65202  -0.19666  1.000 99.96606  ? 228 THR   B OG1 1 
ATOM   3500 C CG2 . THR   B 2 135 ? 44.53282 -5.88719  -2.11447  1.000 85.65141  ? 228 THR   B CG2 1 
ATOM   3501 N N   . MET   B 2 136 ? 41.40562 -6.35650  -4.28019  1.000 93.76167  ? 229 MET   B N   1 
ATOM   3502 C CA  . MET   B 2 136 ? 41.43043 -6.76628  -5.67986  1.000 85.42626  ? 229 MET   B CA  1 
ATOM   3503 C C   . MET   B 2 136 ? 40.77503 -5.72408  -6.57727  1.000 86.35391  ? 229 MET   B C   1 
ATOM   3504 O O   . MET   B 2 136 ? 41.24478 -5.48075  -7.69460  1.000 83.09131  ? 229 MET   B O   1 
ATOM   3505 C CB  . MET   B 2 136 ? 40.74559 -8.12372  -5.84003  1.000 90.10294  ? 229 MET   B CB  1 
ATOM   3506 C CG  . MET   B 2 136 ? 40.89169 -8.75408  -7.22080  1.000 88.73280  ? 229 MET   B CG  1 
ATOM   3507 S SD  . MET   B 2 136 ? 42.56343 -9.33092  -7.57662  1.000 110.29551 ? 229 MET   B SD  1 
ATOM   3508 C CE  . MET   B 2 136 ? 43.16583 -8.02544  -8.64320  1.000 86.74871  ? 229 MET   B CE  1 
ATOM   3509 N N   . GLU   B 2 137 ? 39.69188 -5.09529  -6.10976  1.000 83.81735  ? 230 GLU   B N   1 
ATOM   3510 C CA  . GLU   B 2 137 ? 39.01519 -4.10094  -6.93705  1.000 78.26063  ? 230 GLU   B CA  1 
ATOM   3511 C C   . GLU   B 2 137 ? 39.90026 -2.88695  -7.18808  1.000 82.46158  ? 230 GLU   B C   1 
ATOM   3512 O O   . GLU   B 2 137 ? 39.81845 -2.27070  -8.25636  1.000 78.99232  ? 230 GLU   B O   1 
ATOM   3513 C CB  . GLU   B 2 137 ? 37.69234 -3.67399  -6.29409  1.000 80.24692  ? 230 GLU   B CB  1 
ATOM   3514 C CG  . GLU   B 2 137 ? 37.83458 -2.82693  -5.03780  1.000 83.92162  ? 230 GLU   B CG  1 
ATOM   3515 C CD  . GLU   B 2 137 ? 36.69676 -1.83720  -4.86926  1.000 82.98827  ? 230 GLU   B CD  1 
ATOM   3516 O OE1 . GLU   B 2 137 ? 35.77826 -1.83703  -5.71474  1.000 83.24677  ? 230 GLU   B OE1 1 
ATOM   3517 O OE2 . GLU   B 2 137 ? 36.72222 -1.05470  -3.89595  1.000 87.39371  ? 230 GLU   B OE2 1 
ATOM   3518 N N   . LEU   B 2 138 ? 40.75487 -2.53240  -6.22595  1.000 82.59307  ? 231 LEU   B N   1 
ATOM   3519 C CA  . LEU   B 2 138 ? 41.68182 -1.42671  -6.43886  1.000 84.08102  ? 231 LEU   B CA  1 
ATOM   3520 C C   . LEU   B 2 138 ? 42.76964 -1.80637  -7.43462  1.000 85.70796  ? 231 LEU   B C   1 
ATOM   3521 O O   . LEU   B 2 138 ? 43.14166 -0.99834  -8.29299  1.000 81.84746  ? 231 LEU   B O   1 
ATOM   3522 C CB  . LEU   B 2 138 ? 42.29473 -0.98923  -5.10867  1.000 82.16092  ? 231 LEU   B CB  1 
ATOM   3523 C CG  . LEU   B 2 138 ? 41.47287 0.00385   -4.28589  1.000 88.14139  ? 231 LEU   B CG  1 
ATOM   3524 C CD1 . LEU   B 2 138 ? 42.09516 0.21606   -2.91595  1.000 85.11913  ? 231 LEU   B CD1 1 
ATOM   3525 C CD2 . LEU   B 2 138 ? 41.35578 1.32410   -5.02883  1.000 84.13756  ? 231 LEU   B CD2 1 
ATOM   3526 N N   . MET   B 2 139 ? 43.28711 -3.03359  -7.34019  1.000 84.60597  ? 232 MET   B N   1 
ATOM   3527 C CA  . MET   B 2 139 ? 44.31193 -3.47609  -8.27993  1.000 88.95922  ? 232 MET   B CA  1 
ATOM   3528 C C   . MET   B 2 139 ? 43.75759 -3.58021  -9.69520  1.000 86.83703  ? 232 MET   B C   1 
ATOM   3529 O O   . MET   B 2 139 ? 44.45148 -3.24922  -10.66369 1.000 82.07087  ? 232 MET   B O   1 
ATOM   3530 C CB  . MET   B 2 139 ? 44.89596 -4.81543  -7.82999  1.000 94.31954  ? 232 MET   B CB  1 
ATOM   3531 C CG  . MET   B 2 139 ? 45.75779 -4.72652  -6.58063  1.000 88.88615  ? 232 MET   B CG  1 
ATOM   3532 S SD  . MET   B 2 139 ? 46.52312 -6.29643  -6.13167  1.000 124.22735 ? 232 MET   B SD  1 
ATOM   3533 C CE  . MET   B 2 139 ? 45.08737 -7.26084  -5.66954  1.000 95.74181  ? 232 MET   B CE  1 
ATOM   3534 N N   . ILE   B 2 140 ? 42.50775 -4.02946  -9.83509  1.000 88.19301  ? 233 ILE   B N   1 
ATOM   3535 C CA  . ILE   B 2 140 ? 41.90358 -4.14720  -11.16040 1.000 75.09516  ? 233 ILE   B CA  1 
ATOM   3536 C C   . ILE   B 2 140 ? 41.72989 -2.77018  -11.78718 1.000 78.25187  ? 233 ILE   B C   1 
ATOM   3537 O O   . ILE   B 2 140 ? 42.14726 -2.52928  -12.92611 1.000 77.86201  ? 233 ILE   B O   1 
ATOM   3538 C CB  . ILE   B 2 140 ? 40.56318 -4.90074  -11.08009 1.000 83.87109  ? 233 ILE   B CB  1 
ATOM   3539 C CG1 . ILE   B 2 140 ? 40.79174 -6.37458  -10.74319 1.000 83.82780  ? 233 ILE   B CG1 1 
ATOM   3540 C CG2 . ILE   B 2 140 ? 39.79549 -4.76848  -12.39062 1.000 78.78762  ? 233 ILE   B CG2 1 
ATOM   3541 C CD1 . ILE   B 2 140 ? 39.51383 -7.17284  -10.61047 1.000 85.66549  ? 233 ILE   B CD1 1 
ATOM   3542 N N   . MET   B 2 141 ? 41.11472 -1.84296  -11.04764 1.000 78.12133  ? 234 MET   B N   1 
ATOM   3543 C CA  . MET   B 2 141 ? 40.84401 -0.51745  -11.59529 1.000 76.77798  ? 234 MET   B CA  1 
ATOM   3544 C C   . MET   B 2 141 ? 42.12639 0.25763   -11.87050 1.000 78.59216  ? 234 MET   B C   1 
ATOM   3545 O O   . MET   B 2 141 ? 42.18023 1.04392   -12.82329 1.000 79.86430  ? 234 MET   B O   1 
ATOM   3546 C CB  . MET   B 2 141 ? 39.93905 0.26849   -10.64516 1.000 75.99041  ? 234 MET   B CB  1 
ATOM   3547 C CG  . MET   B 2 141 ? 38.55186 -0.33143  -10.48229 1.000 77.50910  ? 234 MET   B CG  1 
ATOM   3548 S SD  . MET   B 2 141 ? 37.45311 0.65515   -9.44546  1.000 83.68690  ? 234 MET   B SD  1 
ATOM   3549 C CE  . MET   B 2 141 ? 38.31280 0.59269   -7.87701  1.000 69.53370  ? 234 MET   B CE  1 
ATOM   3550 N N   . LYS   B 2 142 ? 43.16467 0.05330   -11.05818 1.000 72.58599  ? 235 LYS   B N   1 
ATOM   3551 C CA  . LYS   B 2 142 ? 44.42587 0.74667   -11.29861 1.000 75.54681  ? 235 LYS   B CA  1 
ATOM   3552 C C   . LYS   B 2 142 ? 45.17228 0.14298   -12.48148 1.000 79.59221  ? 235 LYS   B C   1 
ATOM   3553 O O   . LYS   B 2 142 ? 45.81163 0.86795   -13.25284 1.000 82.62529  ? 235 LYS   B O   1 
ATOM   3554 C CB  . LYS   B 2 142 ? 45.29308 0.71639   -10.04056 1.000 82.01187  ? 235 LYS   B CB  1 
ATOM   3555 C CG  . LYS   B 2 142 ? 44.79663 1.62576   -8.92921  1.000 84.67069  ? 235 LYS   B CG  1 
ATOM   3556 C CD  . LYS   B 2 142 ? 45.48566 1.32145   -7.61000  1.000 79.18937  ? 235 LYS   B CD  1 
ATOM   3557 C CE  . LYS   B 2 142 ? 46.98721 1.52868   -7.70379  1.000 87.11429  ? 235 LYS   B CE  1 
ATOM   3558 N NZ  . LYS   B 2 142 ? 47.66137 1.24000   -6.40936  1.000 88.37404  ? 235 LYS   B NZ  1 
ATOM   3559 N N   . ALA   B 2 143 ? 45.10472 -1.18185  -12.64130 1.000 76.92497  ? 236 ALA   B N   1 
ATOM   3560 C CA  . ALA   B 2 143 ? 45.76897 -1.82214  -13.77183 1.000 84.46828  ? 236 ALA   B CA  1 
ATOM   3561 C C   . ALA   B 2 143 ? 45.07397 -1.50117  -15.08846 1.000 80.15118  ? 236 ALA   B C   1 
ATOM   3562 O O   . ALA   B 2 143 ? 45.72961 -1.44267  -16.13463 1.000 89.87762  ? 236 ALA   B O   1 
ATOM   3563 C CB  . ALA   B 2 143 ? 45.83402 -3.33486  -13.56203 1.000 83.29975  ? 236 ALA   B CB  1 
ATOM   3564 N N   . LEU   B 2 144 ? 43.75939 -1.29249  -15.06110 1.000 82.75665  ? 237 LEU   B N   1 
ATOM   3565 C CA  . LEU   B 2 144 ? 43.00742 -0.91038  -16.24903 1.000 75.03790  ? 237 LEU   B CA  1 
ATOM   3566 C C   . LEU   B 2 144 ? 43.07027 0.58616   -16.53106 1.000 78.88484  ? 237 LEU   B C   1 
ATOM   3567 O O   . LEU   B 2 144 ? 42.35657 1.06109   -17.42256 1.000 81.44165  ? 237 LEU   B O   1 
ATOM   3568 C CB  . LEU   B 2 144 ? 41.54653 -1.35032  -16.11217 1.000 78.88868  ? 237 LEU   B CB  1 
ATOM   3569 C CG  . LEU   B 2 144 ? 41.29124 -2.85638  -16.01892 1.000 80.84047  ? 237 LEU   B CG  1 
ATOM   3570 C CD1 . LEU   B 2 144 ? 39.80503 -3.14397  -15.85943 1.000 65.27348  ? 237 LEU   B CD1 1 
ATOM   3571 C CD2 . LEU   B 2 144 ? 41.85167 -3.57007  -17.23768 1.000 74.77734  ? 237 LEU   B CD2 1 
ATOM   3572 N N   . LYS   B 2 145 ? 43.90281 1.32705   -15.79400 1.000 76.91974  ? 238 LYS   B N   1 
ATOM   3573 C CA  . LYS   B 2 145 ? 44.01561 2.78134   -15.93150 1.000 77.15967  ? 238 LYS   B CA  1 
ATOM   3574 C C   . LYS   B 2 145 ? 42.65991 3.46436   -15.76582 1.000 78.18063  ? 238 LYS   B C   1 
ATOM   3575 O O   . LYS   B 2 145 ? 42.39065 4.50065   -16.37968 1.000 78.23145  ? 238 LYS   B O   1 
ATOM   3576 C CB  . LYS   B 2 145 ? 44.66116 3.16586   -17.26661 1.000 88.18271  ? 238 LYS   B CB  1 
ATOM   3577 C CG  . LYS   B 2 145 ? 46.06544 2.60955   -17.45899 1.000 84.84538  ? 238 LYS   B CG  1 
ATOM   3578 C CD  . LYS   B 2 145 ? 47.00096 3.07473   -16.35168 1.000 103.19337 ? 238 LYS   B CD  1 
ATOM   3579 C CE  . LYS   B 2 145 ? 47.20784 4.58208   -16.38812 1.000 106.64586 ? 238 LYS   B CE  1 
ATOM   3580 N NZ  . LYS   B 2 145 ? 47.86130 5.02175   -17.65209 1.000 113.42521 ? 238 LYS   B NZ  1 
ATOM   3581 N N   . TRP   B 2 146 ? 41.79849 2.87389   -14.93419 1.000 71.44315  ? 239 TRP   B N   1 
ATOM   3582 C CA  . TRP   B 2 146 ? 40.46457 3.38900   -14.62810 1.000 76.34464  ? 239 TRP   B CA  1 
ATOM   3583 C C   . TRP   B 2 146 ? 39.59050 3.53545   -15.87053 1.000 76.74167  ? 239 TRP   B C   1 
ATOM   3584 O O   . TRP   B 2 146 ? 38.63234 4.31565   -15.87011 1.000 72.30016  ? 239 TRP   B O   1 
ATOM   3585 C CB  . TRP   B 2 146 ? 40.54508 4.72239   -13.87554 1.000 74.22060  ? 239 TRP   B CB  1 
ATOM   3586 C CG  . TRP   B 2 146 ? 41.25511 4.61785   -12.55938 1.000 74.31294  ? 239 TRP   B CG  1 
ATOM   3587 C CD1 . TRP   B 2 146 ? 42.58726 4.80255   -12.32870 1.000 67.41966  ? 239 TRP   B CD1 1 
ATOM   3588 C CD2 . TRP   B 2 146 ? 40.66955 4.29670   -11.29255 1.000 75.02125  ? 239 TRP   B CD2 1 
ATOM   3589 N NE1 . TRP   B 2 146 ? 42.86669 4.61952   -10.99610 1.000 74.60300  ? 239 TRP   B NE1 1 
ATOM   3590 C CE2 . TRP   B 2 146 ? 41.70607 4.30781   -10.33831 1.000 73.16163  ? 239 TRP   B CE2 1 
ATOM   3591 C CE3 . TRP   B 2 146 ? 39.36926 4.00245   -10.87234 1.000 71.24273  ? 239 TRP   B CE3 1 
ATOM   3592 C CZ2 . TRP   B 2 146 ? 41.48270 4.03591   -8.99023  1.000 73.61417  ? 239 TRP   B CZ2 1 
ATOM   3593 C CZ3 . TRP   B 2 146 ? 39.14964 3.73361   -9.53364  1.000 67.80845  ? 239 TRP   B CZ3 1 
ATOM   3594 C CH2 . TRP   B 2 146 ? 40.20050 3.75162   -8.60872  1.000 79.67819  ? 239 TRP   B CH2 1 
ATOM   3595 N N   . ARG   B 2 147 ? 39.89963 2.79560   -16.93465 1.000 73.96611  ? 240 ARG   B N   1 
ATOM   3596 C CA  . ARG   B 2 147 ? 39.07920 2.78708   -18.14518 1.000 74.52677  ? 240 ARG   B CA  1 
ATOM   3597 C C   . ARG   B 2 147 ? 38.03121 1.69641   -17.96536 1.000 67.93600  ? 240 ARG   B C   1 
ATOM   3598 O O   . ARG   B 2 147 ? 38.22287 0.54311   -18.35536 1.000 73.72728  ? 240 ARG   B O   1 
ATOM   3599 C CB  . ARG   B 2 147 ? 39.93971 2.56642   -19.38322 1.000 77.87146  ? 240 ARG   B CB  1 
ATOM   3600 C CG  . ARG   B 2 147 ? 41.11350 3.53069   -19.49080 1.000 79.49361  ? 240 ARG   B CG  1 
ATOM   3601 C CD  . ARG   B 2 147 ? 40.65121 4.97818   -19.40522 1.000 87.69818  ? 240 ARG   B CD  1 
ATOM   3602 N NE  . ARG   B 2 147 ? 40.10782 5.46223   -20.66816 1.000 89.53876  ? 240 ARG   B NE  1 
ATOM   3603 C CZ  . ARG   B 2 147 ? 40.75175 6.27385   -21.49562 1.000 103.79648 ? 240 ARG   B CZ  1 
ATOM   3604 N NH1 . ARG   B 2 147 ? 41.96269 6.72715   -21.21504 1.000 96.30706  ? 240 ARG   B NH1 1 
ATOM   3605 N NH2 . ARG   B 2 147 ? 40.16385 6.64448   -22.63009 1.000 101.47783 ? 240 ARG   B NH2 1 
ATOM   3606 N N   . LEU   B 2 148 ? 36.90518 2.06890   -17.35609 1.000 70.40416  ? 241 LEU   B N   1 
ATOM   3607 C CA  . LEU   B 2 148 ? 35.88070 1.11844   -16.94231 1.000 63.98612  ? 241 LEU   B CA  1 
ATOM   3608 C C   . LEU   B 2 148 ? 34.53960 1.38155   -17.61950 1.000 75.14863  ? 241 LEU   B C   1 
ATOM   3609 O O   . LEU   B 2 148 ? 33.49076 1.03286   -17.07423 1.000 71.75445  ? 241 LEU   B O   1 
ATOM   3610 C CB  . LEU   B 2 148 ? 35.71416 1.14639   -15.42419 1.000 73.01809  ? 241 LEU   B CB  1 
ATOM   3611 C CG  . LEU   B 2 148 ? 37.00408 1.05026   -14.60944 1.000 73.37252  ? 241 LEU   B CG  1 
ATOM   3612 C CD1 . LEU   B 2 148 ? 36.73442 1.35243   -13.14924 1.000 69.54051  ? 241 LEU   B CD1 1 
ATOM   3613 C CD2 . LEU   B 2 148 ? 37.63398 -0.32250  -14.76174 1.000 66.03568  ? 241 LEU   B CD2 1 
ATOM   3614 N N   . SER   B 2 149 ? 34.55018 1.98366   -18.80855 1.000 66.36681  ? 242 SER   B N   1 
ATOM   3615 C CA  . SER   B 2 149 ? 33.32802 2.28643   -19.55365 1.000 64.41251  ? 242 SER   B CA  1 
ATOM   3616 C C   . SER   B 2 149 ? 33.39256 1.71524   -20.96888 1.000 76.04596  ? 242 SER   B C   1 
ATOM   3617 O O   . SER   B 2 149 ? 33.39322 2.46449   -21.95326 1.000 75.48549  ? 242 SER   B O   1 
ATOM   3618 C CB  . SER   B 2 149 ? 33.08605 3.79331   -19.59046 1.000 67.96689  ? 242 SER   B CB  1 
ATOM   3619 O OG  . SER   B 2 149 ? 32.98401 4.32431   -18.27967 1.000 79.53318  ? 242 SER   B OG  1 
ATOM   3620 N N   . PRO   B 2 150 ? 33.43588 0.39206   -21.11081 1.000 75.09083  ? 243 PRO   B N   1 
ATOM   3621 C CA  . PRO   B 2 150 ? 33.46885 -0.20771  -22.44427 1.000 65.10090  ? 243 PRO   B CA  1 
ATOM   3622 C C   . PRO   B 2 150 ? 32.06908 -0.42778  -23.00082 1.000 73.93441  ? 243 PRO   B C   1 
ATOM   3623 O O   . PRO   B 2 150 ? 31.06835 -0.41116  -22.28134 1.000 75.73101  ? 243 PRO   B O   1 
ATOM   3624 C CB  . PRO   B 2 150 ? 34.16770 -1.54891  -22.19121 1.000 71.87340  ? 243 PRO   B CB  1 
ATOM   3625 C CG  . PRO   B 2 150 ? 33.67736 -1.93148  -20.83536 1.000 71.99509  ? 243 PRO   B CG  1 
ATOM   3626 C CD  . PRO   B 2 150 ? 33.49836 -0.64137  -20.05957 1.000 72.75130  ? 243 PRO   B CD  1 
ATOM   3627 N N   . LEU   B 2 151 ? 32.01895 -0.63474  -24.31393 1.000 67.12644  ? 244 LEU   B N   1 
ATOM   3628 C CA  . LEU   B 2 151 ? 30.78393 -1.02096  -24.99220 1.000 75.35871  ? 244 LEU   B CA  1 
ATOM   3629 C C   . LEU   B 2 151 ? 30.74059 -2.54327  -25.02147 1.000 77.13130  ? 244 LEU   B C   1 
ATOM   3630 O O   . LEU   B 2 151 ? 31.38560 -3.18030  -25.85754 1.000 82.72437  ? 244 LEU   B O   1 
ATOM   3631 C CB  . LEU   B 2 151 ? 30.72024 -0.41842  -26.39050 1.000 65.99409  ? 244 LEU   B CB  1 
ATOM   3632 C CG  . LEU   B 2 151 ? 30.70795 1.11178   -26.43857 1.000 77.89031  ? 244 LEU   B CG  1 
ATOM   3633 C CD1 . LEU   B 2 151 ? 30.52975 1.60836   -27.86335 1.000 67.84956  ? 244 LEU   B CD1 1 
ATOM   3634 C CD2 . LEU   B 2 151 ? 29.62444 1.67727   -25.52992 1.000 75.81454  ? 244 LEU   B CD2 1 
ATOM   3635 N N   . THR   B 2 152 ? 29.97908 -3.12749  -24.10022 1.000 69.06211  ? 245 THR   B N   1 
ATOM   3636 C CA  . THR   B 2 152 ? 29.97478 -4.56940  -23.91781 1.000 71.20415  ? 245 THR   B CA  1 
ATOM   3637 C C   . THR   B 2 152 ? 29.35697 -5.27179  -25.12677 1.000 70.75900  ? 245 THR   B C   1 
ATOM   3638 O O   . THR   B 2 152 ? 28.78587 -4.64907  -26.02719 1.000 68.66464  ? 245 THR   B O   1 
ATOM   3639 C CB  . THR   B 2 152 ? 29.21225 -4.94518  -22.64779 1.000 68.72168  ? 245 THR   B CB  1 
ATOM   3640 O OG1 . THR   B 2 152 ? 27.86136 -4.47755  -22.74517 1.000 72.20314  ? 245 THR   B OG1 1 
ATOM   3641 C CG2 . THR   B 2 152 ? 29.87393 -4.32699  -21.42217 1.000 67.61501  ? 245 THR   B CG2 1 
ATOM   3642 N N   . ILE   B 2 153 ? 29.48479 -6.60050  -25.13538 1.000 67.60761  ? 246 ILE   B N   1 
ATOM   3643 C CA  . ILE   B 2 153 ? 28.88417 -7.40025  -26.19891 1.000 67.59429  ? 246 ILE   B CA  1 
ATOM   3644 C C   . ILE   B 2 153 ? 27.36701 -7.27241  -26.16551 1.000 70.30531  ? 246 ILE   B C   1 
ATOM   3645 O O   . ILE   B 2 153 ? 26.70940 -7.20017  -27.21129 1.000 69.04397  ? 246 ILE   B O   1 
ATOM   3646 C CB  . ILE   B 2 153 ? 29.33082 -8.86911  -26.07595 1.000 69.48798  ? 246 ILE   B CB  1 
ATOM   3647 C CG1 . ILE   B 2 153 ? 30.85571 -8.97320  -26.12178 1.000 70.56649  ? 246 ILE   B CG1 1 
ATOM   3648 C CG2 . ILE   B 2 153 ? 28.70581 -9.71434  -27.17053 1.000 69.09919  ? 246 ILE   B CG2 1 
ATOM   3649 C CD1 . ILE   B 2 153 ? 31.37244 -10.38423 -25.94236 1.000 71.12537  ? 246 ILE   B CD1 1 
ATOM   3650 N N   . VAL   B 2 154 ? 26.78779 -7.23190  -24.96410 1.000 66.57625  ? 247 VAL   B N   1 
ATOM   3651 C CA  . VAL   B 2 154 ? 25.33669 -7.15936  -24.84010 1.000 60.26774  ? 247 VAL   B CA  1 
ATOM   3652 C C   . VAL   B 2 154 ? 24.80835 -5.75160  -25.08980 1.000 60.62838  ? 247 VAL   B C   1 
ATOM   3653 O O   . VAL   B 2 154 ? 23.63733 -5.59509  -25.45791 1.000 66.53058  ? 247 VAL   B O   1 
ATOM   3654 C CB  . VAL   B 2 154 ? 24.89362 -7.67125  -23.45782 1.000 63.84317  ? 247 VAL   B CB  1 
ATOM   3655 C CG1 . VAL   B 2 154 ? 25.22372 -6.65664  -22.37029 1.000 68.89438  ? 247 VAL   B CG1 1 
ATOM   3656 C CG2 . VAL   B 2 154 ? 23.40943 -8.01751  -23.45970 1.000 63.48836  ? 247 VAL   B CG2 1 
ATOM   3657 N N   . SER   B 2 155 ? 25.63858 -4.72001  -24.91214 1.000 61.16397  ? 248 SER   B N   1 
ATOM   3658 C CA  . SER   B 2 155 ? 25.18780 -3.36182  -25.19504 1.000 65.68138  ? 248 SER   B CA  1 
ATOM   3659 C C   . SER   B 2 155 ? 25.00931 -3.13318  -26.68961 1.000 67.00425  ? 248 SER   B C   1 
ATOM   3660 O O   . SER   B 2 155 ? 24.12799 -2.36764  -27.09655 1.000 74.14993  ? 248 SER   B O   1 
ATOM   3661 C CB  . SER   B 2 155 ? 26.17148 -2.34583  -24.61600 1.000 60.53021  ? 248 SER   B CB  1 
ATOM   3662 O OG  . SER   B 2 155 ? 27.44525 -2.46523  -25.22338 1.000 69.80207  ? 248 SER   B OG  1 
ATOM   3663 N N   . TRP   B 2 156 ? 25.83372 -3.78003  -27.51773 1.000 67.77331  ? 249 TRP   B N   1 
ATOM   3664 C CA  . TRP   B 2 156 ? 25.65885 -3.67871  -28.96293 1.000 65.81311  ? 249 TRP   B CA  1 
ATOM   3665 C C   . TRP   B 2 156 ? 24.36194 -4.34036  -29.40935 1.000 65.06947  ? 249 TRP   B C   1 
ATOM   3666 O O   . TRP   B 2 156 ? 23.66900 -3.82456  -30.29449 1.000 65.37237  ? 249 TRP   B O   1 
ATOM   3667 C CB  . TRP   B 2 156 ? 26.85060 -4.30388  -29.68679 1.000 68.86740  ? 249 TRP   B CB  1 
ATOM   3668 C CG  . TRP   B 2 156 ? 28.06464 -3.43312  -29.72461 1.000 70.80081  ? 249 TRP   B CG  1 
ATOM   3669 C CD1 . TRP   B 2 156 ? 29.22996 -3.61863  -29.04068 1.000 68.65349  ? 249 TRP   B CD1 1 
ATOM   3670 C CD2 . TRP   B 2 156 ? 28.23436 -2.23511  -30.48987 1.000 68.23838  ? 249 TRP   B CD2 1 
ATOM   3671 N NE1 . TRP   B 2 156 ? 30.11633 -2.61055  -29.33422 1.000 67.91899  ? 249 TRP   B NE1 1 
ATOM   3672 C CE2 . TRP   B 2 156 ? 29.52817 -1.74767  -30.22116 1.000 72.83103  ? 249 TRP   B CE2 1 
ATOM   3673 C CE3 . TRP   B 2 156 ? 27.41712 -1.52689  -31.37603 1.000 75.57135  ? 249 TRP   B CE3 1 
ATOM   3674 C CZ2 . TRP   B 2 156 ? 30.02374 -0.58538  -30.80688 1.000 70.45008  ? 249 TRP   B CZ2 1 
ATOM   3675 C CZ3 . TRP   B 2 156 ? 27.91079 -0.37322  -31.95590 1.000 78.41007  ? 249 TRP   B CZ3 1 
ATOM   3676 C CH2 . TRP   B 2 156 ? 29.20144 0.08577   -31.66905 1.000 82.48713  ? 249 TRP   B CH2 1 
ATOM   3677 N N   . LEU   B 2 157 ? 24.02046 -5.48524  -28.81094 1.000 69.71776  ? 250 LEU   B N   1 
ATOM   3678 C CA  . LEU   B 2 157 ? 22.76640 -6.15144  -29.14501 1.000 65.96682  ? 250 LEU   B CA  1 
ATOM   3679 C C   . LEU   B 2 157 ? 21.56368 -5.27201  -28.82940 1.000 69.68831  ? 250 LEU   B C   1 
ATOM   3680 O O   . LEU   B 2 157 ? 20.55660 -5.31860  -29.54502 1.000 63.11592  ? 250 LEU   B O   1 
ATOM   3681 C CB  . LEU   B 2 157 ? 22.66707 -7.48211  -28.39888 1.000 68.55704  ? 250 LEU   B CB  1 
ATOM   3682 C CG  . LEU   B 2 157 ? 21.38774 -8.29450  -28.61017 1.000 69.45855  ? 250 LEU   B CG  1 
ATOM   3683 C CD1 . LEU   B 2 157 ? 21.21867 -8.65552  -30.07804 1.000 68.84107  ? 250 LEU   B CD1 1 
ATOM   3684 C CD2 . LEU   B 2 157 ? 21.38817 -9.54327  -27.73872 1.000 81.95213  ? 250 LEU   B CD2 1 
ATOM   3685 N N   . ASN   B 2 158 ? 21.64750 -4.46642  -27.76751 1.000 76.78322  ? 251 ASN   B N   1 
ATOM   3686 C CA  . ASN   B 2 158 ? 20.57150 -3.52719  -27.46791 1.000 76.77592  ? 251 ASN   B CA  1 
ATOM   3687 C C   . ASN   B 2 158 ? 20.42490 -2.48999  -28.57512 1.000 76.71863  ? 251 ASN   B C   1 
ATOM   3688 O O   . ASN   B 2 158 ? 19.30425 -2.11232  -28.93871 1.000 79.16272  ? 251 ASN   B O   1 
ATOM   3689 C CB  . ASN   B 2 158 ? 20.82751 -2.84597  -26.12295 1.000 74.61804  ? 251 ASN   B CB  1 
ATOM   3690 C CG  . ASN   B 2 158 ? 19.76981 -3.17972  -25.08733 1.000 83.01260  ? 251 ASN   B CG  1 
ATOM   3691 O OD1 . ASN   B 2 158 ? 19.93863 -4.09477  -24.28191 1.000 88.23832  ? 251 ASN   B OD1 1 
ATOM   3692 N ND2 . ASN   B 2 158 ? 18.67059 -2.43514  -25.10408 1.000 79.69276  ? 251 ASN   B ND2 1 
ATOM   3693 N N   . VAL   B 2 159 ? 21.54720 -2.02016  -29.12490 1.000 81.05207  ? 252 VAL   B N   1 
ATOM   3694 C CA  . VAL   B 2 159 ? 21.49394 -1.06857  -30.23039 1.000 69.02264  ? 252 VAL   B CA  1 
ATOM   3695 C C   . VAL   B 2 159 ? 20.90496 -1.73171  -31.46855 1.000 78.76728  ? 252 VAL   B C   1 
ATOM   3696 O O   . VAL   B 2 159 ? 20.05161 -1.15902  -32.15686 1.000 77.43656  ? 252 VAL   B O   1 
ATOM   3697 C CB  . VAL   B 2 159 ? 22.89463 -0.49408  -30.51498 1.000 79.53804  ? 252 VAL   B CB  1 
ATOM   3698 C CG1 . VAL   B 2 159 ? 22.83400 0.52083   -31.64766 1.000 86.70741  ? 252 VAL   B CG1 1 
ATOM   3699 C CG2 . VAL   B 2 159 ? 23.48881 0.13196   -29.26201 1.000 70.68100  ? 252 VAL   B CG2 1 
ATOM   3700 N N   . TYR   B 2 160 ? 21.34901 -2.95506  -31.76529 1.000 76.75441  ? 253 TYR   B N   1 
ATOM   3701 C CA  . TYR   B 2 160 ? 20.88504 -3.64177  -32.96518 1.000 78.65641  ? 253 TYR   B CA  1 
ATOM   3702 C C   . TYR   B 2 160 ? 19.40255 -3.98016  -32.88013 1.000 83.60605  ? 253 TYR   B C   1 
ATOM   3703 O O   . TYR   B 2 160 ? 18.71162 -3.99112  -33.90520 1.000 80.99039  ? 253 TYR   B O   1 
ATOM   3704 C CB  . TYR   B 2 160 ? 21.70427 -4.91320  -33.19972 1.000 79.59894  ? 253 TYR   B CB  1 
ATOM   3705 C CG  . TYR   B 2 160 ? 23.19409 -4.68498  -33.35967 1.000 77.74936  ? 253 TYR   B CG  1 
ATOM   3706 C CD1 . TYR   B 2 160 ? 23.69641 -3.43825  -33.71360 1.000 76.18280  ? 253 TYR   B CD1 1 
ATOM   3707 C CD2 . TYR   B 2 160 ? 24.09814 -5.72172  -33.16198 1.000 70.11483  ? 253 TYR   B CD2 1 
ATOM   3708 C CE1 . TYR   B 2 160 ? 25.05430 -3.23079  -33.85962 1.000 76.01708  ? 253 TYR   B CE1 1 
ATOM   3709 C CE2 . TYR   B 2 160 ? 25.45821 -5.52245  -33.30755 1.000 65.91431  ? 253 TYR   B CE2 1 
ATOM   3710 C CZ  . TYR   B 2 160 ? 25.92973 -4.27619  -33.65627 1.000 71.22341  ? 253 TYR   B CZ  1 
ATOM   3711 O OH  . TYR   B 2 160 ? 27.28195 -4.07304  -33.80240 1.000 76.37473  ? 253 TYR   B OH  1 
ATOM   3712 N N   . MET   B 2 161 ? 18.89618 -4.25290  -31.67607 1.000 77.67543  ? 254 MET   B N   1 
ATOM   3713 C CA  . MET   B 2 161 ? 17.48262 -4.57272  -31.52286 1.000 84.54722  ? 254 MET   B CA  1 
ATOM   3714 C C   . MET   B 2 161 ? 16.60197 -3.33456  -31.61902 1.000 88.65694  ? 254 MET   B C   1 
ATOM   3715 O O   . MET   B 2 161 ? 15.44302 -3.43518  -32.03781 1.000 91.72092  ? 254 MET   B O   1 
ATOM   3716 C CB  . MET   B 2 161 ? 17.23995 -5.28135  -30.18951 1.000 74.83857  ? 254 MET   B CB  1 
ATOM   3717 C CG  . MET   B 2 161 ? 17.73466 -6.71609  -30.15033 1.000 69.13918  ? 254 MET   B CG  1 
ATOM   3718 S SD  . MET   B 2 161 ? 16.94610 -7.73686  -31.40650 1.000 88.74544  ? 254 MET   B SD  1 
ATOM   3719 C CE  . MET   B 2 161 ? 15.21903 -7.46616  -31.01660 1.000 87.66549  ? 254 MET   B CE  1 
ATOM   3720 N N   . GLN   B 2 162 ? 17.12382 -2.16707  -31.23962 1.000 86.60618  ? 255 GLN   B N   1 
ATOM   3721 C CA  . GLN   B 2 162 ? 16.32980 -0.94503  -31.31569 1.000 90.32104  ? 255 GLN   B CA  1 
ATOM   3722 C C   . GLN   B 2 162 ? 16.16821 -0.48206  -32.75880 1.000 98.01436  ? 255 GLN   B C   1 
ATOM   3723 O O   . GLN   B 2 162 ? 15.06705 -0.11688  -33.18395 1.000 94.74585  ? 255 GLN   B O   1 
ATOM   3724 C CB  . GLN   B 2 162 ? 16.97265 0.15005   -30.46636 1.000 90.29271  ? 255 GLN   B CB  1 
ATOM   3725 C CG  . GLN   B 2 162 ? 16.17278 1.44101   -30.40966 1.000 96.06468  ? 255 GLN   B CG  1 
ATOM   3726 C CD  . GLN   B 2 162 ? 14.81197 1.25365   -29.76774 1.000 98.47827  ? 255 GLN   B CD  1 
ATOM   3727 O OE1 . GLN   B 2 162 ? 14.63686 0.40796   -28.89014 1.000 100.24464 ? 255 GLN   B OE1 1 
ATOM   3728 N NE2 . GLN   B 2 162 ? 13.83857 2.04193   -30.20577 1.000 105.45656 ? 255 GLN   B NE2 1 
ATOM   3729 N N   . VAL   B 2 163 ? 17.25855 -0.49143  -33.52892 1.000 89.03725  ? 256 VAL   B N   1 
ATOM   3730 C CA  . VAL   B 2 163 ? 17.19169 -0.05857  -34.92094 1.000 95.67661  ? 256 VAL   B CA  1 
ATOM   3731 C C   . VAL   B 2 163 ? 16.34419 -1.01784  -35.74760 1.000 93.62435  ? 256 VAL   B C   1 
ATOM   3732 O O   . VAL   B 2 163 ? 15.66296 -0.59876  -36.69151 1.000 88.92400  ? 256 VAL   B O   1 
ATOM   3733 C CB  . VAL   B 2 163 ? 18.61293 0.08715   -35.49588 1.000 82.97092  ? 256 VAL   B CB  1 
ATOM   3734 C CG1 . VAL   B 2 163 ? 18.56139 0.63258   -36.91650 1.000 86.11533  ? 256 VAL   B CG1 1 
ATOM   3735 C CG2 . VAL   B 2 163 ? 19.45304 0.98942   -34.60523 1.000 84.92843  ? 256 VAL   B CG2 1 
ATOM   3736 N N   . ALA   B 2 164 ? 16.36102 -2.31019  -35.41028 1.000 85.39042  ? 257 ALA   B N   1 
ATOM   3737 C CA  . ALA   B 2 164 ? 15.54987 -3.27646  -36.14446 1.000 96.94535  ? 257 ALA   B CA  1 
ATOM   3738 C C   . ALA   B 2 164 ? 14.06474 -2.97919  -35.99246 1.000 102.53044 ? 257 ALA   B C   1 
ATOM   3739 O O   . ALA   B 2 164 ? 13.28800 -3.15527  -36.93822 1.000 97.73735  ? 257 ALA   B O   1 
ATOM   3740 C CB  . ALA   B 2 164 ? 15.86712 -4.69504  -35.67201 1.000 90.34211  ? 257 ALA   B CB  1 
ATOM   3741 N N   . TYR   B 2 165 ? 13.65129 -2.52238  -34.81261 1.000 98.80620  ? 258 TYR   B N   1 
ATOM   3742 C CA  . TYR   B 2 165 ? 12.25495 -2.17415  -34.58889 1.000 95.81869  ? 258 TYR   B CA  1 
ATOM   3743 C C   . TYR   B 2 165 ? 12.09222 -0.66676  -34.45348 1.000 101.33439 ? 258 TYR   B C   1 
ATOM   3744 O O   . TYR   B 2 165 ? 11.60051 -0.17406  -33.43333 1.000 115.20137 ? 258 TYR   B O   1 
ATOM   3745 C CB  . TYR   B 2 165 ? 11.71429 -2.89656  -33.35404 1.000 96.17239  ? 258 TYR   B CB  1 
ATOM   3746 C CG  . TYR   B 2 165 ? 11.44615 -4.36215  -33.60042 1.000 100.19543 ? 258 TYR   B CG  1 
ATOM   3747 C CD1 . TYR   B 2 165 ? 12.46751 -5.29915  -33.51576 1.000 95.02783  ? 258 TYR   B CD1 1 
ATOM   3748 C CD2 . TYR   B 2 165 ? 10.17273 -4.80789  -33.93015 1.000 98.62292  ? 258 TYR   B CD2 1 
ATOM   3749 C CE1 . TYR   B 2 165 ? 12.22688 -6.64058  -33.74786 1.000 98.03162  ? 258 TYR   B CE1 1 
ATOM   3750 C CE2 . TYR   B 2 165 ? 9.92205  -6.14654  -34.16228 1.000 92.56945  ? 258 TYR   B CE2 1 
ATOM   3751 C CZ  . TYR   B 2 165 ? 10.95179 -7.05836  -34.06991 1.000 94.40913  ? 258 TYR   B CZ  1 
ATOM   3752 O OH  . TYR   B 2 165 ? 10.70337 -8.39213  -34.29977 1.000 99.19467  ? 258 TYR   B OH  1 
ATOM   3753 N N   . LEU   B 2 166 ? 12.50960 0.06912   -35.47793 1.000 100.49904 ? 259 LEU   B N   1 
ATOM   3754 C CA  . LEU   B 2 166 ? 12.33357 1.51160   -35.53494 1.000 112.11824 ? 259 LEU   B CA  1 
ATOM   3755 C C   . LEU   B 2 166 ? 11.20972 1.85740   -36.50026 1.000 127.17709 ? 259 LEU   B C   1 
ATOM   3756 O O   . LEU   B 2 166 ? 11.04873 1.21311   -37.54110 1.000 119.52502 ? 259 LEU   B O   1 
ATOM   3757 C CB  . LEU   B 2 166 ? 13.62305 2.20988   -35.97093 1.000 111.69035 ? 259 LEU   B CB  1 
ATOM   3758 C CG  . LEU   B 2 166 ? 14.59674 2.61875   -34.86603 1.000 108.86474 ? 259 LEU   B CG  1 
ATOM   3759 C CD1 . LEU   B 2 166 ? 15.81073 3.31489   -35.45802 1.000 106.21598 ? 259 LEU   B CD1 1 
ATOM   3760 C CD2 . LEU   B 2 166 ? 13.90384 3.51229   -33.84942 1.000 108.26025 ? 259 LEU   B CD2 1 
ATOM   3761 N N   . ASN   B 2 167 ? 10.43600 2.87586   -36.14738 1.000 142.51270 ? 260 ASN   B N   1 
ATOM   3762 C CA  . ASN   B 2 167 ? 9.35573  3.37887   -36.97634 1.000 156.49736 ? 260 ASN   B CA  1 
ATOM   3763 C C   . ASN   B 2 167 ? 9.76240  4.72851   -37.56348 1.000 175.13676 ? 260 ASN   B C   1 
ATOM   3764 O O   . ASN   B 2 167 ? 10.93679 5.11475   -37.53558 1.000 171.23841 ? 260 ASN   B O   1 
ATOM   3765 C CB  . ASN   B 2 167 ? 8.06792  3.47247   -36.15532 1.000 157.01303 ? 260 ASN   B CB  1 
ATOM   3766 C CG  . ASN   B 2 167 ? 7.82273  2.23413   -35.31461 1.000 150.52065 ? 260 ASN   B CG  1 
ATOM   3767 O OD1 . ASN   B 2 167 ? 7.75252  2.30746   -34.08767 1.000 146.08279 ? 260 ASN   B OD1 1 
ATOM   3768 N ND2 . ASN   B 2 167 ? 7.69488  1.08728   -35.97178 1.000 147.57704 ? 260 ASN   B ND2 1 
ATOM   3769 N N   . ASP   B 2 168 ? 8.78210  5.45528   -38.10167 1.000 186.40170 ? 261 ASP   B N   1 
ATOM   3770 C CA  . ASP   B 2 168 ? 9.05573  6.79618   -38.60223 1.000 192.04628 ? 261 ASP   B CA  1 
ATOM   3771 C C   . ASP   B 2 168 ? 9.23850  7.81225   -37.48404 1.000 188.26841 ? 261 ASP   B C   1 
ATOM   3772 O O   . ASP   B 2 168 ? 9.61947  8.95356   -37.76530 1.000 190.27033 ? 261 ASP   B O   1 
ATOM   3773 C CB  . ASP   B 2 168 ? 7.93778  7.25077   -39.54145 1.000 202.18763 ? 261 ASP   B CB  1 
ATOM   3774 C CG  . ASP   B 2 168 ? 8.03776  6.61449   -40.91319 1.000 209.19143 ? 261 ASP   B CG  1 
ATOM   3775 O OD1 . ASP   B 2 168 ? 9.16737  6.28835   -41.33518 1.000 212.25177 ? 261 ASP   B OD1 1 
ATOM   3776 O OD2 . ASP   B 2 168 ? 6.98982  6.44286   -41.57034 1.000 213.74054 ? 261 ASP   B OD2 1 
ATOM   3777 N N   . LEU   B 2 169 ? 8.97634  7.42995   -36.23174 1.000 170.62239 ? 262 LEU   B N   1 
ATOM   3778 C CA  . LEU   B 2 169 ? 9.23457  8.33146   -35.11489 1.000 164.57345 ? 262 LEU   B CA  1 
ATOM   3779 C C   . LEU   B 2 169 ? 10.72740 8.55179   -34.91163 1.000 161.76453 ? 262 LEU   B C   1 
ATOM   3780 O O   . LEU   B 2 169 ? 11.13524 9.61793   -34.43633 1.000 158.85589 ? 262 LEU   B O   1 
ATOM   3781 C CB  . LEU   B 2 169 ? 8.60263  7.78677   -33.83156 1.000 156.63253 ? 262 LEU   B CB  1 
ATOM   3782 C CG  . LEU   B 2 169 ? 7.07766  7.82056   -33.68186 1.000 144.40087 ? 262 LEU   B CG  1 
ATOM   3783 C CD1 . LEU   B 2 169 ? 6.40033  6.72161   -34.49211 1.000 143.35329 ? 262 LEU   B CD1 1 
ATOM   3784 C CD2 . LEU   B 2 169 ? 6.68731  7.72271   -32.21390 1.000 128.83673 ? 262 LEU   B CD2 1 
ATOM   3785 N N   . HIS   B 2 170 ? 11.54888 7.55951   -35.25921 1.000 163.27051 ? 263 HIS   B N   1 
ATOM   3786 C CA  . HIS   B 2 170 ? 13.00587 7.62618   -35.15314 1.000 157.17896 ? 263 HIS   B CA  1 
ATOM   3787 C C   . HIS   B 2 170 ? 13.47964 7.94224   -33.73820 1.000 151.93484 ? 263 HIS   B C   1 
ATOM   3788 O O   . HIS   B 2 170 ? 14.59134 8.44784   -33.55276 1.000 147.90783 ? 263 HIS   B O   1 
ATOM   3789 C CB  . HIS   B 2 170 ? 13.59062 8.64174   -36.14266 1.000 155.36004 ? 263 HIS   B CB  1 
ATOM   3790 C CG  . HIS   B 2 170 ? 13.61480 8.15913   -37.55951 1.000 160.22636 ? 263 HIS   B CG  1 
ATOM   3791 N ND1 . HIS   B 2 170 ? 13.23380 6.88388   -37.91734 1.000 163.89648 ? 263 HIS   B ND1 1 
ATOM   3792 C CD2 . HIS   B 2 170 ? 13.97806 8.77906   -38.70729 1.000 157.45890 ? 263 HIS   B CD2 1 
ATOM   3793 C CE1 . HIS   B 2 170 ? 13.35951 6.73938   -39.22442 1.000 166.20906 ? 263 HIS   B CE1 1 
ATOM   3794 N NE2 . HIS   B 2 170 ? 13.80924 7.87477   -39.72763 1.000 159.57512 ? 263 HIS   B NE2 1 
ATOM   3795 N N   . GLU   B 2 171 ? 12.66002 7.65275   -32.72967 1.000 151.52651 ? 264 GLU   B N   1 
ATOM   3796 C CA  . GLU   B 2 171 ? 13.04027 7.87780   -31.33619 1.000 144.17956 ? 264 GLU   B CA  1 
ATOM   3797 C C   . GLU   B 2 171 ? 13.88799 6.69318   -30.88936 1.000 134.52897 ? 264 GLU   B C   1 
ATOM   3798 O O   . GLU   B 2 171 ? 13.37741 5.65651   -30.46292 1.000 127.51899 ? 264 GLU   B O   1 
ATOM   3799 C CB  . GLU   B 2 171 ? 11.80802 8.05676   -30.45853 1.000 142.69618 ? 264 GLU   B CB  1 
ATOM   3800 C CG  . GLU   B 2 171 ? 12.11215 8.65819   -29.09842 1.000 136.69621 ? 264 GLU   B CG  1 
ATOM   3801 C CD  . GLU   B 2 171 ? 12.67133 10.06411  -29.20026 1.000 140.53070 ? 264 GLU   B CD  1 
ATOM   3802 O OE1 . GLU   B 2 171 ? 12.11703 10.87093  -29.97649 1.000 134.45146 ? 264 GLU   B OE1 1 
ATOM   3803 O OE2 . GLU   B 2 171 ? 13.67026 10.35962  -28.51127 1.000 139.52884 ? 264 GLU   B OE2 1 
ATOM   3804 N N   . VAL   B 2 172 ? 15.21163 6.85424   -30.98665 1.000 121.30400 ? 265 VAL   B N   1 
ATOM   3805 C CA  . VAL   B 2 172 ? 16.13366 5.74313   -30.75198 1.000 114.30495 ? 265 VAL   B CA  1 
ATOM   3806 C C   . VAL   B 2 172 ? 16.42952 5.50345   -29.28003 1.000 101.53124 ? 265 VAL   B C   1 
ATOM   3807 O O   . VAL   B 2 172 ? 17.04786 4.48609   -28.94247 1.000 98.34285  ? 265 VAL   B O   1 
ATOM   3808 C CB  . VAL   B 2 172 ? 17.45164 5.98250   -31.51488 1.000 112.44579 ? 265 VAL   B CB  1 
ATOM   3809 C CG1 . VAL   B 2 172 ? 18.39374 6.86132   -30.70291 1.000 101.87912 ? 265 VAL   B CG1 1 
ATOM   3810 C CG2 . VAL   B 2 172 ? 18.11265 4.65849   -31.89347 1.000 105.76270 ? 265 VAL   B CG2 1 
ATOM   3811 N N   . LEU   B 2 173 ? 15.99849 6.39783   -28.38956 1.000 101.04614 ? 266 LEU   B N   1 
ATOM   3812 C CA  . LEU   B 2 173 ? 16.29733 6.26428   -26.96967 1.000 93.85649  ? 266 LEU   B CA  1 
ATOM   3813 C C   . LEU   B 2 173 ? 15.20846 5.55724   -26.17360 1.000 91.15827  ? 266 LEU   B C   1 
ATOM   3814 O O   . LEU   B 2 173 ? 15.49527 5.05401   -25.08192 1.000 86.85412  ? 266 LEU   B O   1 
ATOM   3815 C CB  . LEU   B 2 173 ? 16.55975 7.64107   -26.34798 1.000 88.55217  ? 266 LEU   B CB  1 
ATOM   3816 C CG  . LEU   B 2 173 ? 17.83029 8.34401   -26.82450 1.000 87.19009  ? 266 LEU   B CG  1 
ATOM   3817 C CD1 . LEU   B 2 173 ? 18.09268 9.61121   -26.01871 1.000 83.96599  ? 266 LEU   B CD1 1 
ATOM   3818 C CD2 . LEU   B 2 173 ? 19.01577 7.39329   -26.74378 1.000 88.28027  ? 266 LEU   B CD2 1 
ATOM   3819 N N   . LEU   B 2 174 ? 13.97809 5.50830   -26.67615 1.000 91.48748  ? 267 LEU   B N   1 
ATOM   3820 C CA  . LEU   B 2 174 ? 12.91257 4.78928   -25.98944 1.000 87.78471  ? 267 LEU   B CA  1 
ATOM   3821 C C   . LEU   B 2 174 ? 12.90834 3.33808   -26.45004 1.000 97.55425  ? 267 LEU   B C   1 
ATOM   3822 O O   . LEU   B 2 174 ? 12.76164 3.08491   -27.65356 1.000 101.93647 ? 267 LEU   B O   1 
ATOM   3823 C CB  . LEU   B 2 174 ? 11.56151 5.42752   -26.26456 1.000 89.83042  ? 267 LEU   B CB  1 
ATOM   3824 C CG  . LEU   B 2 174 ? 10.47139 5.16727   -25.22264 1.000 85.77409  ? 267 LEU   B CG  1 
ATOM   3825 C CD1 . LEU   B 2 174 ? 10.61486 6.12733   -24.05071 1.000 81.68386  ? 267 LEU   B CD1 1 
ATOM   3826 C CD2 . LEU   B 2 174 ? 9.08332  5.26594   -25.83655 1.000 89.90312  ? 267 LEU   B CD2 1 
ATOM   3827 N N   . PRO   B 2 175 ? 13.06682 2.36712   -25.55071 1.000 91.57334  ? 268 PRO   B N   1 
ATOM   3828 C CA  . PRO   B 2 175 ? 13.18603 0.97108   -25.98950 1.000 93.20034  ? 268 PRO   B CA  1 
ATOM   3829 C C   . PRO   B 2 175 ? 11.87362 0.43039   -26.53579 1.000 97.17007  ? 268 PRO   B C   1 
ATOM   3830 O O   . PRO   B 2 175 ? 10.79426 0.71447   -26.01098 1.000 95.71428  ? 268 PRO   B O   1 
ATOM   3831 C CB  . PRO   B 2 175 ? 13.60500 0.23417   -24.71231 1.000 94.62838  ? 268 PRO   B CB  1 
ATOM   3832 C CG  . PRO   B 2 175 ? 13.06604 1.07686   -23.60412 1.000 94.16884  ? 268 PRO   B CG  1 
ATOM   3833 C CD  . PRO   B 2 175 ? 13.16974 2.50013   -24.08705 1.000 88.33537  ? 268 PRO   B CD  1 
ATOM   3834 N N   . GLN   B 2 176 ? 11.98122 -0.36602  -27.60381 1.000 94.17156  ? 269 GLN   B N   1 
ATOM   3835 C CA  . GLN   B 2 176 ? 10.80582 -0.98031  -28.22098 1.000 96.39056  ? 269 GLN   B CA  1 
ATOM   3836 C C   . GLN   B 2 176 ? 11.29423 -2.12104  -29.11533 1.000 97.35678  ? 269 GLN   B C   1 
ATOM   3837 O O   . GLN   B 2 176 ? 11.71865 -1.87947  -30.24860 1.000 102.39314 ? 269 GLN   B O   1 
ATOM   3838 C CB  . GLN   B 2 176 ? 9.99827  0.04231   -29.00703 1.000 96.62400  ? 269 GLN   B CB  1 
ATOM   3839 C CG  . GLN   B 2 176 ? 8.63460  -0.45649  -29.47519 1.000 108.59642 ? 269 GLN   B CG  1 
ATOM   3840 C CD  . GLN   B 2 176 ? 8.70111  -1.22311  -30.78307 1.000 113.03961 ? 269 GLN   B CD  1 
ATOM   3841 O OE1 . GLN   B 2 176 ? 9.45015  -0.86130  -31.68981 1.000 111.81507 ? 269 GLN   B OE1 1 
ATOM   3842 N NE2 . GLN   B 2 176 ? 7.91730  -2.29033  -30.88495 1.000 102.72709 ? 269 GLN   B NE2 1 
ATOM   3843 N N   . TYR   B 2 177 ? 11.23140 -3.34167  -28.59656 1.000 92.76642  ? 270 TYR   B N   1 
ATOM   3844 C CA  . TYR   B 2 177 ? 11.55156 -4.54613  -29.35159 1.000 92.85444  ? 270 TYR   B CA  1 
ATOM   3845 C C   . TYR   B 2 177 ? 11.10165 -5.75621  -28.53540 1.000 82.27270  ? 270 TYR   B C   1 
ATOM   3846 O O   . TYR   B 2 177 ? 10.98941 -5.66810  -27.30869 1.000 94.99674  ? 270 TYR   B O   1 
ATOM   3847 C CB  . TYR   B 2 177 ? 13.05454 -4.63307  -29.67159 1.000 87.27588  ? 270 TYR   B CB  1 
ATOM   3848 C CG  . TYR   B 2 177 ? 13.96941 -4.50595  -28.47551 1.000 95.16467  ? 270 TYR   B CG  1 
ATOM   3849 C CD1 . TYR   B 2 177 ? 14.31663 -5.61824  -27.71854 1.000 82.86958  ? 270 TYR   B CD1 1 
ATOM   3850 C CD2 . TYR   B 2 177 ? 14.50087 -3.27521  -28.11398 1.000 88.11743  ? 270 TYR   B CD2 1 
ATOM   3851 C CE1 . TYR   B 2 177 ? 15.15663 -5.50512  -26.62811 1.000 79.43468  ? 270 TYR   B CE1 1 
ATOM   3852 C CE2 . TYR   B 2 177 ? 15.34200 -3.15277  -27.02587 1.000 82.51290  ? 270 TYR   B CE2 1 
ATOM   3853 C CZ  . TYR   B 2 177 ? 15.66649 -4.27017  -26.28677 1.000 86.14389  ? 270 TYR   B CZ  1 
ATOM   3854 O OH  . TYR   B 2 177 ? 16.50458 -4.15062  -25.20348 1.000 82.67344  ? 270 TYR   B OH  1 
ATOM   3855 N N   . PRO   B 2 178 ? 10.82696 -6.88178  -29.19514 1.000 89.08336  ? 271 PRO   B N   1 
ATOM   3856 C CA  . PRO   B 2 178 ? 10.38073 -8.07513  -28.46372 1.000 82.88282  ? 271 PRO   B CA  1 
ATOM   3857 C C   . PRO   B 2 178 ? 11.44490 -8.57641  -27.49834 1.000 82.42963  ? 271 PRO   B C   1 
ATOM   3858 O O   . PRO   B 2 178 ? 12.61113 -8.74796  -27.86084 1.000 74.19843  ? 271 PRO   B O   1 
ATOM   3859 C CB  . PRO   B 2 178 ? 10.10553 -9.09173  -29.57832 1.000 74.15239  ? 271 PRO   B CB  1 
ATOM   3860 C CG  . PRO   B 2 178 ? 9.85057  -8.26313  -30.79206 1.000 92.08101  ? 271 PRO   B CG  1 
ATOM   3861 C CD  . PRO   B 2 178 ? 10.74331 -7.06780  -30.65306 1.000 83.31273  ? 271 PRO   B CD  1 
ATOM   3862 N N   . GLN   B 2 179 ? 11.02609 -8.81037  -26.25322 1.000 75.32228  ? 272 GLN   B N   1 
ATOM   3863 C CA  . GLN   B 2 179 ? 11.92893 -9.37983  -25.26084 1.000 80.45348  ? 272 GLN   B CA  1 
ATOM   3864 C C   . GLN   B 2 179 ? 12.21114 -10.84814 -25.54251 1.000 79.89102  ? 272 GLN   B C   1 
ATOM   3865 O O   . GLN   B 2 179 ? 13.24633 -11.37264 -25.11592 1.000 79.01891  ? 272 GLN   B O   1 
ATOM   3866 C CB  . GLN   B 2 179 ? 11.33380 -9.22167  -23.86311 1.000 81.43227  ? 272 GLN   B CB  1 
ATOM   3867 C CG  . GLN   B 2 179 ? 10.89386 -7.80902  -23.52514 1.000 85.89288  ? 272 GLN   B CG  1 
ATOM   3868 C CD  . GLN   B 2 179 ? 10.01757 -7.75713  -22.28845 1.000 97.98853  ? 272 GLN   B CD  1 
ATOM   3869 O OE1 . GLN   B 2 179 ? 9.12998  -8.59093  -22.10729 1.000 99.75011  ? 272 GLN   B OE1 1 
ATOM   3870 N NE2 . GLN   B 2 179 ? 10.26607 -6.77769  -21.42725 1.000 96.18148  ? 272 GLN   B NE2 1 
ATOM   3871 N N   . GLN   B 2 180 ? 11.30535 -11.52155 -26.25526 1.000 82.05739  ? 273 GLN   B N   1 
ATOM   3872 C CA  . GLN   B 2 180 ? 11.45455 -12.95269 -26.49634 1.000 83.34958  ? 273 GLN   B CA  1 
ATOM   3873 C C   . GLN   B 2 180 ? 12.68535 -13.24599 -27.34600 1.000 84.73973  ? 273 GLN   B C   1 
ATOM   3874 O O   . GLN   B 2 180 ? 13.52290 -14.07634 -26.97733 1.000 84.70755  ? 273 GLN   B O   1 
ATOM   3875 C CB  . GLN   B 2 180 ? 10.19247 -13.50347 -27.16299 1.000 95.88824  ? 273 GLN   B CB  1 
ATOM   3876 C CG  . GLN   B 2 180 ? 10.21589 -15.00604 -27.41775 1.000 100.93575 ? 273 GLN   B CG  1 
ATOM   3877 C CD  . GLN   B 2 180 ? 9.90424  -15.82351 -26.17602 1.000 107.05635 ? 273 GLN   B CD  1 
ATOM   3878 O OE1 . GLN   B 2 180 ? 10.42761 -15.56153 -25.09348 1.000 95.47935  ? 273 GLN   B OE1 1 
ATOM   3879 N NE2 . GLN   B 2 180 ? 9.04003  -16.81906 -26.32874 1.000 99.55022  ? 273 GLN   B NE2 1 
ATOM   3880 N N   . ILE   B 2 181 ? 12.81457 -12.57294 -28.49158 1.000 82.73941  ? 274 ILE   B N   1 
ATOM   3881 C CA  . ILE   B 2 181 ? 13.94867 -12.84186 -29.37001 1.000 79.47417  ? 274 ILE   B CA  1 
ATOM   3882 C C   . ILE   B 2 181 ? 15.23412 -12.19882 -28.86178 1.000 76.27048  ? 274 ILE   B C   1 
ATOM   3883 O O   . ILE   B 2 181 ? 16.32710 -12.61943 -29.26293 1.000 77.48060  ? 274 ILE   B O   1 
ATOM   3884 C CB  . ILE   B 2 181 ? 13.65787 -12.38122 -30.80970 1.000 81.04989  ? 274 ILE   B CB  1 
ATOM   3885 C CG1 . ILE   B 2 181 ? 14.22778 -10.98382 -31.06079 1.000 73.15985  ? 274 ILE   B CG1 1 
ATOM   3886 C CG2 . ILE   B 2 181 ? 12.15641 -12.39954 -31.08586 1.000 90.98243  ? 274 ILE   B CG2 1 
ATOM   3887 C CD1 . ILE   B 2 181 ? 14.92518 -10.84464 -32.39851 1.000 86.01006  ? 274 ILE   B CD1 1 
ATOM   3888 N N   . PHE   B 2 182 ? 15.14070 -11.19482 -27.98631 1.000 75.71978  ? 275 PHE   B N   1 
ATOM   3889 C CA  . PHE   B 2 182 ? 16.34872 -10.59279 -27.43102 1.000 77.58022  ? 275 PHE   B CA  1 
ATOM   3890 C C   . PHE   B 2 182 ? 17.09931 -11.58850 -26.55656 1.000 71.49294  ? 275 PHE   B C   1 
ATOM   3891 O O   . PHE   B 2 182 ? 18.32354 -11.72661 -26.66216 1.000 71.36433  ? 275 PHE   B O   1 
ATOM   3892 C CB  . PHE   B 2 182 ? 15.99762 -9.33466  -26.63562 1.000 69.98086  ? 275 PHE   B CB  1 
ATOM   3893 C CG  . PHE   B 2 182 ? 17.17955 -8.69708  -25.95295 1.000 70.19897  ? 275 PHE   B CG  1 
ATOM   3894 C CD1 . PHE   B 2 182 ? 17.98373 -7.79506  -26.62990 1.000 71.65200  ? 275 PHE   B CD1 1 
ATOM   3895 C CD2 . PHE   B 2 182 ? 17.48395 -8.99635  -24.63287 1.000 72.42786  ? 275 PHE   B CD2 1 
ATOM   3896 C CE1 . PHE   B 2 182 ? 19.07036 -7.20498  -26.00639 1.000 73.82471  ? 275 PHE   B CE1 1 
ATOM   3897 C CE2 . PHE   B 2 182 ? 18.57068 -8.41062  -24.00416 1.000 76.96858  ? 275 PHE   B CE2 1 
ATOM   3898 C CZ  . PHE   B 2 182 ? 19.36387 -7.51284  -24.69307 1.000 71.86645  ? 275 PHE   B CZ  1 
ATOM   3899 N N   . ILE   B 2 183 ? 16.37778 -12.29325 -25.68041 1.000 75.55236  ? 276 ILE   B N   1 
ATOM   3900 C CA  . ILE   B 2 183 ? 17.02020 -13.26991 -24.81074 1.000 78.19095  ? 276 ILE   B CA  1 
ATOM   3901 C C   . ILE   B 2 183 ? 17.46304 -14.50094 -25.58764 1.000 77.48629  ? 276 ILE   B C   1 
ATOM   3902 O O   . ILE   B 2 183 ? 18.32156 -15.25296 -25.11277 1.000 82.80399  ? 276 ILE   B O   1 
ATOM   3903 C CB  . ILE   B 2 183 ? 16.08715 -13.67252 -23.65330 1.000 79.71799  ? 276 ILE   B CB  1 
ATOM   3904 C CG1 . ILE   B 2 183 ? 14.92672 -14.51853 -24.17596 1.000 80.67569  ? 276 ILE   B CG1 1 
ATOM   3905 C CG2 . ILE   B 2 183 ? 15.56428 -12.43525 -22.93483 1.000 70.13850  ? 276 ILE   B CG2 1 
ATOM   3906 C CD1 . ILE   B 2 183 ? 14.51401 -15.62233 -23.24227 1.000 84.58399  ? 276 ILE   B CD1 1 
ATOM   3907 N N   . GLN   B 2 184 ? 16.89720 -14.73119 -26.77487 1.000 77.30828  ? 277 GLN   B N   1 
ATOM   3908 C CA  . GLN   B 2 184 ? 17.34891 -15.84709 -27.59833 1.000 80.88553  ? 277 GLN   B CA  1 
ATOM   3909 C C   . GLN   B 2 184 ? 18.70133 -15.54653 -28.22998 1.000 73.85884  ? 277 GLN   B C   1 
ATOM   3910 O O   . GLN   B 2 184 ? 19.57757 -16.41746 -28.28047 1.000 80.01145  ? 277 GLN   B O   1 
ATOM   3911 C CB  . GLN   B 2 184 ? 16.30992 -16.16375 -28.67398 1.000 84.19384  ? 277 GLN   B CB  1 
ATOM   3912 C CG  . GLN   B 2 184 ? 14.97487 -16.63945 -28.12809 1.000 90.50019  ? 277 GLN   B CG  1 
ATOM   3913 C CD  . GLN   B 2 184 ? 13.94588 -16.87015 -29.21888 1.000 102.21798 ? 277 GLN   B CD  1 
ATOM   3914 O OE1 . GLN   B 2 184 ? 14.23407 -16.71480 -30.40584 1.000 106.91712 ? 277 GLN   B OE1 1 
ATOM   3915 N NE2 . GLN   B 2 184 ? 12.73734 -17.24607 -28.81971 1.000 98.81928  ? 277 GLN   B NE2 1 
ATOM   3916 N N   . ILE   B 2 185 ? 18.88953 -14.31854 -28.71644 1.000 76.06488  ? 278 ILE   B N   1 
ATOM   3917 C CA  . ILE   B 2 185 ? 20.17843 -13.93553 -29.28240 1.000 76.08454  ? 278 ILE   B CA  1 
ATOM   3918 C C   . ILE   B 2 185 ? 21.21207 -13.76323 -28.17740 1.000 73.69401  ? 278 ILE   B C   1 
ATOM   3919 O O   . ILE   B 2 185 ? 22.38609 -14.11670 -28.34382 1.000 75.11291  ? 278 ILE   B O   1 
ATOM   3920 C CB  . ILE   B 2 185 ? 20.02823 -12.65820 -30.12736 1.000 75.25711  ? 278 ILE   B CB  1 
ATOM   3921 C CG1 . ILE   B 2 185 ? 18.94379 -12.85114 -31.18785 1.000 78.11941  ? 278 ILE   B CG1 1 
ATOM   3922 C CG2 . ILE   B 2 185 ? 21.34953 -12.28929 -30.77991 1.000 72.46966  ? 278 ILE   B CG2 1 
ATOM   3923 C CD1 . ILE   B 2 185 ? 18.61057 -11.59209 -31.94880 1.000 74.52482  ? 278 ILE   B CD1 1 
ATOM   3924 N N   . ALA   B 2 186 ? 20.79447 -13.21994 -27.03163 1.000 70.42165  ? 279 ALA   B N   1 
ATOM   3925 C CA  . ALA   B 2 186 ? 21.69996 -13.11615 -25.89279 1.000 72.53412  ? 279 ALA   B CA  1 
ATOM   3926 C C   . ALA   B 2 186 ? 22.12819 -14.49487 -25.40801 1.000 72.27925  ? 279 ALA   B C   1 
ATOM   3927 O O   . ALA   B 2 186 ? 23.25938 -14.67508 -24.94115 1.000 75.14688  ? 279 ALA   B O   1 
ATOM   3928 C CB  . ALA   B 2 186 ? 21.03497 -12.32944 -24.76420 1.000 65.22181  ? 279 ALA   B CB  1 
ATOM   3929 N N   . GLU   B 2 187 ? 21.23346 -15.48081 -25.51253 1.000 77.11146  ? 280 GLU   B N   1 
ATOM   3930 C CA  . GLU   B 2 187 ? 21.58562 -16.85041 -25.15429 1.000 76.49437  ? 280 GLU   B CA  1 
ATOM   3931 C C   . GLU   B 2 187 ? 22.72023 -17.37136 -26.02629 1.000 83.99973  ? 280 GLU   B C   1 
ATOM   3932 O O   . GLU   B 2 187 ? 23.61211 -18.07892 -25.54341 1.000 76.63754  ? 280 GLU   B O   1 
ATOM   3933 C CB  . GLU   B 2 187 ? 20.35515 -17.74838 -25.27649 1.000 91.07440  ? 280 GLU   B CB  1 
ATOM   3934 C CG  . GLU   B 2 187 ? 20.61331 -19.21857 -25.00642 1.000 91.93620  ? 280 GLU   B CG  1 
ATOM   3935 C CD  . GLU   B 2 187 ? 19.36046 -20.05949 -25.15206 1.000 113.60161 ? 280 GLU   B CD  1 
ATOM   3936 O OE1 . GLU   B 2 187 ? 18.27528 -19.48002 -25.36925 1.000 112.59350 ? 280 GLU   B OE1 1 
ATOM   3937 O OE2 . GLU   B 2 187 ? 19.45993 -21.29934 -25.05095 1.000 124.48329 ? 280 GLU   B OE2 1 
ATOM   3938 N N   . LEU   B 2 188 ? 22.70274 -17.03244 -27.31652 1.000 79.87214  ? 281 LEU   B N   1 
ATOM   3939 C CA  . LEU   B 2 188 ? 23.79817 -17.42595 -28.19512 1.000 80.26184  ? 281 LEU   B CA  1 
ATOM   3940 C C   . LEU   B 2 188 ? 25.08485 -16.69607 -27.82987 1.000 81.74589  ? 281 LEU   B C   1 
ATOM   3941 O O   . LEU   B 2 188 ? 26.17563 -17.27483 -27.89806 1.000 79.76883  ? 281 LEU   B O   1 
ATOM   3942 C CB  . LEU   B 2 188 ? 23.42127 -17.15932 -29.65196 1.000 71.34299  ? 281 LEU   B CB  1 
ATOM   3943 C CG  . LEU   B 2 188 ? 24.50155 -17.44502 -30.69533 1.000 84.74875  ? 281 LEU   B CG  1 
ATOM   3944 C CD1 . LEU   B 2 188 ? 24.98687 -18.88018 -30.57763 1.000 85.94017  ? 281 LEU   B CD1 1 
ATOM   3945 C CD2 . LEU   B 2 188 ? 23.98469 -17.16128 -32.09667 1.000 80.84234  ? 281 LEU   B CD2 1 
ATOM   3946 N N   . LEU   B 2 189 ? 24.97697 -15.42653 -27.43259 1.000 75.67336  ? 282 LEU   B N   1 
ATOM   3947 C CA  . LEU   B 2 189 ? 26.16669 -14.65939 -27.07836 1.000 77.36590  ? 282 LEU   B CA  1 
ATOM   3948 C C   . LEU   B 2 189 ? 26.75506 -15.12419 -25.75180 1.000 79.02235  ? 282 LEU   B C   1 
ATOM   3949 O O   . LEU   B 2 189 ? 27.97892 -15.11295 -25.57325 1.000 78.83492  ? 282 LEU   B O   1 
ATOM   3950 C CB  . LEU   B 2 189 ? 25.83117 -13.16994 -27.02862 1.000 72.12071  ? 282 LEU   B CB  1 
ATOM   3951 C CG  . LEU   B 2 189 ? 25.60920 -12.50526 -28.38722 1.000 71.50678  ? 282 LEU   B CG  1 
ATOM   3952 C CD1 . LEU   B 2 189 ? 25.00178 -11.12330 -28.21609 1.000 74.81987  ? 282 LEU   B CD1 1 
ATOM   3953 C CD2 . LEU   B 2 189 ? 26.92283 -12.42313 -29.14975 1.000 74.17425  ? 282 LEU   B CD2 1 
ATOM   3954 N N   . ASP   B 2 190 ? 25.90198 -15.53267 -24.80770 1.000 78.03307  ? 283 ASP   B N   1 
ATOM   3955 C CA  . ASP   B 2 190 ? 26.40367 -16.04127 -23.53482 1.000 77.99052  ? 283 ASP   B CA  1 
ATOM   3956 C C   . ASP   B 2 190 ? 27.23625 -17.30168 -23.72704 1.000 88.25004  ? 283 ASP   B C   1 
ATOM   3957 O O   . ASP   B 2 190 ? 28.18712 -17.53995 -22.97403 1.000 87.58764  ? 283 ASP   B O   1 
ATOM   3958 C CB  . ASP   B 2 190 ? 25.24235 -16.31291 -22.57693 1.000 77.78744  ? 283 ASP   B CB  1 
ATOM   3959 C CG  . ASP   B 2 190 ? 24.56578 -15.04054 -22.10076 1.000 84.82675  ? 283 ASP   B CG  1 
ATOM   3960 O OD1 . ASP   B 2 190 ? 25.21864 -13.97578 -22.11194 1.000 78.49513  ? 283 ASP   B OD1 1 
ATOM   3961 O OD2 . ASP   B 2 190 ? 23.38246 -15.10836 -21.70637 1.000 86.09382  ? 283 ASP   B OD2 1 
ATOM   3962 N N   . LEU   B 2 191 ? 26.90192 -18.11497 -24.72931 1.000 84.41326  ? 284 LEU   B N   1 
ATOM   3963 C CA  . LEU   B 2 191 ? 27.68830 -19.31245 -25.00250 1.000 84.49960  ? 284 LEU   B CA  1 
ATOM   3964 C C   . LEU   B 2 191 ? 29.01614 -18.95626 -25.65940 1.000 93.36545  ? 284 LEU   B C   1 
ATOM   3965 O O   . LEU   B 2 191 ? 30.06837 -19.48628 -25.28378 1.000 93.10462  ? 284 LEU   B O   1 
ATOM   3966 C CB  . LEU   B 2 191 ? 26.88939 -20.27278 -25.88468 1.000 95.07111  ? 284 LEU   B CB  1 
ATOM   3967 C CG  . LEU   B 2 191 ? 27.58759 -21.57600 -26.27343 1.000 96.44239  ? 284 LEU   B CG  1 
ATOM   3968 C CD1 . LEU   B 2 191 ? 27.90316 -22.40025 -25.03551 1.000 103.69292 ? 284 LEU   B CD1 1 
ATOM   3969 C CD2 . LEU   B 2 191 ? 26.73633 -22.37037 -27.25193 1.000 93.94729  ? 284 LEU   B CD2 1 
ATOM   3970 N N   . CYS   B 2 192 ? 28.98561 -18.05040 -26.64106 1.000 89.06643  ? 285 CYS   B N   1 
ATOM   3971 C CA  . CYS   B 2 192 ? 30.19641 -17.71020 -27.38112 1.000 88.72998  ? 285 CYS   B CA  1 
ATOM   3972 C C   . CYS   B 2 192 ? 31.22029 -17.00072 -26.50609 1.000 89.56960  ? 285 CYS   B C   1 
ATOM   3973 O O   . CYS   B 2 192 ? 32.42718 -17.13414 -26.73885 1.000 91.91757  ? 285 CYS   B O   1 
ATOM   3974 C CB  . CYS   B 2 192 ? 29.84770 -16.84037 -28.58891 1.000 92.82947  ? 285 CYS   B CB  1 
ATOM   3975 S SG  . CYS   B 2 192 ? 28.77985 -17.63916 -29.80553 1.000 98.14896  ? 285 CYS   B SG  1 
ATOM   3976 N N   . VAL   B 2 193 ? 30.76672 -16.24584 -25.50191 1.000 87.77514  ? 286 VAL   B N   1 
ATOM   3977 C CA  . VAL   B 2 193 ? 31.69776 -15.50889 -24.65686 1.000 90.44881  ? 286 VAL   B CA  1 
ATOM   3978 C C   . VAL   B 2 193 ? 32.49843 -16.44275 -23.75808 1.000 80.13820  ? 286 VAL   B C   1 
ATOM   3979 O O   . VAL   B 2 193 ? 33.55594 -16.05173 -23.25106 1.000 86.20996  ? 286 VAL   B O   1 
ATOM   3980 C CB  . VAL   B 2 193 ? 30.94974 -14.44926 -23.82315 1.000 84.76259  ? 286 VAL   B CB  1 
ATOM   3981 C CG1 . VAL   B 2 193 ? 30.26418 -15.08916 -22.62614 1.000 84.74875  ? 286 VAL   B CG1 1 
ATOM   3982 C CG2 . VAL   B 2 193 ? 31.90142 -13.34044 -23.38357 1.000 72.39391  ? 286 VAL   B CG2 1 
ATOM   3983 N N   . LEU   B 2 194 ? 32.02854 -17.67646 -23.55254 1.000 83.80931  ? 287 LEU   B N   1 
ATOM   3984 C CA  . LEU   B 2 194 ? 32.79484 -18.63310 -22.76165 1.000 90.51037  ? 287 LEU   B CA  1 
ATOM   3985 C C   . LEU   B 2 194 ? 34.05440 -19.08129 -23.49325 1.000 91.63740  ? 287 LEU   B C   1 
ATOM   3986 O O   . LEU   B 2 194 ? 35.04716 -19.44299 -22.85102 1.000 101.52882 ? 287 LEU   B O   1 
ATOM   3987 C CB  . LEU   B 2 194 ? 31.92375 -19.83810 -22.40642 1.000 89.87483  ? 287 LEU   B CB  1 
ATOM   3988 C CG  . LEU   B 2 194 ? 30.62571 -19.53291 -21.65403 1.000 88.96239  ? 287 LEU   B CG  1 
ATOM   3989 C CD1 . LEU   B 2 194 ? 29.88141 -20.81646 -21.32360 1.000 98.26104  ? 287 LEU   B CD1 1 
ATOM   3990 C CD2 . LEU   B 2 194 ? 30.90590 -18.73111 -20.39100 1.000 85.39862  ? 287 LEU   B CD2 1 
ATOM   3991 N N   . ASP   B 2 195 ? 34.03501 -19.06518 -24.82460 1.000 90.98528  ? 288 ASP   B N   1 
ATOM   3992 C CA  . ASP   B 2 195 ? 35.21398 -19.40055 -25.61064 1.000 102.04428 ? 288 ASP   B CA  1 
ATOM   3993 C C   . ASP   B 2 195 ? 36.11566 -18.17694 -25.71598 1.000 101.55978 ? 288 ASP   B C   1 
ATOM   3994 O O   . ASP   B 2 195 ? 35.64833 -17.07556 -26.02107 1.000 100.57885 ? 288 ASP   B O   1 
ATOM   3995 C CB  . ASP   B 2 195 ? 34.80483 -19.89231 -26.99977 1.000 99.55070  ? 288 ASP   B CB  1 
ATOM   3996 C CG  . ASP   B 2 195 ? 35.92364 -20.62853 -27.71770 1.000 98.39638  ? 288 ASP   B CG  1 
ATOM   3997 O OD1 . ASP   B 2 195 ? 37.09018 -20.19334 -27.62414 1.000 103.85680 ? 288 ASP   B OD1 1 
ATOM   3998 O OD2 . ASP   B 2 195 ? 35.63282 -21.64913 -28.37637 1.000 116.44075 ? 288 ASP   B OD2 1 
ATOM   3999 N N   . VAL   B 2 196 ? 37.41190 -18.37428 -25.46524 1.000 101.56630 ? 289 VAL   B N   1 
ATOM   4000 C CA  . VAL   B 2 196 ? 38.33811 -17.24727 -25.41262 1.000 107.11237 ? 289 VAL   B CA  1 
ATOM   4001 C C   . VAL   B 2 196 ? 38.61181 -16.69179 -26.80501 1.000 106.37564 ? 289 VAL   B C   1 
ATOM   4002 O O   . VAL   B 2 196 ? 38.92197 -15.50323 -26.95603 1.000 105.05348 ? 289 VAL   B O   1 
ATOM   4003 C CB  . VAL   B 2 196 ? 39.64097 -17.66838 -24.70858 1.000 107.98130 ? 289 VAL   B CB  1 
ATOM   4004 C CG1 . VAL   B 2 196 ? 40.46962 -16.44539 -24.34398 1.000 102.35040 ? 289 VAL   B CG1 1 
ATOM   4005 C CG2 . VAL   B 2 196 ? 39.32931 -18.50376 -23.47586 1.000 107.04748 ? 289 VAL   B CG2 1 
ATOM   4006 N N   . ASP   B 2 197 ? 38.49540 -17.52306 -27.84146 1.000 110.46901 ? 290 ASP   B N   1 
ATOM   4007 C CA  . ASP   B 2 197 ? 38.78883 -17.08941 -29.20382 1.000 108.11092 ? 290 ASP   B CA  1 
ATOM   4008 C C   . ASP   B 2 197 ? 37.81012 -16.04605 -29.73144 1.000 106.14116 ? 290 ASP   B C   1 
ATOM   4009 O O   . ASP   B 2 197 ? 37.99468 -15.57290 -30.85864 1.000 104.82460 ? 290 ASP   B O   1 
ATOM   4010 C CB  . ASP   B 2 197 ? 38.81159 -18.29723 -30.14289 1.000 112.12248 ? 290 ASP   B CB  1 
ATOM   4011 C CG  . ASP   B 2 197 ? 40.01537 -19.19045 -29.91353 1.000 116.29033 ? 290 ASP   B CG  1 
ATOM   4012 O OD1 . ASP   B 2 197 ? 41.07753 -18.66711 -29.51601 1.000 119.70583 ? 290 ASP   B OD1 1 
ATOM   4013 O OD2 . ASP   B 2 197 ? 39.90065 -20.41457 -30.13285 1.000 117.90708 ? 290 ASP   B OD2 1 
ATOM   4014 N N   . CYS   B 2 198 ? 36.78453 -15.67451 -28.96135 1.000 106.39427 ? 291 CYS   B N   1 
ATOM   4015 C CA  . CYS   B 2 198 ? 35.86075 -14.64099 -29.41541 1.000 98.63764  ? 291 CYS   B CA  1 
ATOM   4016 C C   . CYS   B 2 198 ? 36.51148 -13.26440 -29.41116 1.000 98.58490  ? 291 CYS   B C   1 
ATOM   4017 O O   . CYS   B 2 198 ? 36.08147 -12.37545 -30.15550 1.000 92.42622  ? 291 CYS   B O   1 
ATOM   4018 C CB  . CYS   B 2 198 ? 34.60908 -14.62973 -28.53913 1.000 97.96787  ? 291 CYS   B CB  1 
ATOM   4019 S SG  . CYS   B 2 198 ? 34.90034 -14.09055 -26.83837 1.000 95.16355  ? 291 CYS   B SG  1 
ATOM   4020 N N   . LEU   B 2 199 ? 37.54363 -13.06886 -28.58549 1.000 94.35125  ? 292 LEU   B N   1 
ATOM   4021 C CA  . LEU   B 2 199 ? 38.19462 -11.76728 -28.49379 1.000 97.32189  ? 292 LEU   B CA  1 
ATOM   4022 C C   . LEU   B 2 199 ? 38.91002 -11.38343 -29.78196 1.000 104.27195 ? 292 LEU   B C   1 
ATOM   4023 O O   . LEU   B 2 199 ? 39.26644 -10.21236 -29.95117 1.000 103.54692 ? 292 LEU   B O   1 
ATOM   4024 C CB  . LEU   B 2 199 ? 39.17907 -11.75234 -27.32364 1.000 101.11015 ? 292 LEU   B CB  1 
ATOM   4025 C CG  . LEU   B 2 199 ? 38.57180 -11.93798 -25.93181 1.000 93.87884  ? 292 LEU   B CG  1 
ATOM   4026 C CD1 . LEU   B 2 199 ? 39.65275 -11.86364 -24.86620 1.000 96.76220  ? 292 LEU   B CD1 1 
ATOM   4027 C CD2 . LEU   B 2 199 ? 37.48336 -10.90502 -25.67635 1.000 84.74724  ? 292 LEU   B CD2 1 
ATOM   4028 N N   . GLU   B 2 200 ? 39.13290 -12.34072 -30.68623 1.000 102.57278 ? 293 GLU   B N   1 
ATOM   4029 C CA  . GLU   B 2 200 ? 39.67171 -12.00792 -32.00058 1.000 102.32823 ? 293 GLU   B CA  1 
ATOM   4030 C C   . GLU   B 2 200 ? 38.75914 -11.03454 -32.73545 1.000 98.44016  ? 293 GLU   B C   1 
ATOM   4031 O O   . GLU   B 2 200 ? 39.23266 -10.14492 -33.45249 1.000 100.52403 ? 293 GLU   B O   1 
ATOM   4032 C CB  . GLU   B 2 200 ? 39.86800 -13.28295 -32.82142 1.000 100.04868 ? 293 GLU   B CB  1 
ATOM   4033 C CG  . GLU   B 2 200 ? 40.20775 -13.03956 -34.28322 1.000 105.69103 ? 293 GLU   B CG  1 
ATOM   4034 C CD  . GLU   B 2 200 ? 40.16481 -14.30817 -35.11123 1.000 106.24343 ? 293 GLU   B CD  1 
ATOM   4035 O OE1 . GLU   B 2 200 ? 40.08722 -15.40451 -34.51849 1.000 109.20696 ? 293 GLU   B OE1 1 
ATOM   4036 O OE2 . GLU   B 2 200 ? 40.20395 -14.20933 -36.35572 1.000 105.05770 ? 293 GLU   B OE2 1 
ATOM   4037 N N   . PHE   B 2 201 ? 37.44865 -11.18150 -32.56085 1.000 88.26475  ? 294 PHE   B N   1 
ATOM   4038 C CA  . PHE   B 2 201 ? 36.44785 -10.34483 -33.20336 1.000 90.19549  ? 294 PHE   B CA  1 
ATOM   4039 C C   . PHE   B 2 201 ? 36.01019 -9.22157  -32.27357 1.000 85.34885  ? 294 PHE   B C   1 
ATOM   4040 O O   . PHE   B 2 201 ? 35.86073 -9.43841  -31.06540 1.000 83.04746  ? 294 PHE   B O   1 
ATOM   4041 C CB  . PHE   B 2 201 ? 35.22777 -11.17547 -33.60243 1.000 87.87446  ? 294 PHE   B CB  1 
ATOM   4042 C CG  . PHE   B 2 201 ? 35.57520 -12.49157 -34.23440 1.000 91.75821  ? 294 PHE   B CG  1 
ATOM   4043 C CD1 . PHE   B 2 201 ? 36.04719 -12.54679 -35.53474 1.000 86.23083  ? 294 PHE   B CD1 1 
ATOM   4044 C CD2 . PHE   B 2 201 ? 35.43130 -13.67379 -33.52710 1.000 87.47893  ? 294 PHE   B CD2 1 
ATOM   4045 C CE1 . PHE   B 2 201 ? 36.37078 -13.75665 -36.11820 1.000 92.25414  ? 294 PHE   B CE1 1 
ATOM   4046 C CE2 . PHE   B 2 201 ? 35.75205 -14.88740 -34.10550 1.000 96.86865  ? 294 PHE   B CE2 1 
ATOM   4047 C CZ  . PHE   B 2 201 ? 36.22214 -14.92859 -35.40256 1.000 95.10753  ? 294 PHE   B CZ  1 
ATOM   4048 N N   . PRO   B 2 202 ? 35.81349 -8.01718  -32.80824 1.000 81.09715  ? 295 PRO   B N   1 
ATOM   4049 C CA  . PRO   B 2 202 ? 35.32463 -6.91476  -31.97358 1.000 75.80284  ? 295 PRO   B CA  1 
ATOM   4050 C C   . PRO   B 2 202 ? 33.95106 -7.22687  -31.39971 1.000 85.01418  ? 295 PRO   B C   1 
ATOM   4051 O O   . PRO   B 2 202 ? 33.18965 -8.02490  -31.95179 1.000 75.45962  ? 295 PRO   B O   1 
ATOM   4052 C CB  . PRO   B 2 202 ? 35.27103 -5.72928  -32.94446 1.000 79.21850  ? 295 PRO   B CB  1 
ATOM   4053 C CG  . PRO   B 2 202 ? 36.22893 -6.08979  -34.03771 1.000 75.37664  ? 295 PRO   B CG  1 
ATOM   4054 C CD  . PRO   B 2 202 ? 36.13069 -7.57957  -34.17780 1.000 75.04957  ? 295 PRO   B CD  1 
ATOM   4055 N N   . TYR   B 2 203 ? 33.64238 -6.58098  -30.27046 1.000 75.71430  ? 296 TYR   B N   1 
ATOM   4056 C CA  . TYR   B 2 203 ? 32.37427 -6.83400  -29.59128 1.000 70.89014  ? 296 TYR   B CA  1 
ATOM   4057 C C   . TYR   B 2 203 ? 31.18830 -6.51448  -30.49262 1.000 68.29326  ? 296 TYR   B C   1 
ATOM   4058 O O   . TYR   B 2 203 ? 30.18183 -7.23234  -30.48311 1.000 73.55124  ? 296 TYR   B O   1 
ATOM   4059 C CB  . TYR   B 2 203 ? 32.29274 -6.02248  -28.29684 1.000 74.10030  ? 296 TYR   B CB  1 
ATOM   4060 C CG  . TYR   B 2 203 ? 33.17891 -6.52868  -27.17900 1.000 75.99723  ? 296 TYR   B CG  1 
ATOM   4061 C CD1 . TYR   B 2 203 ? 33.88543 -7.71899  -27.30515 1.000 78.87249  ? 296 TYR   B CD1 1 
ATOM   4062 C CD2 . TYR   B 2 203 ? 33.30075 -5.81847  -25.99198 1.000 76.02362  ? 296 TYR   B CD2 1 
ATOM   4063 C CE1 . TYR   B 2 203 ? 34.69365 -8.18170  -26.28171 1.000 79.62564  ? 296 TYR   B CE1 1 
ATOM   4064 C CE2 . TYR   B 2 203 ? 34.10501 -6.27306  -24.96505 1.000 79.23825  ? 296 TYR   B CE2 1 
ATOM   4065 C CZ  . TYR   B 2 203 ? 34.79888 -7.45395  -25.11464 1.000 85.14895  ? 296 TYR   B CZ  1 
ATOM   4066 O OH  . TYR   B 2 203 ? 35.60052 -7.90696  -24.09126 1.000 82.23281  ? 296 TYR   B OH  1 
ATOM   4067 N N   . GLY   B 2 204 ? 31.28574 -5.43978  -31.27806 1.000 68.36711  ? 297 GLY   B N   1 
ATOM   4068 C CA  . GLY   B 2 204 ? 30.21733 -5.11665  -32.20712 1.000 73.45647  ? 297 GLY   B CA  1 
ATOM   4069 C C   . GLY   B 2 204 ? 30.05039 -6.14898  -33.30361 1.000 76.85665  ? 297 GLY   B C   1 
ATOM   4070 O O   . GLY   B 2 204 ? 28.93660 -6.36858  -33.79078 1.000 74.76673  ? 297 GLY   B O   1 
ATOM   4071 N N   . ILE   B 2 205 ? 31.14582 -6.79464  -33.70797 1.000 75.63847  ? 298 ILE   B N   1 
ATOM   4072 C CA  . ILE   B 2 205 ? 31.05965 -7.84729  -34.71520 1.000 70.65370  ? 298 ILE   B CA  1 
ATOM   4073 C C   . ILE   B 2 205 ? 30.39067 -9.08866  -34.13558 1.000 73.47635  ? 298 ILE   B C   1 
ATOM   4074 O O   . ILE   B 2 205 ? 29.58018 -9.74404  -34.80337 1.000 82.24227  ? 298 ILE   B O   1 
ATOM   4075 C CB  . ILE   B 2 205 ? 32.46081 -8.16090  -35.27279 1.000 76.09784  ? 298 ILE   B CB  1 
ATOM   4076 C CG1 . ILE   B 2 205 ? 32.97181 -6.99986  -36.12670 1.000 78.36742  ? 298 ILE   B CG1 1 
ATOM   4077 C CG2 . ILE   B 2 205 ? 32.44599 -9.43826  -36.08764 1.000 74.64341  ? 298 ILE   B CG2 1 
ATOM   4078 C CD1 . ILE   B 2 205 ? 32.27702 -6.87822  -37.46292 1.000 91.21474  ? 298 ILE   B CD1 1 
ATOM   4079 N N   . LEU   B 2 206 ? 30.70973 -9.42451  -32.88198 1.000 73.88406  ? 299 LEU   B N   1 
ATOM   4080 C CA  . LEU   B 2 206 ? 30.14220 -10.61726 -32.25881 1.000 77.27046  ? 299 LEU   B CA  1 
ATOM   4081 C C   . LEU   B 2 206 ? 28.62856 -10.51236 -32.12203 1.000 69.52618  ? 299 LEU   B C   1 
ATOM   4082 O O   . LEU   B 2 206 ? 27.90574 -11.47735 -32.39721 1.000 78.45689  ? 299 LEU   B O   1 
ATOM   4083 C CB  . LEU   B 2 206 ? 30.78467 -10.84942 -30.89112 1.000 70.89696  ? 299 LEU   B CB  1 
ATOM   4084 C CG  . LEU   B 2 206 ? 32.19444 -11.44015 -30.87946 1.000 79.47275  ? 299 LEU   B CG  1 
ATOM   4085 C CD1 . LEU   B 2 206 ? 32.80729 -11.32703 -29.49446 1.000 85.81918  ? 299 LEU   B CD1 1 
ATOM   4086 C CD2 . LEU   B 2 206 ? 32.15755 -12.89094 -31.33028 1.000 79.17831  ? 299 LEU   B CD2 1 
ATOM   4087 N N   . ALA   B 2 207 ? 28.12994 -9.35137  -31.69131 1.000 61.27357  ? 300 ALA   B N   1 
ATOM   4088 C CA  . ALA   B 2 207 ? 26.68978 -9.18662  -31.52080 1.000 71.62780  ? 300 ALA   B CA  1 
ATOM   4089 C C   . ALA   B 2 207 ? 25.96516 -9.21830  -32.86114 1.000 66.69091  ? 300 ALA   B C   1 
ATOM   4090 O O   . ALA   B 2 207 ? 24.88590 -9.81154  -32.97540 1.000 67.14533  ? 300 ALA   B O   1 
ATOM   4091 C CB  . ALA   B 2 207 ? 26.39266 -7.88358  -30.77894 1.000 60.24892  ? 300 ALA   B CB  1 
ATOM   4092 N N   . ALA   B 2 208 ? 26.54342 -8.58949  -33.88754 1.000 71.13261  ? 301 ALA   B N   1 
ATOM   4093 C CA  . ALA   B 2 208 ? 25.90953 -8.58780  -35.20214 1.000 75.45498  ? 301 ALA   B CA  1 
ATOM   4094 C C   . ALA   B 2 208 ? 25.87779 -9.98782  -35.80200 1.000 68.33529  ? 301 ALA   B C   1 
ATOM   4095 O O   . ALA   B 2 208 ? 24.92317 -10.35148 -36.49910 1.000 71.87470  ? 301 ALA   B O   1 
ATOM   4096 C CB  . ALA   B 2 208 ? 26.63567 -7.62009  -36.13592 1.000 72.69075  ? 301 ALA   B CB  1 
ATOM   4097 N N   . SER   B 2 209 ? 26.91250 -10.79026 -35.53938 1.000 72.35090  ? 302 SER   B N   1 
ATOM   4098 C CA  . SER   B 2 209 ? 26.94005 -12.15355 -36.05780 1.000 75.95970  ? 302 SER   B CA  1 
ATOM   4099 C C   . SER   B 2 209 ? 25.89796 -13.03472 -35.38113 1.000 79.97031  ? 302 SER   B C   1 
ATOM   4100 O O   . SER   B 2 209 ? 25.33407 -13.92770 -36.02364 1.000 79.49684  ? 302 SER   B O   1 
ATOM   4101 C CB  . SER   B 2 209 ? 28.33448 -12.75368 -35.88343 1.000 81.17317  ? 302 SER   B CB  1 
ATOM   4102 O OG  . SER   B 2 209 ? 29.32255 -11.92457 -36.46910 1.000 85.04504  ? 302 SER   B OG  1 
ATOM   4103 N N   . ALA   B 2 210 ? 25.63242 -12.80628 -34.09219 1.000 73.69113  ? 303 ALA   B N   1 
ATOM   4104 C CA  . ALA   B 2 210 ? 24.60299 -13.57819 -33.40313 1.000 70.64224  ? 303 ALA   B CA  1 
ATOM   4105 C C   . ALA   B 2 210 ? 23.20902 -13.17506 -33.86602 1.000 69.31295  ? 303 ALA   B C   1 
ATOM   4106 O O   . ALA   B 2 210 ? 22.31352 -14.02147 -33.96739 1.000 77.94993  ? 303 ALA   B O   1 
ATOM   4107 C CB  . ALA   B 2 210 ? 24.73828 -13.40560 -31.89106 1.000 68.92177  ? 303 ALA   B CB  1 
ATOM   4108 N N   . LEU   B 2 211 ? 23.00450 -11.88556 -34.14478 1.000 73.60252  ? 304 LEU   B N   1 
ATOM   4109 C CA  . LEU   B 2 211 ? 21.72262 -11.43853 -34.68045 1.000 83.39437  ? 304 LEU   B CA  1 
ATOM   4110 C C   . LEU   B 2 211 ? 21.49448 -11.98210 -36.08550 1.000 75.08272  ? 304 LEU   B C   1 
ATOM   4111 O O   . LEU   B 2 211 ? 20.35968 -12.30678 -36.45530 1.000 81.20272  ? 304 LEU   B O   1 
ATOM   4112 C CB  . LEU   B 2 211 ? 21.65733 -9.91049  -34.67168 1.000 84.01861  ? 304 LEU   B CB  1 
ATOM   4113 C CG  . LEU   B 2 211 ? 20.51469 -9.22716  -35.42777 1.000 82.27033  ? 304 LEU   B CG  1 
ATOM   4114 C CD1 . LEU   B 2 211 ? 19.15591 -9.72106  -34.95902 1.000 80.45131  ? 304 LEU   B CD1 1 
ATOM   4115 C CD2 . LEU   B 2 211 ? 20.61248 -7.72567  -35.26090 1.000 85.17278  ? 304 LEU   B CD2 1 
ATOM   4116 N N   . TYR   B 2 212 ? 22.56205 -12.09594 -36.87918 1.000 81.59304  ? 305 TYR   B N   1 
ATOM   4117 C CA  . TYR   B 2 212 ? 22.42787 -12.64872 -38.22266 1.000 77.82446  ? 305 TYR   B CA  1 
ATOM   4118 C C   . TYR   B 2 212 ? 21.92372 -14.08611 -38.18453 1.000 78.62456  ? 305 TYR   B C   1 
ATOM   4119 O O   . TYR   B 2 212 ? 21.08987 -14.48073 -39.00834 1.000 83.88029  ? 305 TYR   B O   1 
ATOM   4120 C CB  . TYR   B 2 212 ? 23.76432 -12.57434 -38.95978 1.000 75.83067  ? 305 TYR   B CB  1 
ATOM   4121 C CG  . TYR   B 2 212 ? 23.82239 -13.47003 -40.17404 1.000 79.35792  ? 305 TYR   B CG  1 
ATOM   4122 C CD1 . TYR   B 2 212 ? 23.18348 -13.11243 -41.35155 1.000 83.64325  ? 305 TYR   B CD1 1 
ATOM   4123 C CD2 . TYR   B 2 212 ? 24.50859 -14.67631 -40.14086 1.000 78.96608  ? 305 TYR   B CD2 1 
ATOM   4124 C CE1 . TYR   B 2 212 ? 23.22669 -13.92687 -42.46415 1.000 80.73134  ? 305 TYR   B CE1 1 
ATOM   4125 C CE2 . TYR   B 2 212 ? 24.55792 -15.49951 -41.24797 1.000 90.72692  ? 305 TYR   B CE2 1 
ATOM   4126 C CZ  . TYR   B 2 212 ? 23.91497 -15.11861 -42.40729 1.000 89.37121  ? 305 TYR   B CZ  1 
ATOM   4127 O OH  . TYR   B 2 212 ? 23.95943 -15.93126 -43.51596 1.000 90.93259  ? 305 TYR   B OH  1 
ATOM   4128 N N   . HIS   B 2 213 ? 22.41945 -14.88572 -37.23616 1.000 80.44432  ? 306 HIS   B N   1 
ATOM   4129 C CA  . HIS   B 2 213 ? 22.01108 -16.28315 -37.15156 1.000 83.33473  ? 306 HIS   B CA  1 
ATOM   4130 C C   . HIS   B 2 213 ? 20.54582 -16.44147 -36.76704 1.000 76.21881  ? 306 HIS   B C   1 
ATOM   4131 O O   . HIS   B 2 213 ? 19.95942 -17.49473 -37.03824 1.000 83.18421  ? 306 HIS   B O   1 
ATOM   4132 C CB  . HIS   B 2 213 ? 22.89738 -17.03357 -36.15516 1.000 79.80666  ? 306 HIS   B CB  1 
ATOM   4133 C CG  . HIS   B 2 213 ? 24.24634 -17.39308 -36.69790 1.000 89.42725  ? 306 HIS   B CG  1 
ATOM   4134 N ND1 . HIS   B 2 213 ? 25.37211 -16.63260 -36.46438 1.000 85.56652  ? 306 HIS   B ND1 1 
ATOM   4135 C CD2 . HIS   B 2 213 ? 24.64803 -18.43155 -37.46859 1.000 82.46399  ? 306 HIS   B CD2 1 
ATOM   4136 C CE1 . HIS   B 2 213 ? 26.40946 -17.18888 -37.06462 1.000 87.51783  ? 306 HIS   B CE1 1 
ATOM   4137 N NE2 . HIS   B 2 213 ? 25.99700 -18.28177 -37.68114 1.000 89.33446  ? 306 HIS   B NE2 1 
ATOM   4138 N N   . PHE   B 2 214 ? 19.94242 -15.42737 -36.14918 1.000 76.15773  ? 307 PHE   B N   1 
ATOM   4139 C CA  . PHE   B 2 214 ? 18.52799 -15.45240 -35.80420 1.000 84.29650  ? 307 PHE   B CA  1 
ATOM   4140 C C   . PHE   B 2 214 ? 17.67688 -14.62114 -36.75505 1.000 83.03825  ? 307 PHE   B C   1 
ATOM   4141 O O   . PHE   B 2 214 ? 16.48640 -14.42330 -36.49215 1.000 88.90993  ? 307 PHE   B O   1 
ATOM   4142 C CB  . PHE   B 2 214 ? 18.32442 -14.97245 -34.36574 1.000 73.31323  ? 307 PHE   B CB  1 
ATOM   4143 C CG  . PHE   B 2 214 ? 18.74393 -15.97437 -33.32893 1.000 74.40289  ? 307 PHE   B CG  1 
ATOM   4144 C CD1 . PHE   B 2 214 ? 17.84530 -16.91643 -32.85358 1.000 75.07111  ? 307 PHE   B CD1 1 
ATOM   4145 C CD2 . PHE   B 2 214 ? 20.03614 -15.97766 -32.83154 1.000 71.07448  ? 307 PHE   B CD2 1 
ATOM   4146 C CE1 . PHE   B 2 214 ? 18.22812 -17.84334 -31.89857 1.000 83.96934  ? 307 PHE   B CE1 1 
ATOM   4147 C CE2 . PHE   B 2 214 ? 20.42563 -16.90177 -31.87640 1.000 82.07956  ? 307 PHE   B CE2 1 
ATOM   4148 C CZ  . PHE   B 2 214 ? 19.52053 -17.83569 -31.40982 1.000 81.03214  ? 307 PHE   B CZ  1 
ATOM   4149 N N   . SER   B 2 215 ? 18.25652 -14.13230 -37.85090 1.000 84.68576  ? 308 SER   B N   1 
ATOM   4150 C CA  . SER   B 2 215 ? 17.51023 -13.33681 -38.81752 1.000 81.46140  ? 308 SER   B CA  1 
ATOM   4151 C C   . SER   B 2 215 ? 18.10140 -13.47979 -40.21466 1.000 78.68867  ? 308 SER   B C   1 
ATOM   4152 O O   . SER   B 2 215 ? 17.98840 -14.54114 -40.83625 1.000 78.79452  ? 308 SER   B O   1 
ATOM   4153 C CB  . SER   B 2 215 ? 17.48630 -11.86715 -38.39377 1.000 75.31503  ? 308 SER   B CB  1 
ATOM   4154 O OG  . SER   B 2 215 ? 18.79832 -11.36256 -38.22339 1.000 80.19279  ? 308 SER   B OG  1 
ATOM   4155 N N   . SER   B 2 216 ? 18.73424 -12.42195 -40.71501 1.000 78.35551  ? 309 SER   B N   1 
ATOM   4156 C CA  . SER   B 2 216 ? 19.29299 -12.43305 -42.05996 1.000 83.69624  ? 309 SER   B CA  1 
ATOM   4157 C C   . SER   B 2 216 ? 20.40401 -11.39639 -42.13882 1.000 83.92478  ? 309 SER   B C   1 
ATOM   4158 O O   . SER   B 2 216 ? 20.58288 -10.57510 -41.23603 1.000 82.47325  ? 309 SER   B O   1 
ATOM   4159 C CB  . SER   B 2 216 ? 18.21547 -12.15814 -43.11347 1.000 90.88995  ? 309 SER   B CB  1 
ATOM   4160 O OG  . SER   B 2 216 ? 17.63378 -10.88036 -42.91771 1.000 86.75734  ? 309 SER   B OG  1 
ATOM   4161 N N   . SER   B 2 217 ? 21.15405 -11.44897 -43.24247 1.000 91.47556  ? 310 SER   B N   1 
ATOM   4162 C CA  . SER   B 2 217 ? 22.21722 -10.47881 -43.47233 1.000 85.99498  ? 310 SER   B CA  1 
ATOM   4163 C C   . SER   B 2 217 ? 21.67327 -9.10388  -43.83294 1.000 85.96822  ? 310 SER   B C   1 
ATOM   4164 O O   . SER   B 2 217 ? 22.36790 -8.10280  -43.62668 1.000 84.72774  ? 310 SER   B O   1 
ATOM   4165 C CB  . SER   B 2 217 ? 23.15422 -10.97758 -44.57434 1.000 93.02166  ? 310 SER   B CB  1 
ATOM   4166 O OG  . SER   B 2 217 ? 22.44399 -11.23039 -45.77467 1.000 105.35598 ? 310 SER   B OG  1 
ATOM   4167 N N   . GLU   B 2 218 ? 20.45106 -9.03342  -44.36442 1.000 88.71738  ? 311 GLU   B N   1 
ATOM   4168 C CA  . GLU   B 2 218 ? 19.85270 -7.74107  -44.68100 1.000 87.15966  ? 311 GLU   B CA  1 
ATOM   4169 C C   . GLU   B 2 218 ? 19.48622 -6.98594  -43.41002 1.000 80.98131  ? 311 GLU   B C   1 
ATOM   4170 O O   . GLU   B 2 218 ? 19.79569 -5.79672  -43.27118 1.000 88.71868  ? 311 GLU   B O   1 
ATOM   4171 C CB  . GLU   B 2 218 ? 18.62252 -7.93133  -45.57085 1.000 93.68173  ? 311 GLU   B CB  1 
ATOM   4172 C CG  . GLU   B 2 218 ? 18.92603 -8.45179  -46.96937 1.000 88.60230  ? 311 GLU   B CG  1 
ATOM   4173 C CD  . GLU   B 2 218 ? 19.24306 -9.93662  -46.99718 1.000 98.13960  ? 311 GLU   B CD  1 
ATOM   4174 O OE1 . GLU   B 2 218 ? 19.01095 -10.61758 -45.97643 1.000 99.33875  ? 311 GLU   B OE1 1 
ATOM   4175 O OE2 . GLU   B 2 218 ? 19.72621 -10.42309 -48.04116 1.000 109.95186 ? 311 GLU   B OE2 1 
ATOM   4176 N N   . LEU   B 2 219 ? 18.82380 -7.66315  -42.46807 1.000 88.78707  ? 312 LEU   B N   1 
ATOM   4177 C CA  . LEU   B 2 219 ? 18.51141 -7.03104  -41.19063 1.000 79.09439  ? 312 LEU   B CA  1 
ATOM   4178 C C   . LEU   B 2 219 ? 19.78150 -6.71450  -40.41308 1.000 78.60235  ? 312 LEU   B C   1 
ATOM   4179 O O   . LEU   B 2 219 ? 19.86123 -5.68620  -39.73083 1.000 73.65605  ? 312 LEU   B O   1 
ATOM   4180 C CB  . LEU   B 2 219 ? 17.59018 -7.93001  -40.36565 1.000 85.09330  ? 312 LEU   B CB  1 
ATOM   4181 C CG  . LEU   B 2 219 ? 17.18637 -7.38317  -38.99354 1.000 83.41058  ? 312 LEU   B CG  1 
ATOM   4182 C CD1 . LEU   B 2 219 ? 16.37422 -6.10621  -39.14860 1.000 92.94489  ? 312 LEU   B CD1 1 
ATOM   4183 C CD2 . LEU   B 2 219 ? 16.41873 -8.42101  -38.18539 1.000 88.61198  ? 312 LEU   B CD2 1 
ATOM   4184 N N   . MET   B 2 220 ? 20.78599 -7.58897  -40.50512 1.000 76.02759  ? 313 MET   B N   1 
ATOM   4185 C CA  . MET   B 2 220 ? 22.05607 -7.34128  -39.83052 1.000 82.79178  ? 313 MET   B CA  1 
ATOM   4186 C C   . MET   B 2 220 ? 22.69111 -6.04742  -40.32359 1.000 85.58776  ? 313 MET   B C   1 
ATOM   4187 O O   . MET   B 2 220 ? 23.04188 -5.16987  -39.52646 1.000 78.33473  ? 313 MET   B O   1 
ATOM   4188 C CB  . MET   B 2 220 ? 22.99725 -8.52944  -40.04657 1.000 85.93748  ? 313 MET   B CB  1 
ATOM   4189 C CG  . MET   B 2 220 ? 24.36623 -8.41219  -39.37926 1.000 83.40369  ? 313 MET   B CG  1 
ATOM   4190 S SD  . MET   B 2 220 ? 25.58427 -7.47800  -40.33274 1.000 85.20779  ? 313 MET   B SD  1 
ATOM   4191 C CE  . MET   B 2 220 ? 25.34974 -8.17823  -41.96491 1.000 94.68310  ? 313 MET   B CE  1 
ATOM   4192 N N   . GLN   B 2 221 ? 22.84195 -5.91101  -41.64338 1.000 87.72035  ? 314 GLN   B N   1 
ATOM   4193 C CA  . GLN   B 2 221 ? 23.47649 -4.72187  -42.20128 1.000 92.50453  ? 314 GLN   B CA  1 
ATOM   4194 C C   . GLN   B 2 221 ? 22.62684 -3.47596  -41.98696 1.000 89.17142  ? 314 GLN   B C   1 
ATOM   4195 O O   . GLN   B 2 221 ? 23.16817 -2.37024  -41.87154 1.000 92.58262  ? 314 GLN   B O   1 
ATOM   4196 C CB  . GLN   B 2 221 ? 23.75308 -4.93306  -43.69004 1.000 83.90076  ? 314 GLN   B CB  1 
ATOM   4197 C CG  . GLN   B 2 221 ? 24.65704 -3.88739  -44.32009 1.000 92.33115  ? 314 GLN   B CG  1 
ATOM   4198 C CD  . GLN   B 2 221 ? 25.10350 -4.27479  -45.71710 1.000 88.77638  ? 314 GLN   B CD  1 
ATOM   4199 O OE1 . GLN   B 2 221 ? 24.62649 -5.25873  -46.28319 1.000 97.94356  ? 314 GLN   B OE1 1 
ATOM   4200 N NE2 . GLN   B 2 221 ? 26.02813 -3.50433  -46.27828 1.000 99.85582  ? 314 GLN   B NE2 1 
ATOM   4201 N N   . LYS   B 2 222 ? 21.30322 -3.63319  -41.92476 1.000 92.76708  ? 315 LYS   B N   1 
ATOM   4202 C CA  . LYS   B 2 222 ? 20.42874 -2.48339  -41.72064 1.000 91.17143  ? 315 LYS   B CA  1 
ATOM   4203 C C   . LYS   B 2 222 ? 20.61279 -1.88541  -40.33102 1.000 93.15325  ? 315 LYS   B C   1 
ATOM   4204 O O   . LYS   B 2 222 ? 20.53262 -0.66317  -40.15861 1.000 97.10674  ? 315 LYS   B O   1 
ATOM   4205 C CB  . LYS   B 2 222 ? 18.97249 -2.89535  -41.94448 1.000 95.80308  ? 315 LYS   B CB  1 
ATOM   4206 C CG  . LYS   B 2 222 ? 17.94285 -1.86044  -41.51646 1.000 102.09726 ? 315 LYS   B CG  1 
ATOM   4207 C CD  . LYS   B 2 222 ? 16.53063 -2.40749  -41.65514 1.000 108.74775 ? 315 LYS   B CD  1 
ATOM   4208 C CE  . LYS   B 2 222 ? 15.50361 -1.43674  -41.09635 1.000 116.33470 ? 315 LYS   B CE  1 
ATOM   4209 N NZ  . LYS   B 2 222 ? 14.11940 -1.97751  -41.18778 1.000 110.61071 ? 315 LYS   B NZ  1 
ATOM   4210 N N   . VAL   B 2 223 ? 20.87680 -2.72636  -39.33237 1.000 88.77699  ? 316 VAL   B N   1 
ATOM   4211 C CA  . VAL   B 2 223 ? 20.91810 -2.28934  -37.94065 1.000 90.42177  ? 316 VAL   B CA  1 
ATOM   4212 C C   . VAL   B 2 223 ? 22.32661 -2.23300  -37.37180 1.000 87.06327  ? 316 VAL   B C   1 
ATOM   4213 O O   . VAL   B 2 223 ? 22.51727 -1.63562  -36.29952 1.000 77.60849  ? 316 VAL   B O   1 
ATOM   4214 C CB  . VAL   B 2 223 ? 20.03111 -3.18162  -37.04833 1.000 91.23836  ? 316 VAL   B CB  1 
ATOM   4215 C CG1 . VAL   B 2 223 ? 18.70066 -3.43098  -37.72620 1.000 88.26768  ? 316 VAL   B CG1 1 
ATOM   4216 C CG2 . VAL   B 2 223 ? 20.73248 -4.49121  -36.75156 1.000 76.78506  ? 316 VAL   B CG2 1 
ATOM   4217 N N   . SER   B 2 224 ? 23.31623 -2.83262  -38.03657 1.000 89.23793  ? 317 SER   B N   1 
ATOM   4218 C CA  . SER   B 2 224 ? 24.68848 -2.80392  -37.55197 1.000 86.46586  ? 317 SER   B CA  1 
ATOM   4219 C C   . SER   B 2 224 ? 25.61615 -1.94172  -38.39214 1.000 88.50472  ? 317 SER   B C   1 
ATOM   4220 O O   . SER   B 2 224 ? 26.65159 -1.50345  -37.88183 1.000 90.21280  ? 317 SER   B O   1 
ATOM   4221 C CB  . SER   B 2 224 ? 25.26725 -4.22543  -37.48799 1.000 80.29582  ? 317 SER   B CB  1 
ATOM   4222 O OG  . SER   B 2 224 ? 25.32507 -4.81230  -38.77850 1.000 89.52069  ? 317 SER   B OG  1 
ATOM   4223 N N   . GLY   B 2 225 ? 25.27603 -1.68728  -39.65519 1.000 88.41265  ? 318 GLY   B N   1 
ATOM   4224 C CA  . GLY   B 2 225 ? 26.12945 -0.92811  -40.54124 1.000 92.01271  ? 318 GLY   B CA  1 
ATOM   4225 C C   . GLY   B 2 225 ? 27.30297 -1.69111  -41.11117 1.000 102.92450 ? 318 GLY   B C   1 
ATOM   4226 O O   . GLY   B 2 225 ? 27.98925 -1.16522  -41.99713 1.000 108.00183 ? 318 GLY   B O   1 
ATOM   4227 N N   . TYR   B 2 226 ? 27.55573 -2.91138  -40.64443 1.000 95.20143  ? 319 TYR   B N   1 
ATOM   4228 C CA  . TYR   B 2 226 ? 28.68615 -3.70274  -41.10922 1.000 97.08528  ? 319 TYR   B CA  1 
ATOM   4229 C C   . TYR   B 2 226 ? 28.27329 -4.54797  -42.30749 1.000 105.02847 ? 319 TYR   B C   1 
ATOM   4230 O O   . TYR   B 2 226 ? 27.20970 -5.17672  -42.29732 1.000 99.91747  ? 319 TYR   B O   1 
ATOM   4231 C CB  . TYR   B 2 226 ? 29.21623 -4.59947  -39.98888 1.000 95.91026  ? 319 TYR   B CB  1 
ATOM   4232 C CG  . TYR   B 2 226 ? 29.66206 -3.85179  -38.75001 1.000 95.80478  ? 319 TYR   B CG  1 
ATOM   4233 C CD1 . TYR   B 2 226 ? 30.05723 -2.52133  -38.81856 1.000 98.57925  ? 319 TYR   B CD1 1 
ATOM   4234 C CD2 . TYR   B 2 226 ? 29.68653 -4.47825  -37.51126 1.000 91.49544  ? 319 TYR   B CD2 1 
ATOM   4235 C CE1 . TYR   B 2 226 ? 30.46289 -1.83669  -37.68824 1.000 99.59211  ? 319 TYR   B CE1 1 
ATOM   4236 C CE2 . TYR   B 2 226 ? 30.09196 -3.80257  -36.37588 1.000 92.34222  ? 319 TYR   B CE2 1 
ATOM   4237 C CZ  . TYR   B 2 226 ? 30.47878 -2.48219  -36.47040 1.000 87.88017  ? 319 TYR   B CZ  1 
ATOM   4238 O OH  . TYR   B 2 226 ? 30.88285 -1.80446  -35.34364 1.000 94.55612  ? 319 TYR   B OH  1 
ATOM   4239 N N   . GLN   B 2 227 ? 29.11831 -4.56159  -43.33486 1.000 111.71946 ? 320 GLN   B N   1 
ATOM   4240 C CA  . GLN   B 2 227 ? 28.85191 -5.37031  -44.51216 1.000 107.01601 ? 320 GLN   B CA  1 
ATOM   4241 C C   . GLN   B 2 227 ? 29.01673 -6.85371  -44.17758 1.000 104.20582 ? 320 GLN   B C   1 
ATOM   4242 O O   . GLN   B 2 227 ? 29.54002 -7.22899  -43.12402 1.000 107.59534 ? 320 GLN   B O   1 
ATOM   4243 C CB  . GLN   B 2 227 ? 29.77979 -4.96294  -45.65790 1.000 110.16486 ? 320 GLN   B CB  1 
ATOM   4244 C CG  . GLN   B 2 227 ? 29.26972 -5.32817  -47.04583 1.000 125.65229 ? 320 GLN   B CG  1 
ATOM   4245 C CD  . GLN   B 2 227 ? 30.24126 -4.94712  -48.14500 1.000 130.38616 ? 320 GLN   B CD  1 
ATOM   4246 O OE1 . GLN   B 2 227 ? 30.09973 -5.37590  -49.29018 1.000 133.60115 ? 320 GLN   B OE1 1 
ATOM   4247 N NE2 . GLN   B 2 227 ? 31.23471 -4.13563  -47.80200 1.000 133.60125 ? 320 GLN   B NE2 1 
ATOM   4248 N N   . TRP   B 2 228 ? 28.55339 -7.70658  -45.09561 1.000 95.27077  ? 321 TRP   B N   1 
ATOM   4249 C CA  . TRP   B 2 228 ? 28.62487 -9.14717  -44.86998 1.000 100.28290 ? 321 TRP   B CA  1 
ATOM   4250 C C   . TRP   B 2 228 ? 30.06652 -9.62352  -44.73744 1.000 107.67748 ? 321 TRP   B C   1 
ATOM   4251 O O   . TRP   B 2 228 ? 30.35659 -10.53386 -43.95220 1.000 107.65563 ? 321 TRP   B O   1 
ATOM   4252 C CB  . TRP   B 2 228 ? 27.92017 -9.89404  -46.00155 1.000 100.50570 ? 321 TRP   B CB  1 
ATOM   4253 C CG  . TRP   B 2 228 ? 28.24470 -11.35456 -46.02463 1.000 96.37385  ? 321 TRP   B CG  1 
ATOM   4254 C CD1 . TRP   B 2 228 ? 29.02460 -12.00735 -46.93404 1.000 101.83387 ? 321 TRP   B CD1 1 
ATOM   4255 C CD2 . TRP   B 2 228 ? 27.81621 -12.34256 -45.08055 1.000 99.36830  ? 321 TRP   B CD2 1 
ATOM   4256 N NE1 . TRP   B 2 228 ? 29.09928 -13.34329 -46.62097 1.000 107.05693 ? 321 TRP   B NE1 1 
ATOM   4257 C CE2 . TRP   B 2 228 ? 28.36613 -13.57437 -45.48680 1.000 97.22694  ? 321 TRP   B CE2 1 
ATOM   4258 C CE3 . TRP   B 2 228 ? 27.01643 -12.30600 -43.93413 1.000 85.22184  ? 321 TRP   B CE3 1 
ATOM   4259 C CZ2 . TRP   B 2 228 ? 28.14240 -14.75754 -44.78767 1.000 99.85804  ? 321 TRP   B CZ2 1 
ATOM   4260 C CZ3 . TRP   B 2 228 ? 26.79580 -13.48149 -43.24213 1.000 85.23195  ? 321 TRP   B CZ3 1 
ATOM   4261 C CH2 . TRP   B 2 228 ? 27.35646 -14.69012 -43.67060 1.000 91.93664  ? 321 TRP   B CH2 1 
ATOM   4262 N N   . CYS   B 2 229 ? 30.98470 -9.02349  -45.49814 1.000 110.99283 ? 322 CYS   B N   1 
ATOM   4263 C CA  . CYS   B 2 229 ? 32.38276 -9.43419  -45.44073 1.000 109.66319 ? 322 CYS   B CA  1 
ATOM   4264 C C   . CYS   B 2 229 ? 33.03262 -9.10346  -44.10308 1.000 105.32222 ? 322 CYS   B C   1 
ATOM   4265 O O   . CYS   B 2 229 ? 34.02996 -9.73676  -43.73990 1.000 107.22013 ? 322 CYS   B O   1 
ATOM   4266 C CB  . CYS   B 2 229 ? 33.16792 -8.78026  -46.57874 1.000 109.10373 ? 322 CYS   B CB  1 
ATOM   4267 S SG  . CYS   B 2 229 ? 33.08092 -6.97490  -46.60228 1.000 116.44886 ? 322 CYS   B SG  1 
ATOM   4268 N N   . ASP   B 2 230 ? 32.49127 -8.13293  -43.36240 1.000 106.00656 ? 323 ASP   B N   1 
ATOM   4269 C CA  . ASP   B 2 230 ? 33.06327 -7.79001  -42.06485 1.000 110.17548 ? 323 ASP   B CA  1 
ATOM   4270 C C   . ASP   B 2 230 ? 32.78084 -8.86316  -41.02162 1.000 101.90077 ? 323 ASP   B C   1 
ATOM   4271 O O   . ASP   B 2 230 ? 33.59587 -9.07436  -40.11621 1.000 98.88498  ? 323 ASP   B O   1 
ATOM   4272 C CB  . ASP   B 2 230 ? 32.52304 -6.44115  -41.58760 1.000 99.80016  ? 323 ASP   B CB  1 
ATOM   4273 C CG  . ASP   B 2 230 ? 32.81635 -5.31650  -42.56061 1.000 107.51228 ? 323 ASP   B CG  1 
ATOM   4274 O OD1 . ASP   B 2 230 ? 33.74479 -5.46568  -43.38307 1.000 114.93824 ? 323 ASP   B OD1 1 
ATOM   4275 O OD2 . ASP   B 2 230 ? 32.12137 -4.28041  -42.49867 1.000 106.78185 ? 323 ASP   B OD2 1 
ATOM   4276 N N   . ILE   B 2 231 ? 31.64431 -9.55024  -41.12986 1.000 96.47827  ? 324 ILE   B N   1 
ATOM   4277 C CA  . ILE   B 2 231 ? 31.22351 -10.52913 -40.13489 1.000 99.20111  ? 324 ILE   B CA  1 
ATOM   4278 C C   . ILE   B 2 231 ? 31.34267 -11.95793 -40.63163 1.000 97.05343  ? 324 ILE   B C   1 
ATOM   4279 O O   . ILE   B 2 231 ? 31.06017 -12.88973 -39.86372 1.000 92.74087  ? 324 ILE   B O   1 
ATOM   4280 C CB  . ILE   B 2 231 ? 29.78533 -10.25716 -39.65489 1.000 92.83914  ? 324 ILE   B CB  1 
ATOM   4281 C CG1 . ILE   B 2 231 ? 28.77818 -10.68858 -40.72152 1.000 95.60229  ? 324 ILE   B CG1 1 
ATOM   4282 C CG2 . ILE   B 2 231 ? 29.60191 -8.78394  -39.32232 1.000 87.37683  ? 324 ILE   B CG2 1 
ATOM   4283 C CD1 . ILE   B 2 231 ? 27.34506 -10.66678 -40.24606 1.000 90.34908  ? 324 ILE   B CD1 1 
ATOM   4284 N N   . GLU   B 2 232 ? 31.75053 -12.16843 -41.88684 1.000 91.05215  ? 325 GLU   B N   1 
ATOM   4285 C CA  . GLU   B 2 232 ? 31.79986 -13.52462 -42.42691 1.000 95.33225  ? 325 GLU   B CA  1 
ATOM   4286 C C   . GLU   B 2 232 ? 32.75647 -14.40461 -41.63295 1.000 94.21817  ? 325 GLU   B C   1 
ATOM   4287 O O   . GLU   B 2 232 ? 32.44876 -15.56779 -41.34656 1.000 99.18941  ? 325 GLU   B O   1 
ATOM   4288 C CB  . GLU   B 2 232 ? 32.20203 -13.49591 -43.90145 1.000 98.94946  ? 325 GLU   B CB  1 
ATOM   4289 C CG  . GLU   B 2 232 ? 32.37465 -14.88045 -44.50988 1.000 91.33288  ? 325 GLU   B CG  1 
ATOM   4290 C CD  . GLU   B 2 232 ? 32.74826 -14.83417 -45.97676 1.000 109.17078 ? 325 GLU   B CD  1 
ATOM   4291 O OE1 . GLU   B 2 232 ? 32.76206 -13.72668 -46.55368 1.000 108.79164 ? 325 GLU   B OE1 1 
ATOM   4292 O OE2 . GLU   B 2 232 ? 33.02874 -15.90654 -46.55263 1.000 118.05508 ? 325 GLU   B OE2 1 
ATOM   4293 N N   . ASN   B 2 233 ? 33.92251 -13.86795 -41.26792 1.000 91.18259  ? 326 ASN   B N   1 
ATOM   4294 C CA  . ASN   B 2 233 ? 34.86968 -14.64320 -40.47466 1.000 92.75373  ? 326 ASN   B CA  1 
ATOM   4295 C C   . ASN   B 2 233 ? 34.29598 -14.96060 -39.09965 1.000 97.90298  ? 326 ASN   B C   1 
ATOM   4296 O O   . ASN   B 2 233 ? 34.50947 -16.05500 -38.56478 1.000 96.25528  ? 326 ASN   B O   1 
ATOM   4297 C CB  . ASN   B 2 233 ? 36.19123 -13.88460 -40.34677 1.000 102.67638 ? 326 ASN   B CB  1 
ATOM   4298 C CG  . ASN   B 2 233 ? 37.36428 -14.80070 -40.05451 1.000 110.01042 ? 326 ASN   B CG  1 
ATOM   4299 O OD1 . ASN   B 2 233 ? 37.43619 -15.91794 -40.56624 1.000 104.85721 ? 326 ASN   B OD1 1 
ATOM   4300 N ND2 . ASN   B 2 233 ? 38.29072 -14.33146 -39.22778 1.000 109.67605 ? 326 ASN   B ND2 1 
ATOM   4301 N N   . CYS   B 2 234 ? 33.55315 -14.01717 -38.51650 1.000 89.35172  ? 327 CYS   B N   1 
ATOM   4302 C CA  . CYS   B 2 234 ? 32.94957 -14.25538 -37.20992 1.000 90.19775  ? 327 CYS   B CA  1 
ATOM   4303 C C   . CYS   B 2 234 ? 31.75148 -15.18870 -37.31694 1.000 92.99436  ? 327 CYS   B C   1 
ATOM   4304 O O   . CYS   B 2 234 ? 31.56407 -16.06458 -36.46431 1.000 88.89211  ? 327 CYS   B O   1 
ATOM   4305 C CB  . CYS   B 2 234 ? 32.53953 -12.93043 -36.56988 1.000 86.76747  ? 327 CYS   B CB  1 
ATOM   4306 S SG  . CYS   B 2 234 ? 31.79440 -13.09028 -34.92991 1.000 86.62808  ? 327 CYS   B SG  1 
ATOM   4307 N N   . VAL   B 2 235 ? 30.92789 -15.01336 -38.35405 1.000 94.40095  ? 328 VAL   B N   1 
ATOM   4308 C CA  . VAL   B 2 235 ? 29.78250 -15.89706 -38.55425 1.000 81.40153  ? 328 VAL   B CA  1 
ATOM   4309 C C   . VAL   B 2 235 ? 30.24857 -17.33396 -38.74346 1.000 95.83998  ? 328 VAL   B C   1 
ATOM   4310 O O   . VAL   B 2 235 ? 29.67012 -18.26934 -38.17700 1.000 96.95194  ? 328 VAL   B O   1 
ATOM   4311 C CB  . VAL   B 2 235 ? 28.93207 -15.41150 -39.74403 1.000 94.96942  ? 328 VAL   B CB  1 
ATOM   4312 C CG1 . VAL   B 2 235 ? 27.96598 -16.49747 -40.19293 1.000 90.52050  ? 328 VAL   B CG1 1 
ATOM   4313 C CG2 . VAL   B 2 235 ? 28.16934 -14.15069 -39.36943 1.000 86.91516  ? 328 VAL   B CG2 1 
ATOM   4314 N N   . LYS   B 2 236 ? 31.31172 -17.53156 -39.52814 1.000 98.60783  ? 329 LYS   B N   1 
ATOM   4315 C CA  . LYS   B 2 236 ? 31.83648 -18.87736 -39.73217 1.000 102.55112 ? 329 LYS   B CA  1 
ATOM   4316 C C   . LYS   B 2 236 ? 32.38304 -19.46622 -38.43841 1.000 102.77731 ? 329 LYS   B C   1 
ATOM   4317 O O   . LYS   B 2 236 ? 32.27868 -20.67772 -38.21647 1.000 102.64524 ? 329 LYS   B O   1 
ATOM   4318 C CB  . LYS   B 2 236 ? 32.91881 -18.86562 -40.81345 1.000 109.10635 ? 329 LYS   B CB  1 
ATOM   4319 C CG  . LYS   B 2 236 ? 33.43338 -20.24919 -41.18836 1.000 121.19390 ? 329 LYS   B CG  1 
ATOM   4320 C CD  . LYS   B 2 236 ? 34.37238 -20.19513 -42.38260 1.000 123.66049 ? 329 LYS   B CD  1 
ATOM   4321 C CE  . LYS   B 2 236 ? 35.63127 -19.40532 -42.06797 1.000 124.57774 ? 329 LYS   B CE  1 
ATOM   4322 N NZ  . LYS   B 2 236 ? 36.57988 -19.40029 -43.21604 1.000 121.55060 ? 329 LYS   B NZ  1 
ATOM   4323 N N   . TRP   B 2 237 ? 32.96167 -18.63163 -37.57148 1.000 97.30703  ? 330 TRP   B N   1 
ATOM   4324 C CA  . TRP   B 2 237 ? 33.43400 -19.12681 -36.28228 1.000 101.50930 ? 330 TRP   B CA  1 
ATOM   4325 C C   . TRP   B 2 237 ? 32.27232 -19.39142 -35.33254 1.000 97.10751  ? 330 TRP   B C   1 
ATOM   4326 O O   . TRP   B 2 237 ? 32.30361 -20.35347 -34.55685 1.000 99.41449  ? 330 TRP   B O   1 
ATOM   4327 C CB  . TRP   B 2 237 ? 34.41591 -18.13552 -35.66029 1.000 94.56347  ? 330 TRP   B CB  1 
ATOM   4328 C CG  . TRP   B 2 237 ? 34.73389 -18.45250 -34.23381 1.000 104.92175 ? 330 TRP   B CG  1 
ATOM   4329 C CD1 . TRP   B 2 237 ? 35.66575 -19.33903 -33.77891 1.000 103.69379 ? 330 TRP   B CD1 1 
ATOM   4330 C CD2 . TRP   B 2 237 ? 34.11233 -17.89143 -33.07119 1.000 96.72916  ? 330 TRP   B CD2 1 
ATOM   4331 N NE1 . TRP   B 2 237 ? 35.66546 -19.36249 -32.40502 1.000 98.88296  ? 330 TRP   B NE1 1 
ATOM   4332 C CE2 . TRP   B 2 237 ? 34.72058 -18.48248 -31.94633 1.000 104.23109 ? 330 TRP   B CE2 1 
ATOM   4333 C CE3 . TRP   B 2 237 ? 33.10152 -16.94565 -32.87257 1.000 94.66939  ? 330 TRP   B CE3 1 
ATOM   4334 C CZ2 . TRP   B 2 237 ? 34.35208 -18.15801 -30.64185 1.000 100.43880 ? 330 TRP   B CZ2 1 
ATOM   4335 C CZ3 . TRP   B 2 237 ? 32.73707 -16.62526 -31.57706 1.000 93.49393  ? 330 TRP   B CZ3 1 
ATOM   4336 C CH2 . TRP   B 2 237 ? 33.35993 -17.23052 -30.47917 1.000 95.12835  ? 330 TRP   B CH2 1 
ATOM   4337 N N   . MET   B 2 238 ? 31.24256 -18.54634 -35.37463 1.000 92.90798  ? 331 MET   B N   1 
ATOM   4338 C CA  . MET   B 2 238 ? 30.04457 -18.72993 -34.56353 1.000 91.46018  ? 331 MET   B CA  1 
ATOM   4339 C C   . MET   B 2 238 ? 29.17296 -19.88249 -35.05178 1.000 99.33404  ? 331 MET   B C   1 
ATOM   4340 O O   . MET   B 2 238 ? 28.15867 -20.18518 -34.41188 1.000 100.21131 ? 331 MET   B O   1 
ATOM   4341 C CB  . MET   B 2 238 ? 29.24068 -17.42575 -34.54743 1.000 83.03004  ? 331 MET   B CB  1 
ATOM   4342 C CG  . MET   B 2 238 ? 28.21038 -17.30842 -33.43417 1.000 81.37087  ? 331 MET   B CG  1 
ATOM   4343 S SD  . MET   B 2 238 ? 27.48610 -15.66103 -33.33851 1.000 85.53870  ? 331 MET   B SD  1 
ATOM   4344 C CE  . MET   B 2 238 ? 28.90599 -14.69234 -32.83189 1.000 77.93629  ? 331 MET   B CE  1 
ATOM   4345 N N   . VAL   B 2 239 ? 29.55169 -20.53275 -36.15494 1.000 97.84776  ? 332 VAL   B N   1 
ATOM   4346 C CA  . VAL   B 2 239 ? 28.72299 -21.60110 -36.72330 1.000 107.63416 ? 332 VAL   B CA  1 
ATOM   4347 C C   . VAL   B 2 239 ? 28.41422 -22.70262 -35.71135 1.000 103.71936 ? 332 VAL   B C   1 
ATOM   4348 O O   . VAL   B 2 239 ? 27.22600 -23.01728 -35.52358 1.000 96.67086  ? 332 VAL   B O   1 
ATOM   4349 C CB  . VAL   B 2 239 ? 29.36064 -22.13357 -38.01140 1.000 99.34240  ? 332 VAL   B CB  1 
ATOM   4350 C CG1 . VAL   B 2 239 ? 28.90201 -23.55325 -38.29994 1.000 100.77181 ? 332 VAL   B CG1 1 
ATOM   4351 C CG2 . VAL   B 2 239 ? 29.02978 -21.22038 -39.18054 1.000 102.26257 ? 332 VAL   B CG2 1 
ATOM   4352 N N   . PRO   B 2 240 ? 29.38786 -23.31851 -35.03013 1.000 106.79807 ? 333 PRO   B N   1 
ATOM   4353 C CA  . PRO   B 2 240 ? 29.03707 -24.41666 -34.11472 1.000 106.58451 ? 333 PRO   B CA  1 
ATOM   4354 C C   . PRO   B 2 240 ? 28.18566 -23.97813 -32.93552 1.000 105.61469 ? 333 PRO   B C   1 
ATOM   4355 O O   . PRO   B 2 240 ? 27.32216 -24.74344 -32.48886 1.000 102.61317 ? 333 PRO   B O   1 
ATOM   4356 C CB  . PRO   B 2 240 ? 30.40405 -24.94648 -33.65577 1.000 117.58806 ? 333 PRO   B CB  1 
ATOM   4357 C CG  . PRO   B 2 240 ? 31.37450 -24.45982 -34.67659 1.000 112.62850 ? 333 PRO   B CG  1 
ATOM   4358 C CD  . PRO   B 2 240 ? 30.84961 -23.12422 -35.08800 1.000 108.31978 ? 333 PRO   B CD  1 
ATOM   4359 N N   . PHE   B 2 241 ? 28.39917 -22.76610 -32.41907 1.000 101.82453 ? 334 PHE   B N   1 
ATOM   4360 C CA  . PHE   B 2 241 ? 27.61100 -22.29178 -31.28679 1.000 105.79007 ? 334 PHE   B CA  1 
ATOM   4361 C C   . PHE   B 2 241 ? 26.16155 -22.02785 -31.67645 1.000 98.47068  ? 334 PHE   B C   1 
ATOM   4362 O O   . PHE   B 2 241 ? 25.25850 -22.19123 -30.84757 1.000 94.79549  ? 334 PHE   B O   1 
ATOM   4363 C CB  . PHE   B 2 241 ? 28.23913 -21.02395 -30.70944 1.000 93.51641  ? 334 PHE   B CB  1 
ATOM   4364 C CG  . PHE   B 2 241 ? 29.72489 -21.12060 -30.50292 1.000 94.41017  ? 334 PHE   B CG  1 
ATOM   4365 C CD1 . PHE   B 2 241 ? 30.24294 -21.64595 -29.33066 1.000 103.61455 ? 334 PHE   B CD1 1 
ATOM   4366 C CD2 . PHE   B 2 241 ? 30.60395 -20.67753 -31.47869 1.000 101.38447 ? 334 PHE   B CD2 1 
ATOM   4367 C CE1 . PHE   B 2 241 ? 31.61042 -21.73295 -29.13735 1.000 103.34157 ? 334 PHE   B CE1 1 
ATOM   4368 C CE2 . PHE   B 2 241 ? 31.97106 -20.76184 -31.29177 1.000 101.74201 ? 334 PHE   B CE2 1 
ATOM   4369 C CZ  . PHE   B 2 241 ? 32.47487 -21.29003 -30.11928 1.000 99.25941  ? 334 PHE   B CZ  1 
ATOM   4370 N N   . ALA   B 2 242 ? 25.91865 -21.61985 -32.92403 1.000 91.62098  ? 335 ALA   B N   1 
ATOM   4371 C CA  . ALA   B 2 242 ? 24.55867 -21.29489 -33.34172 1.000 99.91498  ? 335 ALA   B CA  1 
ATOM   4372 C C   . ALA   B 2 242 ? 23.69382 -22.54490 -33.44654 1.000 100.72306 ? 335 ALA   B C   1 
ATOM   4373 O O   . ALA   B 2 242 ? 22.53250 -22.53947 -33.02164 1.000 101.90619 ? 335 ALA   B O   1 
ATOM   4374 C CB  . ALA   B 2 242 ? 24.58332 -20.54495 -34.67303 1.000 100.15344 ? 335 ALA   B CB  1 
ATOM   4375 N N   . MET   B 2 243 ? 24.24120 -23.62747 -34.00436 1.000 93.17064  ? 336 MET   B N   1 
ATOM   4376 C CA  . MET   B 2 243 ? 23.45464 -24.84479 -34.17435 1.000 103.74386 ? 336 MET   B CA  1 
ATOM   4377 C C   . MET   B 2 243 ? 23.20470 -25.55440 -32.85174 1.000 104.39986 ? 336 MET   B C   1 
ATOM   4378 O O   . MET   B 2 243 ? 22.16076 -26.19494 -32.68630 1.000 102.71441 ? 336 MET   B O   1 
ATOM   4379 C CB  . MET   B 2 243 ? 24.14670 -25.78815 -35.15362 1.000 106.25662 ? 336 MET   B CB  1 
ATOM   4380 C CG  . MET   B 2 243 ? 23.85318 -25.47816 -36.60336 1.000 110.06709 ? 336 MET   B CG  1 
ATOM   4381 S SD  . MET   B 2 243 ? 22.11098 -25.65297 -37.03580 1.000 123.61468 ? 336 MET   B SD  1 
ATOM   4382 C CE  . MET   B 2 243 ? 21.62271 -23.94276 -37.21345 1.000 106.70373 ? 336 MET   B CE  1 
ATOM   4383 N N   . VAL   B 2 244 ? 24.14478 -25.46647 -31.90863 1.000 104.92657 ? 337 VAL   B N   1 
ATOM   4384 C CA  . VAL   B 2 244 ? 23.92739 -26.06410 -30.59442 1.000 101.50563 ? 337 VAL   B CA  1 
ATOM   4385 C C   . VAL   B 2 244 ? 22.70663 -25.44246 -29.92837 1.000 107.39961 ? 337 VAL   B C   1 
ATOM   4386 O O   . VAL   B 2 244 ? 21.91151 -26.13505 -29.28117 1.000 108.68645 ? 337 VAL   B O   1 
ATOM   4387 C CB  . VAL   B 2 244 ? 25.19114 -25.91994 -29.72626 1.000 120.03312 ? 337 VAL   B CB  1 
ATOM   4388 C CG1 . VAL   B 2 244 ? 24.89534 -26.30479 -28.29283 1.000 116.49112 ? 337 VAL   B CG1 1 
ATOM   4389 C CG2 . VAL   B 2 244 ? 26.31180 -26.78396 -30.28119 1.000 118.39521 ? 337 VAL   B CG2 1 
ATOM   4390 N N   . ILE   B 2 245 ? 22.52872 -24.13002 -30.09132 1.000 105.24976 ? 338 ILE   B N   1 
ATOM   4391 C CA  . ILE   B 2 245 ? 21.32521 -23.47664 -29.58837 1.000 103.16672 ? 338 ILE   B CA  1 
ATOM   4392 C C   . ILE   B 2 245 ? 20.11030 -23.89983 -30.40525 1.000 107.99179 ? 338 ILE   B C   1 
ATOM   4393 O O   . ILE   B 2 245 ? 19.01217 -24.07776 -29.86418 1.000 112.94836 ? 338 ILE   B O   1 
ATOM   4394 C CB  . ILE   B 2 245 ? 21.50972 -21.94781 -29.58967 1.000 100.48450 ? 338 ILE   B CB  1 
ATOM   4395 C CG1 . ILE   B 2 245 ? 22.72345 -21.55849 -28.74389 1.000 98.41193  ? 338 ILE   B CG1 1 
ATOM   4396 C CG2 . ILE   B 2 245 ? 20.25780 -21.25250 -29.07342 1.000 109.61027 ? 338 ILE   B CG2 1 
ATOM   4397 C CD1 . ILE   B 2 245 ? 22.62257 -21.99298 -27.29881 1.000 102.21079 ? 338 ILE   B CD1 1 
ATOM   4398 N N   . ARG   B 2 246 ? 20.28653 -24.07742 -31.71791 1.000 102.39557 ? 339 ARG   B N   1 
ATOM   4399 C CA  . ARG   B 2 246 ? 19.17354 -24.50220 -32.56085 1.000 103.00397 ? 339 ARG   B CA  1 
ATOM   4400 C C   . ARG   B 2 246 ? 18.77435 -25.94703 -32.28811 1.000 107.19813 ? 339 ARG   B C   1 
ATOM   4401 O O   . ARG   B 2 246 ? 17.59327 -26.29134 -32.40470 1.000 108.02452 ? 339 ARG   B O   1 
ATOM   4402 C CB  . ARG   B 2 246 ? 19.52755 -24.32697 -34.03839 1.000 102.66783 ? 339 ARG   B CB  1 
ATOM   4403 C CG  . ARG   B 2 246 ? 19.59509 -22.88380 -34.51057 1.000 96.66615  ? 339 ARG   B CG  1 
ATOM   4404 C CD  . ARG   B 2 246 ? 18.24540 -22.19449 -34.41683 1.000 94.97612  ? 339 ARG   B CD  1 
ATOM   4405 N NE  . ARG   B 2 246 ? 18.20735 -20.97660 -35.21762 1.000 83.76042  ? 339 ARG   B NE  1 
ATOM   4406 C CZ  . ARG   B 2 246 ? 17.31967 -20.00383 -35.06372 1.000 89.28691  ? 339 ARG   B CZ  1 
ATOM   4407 N NH1 . ARG   B 2 246 ? 16.39145 -20.05751 -34.12243 1.000 93.28540  ? 339 ARG   B NH1 1 
ATOM   4408 N NH2 . ARG   B 2 246 ? 17.36884 -18.94736 -35.87045 1.000 85.57553  ? 339 ARG   B NH2 1 
ATOM   4409 N N   . GLU   B 2 247 ? 19.73406 -26.80423 -31.92978 1.000 113.17880 ? 340 GLU   B N   1 
ATOM   4410 C CA  . GLU   B 2 247 ? 19.40923 -28.20436 -31.67260 1.000 108.83011 ? 340 GLU   B CA  1 
ATOM   4411 C C   . GLU   B 2 247 ? 18.60797 -28.36256 -30.38616 1.000 111.91131 ? 340 GLU   B C   1 
ATOM   4412 O O   . GLU   B 2 247 ? 17.71177 -29.21102 -30.30810 1.000 109.58164 ? 340 GLU   B O   1 
ATOM   4413 C CB  . GLU   B 2 247 ? 20.68614 -29.04389 -31.61589 1.000 110.97795 ? 340 GLU   B CB  1 
ATOM   4414 C CG  . GLU   B 2 247 ? 21.35712 -29.24932 -32.96395 1.000 117.44039 ? 340 GLU   B CG  1 
ATOM   4415 C CD  . GLU   B 2 247 ? 22.52960 -30.20757 -32.89351 1.000 125.38847 ? 340 GLU   B CD  1 
ATOM   4416 O OE1 . GLU   B 2 247 ? 22.67965 -30.88909 -31.85806 1.000 139.82594 ? 340 GLU   B OE1 1 
ATOM   4417 O OE2 . GLU   B 2 247 ? 23.30139 -30.27922 -33.87296 1.000 124.60082 ? 340 GLU   B OE2 1 
ATOM   4418 N N   . THR   B 2 248 ? 18.91245 -27.55831 -29.36803 1.000 107.12358 ? 341 THR   B N   1 
ATOM   4419 C CA  . THR   B 2 248 ? 18.19410 -27.63462 -28.10330 1.000 114.84391 ? 341 THR   B CA  1 
ATOM   4420 C C   . THR   B 2 248 ? 16.95126 -26.75649 -28.06874 1.000 117.91268 ? 341 THR   B C   1 
ATOM   4421 O O   . THR   B 2 248 ? 16.04682 -27.01991 -27.26782 1.000 119.27549 ? 341 THR   B O   1 
ATOM   4422 C CB  . THR   B 2 248 ? 19.11556 -27.24938 -26.93995 1.000 116.66391 ? 341 THR   B CB  1 
ATOM   4423 O OG1 . THR   B 2 248 ? 18.41279 -27.40561 -25.70099 1.000 131.09419 ? 341 THR   B OG1 1 
ATOM   4424 C CG2 . THR   B 2 248 ? 19.58011 -25.80508 -27.07329 1.000 115.71752 ? 341 THR   B CG2 1 
ATOM   4425 N N   . GLY   B 2 249 ? 16.88169 -25.73233 -28.91118 1.000 129.20583 ? 342 GLY   B N   1 
ATOM   4426 C CA  . GLY   B 2 249 ? 15.74641 -24.83589 -28.94987 1.000 124.64767 ? 342 GLY   B CA  1 
ATOM   4427 C C   . GLY   B 2 249 ? 16.04095 -23.50052 -28.28756 1.000 126.24127 ? 342 GLY   B C   1 
ATOM   4428 O O   . GLY   B 2 249 ? 17.05415 -23.30359 -27.61156 1.000 120.38752 ? 342 GLY   B O   1 
ATOM   4429 N N   . SER   B 2 250 ? 15.11652 -22.56742 -28.49507 1.000 133.27715 ? 343 SER   B N   1 
ATOM   4430 C CA  . SER   B 2 250 ? 15.23163 -21.22152 -27.95294 1.000 127.73730 ? 343 SER   B CA  1 
ATOM   4431 C C   . SER   B 2 250 ? 14.54916 -21.15783 -26.59208 1.000 129.93563 ? 343 SER   B C   1 
ATOM   4432 O O   . SER   B 2 250 ? 13.42705 -21.64809 -26.43071 1.000 128.73967 ? 343 SER   B O   1 
ATOM   4433 C CB  . SER   B 2 250 ? 14.60841 -20.20692 -28.91184 1.000 129.58991 ? 343 SER   B CB  1 
ATOM   4434 O OG  . SER   B 2 250 ? 15.00492 -20.45851 -30.25083 1.000 122.25110 ? 343 SER   B OG  1 
ATOM   4435 N N   . SER   B 2 251 ? 15.22683 -20.55435 -25.61894 1.000 132.37500 ? 344 SER   B N   1 
ATOM   4436 C CA  . SER   B 2 251 ? 14.69137 -20.48543 -24.26839 1.000 129.35147 ? 344 SER   B CA  1 
ATOM   4437 C C   . SER   B 2 251 ? 13.53624 -19.48927 -24.18906 1.000 128.68396 ? 344 SER   B C   1 
ATOM   4438 O O   . SER   B 2 251 ? 13.34088 -18.64378 -25.06692 1.000 126.61906 ? 344 SER   B O   1 
ATOM   4439 C CB  . SER   B 2 251 ? 15.78747 -20.09947 -23.27494 1.000 123.51851 ? 344 SER   B CB  1 
ATOM   4440 O OG  . SER   B 2 251 ? 16.80035 -21.08922 -23.22592 1.000 127.38464 ? 344 SER   B OG  1 
ATOM   4441 N N   . LYS   B 2 252 ? 12.76468 -19.60361 -23.11330 1.000 111.79512 ? 345 LYS   B N   1 
ATOM   4442 C CA  . LYS   B 2 252 ? 11.61477 -18.74905 -22.86185 1.000 106.31267 ? 345 LYS   B CA  1 
ATOM   4443 C C   . LYS   B 2 252 ? 11.99996 -17.58634 -21.95466 1.000 102.46268 ? 345 LYS   B C   1 
ATOM   4444 O O   . LYS   B 2 252 ? 12.97795 -17.64684 -21.20525 1.000 96.02571  ? 345 LYS   B O   1 
ATOM   4445 C CB  . LYS   B 2 252 ? 10.47444 -19.54858 -22.22505 1.000 106.01316 ? 345 LYS   B CB  1 
ATOM   4446 C CG  . LYS   B 2 252 ? 9.92805  -20.67022 -23.09281 1.000 110.97063 ? 345 LYS   B CG  1 
ATOM   4447 C CD  . LYS   B 2 252 ? 9.13236  -20.12769 -24.26736 1.000 103.49667 ? 345 LYS   B CD  1 
ATOM   4448 C CE  . LYS   B 2 252 ? 8.48616  -21.25443 -25.05676 1.000 110.81624 ? 345 LYS   B CE  1 
ATOM   4449 N NZ  . LYS   B 2 252 ? 7.60696  -20.74117 -26.14172 1.000 111.14188 ? 345 LYS   B NZ  1 
ATOM   4450 N N   . LEU   B 2 253 ? 11.20909 -16.51846 -22.03248 1.000 101.70776 ? 346 LEU   B N   1 
ATOM   4451 C CA  . LEU   B 2 253 ? 11.44725 -15.34583 -21.20182 1.000 96.07115  ? 346 LEU   B CA  1 
ATOM   4452 C C   . LEU   B 2 253 ? 11.03672 -15.62635 -19.76188 1.000 97.26652  ? 346 LEU   B C   1 
ATOM   4453 O O   . LEU   B 2 253 ? 9.93508  -16.12057 -19.50281 1.000 100.59069 ? 346 LEU   B O   1 
ATOM   4454 C CB  . LEU   B 2 253 ? 10.67868 -14.14344 -21.74718 1.000 93.38646  ? 346 LEU   B CB  1 
ATOM   4455 C CG  . LEU   B 2 253 ? 10.71949 -12.87173 -20.89588 1.000 93.61875  ? 346 LEU   B CG  1 
ATOM   4456 C CD1 . LEU   B 2 253 ? 12.14777 -12.37252 -20.73226 1.000 89.36980  ? 346 LEU   B CD1 1 
ATOM   4457 C CD2 . LEU   B 2 253 ? 9.83421  -11.79213 -21.49946 1.000 85.01976  ? 346 LEU   B CD2 1 
ATOM   4458 N N   . LYS   B 2 254 ? 11.92454 -15.30786 -18.82571 1.000 101.32685 ? 347 LYS   B N   1 
ATOM   4459 C CA  . LYS   B 2 254 ? 11.66850 -15.52977 -17.41169 1.000 100.56036 ? 347 LYS   B CA  1 
ATOM   4460 C C   . LYS   B 2 254 ? 11.09347 -14.28039 -16.75797 1.000 104.71198 ? 347 LYS   B C   1 
ATOM   4461 O O   . LYS   B 2 254 ? 11.39609 -13.15025 -17.15053 1.000 103.32033 ? 347 LYS   B O   1 
ATOM   4462 C CB  . LYS   B 2 254 ? 12.94979 -15.93571 -16.68088 1.000 96.34495  ? 347 LYS   B CB  1 
ATOM   4463 C CG  . LYS   B 2 254 ? 13.42756 -17.34847 -16.95977 1.000 90.42105  ? 347 LYS   B CG  1 
ATOM   4464 C CD  . LYS   B 2 254 ? 14.60488 -17.69802 -16.06135 1.000 101.11118 ? 347 LYS   B CD  1 
ATOM   4465 C CE  . LYS   B 2 254 ? 15.01937 -19.15098 -16.21602 1.000 107.41221 ? 347 LYS   B CE  1 
ATOM   4466 N NZ  . LYS   B 2 254 ? 16.11571 -19.51166 -15.27387 1.000 96.54928  ? 347 LYS   B NZ  1 
ATOM   4467 N N   . HIS   B 2 255 ? 10.25488 -14.50010 -15.75092 1.000 116.30167 ? 348 HIS   B N   1 
ATOM   4468 C CA  . HIS   B 2 255 ? 9.79719  -13.44392 -14.86174 1.000 115.80149 ? 348 HIS   B CA  1 
ATOM   4469 C C   . HIS   B 2 255 ? 10.55244 -13.54088 -13.54401 1.000 116.50833 ? 348 HIS   B C   1 
ATOM   4470 O O   . HIS   B 2 255 ? 10.73087 -14.63369 -12.99809 1.000 117.95444 ? 348 HIS   B O   1 
ATOM   4471 C CB  . HIS   B 2 255 ? 8.29139  -13.53938 -14.60997 1.000 124.58337 ? 348 HIS   B CB  1 
ATOM   4472 C CG  . HIS   B 2 255 ? 7.82516  -12.72940 -13.44011 1.000 128.79499 ? 348 HIS   B CG  1 
ATOM   4473 N ND1 . HIS   B 2 255 ? 7.91825  -11.35467 -13.40102 1.000 130.26481 ? 348 HIS   B ND1 1 
ATOM   4474 C CD2 . HIS   B 2 255 ? 7.27186  -13.10231 -12.26181 1.000 126.02700 ? 348 HIS   B CD2 1 
ATOM   4475 C CE1 . HIS   B 2 255 ? 7.43816  -10.91537 -12.25126 1.000 123.93455 ? 348 HIS   B CE1 1 
ATOM   4476 N NE2 . HIS   B 2 255 ? 7.03942  -11.95568 -11.54176 1.000 121.81315 ? 348 HIS   B NE2 1 
ATOM   4477 N N   . PHE   B 2 256 ? 11.00150 -12.39582 -13.04005 1.000 115.47279 ? 349 PHE   B N   1 
ATOM   4478 C CA  . PHE   B 2 256 ? 11.79314 -12.33525 -11.82001 1.000 118.46485 ? 349 PHE   B CA  1 
ATOM   4479 C C   . PHE   B 2 256 ? 11.05881 -11.50825 -10.77601 1.000 113.26523 ? 349 PHE   B C   1 
ATOM   4480 O O   . PHE   B 2 256 ? 10.56850 -10.41435 -11.07620 1.000 107.32630 ? 349 PHE   B O   1 
ATOM   4481 C CB  . PHE   B 2 256 ? 13.17925 -11.74916 -12.09741 1.000 107.38067 ? 349 PHE   B CB  1 
ATOM   4482 C CG  . PHE   B 2 256 ? 14.01461 -12.59106 -13.01858 1.000 101.83341 ? 349 PHE   B CG  1 
ATOM   4483 C CD1 . PHE   B 2 256 ? 14.72238 -13.67830 -12.53199 1.000 103.23336 ? 349 PHE   B CD1 1 
ATOM   4484 C CD2 . PHE   B 2 256 ? 14.08714 -12.30094 -14.37123 1.000 106.89561 ? 349 PHE   B CD2 1 
ATOM   4485 C CE1 . PHE   B 2 256 ? 15.49031 -14.45937 -13.37592 1.000 100.99391 ? 349 PHE   B CE1 1 
ATOM   4486 C CE2 . PHE   B 2 256 ? 14.85392 -13.07762 -15.22149 1.000 100.08182 ? 349 PHE   B CE2 1 
ATOM   4487 C CZ  . PHE   B 2 256 ? 15.55651 -14.15843 -14.72283 1.000 105.62965 ? 349 PHE   B CZ  1 
ATOM   4488 N N   . ARG   B 2 257 ? 10.98448 -12.03789 -9.55607  1.000 112.65325 ? 350 ARG   B N   1 
ATOM   4489 C CA  . ARG   B 2 257 ? 10.29367 -11.35170 -8.47246  1.000 111.11617 ? 350 ARG   B CA  1 
ATOM   4490 C C   . ARG   B 2 257 ? 10.96614 -10.01768 -8.17496  1.000 105.31467 ? 350 ARG   B C   1 
ATOM   4491 O O   . ARG   B 2 257 ? 12.18249 -9.95084  -7.97507  1.000 101.06847 ? 350 ARG   B O   1 
ATOM   4492 C CB  . ARG   B 2 257 ? 10.28060 -12.22990 -7.22047  1.000 120.31288 ? 350 ARG   B CB  1 
ATOM   4493 C CG  . ARG   B 2 257 ? 9.35665  -11.73707 -6.11872  1.000 117.42663 ? 350 ARG   B CG  1 
ATOM   4494 C CD  . ARG   B 2 257 ? 9.67652  -12.38483 -4.77551  1.000 123.18044 ? 350 ARG   B CD  1 
ATOM   4495 N NE  . ARG   B 2 257 ? 9.83402  -13.83200 -4.86936  1.000 130.78630 ? 350 ARG   B NE  1 
ATOM   4496 C CZ  . ARG   B 2 257 ? 10.99484 -14.46770 -4.77956  1.000 130.04755 ? 350 ARG   B CZ  1 
ATOM   4497 N NH1 . ARG   B 2 257 ? 12.12814 -13.81322 -4.58405  1.000 124.17734 ? 350 ARG   B NH1 1 
ATOM   4498 N NH2 . ARG   B 2 257 ? 11.01868 -15.79338 -4.88589  1.000 127.33506 ? 350 ARG   B NH2 1 
ATOM   4499 N N   . GLY   B 2 258 ? 10.16775 -8.95183  -8.14766  1.000 99.54988  ? 351 GLY   B N   1 
ATOM   4500 C CA  . GLY   B 2 258 ? 10.67682 -7.61703  -7.92940  1.000 97.66512  ? 351 GLY   B CA  1 
ATOM   4501 C C   . GLY   B 2 258 ? 11.14662 -6.90003  -9.17607  1.000 102.67765 ? 351 GLY   B C   1 
ATOM   4502 O O   . GLY   B 2 258 ? 11.35731 -5.68118  -9.12756  1.000 104.64405 ? 351 GLY   B O   1 
ATOM   4503 N N   . VAL   B 2 259 ? 11.31809 -7.61014  -10.28654 1.000 105.16136 ? 352 VAL   B N   1 
ATOM   4504 C CA  . VAL   B 2 259 ? 11.74634 -7.01880  -11.54828 1.000 101.07321 ? 352 VAL   B CA  1 
ATOM   4505 C C   . VAL   B 2 259 ? 10.51496 -6.82616  -12.42127 1.000 99.08076  ? 352 VAL   B C   1 
ATOM   4506 O O   . VAL   B 2 259 ? 9.77893  -7.78388  -12.68901 1.000 107.71395 ? 352 VAL   B O   1 
ATOM   4507 C CB  . VAL   B 2 259 ? 12.79162 -7.89602  -12.25505 1.000 98.52686  ? 352 VAL   B CB  1 
ATOM   4508 C CG1 . VAL   B 2 259 ? 13.26151 -7.23060  -13.53938 1.000 96.38826  ? 352 VAL   B CG1 1 
ATOM   4509 C CG2 . VAL   B 2 259 ? 13.96535 -8.17544  -11.32943 1.000 98.68790  ? 352 VAL   B CG2 1 
ATOM   4510 N N   . ALA   B 2 260 ? 10.28754 -5.59038  -12.86127 1.000 96.95406  ? 353 ALA   B N   1 
ATOM   4511 C CA  . ALA   B 2 260 ? 9.16223  -5.30631  -13.74010 1.000 109.98756 ? 353 ALA   B CA  1 
ATOM   4512 C C   . ALA   B 2 260 ? 9.31454  -6.05524  -15.05944 1.000 110.57431 ? 353 ALA   B C   1 
ATOM   4513 O O   . ALA   B 2 260 ? 10.42442 -6.27165  -15.55329 1.000 104.07333 ? 353 ALA   B O   1 
ATOM   4514 C CB  . ALA   B 2 260 ? 9.04942  -3.80259  -13.99423 1.000 109.07401 ? 353 ALA   B CB  1 
ATOM   4515 N N   . ASP   B 2 261 ? 8.17579  -6.45733  -15.63097 1.000 117.41326 ? 354 ASP   B N   1 
ATOM   4516 C CA  . ASP   B 2 261 ? 8.20403  -7.26006  -16.84989 1.000 118.46647 ? 354 ASP   B CA  1 
ATOM   4517 C C   . ASP   B 2 261 ? 8.74542  -6.47504  -18.03719 1.000 111.56905 ? 354 ASP   B C   1 
ATOM   4518 O O   . ASP   B 2 261 ? 9.30097  -7.06998  -18.96749 1.000 108.82477 ? 354 ASP   B O   1 
ATOM   4519 C CB  . ASP   B 2 261 ? 6.80802  -7.79877  -17.15917 1.000 125.56664 ? 354 ASP   B CB  1 
ATOM   4520 C CG  . ASP   B 2 261 ? 6.39325  -8.90978  -16.21678 1.000 127.99447 ? 354 ASP   B CG  1 
ATOM   4521 O OD1 . ASP   B 2 261 ? 7.28589  -9.61828  -15.70473 1.000 122.41712 ? 354 ASP   B OD1 1 
ATOM   4522 O OD2 . ASP   B 2 261 ? 5.17687  -9.07621  -15.98957 1.000 135.56118 ? 354 ASP   B OD2 1 
ATOM   4523 N N   . GLU   B 2 262 ? 8.60171  -5.14968  -18.02640 1.000 111.72278 ? 355 GLU   B N   1 
ATOM   4524 C CA  . GLU   B 2 262 ? 9.18264  -4.32022  -19.07595 1.000 107.48234 ? 355 GLU   B CA  1 
ATOM   4525 C C   . GLU   B 2 262 ? 10.69892 -4.21419  -18.97275 1.000 102.01119 ? 355 GLU   B C   1 
ATOM   4526 O O   . GLU   B 2 262 ? 11.30881 -3.49430  -19.77127 1.000 104.28638 ? 355 GLU   B O   1 
ATOM   4527 C CB  . GLU   B 2 262 ? 8.54811  -2.92840  -19.04578 1.000 112.53048 ? 355 GLU   B CB  1 
ATOM   4528 C CG  . GLU   B 2 262 ? 8.24781  -2.41877  -17.64714 1.000 115.31491 ? 355 GLU   B CG  1 
ATOM   4529 C CD  . GLU   B 2 262 ? 7.04622  -1.49456  -17.61115 1.000 117.40215 ? 355 GLU   B CD  1 
ATOM   4530 O OE1 . GLU   B 2 262 ? 6.82944  -0.75646  -18.59527 1.000 118.31470 ? 355 GLU   B OE1 1 
ATOM   4531 O OE2 . GLU   B 2 262 ? 6.31065  -1.51598  -16.60180 1.000 122.14806 ? 355 GLU   B OE2 1 
ATOM   4532 N N   . ASP   B 2 263 ? 11.31376 -4.90934  -18.01284 1.000 102.96093 ? 356 ASP   B N   1 
ATOM   4533 C CA  . ASP   B 2 263 ? 12.76277 -4.97120  -17.87884 1.000 88.39407  ? 356 ASP   B CA  1 
ATOM   4534 C C   . ASP   B 2 263 ? 13.24055 -6.39523  -17.61340 1.000 82.23373  ? 356 ASP   B C   1 
ATOM   4535 O O   . ASP   B 2 263 ? 14.41824 -6.59460  -17.29396 1.000 78.27408  ? 356 ASP   B O   1 
ATOM   4536 C CB  . ASP   B 2 263 ? 13.23789 -4.03387  -16.75963 1.000 89.43108  ? 356 ASP   B CB  1 
ATOM   4537 C CG  . ASP   B 2 263 ? 14.72525 -3.74011  -16.83156 1.000 96.88994  ? 356 ASP   B CG  1 
ATOM   4538 O OD1 . ASP   B 2 263 ? 15.15264 -3.05092  -17.78140 1.000 103.77813 ? 356 ASP   B OD1 1 
ATOM   4539 O OD2 . ASP   B 2 263 ? 15.46721 -4.20047  -15.93826 1.000 94.40868  ? 356 ASP   B OD2 1 
ATOM   4540 N N   . ALA   B 2 264 ? 12.36028 -7.39077  -17.75011 1.000 84.82227  ? 357 ALA   B N   1 
ATOM   4541 C CA  . ALA   B 2 264 ? 12.72189 -8.76157  -17.40418 1.000 82.97619  ? 357 ALA   B CA  1 
ATOM   4542 C C   . ALA   B 2 264 ? 13.76719 -9.33650  -18.35138 1.000 82.07622  ? 357 ALA   B C   1 
ATOM   4543 O O   . ALA   B 2 264 ? 14.52261 -10.23464 -17.96263 1.000 80.70066  ? 357 ALA   B O   1 
ATOM   4544 C CB  . ALA   B 2 264 ? 11.47564 -9.64593  -17.39627 1.000 90.29142  ? 357 ALA   B CB  1 
ATOM   4545 N N   . HIS   B 2 265 ? 13.82583 -8.84315  -19.59063 1.000 85.49524  ? 358 HIS   B N   1 
ATOM   4546 C CA  . HIS   B 2 265 ? 14.79505 -9.35809  -20.55101 1.000 80.77237  ? 358 HIS   B CA  1 
ATOM   4547 C C   . HIS   B 2 265 ? 16.21742 -8.91238  -20.23850 1.000 77.50213  ? 358 HIS   B C   1 
ATOM   4548 O O   . HIS   B 2 265 ? 17.16879 -9.57328  -20.66866 1.000 70.72315  ? 358 HIS   B O   1 
ATOM   4549 C CB  . HIS   B 2 265 ? 14.41641 -8.92179  -21.96749 1.000 74.78340  ? 358 HIS   B CB  1 
ATOM   4550 C CG  . HIS   B 2 265 ? 14.45799 -7.43954  -22.17523 1.000 78.06717  ? 358 HIS   B CG  1 
ATOM   4551 N ND1 . HIS   B 2 265 ? 13.53260 -6.58339  -21.61788 1.000 84.24216  ? 358 HIS   B ND1 1 
ATOM   4552 C CD2 . HIS   B 2 265 ? 15.31202 -6.66168  -22.88180 1.000 67.46569  ? 358 HIS   B CD2 1 
ATOM   4553 C CE1 . HIS   B 2 265 ? 13.81606 -5.34206  -21.96983 1.000 76.74051  ? 358 HIS   B CE1 1 
ATOM   4554 N NE2 . HIS   B 2 265 ? 14.89091 -5.36200  -22.73725 1.000 75.37893  ? 358 HIS   B NE2 1 
ATOM   4555 N N   . ASN   B 2 266 ? 16.38510 -7.81526  -19.50219 1.000 78.88703  ? 359 ASN   B N   1 
ATOM   4556 C CA  . ASN   B 2 266 ? 17.70881 -7.29628  -19.18159 1.000 76.38415  ? 359 ASN   B CA  1 
ATOM   4557 C C   . ASN   B 2 266 ? 18.38113 -8.03345  -18.03085 1.000 75.79323  ? 359 ASN   B C   1 
ATOM   4558 O O   . ASN   B 2 266 ? 19.53447 -7.72468  -17.71282 1.000 73.10646  ? 359 ASN   B O   1 
ATOM   4559 C CB  . ASN   B 2 266 ? 17.62094 -5.80342  -18.85234 1.000 70.72965  ? 359 ASN   B CB  1 
ATOM   4560 C CG  . ASN   B 2 266 ? 17.33200 -4.95431  -20.07373 1.000 73.20170  ? 359 ASN   B CG  1 
ATOM   4561 O OD1 . ASN   B 2 266 ? 17.86656 -5.20022  -21.15497 1.000 81.34287  ? 359 ASN   B OD1 1 
ATOM   4562 N ND2 . ASN   B 2 266 ? 16.48099 -3.94904  -19.90807 1.000 70.35100  ? 359 ASN   B ND2 1 
ATOM   4563 N N   . ILE   B 2 267 ? 17.70417 -8.99165  -17.40770 1.000 77.36392  ? 360 ILE   B N   1 
ATOM   4564 C CA  . ILE   B 2 267 ? 18.25502 -9.72271  -16.27282 1.000 76.96828  ? 360 ILE   B CA  1 
ATOM   4565 C C   . ILE   B 2 267 ? 19.07696 -10.89552 -16.78957 1.000 79.46488  ? 360 ILE   B C   1 
ATOM   4566 O O   . ILE   B 2 267 ? 18.62598 -11.64868 -17.66130 1.000 80.36973  ? 360 ILE   B O   1 
ATOM   4567 C CB  . ILE   B 2 267 ? 17.13657 -10.20094 -15.33264 1.000 78.13745  ? 360 ILE   B CB  1 
ATOM   4568 C CG1 . ILE   B 2 267 ? 16.31258 -9.00901  -14.84283 1.000 80.77358  ? 360 ILE   B CG1 1 
ATOM   4569 C CG2 . ILE   B 2 267 ? 17.71830 -10.96486 -14.15571 1.000 86.24591  ? 360 ILE   B CG2 1 
ATOM   4570 C CD1 . ILE   B 2 267 ? 17.13293 -7.95084  -14.14134 1.000 76.80813  ? 360 ILE   B CD1 1 
ATOM   4571 N N   . GLN   B 2 268 ? 20.28575 -11.04878 -16.25389 1.000 75.09897  ? 361 GLN   B N   1 
ATOM   4572 C CA  . GLN   B 2 268 ? 21.15906 -12.13828 -16.66686 1.000 78.30541  ? 361 GLN   B CA  1 
ATOM   4573 C C   . GLN   B 2 268 ? 20.58933 -13.47480 -16.20827 1.000 88.60965  ? 361 GLN   B C   1 
ATOM   4574 O O   . GLN   B 2 268 ? 20.20573 -13.63336 -15.04545 1.000 88.13205  ? 361 GLN   B O   1 
ATOM   4575 C CB  . GLN   B 2 268 ? 22.56253 -11.93575 -16.09773 1.000 71.53775  ? 361 GLN   B CB  1 
ATOM   4576 C CG  . GLN   B 2 268 ? 23.55437 -13.01405 -16.49795 1.000 75.29542  ? 361 GLN   B CG  1 
ATOM   4577 C CD  . GLN   B 2 268 ? 23.81255 -13.04027 -17.99103 1.000 80.57629  ? 361 GLN   B CD  1 
ATOM   4578 O OE1 . GLN   B 2 268 ? 24.01222 -11.99900 -18.61644 1.000 72.68385  ? 361 GLN   B OE1 1 
ATOM   4579 N NE2 . GLN   B 2 268 ? 23.80407 -14.23424 -18.57217 1.000 79.95976  ? 361 GLN   B NE2 1 
ATOM   4580 N N   . THR   B 2 269 ? 20.52950 -14.43273 -17.12626 1.000 82.17082  ? 362 THR   B N   1 
ATOM   4581 C CA  . THR   B 2 269 ? 20.04894 -15.77818 -16.85215 1.000 90.56132  ? 362 THR   B CA  1 
ATOM   4582 C C   . THR   B 2 269 ? 21.22374 -16.75196 -16.84893 1.000 94.23030  ? 362 THR   B C   1 
ATOM   4583 O O   . THR   B 2 269 ? 22.37795 -16.37547 -17.07297 1.000 86.36353  ? 362 THR   B O   1 
ATOM   4584 C CB  . THR   B 2 269 ? 18.99170 -16.19333 -17.87793 1.000 90.16312  ? 362 THR   B CB  1 
ATOM   4585 O OG1 . THR   B 2 269 ? 19.52758 -16.05813 -19.19994 1.000 93.10290  ? 362 THR   B OG1 1 
ATOM   4586 C CG2 . THR   B 2 269 ? 17.74995 -15.32254 -17.74728 1.000 93.92215  ? 362 THR   B CG2 1 
ATOM   4587 N N   . HIS   B 2 270 ? 20.91885 -18.02249 -16.59083 1.000 103.30355 ? 363 HIS   B N   1 
ATOM   4588 C CA  . HIS   B 2 270 ? 21.95133 -19.04975 -16.54642 1.000 106.81833 ? 363 HIS   B CA  1 
ATOM   4589 C C   . HIS   B 2 270 ? 21.32027 -20.41556 -16.76096 1.000 111.42483 ? 363 HIS   B C   1 
ATOM   4590 O O   . HIS   B 2 270 ? 20.34571 -20.76473 -16.08785 1.000 116.37217 ? 363 HIS   B O   1 
ATOM   4591 C CB  . HIS   B 2 270 ? 22.70511 -19.02096 -15.21189 1.000 101.15027 ? 363 HIS   B CB  1 
ATOM   4592 C CG  . HIS   B 2 270 ? 23.58509 -20.21195 -14.99005 1.000 104.80034 ? 363 HIS   B CG  1 
ATOM   4593 N ND1 . HIS   B 2 270 ? 23.17842 -21.31294 -14.26715 1.000 116.13055 ? 363 HIS   B ND1 1 
ATOM   4594 C CD2 . HIS   B 2 270 ? 24.84897 -20.47603 -15.39806 1.000 104.24665 ? 363 HIS   B CD2 1 
ATOM   4595 C CE1 . HIS   B 2 270 ? 24.15432 -22.20277 -14.23733 1.000 117.40487 ? 363 HIS   B CE1 1 
ATOM   4596 N NE2 . HIS   B 2 270 ? 25.17915 -21.71958 -14.91633 1.000 111.63829 ? 363 HIS   B NE2 1 
ATOM   4597 N N   . ARG   B 2 271 ? 21.87609 -21.17431 -17.69693 1.000 111.62663 ? 364 ARG   B N   1 
ATOM   4598 C CA  . ARG   B 2 271 ? 21.56613 -22.58278 -17.88841 1.000 118.15413 ? 364 ARG   B CA  1 
ATOM   4599 C C   . ARG   B 2 271 ? 22.83833 -23.39131 -17.63878 1.000 128.77712 ? 364 ARG   B C   1 
ATOM   4600 O O   . ARG   B 2 271 ? 23.86716 -22.85475 -17.21887 1.000 129.10853 ? 364 ARG   B O   1 
ATOM   4601 C CB  . ARG   B 2 271 ? 21.00726 -22.83384 -19.29086 1.000 131.20871 ? 364 ARG   B CB  1 
ATOM   4602 C CG  . ARG   B 2 271 ? 22.01751 -22.58814 -20.40059 1.000 131.67797 ? 364 ARG   B CG  1 
ATOM   4603 C CD  . ARG   B 2 271 ? 21.79707 -23.51904 -21.58331 1.000 134.67617 ? 364 ARG   B CD  1 
ATOM   4604 N NE  . ARG   B 2 271 ? 20.57871 -23.20871 -22.32119 1.000 127.82229 ? 364 ARG   B NE  1 
ATOM   4605 C CZ  . ARG   B 2 271 ? 20.20956 -23.81464 -23.44150 1.000 127.28291 ? 364 ARG   B CZ  1 
ATOM   4606 N NH1 . ARG   B 2 271 ? 20.94306 -24.77368 -23.98258 1.000 133.79853 ? 364 ARG   B NH1 1 
ATOM   4607 N NH2 . ARG   B 2 271 ? 19.07776 -23.44724 -24.03558 1.000 123.22769 ? 364 ARG   B NH2 1 
ATOM   4608 N N   . ASP   B 2 272 ? 22.76845 -24.69265 -17.90573 1.000 138.89615 ? 365 ASP   B N   1 
ATOM   4609 C CA  . ASP   B 2 272 ? 23.95731 -25.54271 -17.85625 1.000 146.12857 ? 365 ASP   B CA  1 
ATOM   4610 C C   . ASP   B 2 272 ? 24.67091 -25.51112 -19.20951 1.000 149.13725 ? 365 ASP   B C   1 
ATOM   4611 O O   . ASP   B 2 272 ? 24.82264 -26.51752 -19.90066 1.000 152.60446 ? 365 ASP   B O   1 
ATOM   4612 C CB  . ASP   B 2 272 ? 23.58000 -26.96267 -17.45000 1.000 155.95983 ? 365 ASP   B CB  1 
ATOM   4613 C CG  . ASP   B 2 272 ? 24.78430 -27.79281 -17.04632 1.000 163.86191 ? 365 ASP   B CG  1 
ATOM   4614 O OD1 . ASP   B 2 272 ? 25.36607 -27.51583 -15.97588 1.000 166.10576 ? 365 ASP   B OD1 1 
ATOM   4615 O OD2 . ASP   B 2 272 ? 25.14865 -28.72203 -17.79720 1.000 167.79673 ? 365 ASP   B OD2 1 
ATOM   4616 N N   . SER   B 2 273 ? 25.10937 -24.30626 -19.57993 1.000 137.69138 ? 366 SER   B N   1 
ATOM   4617 C CA  . SER   B 2 273 ? 25.69675 -24.06306 -20.89126 1.000 135.18814 ? 366 SER   B CA  1 
ATOM   4618 C C   . SER   B 2 273 ? 27.12118 -24.58526 -21.02250 1.000 134.18394 ? 366 SER   B C   1 
ATOM   4619 O O   . SER   B 2 273 ? 27.68171 -24.52623 -22.12239 1.000 137.22759 ? 366 SER   B O   1 
ATOM   4620 C CB  . SER   B 2 273 ? 25.67291 -22.56511 -21.20675 1.000 128.55869 ? 366 SER   B CB  1 
ATOM   4621 O OG  . SER   B 2 273 ? 26.44430 -21.83506 -20.26953 1.000 132.66949 ? 366 SER   B OG  1 
ATOM   4622 N N   . LEU   B 2 274 ? 27.72178 -25.08514 -19.93992 1.000 130.98492 ? 367 LEU   B N   1 
ATOM   4623 C CA  . LEU   B 2 274 ? 29.06316 -25.64970 -20.04309 1.000 127.13307 ? 367 LEU   B CA  1 
ATOM   4624 C C   . LEU   B 2 274 ? 29.06744 -26.93295 -20.86338 1.000 134.09437 ? 367 LEU   B C   1 
ATOM   4625 O O   . LEU   B 2 274 ? 30.05464 -27.22699 -21.54734 1.000 127.91775 ? 367 LEU   B O   1 
ATOM   4626 C CB  . LEU   B 2 274 ? 29.63733 -25.90132 -18.64915 1.000 122.09019 ? 367 LEU   B CB  1 
ATOM   4627 C CG  . LEU   B 2 274 ? 29.89619 -24.65184 -17.80537 1.000 113.41972 ? 367 LEU   B CG  1 
ATOM   4628 C CD1 . LEU   B 2 274 ? 30.41471 -25.02925 -16.42707 1.000 107.72749 ? 367 LEU   B CD1 1 
ATOM   4629 C CD2 . LEU   B 2 274 ? 30.87189 -23.72385 -18.51354 1.000 102.83397 ? 367 LEU   B CD2 1 
ATOM   4630 N N   . ASP   B 2 275 ? 27.97975 -27.70488 -20.80924 1.000 140.64449 ? 368 ASP   B N   1 
ATOM   4631 C CA  . ASP   B 2 275 ? 27.86806 -28.88644 -21.65756 1.000 144.57742 ? 368 ASP   B CA  1 
ATOM   4632 C C   . ASP   B 2 275 ? 27.71295 -28.49577 -23.12215 1.000 145.06070 ? 368 ASP   B C   1 
ATOM   4633 O O   . ASP   B 2 275 ? 28.26082 -29.15943 -24.01037 1.000 142.65037 ? 368 ASP   B O   1 
ATOM   4634 C CB  . ASP   B 2 275 ? 26.68838 -29.74621 -21.20248 1.000 149.25172 ? 368 ASP   B CB  1 
ATOM   4635 C CG  . ASP   B 2 275 ? 26.57016 -31.04035 -21.98523 1.000 159.50512 ? 368 ASP   B CG  1 
ATOM   4636 O OD1 . ASP   B 2 275 ? 27.58205 -31.48454 -22.56726 1.000 160.66017 ? 368 ASP   B OD1 1 
ATOM   4637 O OD2 . ASP   B 2 275 ? 25.46023 -31.61162 -22.02265 1.000 167.42790 ? 368 ASP   B OD2 1 
ATOM   4638 N N   . LEU   B 2 276 ? 26.97167 -27.41864 -23.39257 1.000 138.73298 ? 369 LEU   B N   1 
ATOM   4639 C CA  . LEU   B 2 276 ? 26.76939 -26.97226 -24.76516 1.000 137.16346 ? 369 LEU   B CA  1 
ATOM   4640 C C   . LEU   B 2 276 ? 28.03429 -26.38168 -25.37408 1.000 131.91044 ? 369 LEU   B C   1 
ATOM   4641 O O   . LEU   B 2 276 ? 28.17061 -26.37325 -26.60222 1.000 126.46794 ? 369 LEU   B O   1 
ATOM   4642 C CB  . LEU   B 2 276 ? 25.63288 -25.94728 -24.82528 1.000 133.02095 ? 369 LEU   B CB  1 
ATOM   4643 C CG  . LEU   B 2 276 ? 24.20661 -26.42872 -24.53079 1.000 136.85698 ? 369 LEU   B CG  1 
ATOM   4644 C CD1 . LEU   B 2 276 ? 23.95926 -27.81221 -25.12066 1.000 139.44109 ? 369 LEU   B CD1 1 
ATOM   4645 C CD2 . LEU   B 2 276 ? 23.89576 -26.40738 -23.04031 1.000 141.69508 ? 369 LEU   B CD2 1 
ATOM   4646 N N   . LEU   B 2 277 ? 28.96122 -25.89279 -24.54720 1.000 128.14096 ? 370 LEU   B N   1 
ATOM   4647 C CA  . LEU   B 2 277 ? 30.19130 -25.31521 -25.07776 1.000 122.33879 ? 370 LEU   B CA  1 
ATOM   4648 C C   . LEU   B 2 277 ? 31.10443 -26.38031 -25.67116 1.000 127.77148 ? 370 LEU   B C   1 
ATOM   4649 O O   . LEU   B 2 277 ? 31.82296 -26.10872 -26.64005 1.000 124.22963 ? 370 LEU   B O   1 
ATOM   4650 C CB  . LEU   B 2 277 ? 30.92250 -24.54018 -23.98090 1.000 110.59815 ? 370 LEU   B CB  1 
ATOM   4651 C CG  . LEU   B 2 277 ? 32.24602 -23.87282 -24.36138 1.000 109.08245 ? 370 LEU   B CG  1 
ATOM   4652 C CD1 . LEU   B 2 277 ? 32.02103 -22.76180 -25.37725 1.000 102.07527 ? 370 LEU   B CD1 1 
ATOM   4653 C CD2 . LEU   B 2 277 ? 32.95573 -23.34433 -23.12475 1.000 102.12193 ? 370 LEU   B CD2 1 
ATOM   4654 N N   . ASP   B 2 278 ? 31.08836 -27.59273 -25.11234 1.000 126.02820 ? 371 ASP   B N   1 
ATOM   4655 C CA  . ASP   B 2 278 ? 31.97005 -28.64578 -25.60446 1.000 129.48963 ? 371 ASP   B CA  1 
ATOM   4656 C C   . ASP   B 2 278 ? 31.51197 -29.18515 -26.95354 1.000 135.63446 ? 371 ASP   B C   1 
ATOM   4657 O O   . ASP   B 2 278 ? 32.34484 -29.60210 -27.76669 1.000 136.89951 ? 371 ASP   B O   1 
ATOM   4658 C CB  . ASP   B 2 278 ? 32.05419 -29.77666 -24.58027 1.000 133.10714 ? 371 ASP   B CB  1 
ATOM   4659 C CG  . ASP   B 2 278 ? 32.41869 -29.27999 -23.19605 1.000 132.44133 ? 371 ASP   B CG  1 
ATOM   4660 O OD1 . ASP   B 2 278 ? 32.95196 -28.15545 -23.08880 1.000 123.77153 ? 371 ASP   B OD1 1 
ATOM   4661 O OD2 . ASP   B 2 278 ? 32.17475 -30.01466 -22.21603 1.000 131.39875 ? 371 ASP   B OD2 1 
ATOM   4662 N N   . LYS   B 2 279 ? 30.20173 -29.18704 -27.21024 1.000 137.15813 ? 372 LYS   B N   1 
ATOM   4663 C CA  . LYS   B 2 279 ? 29.69060 -29.68074 -28.48361 1.000 133.87452 ? 372 LYS   B CA  1 
ATOM   4664 C C   . LYS   B 2 279 ? 30.06827 -28.77659 -29.64900 1.000 133.20459 ? 372 LYS   B C   1 
ATOM   4665 O O   . LYS   B 2 279 ? 30.04953 -29.22820 -30.79904 1.000 139.70462 ? 372 LYS   B O   1 
ATOM   4666 C CB  . LYS   B 2 279 ? 28.17052 -29.83447 -28.41352 1.000 126.00354 ? 372 LYS   B CB  1 
ATOM   4667 C CG  . LYS   B 2 279 ? 27.69860 -30.77648 -27.31915 1.000 129.92948 ? 372 LYS   B CG  1 
ATOM   4668 C CD  . LYS   B 2 279 ? 26.19766 -30.67530 -27.10786 1.000 126.73458 ? 372 LYS   B CD  1 
ATOM   4669 C CE  . LYS   B 2 279 ? 25.75070 -31.52974 -25.93287 1.000 141.41681 ? 372 LYS   B CE  1 
ATOM   4670 N NZ  . LYS   B 2 279 ? 24.31160 -31.32522 -25.61036 1.000 141.88636 ? 372 LYS   B NZ  1 
ATOM   4671 N N   . ALA   B 2 280 ? 30.41179 -27.51911 -29.38018 1.000 136.74323 ? 373 ALA   B N   1 
ATOM   4672 C CA  . ALA   B 2 280 ? 30.80794 -26.57728 -30.41801 1.000 138.87055 ? 373 ALA   B CA  1 
ATOM   4673 C C   . ALA   B 2 280 ? 32.28734 -26.66806 -30.77046 1.000 146.04762 ? 373 ALA   B C   1 
ATOM   4674 O O   . ALA   B 2 280 ? 32.77403 -25.84296 -31.55106 1.000 144.77533 ? 373 ALA   B O   1 
ATOM   4675 C CB  . ALA   B 2 280 ? 30.46501 -25.14859 -29.98836 1.000 126.76259 ? 373 ALA   B CB  1 
ATOM   4676 N N   . ARG   B 2 281 ? 33.00941 -27.64473 -30.21869 1.000 147.85323 ? 374 ARG   B N   1 
ATOM   4677 C CA  . ARG   B 2 281 ? 34.43435 -27.76904 -30.50371 1.000 143.35894 ? 374 ARG   B CA  1 
ATOM   4678 C C   . ARG   B 2 281 ? 34.68229 -28.46318 -31.83830 1.000 151.81634 ? 374 ARG   B C   1 
ATOM   4679 O O   . ARG   B 2 281 ? 35.61616 -28.10287 -32.56383 1.000 157.27344 ? 374 ARG   B O   1 
ATOM   4680 C CB  . ARG   B 2 281 ? 35.12845 -28.52032 -29.36675 1.000 150.67114 ? 374 ARG   B CB  1 
ATOM   4681 C CG  . ARG   B 2 281 ? 36.62201 -28.71627 -29.56475 1.000 160.16534 ? 374 ARG   B CG  1 
ATOM   4682 C CD  . ARG   B 2 281 ? 37.27770 -29.26428 -28.30745 1.000 161.18220 ? 374 ARG   B CD  1 
ATOM   4683 N NE  . ARG   B 2 281 ? 38.67790 -29.60860 -28.52458 1.000 167.71150 ? 374 ARG   B NE  1 
ATOM   4684 C CZ  . ARG   B 2 281 ? 39.68497 -28.75015 -28.43845 1.000 170.67638 ? 374 ARG   B CZ  1 
ATOM   4685 N NH1 . ARG   B 2 281 ? 39.48394 -27.47491 -28.14861 1.000 169.73717 ? 374 ARG   B NH1 1 
ATOM   4686 N NH2 . ARG   B 2 281 ? 40.92507 -29.18178 -28.65081 1.000 172.09974 ? 374 ARG   B NH2 1 
ATOM   4687 N N   . ALA   B 2 282 ? 33.86019 -29.44981 -32.18012 1.000 147.33315 ? 375 ALA   B N   1 
ATOM   4688 C CA  . ALA   B 2 282 ? 34.01085 -30.16860 -33.43988 1.000 140.95681 ? 375 ALA   B CA  1 
ATOM   4689 C C   . ALA   B 2 282 ? 33.52452 -29.32335 -34.61257 1.000 140.42147 ? 375 ALA   B C   1 
ATOM   4690 O O   . ALA   B 2 282 ? 32.32483 -29.24072 -34.87525 1.000 134.02728 ? 375 ALA   B O   1 
ATOM   4691 C CB  . ALA   B 2 282 ? 33.25951 -31.48939 -33.39027 1.000 140.08876 ? 375 ALA   B CB  1 
HETATM 4692 C C11 . A1CAG C 3 .   ? 37.36787 20.27847  -8.64705  1.000 56.90165  ? 301 A1CAG A C11 1 
HETATM 4693 C C12 . A1CAG C 3 .   ? 36.25095 19.81354  -9.54178  1.000 58.65850  ? 301 A1CAG A C12 1 
HETATM 4694 C C13 . A1CAG C 3 .   ? 37.48493 21.83215  -8.61985  1.000 61.68397  ? 301 A1CAG A C13 1 
HETATM 4695 C C14 . A1CAG C 3 .   ? 36.77823 22.82975  -7.89447  1.000 53.28771  ? 301 A1CAG A C14 1 
HETATM 4696 C C15 . A1CAG C 3 .   ? 37.28393 24.14352  -8.22228  1.000 57.96457  ? 301 A1CAG A C15 1 
HETATM 4697 C C17 . A1CAG C 3 .   ? 35.80276 25.69659  -6.70529  1.000 62.19409  ? 301 A1CAG A C17 1 
HETATM 4698 C C18 . A1CAG C 3 .   ? 35.38431 27.18776  -6.18645  1.000 63.39926  ? 301 A1CAG A C18 1 
HETATM 4699 C C19 . A1CAG C 3 .   ? 35.32640 27.39858  -4.60243  1.000 67.81184  ? 301 A1CAG A C19 1 
HETATM 4700 C C20 . A1CAG C 3 .   ? 36.64641 27.78397  -3.85884  1.000 74.11632  ? 301 A1CAG A C20 1 
HETATM 4701 C C21 . A1CAG C 3 .   ? 37.88813 27.89423  -4.54512  1.000 78.45130  ? 301 A1CAG A C21 1 
HETATM 4702 C C23 . A1CAG C 3 .   ? 39.11267 28.47213  -2.63006  1.000 75.98489  ? 301 A1CAG A C23 1 
HETATM 4703 C C24 . A1CAG C 3 .   ? 37.95313 28.39547  -1.84021  1.000 75.77516  ? 301 A1CAG A C24 1 
HETATM 4704 C C25 . A1CAG C 3 .   ? 36.74054 28.05268  -2.46857  1.000 68.97536  ? 301 A1CAG A C25 1 
HETATM 4705 C C01 . A1CAG C 3 .   ? 33.43096 21.56418  -5.06551  1.000 59.01058  ? 301 A1CAG A C01 1 
HETATM 4706 C C02 . A1CAG C 3 .   ? 32.39366 21.25790  -6.17574  1.000 69.67511  ? 301 A1CAG A C02 1 
HETATM 4707 C C03 . A1CAG C 3 .   ? 32.26647 22.31312  -7.27373  1.000 54.36841  ? 301 A1CAG A C03 1 
HETATM 4708 C C04 . A1CAG C 3 .   ? 31.21145 22.26397  -6.21737  1.000 73.22076  ? 301 A1CAG A C04 1 
HETATM 4709 C C06 . A1CAG C 3 .   ? 32.99656 19.13643  -7.45347  1.000 59.34608  ? 301 A1CAG A C06 1 
HETATM 4710 C C08 . A1CAG C 3 .   ? 35.14088 19.02110  -8.68567  1.000 56.76437  ? 301 A1CAG A C08 1 
HETATM 4711 C C09 . A1CAG C 3 .   ? 35.92834 18.49183  -7.53422  1.000 60.37067  ? 301 A1CAG A C09 1 
HETATM 4712 C C10 . A1CAG C 3 .   ? 37.05260 19.53676  -7.29530  1.000 59.39525  ? 301 A1CAG A C10 1 
HETATM 4713 N N05 . A1CAG C 3 .   ? 32.09336 19.84366  -6.56016  1.000 64.81937  ? 301 A1CAG A N05 1 
HETATM 4714 N N16 . A1CAG C 3 .   ? 36.85519 25.47452  -7.71417  1.000 61.74572  ? 301 A1CAG A N16 1 
HETATM 4715 N N22 . A1CAG C 3 .   ? 39.07782 28.22320  -3.96886  1.000 79.53878  ? 301 A1CAG A N22 1 
HETATM 4716 N N27 . A1CAG C 3 .   ? 38.31466 23.92739  -9.15094  1.000 63.37233  ? 301 A1CAG A N27 1 
HETATM 4717 N N28 . A1CAG C 3 .   ? 38.40042 22.55976  -9.35494  1.000 57.14023  ? 301 A1CAG A N28 1 
HETATM 4718 O O07 . A1CAG C 3 .   ? 34.09865 19.86003  -8.08500  1.000 61.85340  ? 301 A1CAG A O07 1 
HETATM 4719 O O26 . A1CAG C 3 .   ? 35.22558 24.76593  -6.24262  1.000 64.67339  ? 301 A1CAG A O26 1 
HETATM 4720 O O29 . A1CAG C 3 .   ? 32.88802 17.97565  -7.71698  1.000 66.31272  ? 301 A1CAG A O29 1 
HETATM 4721 O O   . HOH   D 4 .   ? 29.31326 6.64009   -26.63957 1.000 74.56419  ? 401 HOH   A O   1 
HETATM 4722 O O   . HOH   D 4 .   ? 18.39163 16.62972  -25.70609 1.000 53.69722  ? 402 HOH   A O   1 
HETATM 4723 O O   . HOH   D 4 .   ? 26.59107 18.32752  -6.90942  1.000 65.42951  ? 403 HOH   A O   1 
HETATM 4724 O O   . HOH   D 4 .   ? 21.25457 17.64453  -25.97592 1.000 55.05107  ? 404 HOH   A O   1 
HETATM 4725 O O   . HOH   D 4 .   ? 38.81587 21.84713  -19.00892 1.000 66.58657  ? 405 HOH   A O   1 
HETATM 4726 O O   . HOH   D 4 .   ? 28.47743 8.25285   -28.58109 1.000 61.96607  ? 406 HOH   A O   1 
HETATM 4727 O O   . HOH   D 4 .   ? 21.18228 28.03879  -6.69292  1.000 68.37313  ? 407 HOH   A O   1 
HETATM 4728 O O   . HOH   D 4 .   ? 11.07331 14.13289  -8.22738  1.000 64.74866  ? 408 HOH   A O   1 
HETATM 4729 O O   . HOH   D 4 .   ? 34.36056 17.83852  -14.47758 1.000 56.65241  ? 409 HOH   A O   1 
HETATM 4730 O O   . HOH   D 4 .   ? 16.81395 29.24540  -11.72755 1.000 59.20561  ? 410 HOH   A O   1 
HETATM 4731 O O   . HOH   D 4 .   ? 15.93778 6.59618   -18.05679 1.000 79.02642  ? 411 HOH   A O   1 
HETATM 4732 O O   . HOH   D 4 .   ? 16.33371 18.65922  -14.66922 1.000 51.92357  ? 412 HOH   A O   1 
HETATM 4733 O O   . HOH   D 4 .   ? 26.69684 14.97493  -11.98738 1.000 49.34513  ? 413 HOH   A O   1 
HETATM 4734 O O   . HOH   D 4 .   ? 30.46302 25.62761  -5.76272  1.000 53.74929  ? 414 HOH   A O   1 
HETATM 4735 O O   . HOH   D 4 .   ? 15.19834 13.09014  -21.89479 1.000 58.30100  ? 415 HOH   A O   1 
HETATM 4736 O O   . HOH   D 4 .   ? 25.97316 8.55328   -10.78637 1.000 63.78215  ? 416 HOH   A O   1 
HETATM 4737 O O   . HOH   D 4 .   ? 14.99662 27.50475  -10.79724 1.000 56.43588  ? 417 HOH   A O   1 
HETATM 4738 O O   . HOH   D 4 .   ? 20.86790 18.39725  -14.81398 1.000 52.65327  ? 418 HOH   A O   1 
HETATM 4739 O O   . HOH   D 4 .   ? 34.19488 17.20095  -11.56288 1.000 56.95216  ? 419 HOH   A O   1 
HETATM 4740 O O   . HOH   D 4 .   ? 45.55123 4.84139   -10.12355 1.000 78.24309  ? 420 HOH   A O   1 
HETATM 4741 O O   . HOH   D 4 .   ? 12.86151 23.41447  -12.25963 1.000 54.14758  ? 421 HOH   A O   1 
HETATM 4742 O O   . HOH   D 4 .   ? 14.59928 28.83468  -33.06922 1.000 76.72242  ? 422 HOH   A O   1 
HETATM 4743 O O   . HOH   D 4 .   ? 13.59929 13.73754  -20.10507 1.000 54.98775  ? 423 HOH   A O   1 
HETATM 4744 O O   . HOH   D 4 .   ? 42.25934 31.48625  -15.11215 1.000 72.79778  ? 424 HOH   A O   1 
HETATM 4745 O O   . HOH   D 4 .   ? 16.59667 18.36796  -24.81393 1.000 53.79072  ? 425 HOH   A O   1 
HETATM 4746 O O   . HOH   D 4 .   ? 14.34382 33.45585  -32.56233 1.000 76.30758  ? 426 HOH   A O   1 
HETATM 4747 O O   . HOH   D 4 .   ? 16.28828 19.99339  -30.79401 1.000 62.11790  ? 427 HOH   A O   1 
HETATM 4748 O O   . HOH   D 4 .   ? 11.68620 11.94637  -19.92481 1.000 56.51380  ? 428 HOH   A O   1 
HETATM 4749 O O   . HOH   D 4 .   ? 6.51881  14.14236  -6.98906  1.000 84.00953  ? 429 HOH   A O   1 
HETATM 4750 O O   . HOH   D 4 .   ? 25.68847 2.24537   -4.76046  1.000 70.85820  ? 430 HOH   A O   1 
HETATM 4751 O O   . HOH   D 4 .   ? 43.86268 30.16242  -16.22257 1.000 82.64402  ? 431 HOH   A O   1 
HETATM 4752 O O   . HOH   D 4 .   ? 5.76753  23.98218  -23.60113 1.000 69.26688  ? 432 HOH   A O   1 
HETATM 4753 O O   . HOH   D 4 .   ? 4.45289  15.12844  -6.80385  1.000 77.17261  ? 433 HOH   A O   1 
HETATM 4754 O O   . HOH   D 4 .   ? 14.52952 21.60182  -31.58186 1.000 75.49387  ? 434 HOH   A O   1 
HETATM 4755 O O   . HOH   E 4 .   ? 23.15547 17.94013  -27.98252 1.000 60.74747  ? 401 HOH   B O   1 
HETATM 4756 O O   . HOH   E 4 .   ? 30.41547 16.98264  -29.56114 1.000 71.96269  ? 402 HOH   B O   1 
HETATM 4757 O O   . HOH   E 4 .   ? 16.10153 -12.16101 -18.89259 1.000 79.48887  ? 403 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET   A 4   ? 1.31256 2.05045 1.76742 0.20980  -0.29431 -0.36553 1   MET   A N   
2    C CA  . MET   A 4   ? 1.33917 2.06418 1.78043 0.18074  -0.28093 -0.34335 1   MET   A CA  
3    C C   . MET   A 4   ? 1.52922 2.27890 1.99410 0.16258  -0.27871 -0.35181 1   MET   A C   
4    O O   . MET   A 4   ? 1.48713 2.20468 1.92473 0.15285  -0.28626 -0.33860 1   MET   A O   
5    C CB  . MET   A 4   ? 1.29907 1.93408 1.66615 0.18923  -0.29497 -0.31588 1   MET   A CB  
6    C CG  . MET   A 4   ? 1.21181 1.80467 1.54347 0.16366  -0.26366 -0.28242 1   MET   A CG  
7    S SD  . MET   A 4   ? 1.17458 1.76707 1.50697 0.12342  -0.23569 -0.26425 1   MET   A SD  
8    C CE  . MET   A 4   ? 1.06452 1.73302 1.45921 0.09861  -0.20146 -0.27501 1   MET   A CE  
9    N N   . GLU   A 5   ? 1.67079 2.47427 2.18293 0.15725  -0.26738 -0.37387 2   GLU   A N   
10   C CA  . GLU   A 5   ? 1.62031 2.45150 2.15907 0.14003  -0.26521 -0.38495 2   GLU   A CA  
11   C C   . GLU   A 5   ? 1.52010 2.39101 2.09026 0.09993  -0.22646 -0.37995 2   GLU   A C   
12   O O   . GLU   A 5   ? 1.44052 2.30992 2.00516 0.08517  -0.20283 -0.36441 2   GLU   A O   
13   C CB  . GLU   A 5   ? 1.61438 2.47458 2.18057 0.16279  -0.28290 -0.41471 2   GLU   A CB  
14   C CG  . GLU   A 5   ? 1.66036 2.57112 2.26507 0.16375  -0.26361 -0.43296 2   GLU   A CG  
15   C CD  . GLU   A 5   ? 1.77219 2.68630 2.38140 0.20243  -0.29012 -0.45765 2   GLU   A CD  
16   O OE1 . GLU   A 5   ? 1.84573 2.70784 2.41525 0.23153  -0.32136 -0.45299 2   GLU   A OE1 
17   O OE2 . GLU   A 5   ? 1.66405 2.63013 2.31356 0.20341  -0.27987 -0.48198 2   GLU   A OE2 
18   N N   . ASN   A 6   ? 1.36122 2.26352 1.96090 0.08152  -0.22045 -0.39245 3   ASN   A N   
19   C CA  . ASN   A 6   ? 1.22416 2.15973 1.85058 0.04252  -0.18544 -0.38958 3   ASN   A CA  
20   C C   . ASN   A 6   ? 1.08099 1.98563 1.68198 0.01563  -0.16892 -0.36241 3   ASN   A C   
21   O O   . ASN   A 6   ? 1.03665 1.95649 1.65044 -0.01802 -0.14054 -0.35612 3   ASN   A O   
22   C CB  . ASN   A 6   ? 1.22212 2.19447 1.87207 0.03847  -0.16081 -0.39776 3   ASN   A CB  
23   C CG  . ASN   A 6   ? 1.15890 2.17473 1.84297 0.00554  -0.13303 -0.40730 3   ASN   A CG  
24   O OD1 . ASN   A 6   ? 1.10197 2.16052 1.81699 0.01011  -0.12829 -0.42999 3   ASN   A OD1 
25   N ND2 . ASN   A 6   ? 1.11854 2.12180 1.79504 -0.02805 -0.11500 -0.39064 3   ASN   A ND2 
26   N N   . PHE   A 7   ? 0.95465 1.81355 1.51691 0.02981  -0.18664 -0.34659 4   PHE   A N   
27   C CA  . PHE   A 7   ? 0.81423 1.63647 1.34607 0.00764  -0.17263 -0.32077 4   PHE   A CA  
28   C C   . PHE   A 7   ? 0.83459 1.61620 1.33696 0.00899  -0.19240 -0.31549 4   PHE   A C   
29   O O   . PHE   A 7   ? 0.86134 1.61597 1.33988 0.03720  -0.22300 -0.31984 4   PHE   A O   
30   C CB  . PHE   A 7   ? 0.89012 1.65990 1.37590 0.01981  -0.16620 -0.29576 4   PHE   A CB  
31   C CG  . PHE   A 7   ? 0.86199 1.65392 1.36207 0.00474  -0.13565 -0.28933 4   PHE   A CG  
32   C CD1 . PHE   A 7   ? 0.77734 1.61812 1.31632 -0.02481 -0.11066 -0.29778 4   PHE   A CD1 
33   C CD2 . PHE   A 7   ? 0.70309 1.46411 1.17442 0.01872  -0.13199 -0.27469 4   PHE   A CD2 
34   C CE1 . PHE   A 7   ? 0.75302 1.61011 1.29918 -0.03906 -0.08271 -0.29131 4   PHE   A CE1 
35   C CE2 . PHE   A 7   ? 0.61939 1.39884 1.10080 0.00557  -0.10522 -0.26916 4   PHE   A CE2 
36   C CZ  . PHE   A 7   ? 0.78642 1.61324 1.30384 -0.02288 -0.08056 -0.27720 4   PHE   A CZ  
37   N N   . GLN   A 8   ? 0.73512 1.50929 1.23581 -0.02125 -0.17544 -0.30638 5   GLN   A N   
38   C CA  . GLN   A 8   ? 0.75125 1.48970 1.22573 -0.02386 -0.19080 -0.30259 5   GLN   A CA  
39   C C   . GLN   A 8   ? 0.76014 1.43608 1.18475 -0.03926 -0.17143 -0.27056 5   GLN   A C   
40   O O   . GLN   A 8   ? 0.71320 1.39335 1.14478 -0.06585 -0.14319 -0.25959 5   GLN   A O   
41   C CB  . GLN   A 8   ? 0.73106 1.51824 1.25076 -0.04547 -0.19103 -0.32467 5   GLN   A CB  
42   C CG  . GLN   A 8   ? 0.82162 1.57423 1.31604 -0.04920 -0.20743 -0.32327 5   GLN   A CG  
43   C CD  . GLN   A 8   ? 0.96393 1.76682 1.50564 -0.06967 -0.21022 -0.34779 5   GLN   A CD  
44   O OE1 . GLN   A 8   ? 1.03853 1.81992 1.56601 -0.07913 -0.21994 -0.34872 5   GLN   A OE1 
45   N NE2 . GLN   A 8   ? 0.96918 1.81715 1.55108 -0.07497 -0.19530 -0.35999 5   GLN   A NE2 
46   N N   . LYS   A 9   ? 0.77654 1.39439 1.14989 -0.02241 -0.18674 -0.25640 6   LYS   A N   
47   C CA  . LYS   A 9   ? 0.79615 1.35773 1.12376 -0.03466 -0.16972 -0.22873 6   LYS   A CA  
48   C C   . LYS   A 9   ? 0.70181 1.26111 1.03400 -0.06022 -0.16028 -0.22877 6   LYS   A C   
49   O O   . LYS   A 9   ? 0.71261 1.28376 1.05565 -0.05986 -0.17853 -0.24551 6   LYS   A O   
50   C CB  . LYS   A 9   ? 0.83371 1.33751 1.10632 -0.01276 -0.18825 -0.21685 6   LYS   A CB  
51   C CG  . LYS   A 9   ? 0.77779 1.26907 1.03487 0.00944  -0.19464 -0.21140 6   LYS   A CG  
52   C CD  . LYS   A 9   ? 0.89554 1.32635 1.09427 0.02808  -0.21348 -0.20031 6   LYS   A CD  
53   C CE  . LYS   A 9   ? 0.99555 1.40824 1.17541 0.04801  -0.21983 -0.19420 6   LYS   A CE  
54   N NZ  . LYS   A 9   ? 1.10046 1.45097 1.21953 0.06436  -0.23893 -0.18390 6   LYS   A NZ  
55   N N   . VAL   A 10  ? 0.65478 1.19690 0.97747 -0.08168 -0.13324 -0.21066 7   VAL   A N   
56   C CA  . VAL   A 10  ? 0.77532 1.31137 1.10084 -0.10736 -0.12196 -0.20950 7   VAL   A CA  
57   C C   . VAL   A 10  ? 0.68402 1.15944 0.95986 -0.10835 -0.11693 -0.18899 7   VAL   A C   
58   O O   . VAL   A 10  ? 0.82789 1.28530 1.09192 -0.11585 -0.12335 -0.19264 7   VAL   A O   
59   C CB  . VAL   A 10  ? 0.73452 1.30014 1.09005 -0.13350 -0.09532 -0.20786 7   VAL   A CB  
60   C CG1 . VAL   A 10  ? 0.71249 1.25980 1.06220 -0.16053 -0.08357 -0.20365 7   VAL   A CG1 
61   C CG2 . VAL   A 10  ? 0.75485 1.38695 1.16329 -0.13553 -0.09864 -0.23207 7   VAL   A CG2 
62   N N   . GLU   A 11  ? 0.70362 1.14889 0.95113 -0.10076 -0.10562 -0.16896 8   GLU   A N   
63   C CA  . GLU   A 11  ? 0.73799 1.13197 0.94287 -0.10204 -0.09804 -0.15095 8   GLU   A CA  
64   C C   . GLU   A 11  ? 0.73000 1.09972 0.90775 -0.08697 -0.09370 -0.13474 8   GLU   A C   
65   O O   . GLU   A 11  ? 0.72642 1.11503 0.91983 -0.08529 -0.08503 -0.13111 8   GLU   A O   
66   C CB  . GLU   A 11  ? 0.73864 1.12448 0.94713 -0.12558 -0.07631 -0.14221 8   GLU   A CB  
67   C CG  . GLU   A 11  ? 0.89786 1.23481 1.06662 -0.12538 -0.06824 -0.12618 8   GLU   A CG  
68   C CD  . GLU   A 11  ? 0.91621 1.24224 1.08701 -0.14495 -0.04856 -0.11710 8   GLU   A CD  
69   O OE1 . GLU   A 11  ? 0.95329 1.30661 1.15270 -0.16119 -0.04037 -0.12204 8   GLU   A OE1 
70   O OE2 . GLU   A 11  ? 1.06875 1.35817 1.21124 -0.14398 -0.04138 -0.10567 8   GLU   A OE2 
71   N N   . LYS   A 12  ? 0.65837 0.98640 0.79467 -0.07736 -0.09918 -0.12584 9   LYS   A N   
72   C CA  . LYS   A 12  ? 0.70288 1.00433 0.81058 -0.06726 -0.09286 -0.10983 9   LYS   A CA  
73   C C   . LYS   A 12  ? 0.68765 0.97909 0.79359 -0.07999 -0.06852 -0.09439 9   LYS   A C   
74   O O   . LYS   A 12  ? 0.77579 1.05105 0.87312 -0.09038 -0.06021 -0.09123 9   LYS   A O   
75   C CB  . LYS   A 12  ? 0.73236 0.99285 0.79441 -0.05600 -0.10455 -0.10610 9   LYS   A CB  
76   C CG  . LYS   A 12  ? 0.82455 1.05760 0.85549 -0.04703 -0.09965 -0.09133 9   LYS   A CG  
77   C CD  . LYS   A 12  ? 0.95828 1.14832 0.94250 -0.04615 -0.09809 -0.08339 9   LYS   A CD  
78   C CE  . LYS   A 12  ? 0.87886 1.04105 0.82985 -0.03935 -0.09462 -0.07042 9   LYS   A CE  
79   N NZ  . LYS   A 12  ? 0.92325 1.06456 0.84501 -0.02417 -0.11796 -0.07499 9   LYS   A NZ  
80   N N   . ILE   A 13  ? 0.65192 0.95174 0.76513 -0.07782 -0.05874 -0.08580 10  ILE   A N   
81   C CA  . ILE   A 13  ? 0.70398 0.99505 0.81559 -0.08752 -0.03822 -0.07178 10  ILE   A CA  
82   C C   . ILE   A 13  ? 0.70649 0.96284 0.78374 -0.08167 -0.03304 -0.05905 10  ILE   A C   
83   O O   . ILE   A 13  ? 0.87963 1.12067 0.94859 -0.08857 -0.02054 -0.05157 10  ILE   A O   
84   C CB  . ILE   A 13  ? 0.65549 0.97237 0.79022 -0.08871 -0.03018 -0.06946 10  ILE   A CB  
85   C CG1 . ILE   A 13  ? 0.67556 1.02972 0.84567 -0.09930 -0.02997 -0.08263 10  ILE   A CG1 
86   C CG2 . ILE   A 13  ? 0.65383 0.95755 0.78172 -0.09535 -0.01222 -0.05435 10  ILE   A CG2 
87   C CD1 . ILE   A 13  ? 0.57119 0.95307 0.76309 -0.10128 -0.02087 -0.08240 10  ILE   A CD1 
88   N N   A GLY   A 14  ? 0.77860 1.02186 0.83514 -0.06928 -0.04244 -0.05721 11  GLY   A N   
89   N N   B GLY   A 14  ? 0.80886 1.05178 0.86505 -0.06929 -0.04268 -0.05741 11  GLY   A N   
90   C CA  A GLY   A 14  ? 0.83688 1.04997 0.86132 -0.06662 -0.03553 -0.04577 11  GLY   A CA  
91   C CA  B GLY   A 14  ? 0.83593 1.04690 0.85790 -0.06650 -0.03704 -0.04694 11  GLY   A CA  
92   C C   A GLY   A 14  ? 0.85448 1.05385 0.85748 -0.05502 -0.04675 -0.04386 11  GLY   A C   
93   C C   B GLY   A 14  ? 0.88077 1.07884 0.88265 -0.05568 -0.04570 -0.04335 11  GLY   A C   
94   O O   A GLY   A 14  ? 0.80459 1.01635 0.81690 -0.04607 -0.06213 -0.05235 11  GLY   A O   
95   O O   B GLY   A 14  ? 0.82313 1.03742 0.83966 -0.04853 -0.05500 -0.04795 11  GLY   A O   
96   N N   A GLU   A 15  ? 0.92481 1.09788 0.89853 -0.05549 -0.03890 -0.03342 12  GLU   A N   
97   N N   B GLU   A 15  ? 0.93059 1.09765 0.89678 -0.05505 -0.04207 -0.03565 12  GLU   A N   
98   C CA  A GLU   A 15  ? 0.94582 1.09560 0.88987 -0.04732 -0.04836 -0.02959 12  GLU   A CA  
99   C CA  B GLU   A 15  ? 0.94839 1.09416 0.88768 -0.04832 -0.04766 -0.02961 12  GLU   A CA  
100  C C   A GLU   A 15  ? 0.97557 1.11746 0.91267 -0.05253 -0.03320 -0.01743 12  GLU   A C   
101  C C   B GLU   A 15  ? 0.97885 1.11249 0.90577 -0.05628 -0.02885 -0.01750 12  GLU   A C   
102  O O   A GLU   A 15  ? 0.95839 1.09850 0.89464 -0.06123 -0.01667 -0.01184 12  GLU   A O   
103  O O   B GLU   A 15  ? 0.97732 1.09997 0.89072 -0.06279 -0.01767 -0.01521 12  GLU   A O   
104  C CB  A GLU   A 15  ? 0.93954 1.05540 0.84115 -0.04443 -0.05774 -0.03095 12  GLU   A CB  
105  C CB  B GLU   A 15  ? 0.94336 1.05764 0.84248 -0.04085 -0.06450 -0.03328 12  GLU   A CB  
106  C CG  A GLU   A 15  ? 0.97475 1.05715 0.83660 -0.03767 -0.06792 -0.02559 12  GLU   A CG  
107  C CG  B GLU   A 15  ? 0.97692 1.06428 0.84519 -0.03308 -0.07456 -0.02790 12  GLU   A CG  
108  C CD  A GLU   A 15  ? 1.03645 1.08201 0.85128 -0.03473 -0.07906 -0.02725 12  GLU   A CD  
109  C CD  B GLU   A 15  ? 1.06527 1.10830 0.87913 -0.03089 -0.08370 -0.02568 12  GLU   A CD  
110  O OE1 A GLU   A 15  ? 0.99339 1.04147 0.80811 -0.03790 -0.07773 -0.03297 12  GLU   A OE1 
111  O OE1 B GLU   A 15  ? 1.03016 1.06664 0.83228 -0.03456 -0.08206 -0.02934 12  GLU   A OE1 
112  O OE2 A GLU   A 15  ? 1.08329 1.09400 0.85793 -0.02944 -0.08975 -0.02281 12  GLU   A OE2 
113  O OE2 B GLU   A 15  ? 1.08248 1.09423 0.86220 -0.02600 -0.09258 -0.02025 12  GLU   A OE2 
114  N N   A GLY   A 16  ? 0.95657 1.09458 0.88986 -0.04648 -0.03990 -0.01486 13  GLY   A N   
115  N N   B GLY   A 16  ? 0.95312 1.09042 0.88580 -0.05549 -0.02566 -0.01141 13  GLY   A N   
116  C CA  A GLY   A 16  ? 0.98291 1.11016 0.90607 -0.05154 -0.02886 -0.00448 13  GLY   A CA  
117  C CA  B GLY   A 16  ? 0.94233 1.07142 0.86620 -0.06352 -0.00922 -0.00152 13  GLY   A CA  
118  C C   A GLY   A 16  ? 1.00319 1.09096 0.88144 -0.04922 -0.03728 0.00024  13  GLY   A C   
119  C C   B GLY   A 16  ? 0.94350 1.06271 0.85767 -0.06110 -0.01303 0.00394  13  GLY   A C   
120  O O   A GLY   A 16  ? 1.00502 1.06837 0.85305 -0.04449 -0.04970 -0.00294 13  GLY   A O   
121  O O   B GLY   A 16  ? 0.99298 1.09522 0.88835 -0.05252 -0.02949 0.00153  13  GLY   A O   
122  N N   A THR   A 17  ? 1.00919 1.08751 0.87994 -0.05334 -0.03117 0.00800  14  THR   A N   
123  N N   B THR   A 17  ? 0.93455 1.06323 0.86125 -0.06788 0.00085  0.01050  14  THR   A N   
124  C CA  A THR   A 17  ? 0.96823 1.00384 0.79250 -0.05416 -0.03803 0.01384  14  THR   A CA  
125  C CA  B THR   A 17  ? 0.93554 1.05464 0.85416 -0.06720 -0.00201 0.01543  14  THR   A CA  
126  C C   A THR   A 17  ? 1.00210 1.02087 0.81187 -0.03754 -0.06368 0.00777  14  THR   A C   
127  C C   B THR   A 17  ? 0.93493 1.06811 0.87193 -0.05587 -0.01591 0.00987  14  THR   A C   
128  O O   A THR   A 17  ? 0.98091 0.96714 0.75298 -0.03197 -0.07795 0.00627  14  THR   A O   
129  O O   B THR   A 17  ? 0.96212 1.07799 0.88274 -0.04987 -0.02677 0.01047  14  THR   A O   
130  C CB  A THR   A 17  ? 1.00348 1.03497 0.82663 -0.06436 -0.02539 0.02248  14  THR   A CB  
131  C CB  B THR   A 17  ? 0.88847 1.02053 0.82251 -0.07651 0.01456  0.02147  14  THR   A CB  
132  O OG1 A THR   A 17  ? 1.00628 1.05067 0.83835 -0.07862 -0.00331 0.02644  14  THR   A OG1 
133  O OG1 B THR   A 17  ? 0.89695 1.06012 0.86758 -0.07516 0.01994  0.01919  14  THR   A OG1 
134  C CG2 A THR   A 17  ? 1.03402 1.01721 0.80709 -0.06650 -0.03405 0.02855  14  THR   A CG2 
135  C CG2 B THR   A 17  ? 0.95836 1.08006 0.87570 -0.08732 0.02899  0.02454  14  THR   A CG2 
136  N N   A TYR   A 18  ? 1.06282 1.10320 0.90116 -0.02820 -0.07067 0.00314  15  TYR   A N   
137  N N   B TYR   A 18  ? 0.89142 1.05480 0.86088 -0.05319 -0.01566 0.00350  15  TYR   A N   
138  C CA  A TYR   A 18  ? 1.06042 1.08974 0.89033 -0.00960 -0.09566 -0.00531 15  TYR   A CA  
139  C CA  B TYR   A 18  ? 0.86791 1.05073 0.85777 -0.04332 -0.02684 -0.00441 15  TYR   A CA  
140  C C   A TYR   A 18  ? 1.05814 1.12426 0.92359 0.00226  -0.10676 -0.01997 15  TYR   A C   
141  C C   B TYR   A 18  ? 0.95190 1.12034 0.92451 -0.03096 -0.04745 -0.01268 15  TYR   A C   
142  O O   A TYR   A 18  ? 1.05104 1.10664 0.90535 0.01872  -0.13011 -0.02962 15  TYR   A O   
143  O O   B TYR   A 18  ? 1.01479 1.18130 0.98604 -0.01971 -0.06028 -0.01735 15  TYR   A O   
144  C CB  A TYR   A 18  ? 1.01236 1.04314 0.85084 -0.00456 -0.09820 -0.00447 15  TYR   A CB  
145  C CB  B TYR   A 18  ? 0.88403 1.10121 0.90951 -0.04711 -0.01968 -0.00953 15  TYR   A CB  
146  C CG  A TYR   A 18  ? 1.02304 1.01276 0.82320 -0.01545 -0.09215 0.00811  15  TYR   A CG  
147  C CG  B TYR   A 18  ? 0.82543 1.04132 0.85082 -0.05484 -0.01269 -0.00931 15  TYR   A CG  
148  C CD1 A TYR   A 18  ? 1.02286 0.95754 0.76805 -0.01254 -0.10677 0.01230  15  TYR   A CD1 
149  C CD1 B TYR   A 18  ? 0.76016 0.97495 0.78232 -0.05176 -0.02315 -0.01787 15  TYR   A CD1 
150  C CD2 A TYR   A 18  ? 0.98536 0.98987 0.80277 -0.02937 -0.07264 0.01534  15  TYR   A CD2 
151  C CD2 B TYR   A 18  ? 0.78537 1.00063 0.81376 -0.06390 0.00284  -0.00192 15  TYR   A CD2 
152  C CE1 A TYR   A 18  ? 1.08720 0.98260 0.79556 -0.02599 -0.09999 0.02378  15  TYR   A CE1 
153  C CE1 B TYR   A 18  ? 0.82318 1.03421 0.84323 -0.05853 -0.01757 -0.01856 15  TYR   A CE1 
154  C CE2 A TYR   A 18  ? 0.98334 0.95355 0.76878 -0.04160 -0.06674 0.02536  15  TYR   A CE2 
155  C CE2 B TYR   A 18  ? 0.67292 0.88458 0.69978 -0.06908 0.00821  -0.00306 15  TYR   A CE2 
156  C CZ  A TYR   A 18  ? 0.96805 0.88376 0.69903 -0.04121 -0.07943 0.02972  15  TYR   A CZ  
157  C CZ  B TYR   A 18  ? 0.83986 1.04837 0.86162 -0.06693 -0.00161 -0.01113 15  TYR   A CZ  
158  O OH  A TYR   A 18  ? 1.01284 0.89263 0.71014 -0.05683 -0.07225 0.03973  15  TYR   A OH  
159  O OH  B TYR   A 18  ? 0.79869 1.00132 0.81716 -0.07191 0.00301  -0.01314 15  TYR   A OH  
160  N N   A GLY   A 19  ? 1.18450 1.29228 1.09138 -0.00589 -0.09156 -0.02258 16  GLY   A N   
161  N N   B GLY   A 19  ? 1.11868 1.27522 1.07632 -0.03140 -0.05237 -0.01547 16  GLY   A N   
162  C CA  A GLY   A 19  ? 1.02246 1.16982 0.96775 0.00120  -0.09888 -0.03691 16  GLY   A CA  
163  C CA  B GLY   A 19  ? 1.05017 1.19665 0.99477 -0.01816 -0.07446 -0.02534 16  GLY   A CA  
164  C C   A GLY   A 19  ? 0.98931 1.14755 0.94296 -0.00802 -0.09210 -0.03911 16  GLY   A C   
165  C C   B GLY   A 19  ? 1.00684 1.16851 0.96428 -0.01928 -0.07817 -0.03436 16  GLY   A C   
166  O O   A GLY   A 19  ? 0.99996 1.15378 0.94989 -0.02183 -0.07377 -0.02980 16  GLY   A O   
167  O O   B GLY   A 19  ? 0.97866 1.14385 0.94030 -0.03109 -0.06361 -0.03040 16  GLY   A O   
168  N N   A VAL   A 20  ? 0.96623 1.13917 0.93195 0.00052  -0.10813 -0.05296 17  VAL   A N   
169  N N   B VAL   A 20  ? 0.96022 1.13112 0.92464 -0.00660 -0.09848 -0.04775 17  VAL   A N   
170  C CA  A VAL   A 20  ? 0.87493 1.06417 0.85585 -0.00782 -0.10409 -0.05859 17  VAL   A CA  
171  C CA  B VAL   A 20  ? 0.93149 1.12019 0.91175 -0.00798 -0.10431 -0.05874 17  VAL   A CA  
172  C C   A VAL   A 20  ? 0.84048 1.07981 0.87267 -0.01004 -0.10116 -0.07040 17  VAL   A C   
173  C C   B VAL   A 20  ? 0.84816 1.08686 0.87990 -0.01026 -0.10024 -0.06954 17  VAL   A C   
174  O O   A VAL   A 20  ? 0.84916 1.11027 0.90063 0.00234  -0.11532 -0.08295 17  VAL   A O   
175  O O   B VAL   A 20  ? 0.84553 1.10517 0.89608 0.00170  -0.11245 -0.08043 17  VAL   A O   
176  C CB  A VAL   A 20  ? 0.91861 1.08529 0.87199 0.00132  -0.12517 -0.06639 17  VAL   A CB  
177  C CB  B VAL   A 20  ? 0.92705 1.09440 0.88117 0.00687  -0.13074 -0.06820 17  VAL   A CB  
178  C CG1 A VAL   A 20  ? 0.86616 1.05196 0.83848 -0.00756 -0.12227 -0.07428 17  VAL   A CG1 
179  C CG1 B VAL   A 20  ? 0.88259 1.05533 0.83958 0.00183  -0.13448 -0.07606 17  VAL   A CG1 
180  C CG2 A VAL   A 20  ? 0.98979 1.10384 0.88678 0.00039  -0.12518 -0.05379 17  VAL   A CG2 
181  C CG2 B VAL   A 20  ? 1.02845 1.14177 0.92601 0.01061  -0.13594 -0.05641 17  VAL   A CG2 
182  N N   . VAL   A 21  ? 0.71066 0.96730 0.76355 -0.02586 -0.08268 -0.06705 18  VAL   A N   
183  C CA  . VAL   A 21  ? 0.75037 1.05015 0.84694 -0.03330 -0.07472 -0.07521 18  VAL   A CA  
184  C C   . VAL   A 21  ? 0.76508 1.08260 0.87909 -0.03901 -0.08114 -0.08817 18  VAL   A C   
185  O O   . VAL   A 21  ? 0.65356 0.95206 0.75221 -0.04711 -0.07733 -0.08426 18  VAL   A O   
186  C CB  . VAL   A 21  ? 0.69936 1.00226 0.80402 -0.04773 -0.05120 -0.06256 18  VAL   A CB  
187  C CG1 . VAL   A 21  ? 0.65504 0.99736 0.79801 -0.05753 -0.04228 -0.07011 18  VAL   A CG1 
188  C CG2 . VAL   A 21  ? 0.70232 0.98913 0.79107 -0.04266 -0.04615 -0.05108 18  VAL   A CG2 
189  N N   . TYR   A 22  ? 0.59559 0.95123 0.74294 -0.03503 -0.09072 -0.10503 19  TYR   A N   
190  C CA  . TYR   A 22  ? 0.60634 0.98732 0.77833 -0.04296 -0.09625 -0.11995 19  TYR   A CA  
191  C C   . TYR   A 22  ? 0.65195 1.07591 0.86553 -0.05871 -0.08036 -0.12610 19  TYR   A C   
192  O O   . TYR   A 22  ? 0.67830 1.11964 0.90524 -0.05741 -0.07130 -0.12416 19  TYR   A O   
193  C CB  . TYR   A 22  ? 0.62492 1.01854 0.80309 -0.02530 -0.12366 -0.13872 19  TYR   A CB  
194  C CG  . TYR   A 22  ? 0.70462 1.05221 0.83640 -0.01025 -0.14204 -0.13401 19  TYR   A CG  
195  C CD1 . TYR   A 22  ? 0.87364 1.19905 0.98442 -0.01472 -0.14834 -0.13471 19  TYR   A CD1 
196  C CD2 . TYR   A 22  ? 0.82237 1.14568 0.92787 0.00770  -0.15331 -0.12918 19  TYR   A CD2 
197  C CE1 . TYR   A 22  ? 0.94685 1.22783 1.01016 -0.00222 -0.16408 -0.13025 19  TYR   A CE1 
198  C CE2 . TYR   A 22  ? 0.89458 1.17078 0.95163 0.01922  -0.16945 -0.12396 19  TYR   A CE2 
199  C CZ  . TYR   A 22  ? 0.85708 1.11276 0.89255 0.01398  -0.17421 -0.12436 19  TYR   A CZ  
200  O OH  . TYR   A 22  ? 1.10633 1.31282 1.08867 0.02417  -0.18910 -0.11890 19  TYR   A OH  
201  N N   . LYS   A 23  ? 0.74529 1.18422 0.97661 -0.07483 -0.07687 -0.13385 20  LYS   A N   
202  C CA  . LYS   A 23  ? 0.59252 1.07313 0.86251 -0.09287 -0.06329 -0.14271 20  LYS   A CA  
203  C C   . LYS   A 23  ? 0.61456 1.14035 0.92053 -0.08769 -0.07981 -0.16806 20  LYS   A C   
204  O O   . LYS   A 23  ? 0.64210 1.16574 0.94792 -0.08660 -0.09529 -0.17844 20  LYS   A O   
205  C CB  . LYS   A 23  ? 0.54868 1.01499 0.81463 -0.11666 -0.04835 -0.13555 20  LYS   A CB  
206  C CG  . LYS   A 23  ? 0.55574 1.06113 0.85751 -0.13937 -0.03513 -0.14576 20  LYS   A CG  
207  C CD  . LYS   A 23  ? 0.65075 1.13316 0.94246 -0.16256 -0.02363 -0.13886 20  LYS   A CD  
208  C CE  . LYS   A 23  ? 0.58663 1.10382 0.90961 -0.18882 -0.00966 -0.14857 20  LYS   A CE  
209  N NZ  . LYS   A 23  ? 0.67405 1.16110 0.98196 -0.21208 0.00058  -0.14091 20  LYS   A NZ  
210  N N   . ALA   A 24  ? 0.57921 1.14716 0.91644 -0.08360 -0.07719 -0.17945 21  ALA   A N   
211  C CA  . ALA   A 24  ? 0.56229 1.18124 0.93989 -0.07633 -0.09263 -0.20650 21  ALA   A CA  
212  C C   . ALA   A 24  ? 0.62729 1.29740 1.04794 -0.10125 -0.07293 -0.21829 21  ALA   A C   
213  O O   . ALA   A 24  ? 0.53968 1.20406 0.95531 -0.11955 -0.04838 -0.20455 21  ALA   A O   
214  C CB  . ALA   A 24  ? 0.60759 1.23731 0.98793 -0.04732 -0.10882 -0.21496 21  ALA   A CB  
215  N N   . ARG   A 25  ? 0.53371 1.25394 0.99586 -0.10240 -0.08425 -0.24466 22  ARG   A N   
216  C CA  . ARG   A 25  ? 0.60050 1.37505 1.10682 -0.12872 -0.06563 -0.25954 22  ARG   A CA  
217  C C   . ARG   A 25  ? 0.63525 1.47584 1.19061 -0.11351 -0.07887 -0.29030 22  ARG   A C   
218  O O   . ARG   A 25  ? 0.66281 1.51380 1.22886 -0.09448 -0.10633 -0.30735 22  ARG   A O   
219  C CB  . ARG   A 25  ? 0.65918 1.43077 1.17115 -0.15588 -0.06216 -0.26254 22  ARG   A CB  
220  C CG  . ARG   A 25  ? 0.66458 1.48530 1.21630 -0.18849 -0.04014 -0.27565 22  ARG   A CG  
221  C CD  . ARG   A 25  ? 0.70143 1.51549 1.25743 -0.21237 -0.04144 -0.28104 22  ARG   A CD  
222  N NE  . ARG   A 25  ? 0.83957 1.67272 1.41447 -0.19468 -0.06971 -0.30240 22  ARG   A NE  
223  C CZ  . ARG   A 25  ? 0.90571 1.77983 1.51423 -0.19012 -0.07345 -0.32321 22  ARG   A CZ  
224  N NH1 . ARG   A 25  ? 0.91106 1.81392 1.53866 -0.20254 -0.05029 -0.32698 22  ARG   A NH1 
225  N NH2 . ARG   A 25  ? 0.90872 1.79465 1.53014 -0.17247 -0.10143 -0.34134 22  ARG   A NH2 
226  N N   . ASN   A 26  ? 0.72720 1.59515 1.29916 -0.11834 -0.05850 -0.29338 23  ASN   A N   
227  C CA  . ASN   A 26  ? 0.73944 1.64878 1.34270 -0.10346 -0.06405 -0.31708 23  ASN   A CA  
228  C C   . ASN   A 26  ? 0.82032 1.75452 1.44959 -0.12216 -0.06240 -0.33282 23  ASN   A C   
229  O O   . ASN   A 26  ? 0.83148 1.76405 1.46098 -0.15538 -0.03904 -0.32547 23  ASN   A O   
230  C CB  . ASN   A 26  ? 0.79507 1.72290 1.40395 -0.10781 -0.03953 -0.31576 23  ASN   A CB  
231  C CG  . ASN   A 26  ? 0.89688 1.86753 1.53616 -0.08794 -0.04673 -0.34183 23  ASN   A CG  
232  O OD1 . ASN   A 26  ? 0.79261 1.79745 1.45913 -0.10207 -0.03774 -0.35822 23  ASN   A OD1 
233  N ND2 . ASN   A 26  ? 0.87086 1.83923 1.50497 -0.05495 -0.06346 -0.34669 23  ASN   A ND2 
234  N N   . LYS   A 27  ? 0.91806 1.87246 1.56701 -0.10057 -0.08827 -0.35445 24  LYS   A N   
235  C CA  . LYS   A 27  ? 0.88963 1.86781 1.56399 -0.11687 -0.09017 -0.37046 24  LYS   A CA  
236  C C   . LYS   A 27  ? 0.94519 1.96786 1.65076 -0.13531 -0.06583 -0.38425 24  LYS   A C   
237  O O   . LYS   A 27  ? 0.96112 1.99495 1.67932 -0.16512 -0.05227 -0.38747 24  LYS   A O   
238  C CB  . LYS   A 27  ? 1.01779 2.00314 1.70203 -0.08673 -0.12629 -0.38989 24  LYS   A CB  
239  C CG  . LYS   A 27  ? 1.09762 2.10293 1.80526 -0.10239 -0.13242 -0.40558 24  LYS   A CG  
240  C CD  . LYS   A 27  ? 1.07655 2.08299 1.78827 -0.07046 -0.17018 -0.42337 24  LYS   A CD  
241  C CE  . LYS   A 27  ? 1.12088 2.14862 1.85700 -0.08656 -0.17665 -0.43961 24  LYS   A CE  
242  N NZ  . LYS   A 27  ? 1.19028 2.21688 1.92785 -0.05464 -0.21452 -0.45707 24  LYS   A NZ  
243  N N   . LEU   A 28  ? 1.03615 2.08331 1.75261 -0.11883 -0.06018 -0.39316 25  LEU   A N   
244  C CA  . LEU   A 28  ? 1.00551 2.09692 1.75011 -0.13559 -0.03717 -0.40836 25  LEU   A CA  
245  C C   . LEU   A 28  ? 0.95310 2.02895 1.67882 -0.17021 -0.00220 -0.38788 25  LEU   A C   
246  O O   . LEU   A 28  ? 0.91700 2.00298 1.65109 -0.20272 0.01643  -0.38907 25  LEU   A O   
247  C CB  . LEU   A 28  ? 0.95045 2.07276 1.71163 -0.10484 -0.04436 -0.42716 25  LEU   A CB  
248  C CG  . LEU   A 28  ? 0.97022 2.11685 1.75576 -0.07172 -0.07663 -0.45401 25  LEU   A CG  
249  C CD1 . LEU   A 28  ? 0.86466 2.03823 1.66333 -0.04309 -0.08089 -0.47212 25  LEU   A CD1 
250  C CD2 . LEU   A 28  ? 0.87500 2.05859 1.69471 -0.08927 -0.07653 -0.47430 25  LEU   A CD2 
251  N N   . THR   A 29  ? 0.85899 1.90757 1.55682 -0.16353 0.00617  -0.36885 26  THR   A N   
252  C CA  . THR   A 29  ? 0.77447 1.80599 1.45061 -0.19209 0.03777  -0.34980 26  THR   A CA  
253  C C   . THR   A 29  ? 0.77961 1.76510 1.42654 -0.21831 0.04586  -0.32538 26  THR   A C   
254  O O   . THR   A 29  ? 0.74252 1.70984 1.36947 -0.24551 0.07136  -0.31005 26  THR   A O   
255  C CB  . THR   A 29  ? 0.70701 1.72680 1.36414 -0.17383 0.04244  -0.33960 26  THR   A CB  
256  O OG1 . THR   A 29  ? 0.76983 1.74794 1.39992 -0.15950 0.02768  -0.32057 26  THR   A OG1 
257  C CG2 . THR   A 29  ? 0.80068 1.85989 1.48368 -0.14260 0.02914  -0.36447 26  THR   A CG2 
258  N N   . GLY   A 30  ? 0.80574 1.76976 1.44707 -0.21051 0.02421  -0.32198 27  GLY   A N   
259  C CA  . GLY   A 30  ? 0.78679 1.70490 1.39843 -0.23187 0.02991  -0.29976 27  GLY   A CA  
260  C C   . GLY   A 30  ? 0.64760 1.52675 1.22432 -0.22669 0.03613  -0.27526 27  GLY   A C   
261  O O   . GLY   A 30  ? 0.69149 1.53096 1.24148 -0.24446 0.04265  -0.25636 27  GLY   A O   
262  N N   . GLU   A 31  ? 0.62736 1.51619 1.20338 -0.20274 0.03376  -0.27588 28  GLU   A N   
263  C CA  . GLU   A 31  ? 0.64152 1.49689 1.18626 -0.19754 0.04009  -0.25363 28  GLU   A CA  
264  C C   . GLU   A 31  ? 0.69233 1.52073 1.22216 -0.18155 0.01776  -0.24549 28  GLU   A C   
265  O O   . GLU   A 31  ? 0.64310 1.48410 1.18661 -0.15871 -0.00819 -0.26000 28  GLU   A O   
266  C CB  . GLU   A 31  ? 0.68617 1.56182 1.23609 -0.17631 0.04264  -0.25932 28  GLU   A CB  
267  C CG  . GLU   A 31  ? 0.76885 1.61405 1.28839 -0.17081 0.05012  -0.23787 28  GLU   A CG  
268  C CD  . GLU   A 31  ? 0.85564 1.72192 1.38085 -0.15189 0.05342  -0.24562 28  GLU   A CD  
269  O OE1 . GLU   A 31  ? 0.71871 1.62318 1.27048 -0.14628 0.05344  -0.26723 28  GLU   A OE1 
270  O OE2 . GLU   A 31  ? 0.86867 1.71422 1.37214 -0.14268 0.05582  -0.23118 28  GLU   A OE2 
271  N N   . VAL   A 32  ? 0.52269 1.30194 1.01478 -0.19088 0.02704  -0.21997 29  VAL   A N   
272  C CA  . VAL   A 32  ? 0.58748 1.30998 1.04118 -0.17185 0.00971  -0.20308 29  VAL   A CA  
273  C C   . VAL   A 32  ? 0.53678 1.22985 0.96145 -0.15261 0.01154  -0.18590 29  VAL   A C   
274  O O   . VAL   A 32  ? 0.58213 1.27457 0.99985 -0.16318 0.03143  -0.17620 29  VAL   A O   
275  C CB  . VAL   A 32  ? 0.54023 1.21713 0.96624 -0.19298 0.01668  -0.18648 29  VAL   A CB  
276  C CG1 . VAL   A 32  ? 0.55692 1.25927 1.00989 -0.21115 0.01160  -0.20450 29  VAL   A CG1 
277  C CG2 . VAL   A 32  ? 0.58927 1.24492 0.99547 -0.21535 0.04265  -0.16819 29  VAL   A CG2 
278  N N   . VAL   A 33  ? 0.47268 1.14025 0.87858 -0.12521 -0.00966 -0.18265 30  VAL   A N   
279  C CA  . VAL   A 33  ? 0.47026 1.10653 0.84717 -0.10703 -0.01068 -0.16707 30  VAL   A CA  
280  C C   . VAL   A 33  ? 0.54034 1.12227 0.87869 -0.09613 -0.02356 -0.15131 30  VAL   A C   
281  O O   . VAL   A 33  ? 0.53584 1.10619 0.87010 -0.09999 -0.03278 -0.15392 30  VAL   A O   
282  C CB  . VAL   A 33  ? 0.45510 1.12076 0.84942 -0.08208 -0.02356 -0.18291 30  VAL   A CB  
283  C CG1 . VAL   A 33  ? 0.43045 1.15516 0.86495 -0.09261 -0.00880 -0.20103 30  VAL   A CG1 
284  C CG2 . VAL   A 33  ? 0.56515 1.23412 0.96527 -0.06040 -0.05243 -0.19819 30  VAL   A CG2 
285  N N   . ALA   A 34  ? 0.55864 1.10794 0.86824 -0.08347 -0.02338 -0.13567 31  ALA   A N   
286  C CA  . ALA   A 34  ? 0.53114 1.03193 0.80372 -0.07226 -0.03421 -0.12190 31  ALA   A CA  
287  C C   . ALA   A 34  ? 0.59003 1.08328 0.85206 -0.04648 -0.05306 -0.12658 31  ALA   A C   
288  O O   . ALA   A 34  ? 0.61376 1.11605 0.87931 -0.03836 -0.04991 -0.12668 31  ALA   A O   
289  C CB  . ALA   A 34  ? 0.58589 1.05127 0.83142 -0.08151 -0.01786 -0.09930 31  ALA   A CB  
290  N N   . LEU   A 35  ? 0.55086 1.02405 0.79653 -0.03367 -0.07334 -0.13057 32  LEU   A N   
291  C CA  . LEU   A 35  ? 0.56332 1.02226 0.79327 -0.00876 -0.09502 -0.13580 32  LEU   A CA  
292  C C   . LEU   A 35  ? 0.71864 1.12082 0.90018 -0.00448 -0.09746 -0.11640 32  LEU   A C   
293  O O   . LEU   A 35  ? 0.69338 1.06964 0.85338 -0.00923 -0.10051 -0.11078 32  LEU   A O   
294  C CB  . LEU   A 35  ? 0.63915 1.11584 0.88301 0.00424  -0.11932 -0.15650 32  LEU   A CB  
295  C CG  . LEU   A 35  ? 0.70797 1.24537 1.00159 0.00894  -0.12432 -0.18177 32  LEU   A CG  
296  C CD1 . LEU   A 35  ? 0.60202 1.15346 0.90753 0.02039  -0.14980 -0.20153 32  LEU   A CD1 
297  C CD2 . LEU   A 35  ? 0.71418 1.26141 1.01244 0.02813  -0.12951 -0.18758 32  LEU   A CD2 
298  N N   . LYS   A 36  ? 0.66713 1.05090 0.83152 0.00351  -0.09559 -0.10732 33  LYS   A N   
299  C CA  . LYS   A 36  ? 0.76982 1.10184 0.88866 0.00822  -0.09983 -0.09172 33  LYS   A CA  
300  C C   . LYS   A 36  ? 0.79853 1.11028 0.89652 0.03090  -0.12655 -0.10029 33  LYS   A C   
301  O O   . LYS   A 36  ? 0.76108 1.08463 0.86900 0.04521  -0.13531 -0.10891 33  LYS   A O   
302  C CB  . LYS   A 36  ? 0.72883 1.04867 0.83847 0.00196  -0.08333 -0.07678 33  LYS   A CB  
303  C CG  . LYS   A 36  ? 0.82218 1.09204 0.88722 0.00433  -0.08631 -0.06210 33  LYS   A CG  
304  C CD  . LYS   A 36  ? 0.85182 1.11221 0.91109 -0.01067 -0.06479 -0.04586 33  LYS   A CD  
305  C CE  . LYS   A 36  ? 0.86121 1.14342 0.94089 -0.01075 -0.05609 -0.04597 33  LYS   A CE  
306  N NZ  . LYS   A 36  ? 0.90707 1.17959 0.98072 -0.02358 -0.03818 -0.03120 33  LYS   A NZ  
307  N N   . LYS   A 37  ? 0.78292 1.06164 0.84924 0.03496  -0.14025 -0.09838 34  LYS   A N   
308  C CA  . LYS   A 37  ? 0.85018 1.10251 0.88982 0.05686  -0.16876 -0.10633 34  LYS   A CA  
309  C C   . LYS   A 37  ? 0.96814 1.16179 0.95391 0.05855  -0.17030 -0.08906 34  LYS   A C   
310  O O   . LYS   A 37  ? 0.99457 1.16192 0.95510 0.04282  -0.15498 -0.07335 34  LYS   A O   
311  C CB  . LYS   A 37  ? 0.90550 1.15490 0.93899 0.06034  -0.18504 -0.11589 34  LYS   A CB  
312  C CG  . LYS   A 37  ? 1.00286 1.22284 1.00618 0.08482  -0.21807 -0.12528 34  LYS   A CG  
313  C CD  . LYS   A 37  ? 1.02689 1.24965 1.02857 0.08804  -0.23485 -0.13676 34  LYS   A CD  
314  C CE  . LYS   A 37  ? 1.05522 1.24545 1.02339 0.11453  -0.27090 -0.14657 34  LYS   A CE  
315  N NZ  . LYS   A 37  ? 1.06880 1.26515 1.03784 0.11912  -0.28988 -0.16007 34  LYS   A NZ  
316  N N   . ILE   A 38  ? 0.91762 1.09102 0.88598 0.07716  -0.18859 -0.09306 35  ILE   A N   
317  C CA  . ILE   A 38  ? 1.00138 1.11593 0.91639 0.07803  -0.19181 -0.07777 35  ILE   A CA  
318  C C   . ILE   A 38  ? 1.13522 1.20953 1.01123 0.10028  -0.22468 -0.08518 35  ILE   A C   
319  O O   . ILE   A 38  ? 1.19674 1.28323 1.08683 0.12264  -0.24569 -0.10076 35  ILE   A O   
320  C CB  . ILE   A 38  ? 1.00736 1.12527 0.93079 0.07803  -0.18246 -0.07326 35  ILE   A CB  
321  C CG1 . ILE   A 38  ? 0.93172 1.08528 0.88909 0.05690  -0.15189 -0.06543 35  ILE   A CG1 
322  C CG2 . ILE   A 38  ? 1.05353 1.10793 0.92016 0.07746  -0.18761 -0.05870 35  ILE   A CG2 
323  C CD1 . ILE   A 38  ? 0.80102 0.95941 0.76678 0.05616  -0.14259 -0.06145 35  ILE   A CD1 
324  N N   . ARG   A 39  ? 1.10364 1.12916 0.92899 0.09510  -0.22970 -0.07488 36  ARG   A N   
325  C CA  . ARG   A 39  ? 1.17913 1.15496 0.95549 0.11495  -0.26169 -0.07914 36  ARG   A CA  
326  C C   . ARG   A 39  ? 1.19840 1.12048 0.92964 0.12022  -0.26876 -0.06877 36  ARG   A C   
327  O O   . ARG   A 39  ? 1.28819 1.17087 0.98089 0.10116  -0.25196 -0.04990 36  ARG   A O   
328  C CB  . ARG   A 39  ? 1.32455 1.26516 1.05823 0.10511  -0.26225 -0.07116 36  ARG   A CB  
329  C CG  . ARG   A 39  ? 1.32540 1.31418 1.10037 0.09474  -0.25056 -0.07867 36  ARG   A CG  
330  C CD  . ARG   A 39  ? 1.36293 1.31549 1.09394 0.07965  -0.24198 -0.06719 36  ARG   A CD  
331  N NE  . ARG   A 39  ? 1.45211 1.39948 1.17146 0.09164  -0.26581 -0.07975 36  ARG   A NE  
332  C CZ  . ARG   A 39  ? 1.55639 1.45322 1.22256 0.10876  -0.29521 -0.08192 36  ARG   A CZ  
333  N NH1 . ARG   A 39  ? 1.58019 1.42366 1.19732 0.11551  -0.30471 -0.07198 36  ARG   A NH1 
334  N NH2 . ARG   A 39  ? 1.54010 1.43690 1.19959 0.11915  -0.31678 -0.09449 36  ARG   A NH2 
335  N N   . LEU   A 40  ? 1.23603 1.15725 0.97289 0.14568  -0.29341 -0.08225 37  LEU   A N   
336  C CA  . LEU   A 40  ? 1.31961 1.19055 1.01679 0.15096  -0.30044 -0.07374 37  LEU   A CA  
337  C C   . LEU   A 40  ? 1.36218 1.14889 0.97827 0.15665  -0.32253 -0.06393 37  LEU   A C   
338  O O   . LEU   A 40  ? 1.43171 1.16333 1.00056 0.14891  -0.32026 -0.04959 37  LEU   A O   
339  C CB  . LEU   A 40  ? 1.27861 1.17794 1.01037 0.17755  -0.31868 -0.09301 37  LEU   A CB  
340  C CG  . LEU   A 40  ? 1.13982 1.11691 0.94506 0.17123  -0.29584 -0.10222 37  LEU   A CG  
341  C CD1 . LEU   A 40  ? 1.16254 1.16704 0.99817 0.20006  -0.31606 -0.12444 37  LEU   A CD1 
342  C CD2 . LEU   A 40  ? 1.04476 1.01719 0.84807 0.14537  -0.26467 -0.08338 37  LEU   A CD2 
343  N N   . ASP   A 41  ? 1.37665 1.14994 0.97305 0.16911  -0.34442 -0.07153 38  ASP   A N   
344  C CA  . ASP   A 41  ? 1.44498 1.13361 0.95770 0.17453  -0.36661 -0.06191 38  ASP   A CA  
345  C C   . ASP   A 41  ? 1.42350 1.06875 0.88653 0.14165  -0.33959 -0.03774 38  ASP   A C   
346  O O   . ASP   A 41  ? 1.45419 1.02131 0.84062 0.13911  -0.35076 -0.02524 38  ASP   A O   
347  C CB  . ASP   A 41  ? 1.52946 1.21893 1.03583 0.19563  -0.39647 -0.07707 38  ASP   A CB  
348  C CG  . ASP   A 41  ? 1.51303 1.26592 1.07055 0.18211  -0.37802 -0.08319 38  ASP   A CG  
349  O OD1 . ASP   A 41  ? 1.50181 1.30633 1.10949 0.16145  -0.34502 -0.07917 38  ASP   A OD1 
350  O OD2 . ASP   A 41  ? 1.56642 1.31416 1.11118 0.19250  -0.39802 -0.09225 38  ASP   A OD2 
351  N N   . THR   A 42  ? 1.39493 1.08799 0.89834 0.11654  -0.30456 -0.03168 39  THR   A N   
352  C CA  . THR   A 42  ? 1.38084 1.04478 0.84765 0.08554  -0.27607 -0.01186 39  THR   A CA  
353  C C   . THR   A 42  ? 1.50841 1.17301 0.98316 0.06645  -0.25127 0.00026  39  THR   A C   
354  O O   . THR   A 42  ? 1.35003 0.99888 0.80263 0.03956  -0.22525 0.01497  39  THR   A O   
355  C CB  . THR   A 42  ? 1.42849 1.14098 0.93155 0.07091  -0.25421 -0.01366 39  THR   A CB  
356  O OG1 . THR   A 42  ? 1.45584 1.23937 1.03368 0.06513  -0.23349 -0.01908 39  THR   A OG1 
357  C CG2 . THR   A 42  ? 1.43446 1.15478 0.93902 0.09000  -0.27963 -0.02842 39  THR   A CG2 
358  N N   . GLU   A 43  ? 1.41836 1.10233 0.92464 0.07984  -0.25889 -0.00696 40  GLU   A N   
359  C CA  . GLU   A 43  ? 1.39652 1.08432 0.91420 0.06392  -0.23826 0.00228  40  GLU   A CA  
360  C C   . GLU   A 43  ? 1.47660 1.09335 0.93574 0.07192  -0.25886 0.00755  40  GLU   A C   
361  O O   . GLU   A 43  ? 1.42274 1.03656 0.88920 0.09857  -0.28456 -0.00484 40  GLU   A O   
362  C CB  . GLU   A 43  ? 1.31913 1.08026 0.91353 0.07145  -0.22981 -0.00975 40  GLU   A CB  
363  C CG  . GLU   A 43  ? 1.29921 1.12615 0.94914 0.06405  -0.21172 -0.01546 40  GLU   A CG  
364  C CD  . GLU   A 43  ? 1.35191 1.18719 1.00393 0.03442  -0.17879 -0.00112 40  GLU   A CD  
365  O OE1 . GLU   A 43  ? 1.35105 1.16367 0.98451 0.01896  -0.16529 0.01059  40  GLU   A OE1 
366  O OE2 . GLU   A 43  ? 1.36588 1.23099 1.03903 0.02700  -0.16715 -0.00284 40  GLU   A OE2 
367  N N   . THR   A 44  ? 1.49222 1.05126 0.89263 0.04825  -0.24719 0.02511  41  THR   A N   
368  C CA  . THR   A 44  ? 1.63396 1.11715 0.97163 0.05114  -0.26505 0.03220  41  THR   A CA  
369  C C   . THR   A 44  ? 1.61586 1.11690 0.98581 0.05402  -0.26220 0.02893  41  THR   A C   
370  O O   . THR   A 44  ? 1.61550 1.06753 0.95119 0.07007  -0.28663 0.02655  41  THR   A O   
371  C CB  . THR   A 44  ? 1.63512 1.05697 0.90500 0.01924  -0.24809 0.05185  41  THR   A CB  
372  O OG1 . THR   A 44  ? 1.68330 1.15218 0.99186 -0.01056 -0.20953 0.05888  41  THR   A OG1 
373  C CG2 . THR   A 44  ? 1.74676 1.13228 0.96642 0.02060  -0.25790 0.05471  41  THR   A CG2 
374  N N   . GLU   A 45  ? 1.39497 0.96217 0.82733 0.03974  -0.23416 0.02836  42  GLU   A N   
375  C CA  . GLU   A 45  ? 1.39801 0.98564 0.86197 0.04065  -0.22927 0.02527  42  GLU   A CA  
376  C C   . GLU   A 45  ? 1.34497 0.99373 0.87153 0.06835  -0.24038 0.00604  42  GLU   A C   
377  O O   . GLU   A 45  ? 1.33525 1.02225 0.90341 0.06653  -0.22885 0.00227  42  GLU   A O   
378  C CB  . GLU   A 45  ? 1.34368 0.96407 0.83502 0.00880  -0.19344 0.03570  42  GLU   A CB  
379  C CG  . GLU   A 45  ? 1.54931 1.11704 0.98444 -0.02171 -0.17853 0.05275  42  GLU   A CG  
380  C CD  . GLU   A 45  ? 1.65378 1.14136 1.02327 -0.02359 -0.19572 0.05960  42  GLU   A CD  
381  O OE1 . GLU   A 45  ? 1.56821 1.05493 0.95081 -0.01469 -0.20423 0.05475  42  GLU   A OE1 
382  O OE2 . GLU   A 45  ? 1.70435 1.12678 1.00601 -0.03417 -0.20105 0.06973  42  GLU   A OE2 
383  N N   . GLY   A 46  ? 1.35654 1.01623 0.89023 0.09313  -0.26227 -0.00706 43  GLY   A N   
384  C CA  . GLY   A 46  ? 1.23098 0.95281 0.82573 0.11759  -0.27134 -0.02727 43  GLY   A CA  
385  C C   . GLY   A 46  ? 1.15323 0.95352 0.81449 0.10337  -0.24264 -0.02941 43  GLY   A C   
386  O O   . GLY   A 46  ? 1.23040 1.04074 0.89282 0.08277  -0.22329 -0.01961 43  GLY   A O   
387  N N   . VAL   A 47  ? 1.09426 0.94861 0.80905 0.11488  -0.24012 -0.04295 44  VAL   A N   
388  C CA  . VAL   A 47  ? 1.03324 0.95770 0.80755 0.10127  -0.21364 -0.04472 44  VAL   A CA  
389  C C   . VAL   A 47  ? 1.01958 0.93758 0.78747 0.07153  -0.18559 -0.02627 44  VAL   A C   
390  O O   . VAL   A 47  ? 0.97018 0.85996 0.71822 0.06550  -0.18333 -0.01938 44  VAL   A O   
391  C CB  . VAL   A 47  ? 0.93871 0.91581 0.76369 0.11700  -0.21476 -0.06176 44  VAL   A CB  
392  C CG1 . VAL   A 47  ? 0.93604 0.98049 0.81666 0.10295  -0.18942 -0.06375 44  VAL   A CG1 
393  C CG2 . VAL   A 47  ? 0.86949 0.85140 0.69983 0.14876  -0.24482 -0.08259 44  VAL   A CG2 
394  N N   . PRO   A 48  ? 0.96034 0.90298 0.74431 0.05295  -0.16494 -0.01906 45  PRO   A N   
395  C CA  . PRO   A 48  ? 0.89719 0.83505 0.67596 0.02656  -0.13986 -0.00357 45  PRO   A CA  
396  C C   . PRO   A 48  ? 0.96253 0.93100 0.77446 0.02239  -0.12726 -0.00425 45  PRO   A C   
397  O O   . PRO   A 48  ? 0.90848 0.91970 0.76019 0.03436  -0.12845 -0.01583 45  PRO   A O   
398  C CB  . PRO   A 48  ? 0.91969 0.88852 0.71954 0.01462  -0.12361 -0.00128 45  PRO   A CB  
399  C CG  . PRO   A 48  ? 0.97684 0.94200 0.76948 0.03123  -0.14347 -0.01130 45  PRO   A CG  
400  C CD  . PRO   A 48  ? 0.99332 0.96589 0.79818 0.05583  -0.16542 -0.02580 45  PRO   A CD  
401  N N   . SER   A 49  ? 0.92522 0.87138 0.71913 0.00420  -0.11488 0.00768  46  SER   A N   
402  C CA  . SER   A 49  ? 0.87952 0.84982 0.69994 -0.00074 -0.10419 0.00767  46  SER   A CA  
403  C C   . SER   A 49  ? 0.87661 0.90600 0.74726 -0.00541 -0.08641 0.00507  46  SER   A C   
404  O O   . SER   A 49  ? 0.81438 0.87445 0.71416 0.00039  -0.08362 -0.00112 46  SER   A O   
405  C CB  . SER   A 49  ? 0.91327 0.85200 0.70742 -0.02218 -0.09355 0.02024  46  SER   A CB  
406  O OG  . SER   A 49  ? 1.19457 1.14000 0.98859 -0.04166 -0.07523 0.02904  46  SER   A OG  
407  N N   . THR   A 50  ? 0.77811 0.82080 0.65594 -0.01594 -0.07449 0.00962  47  THR   A N   
408  C CA  . THR   A 50  ? 0.83558 0.92734 0.75588 -0.01992 -0.05965 0.00734  47  THR   A CA  
409  C C   . THR   A 50  ? 0.75195 0.87556 0.69959 -0.00368 -0.06856 -0.00610 47  THR   A C   
410  O O   . THR   A 50  ? 0.73014 0.89279 0.71196 -0.00530 -0.05822 -0.00970 47  THR   A O   
411  C CB  . THR   A 50  ? 0.80085 0.89438 0.71882 -0.03312 -0.04704 0.01384  47  THR   A CB  
412  O OG1 . THR   A 50  ? 0.80249 0.87548 0.69795 -0.02603 -0.05948 0.01069  47  THR   A OG1 
413  C CG2 . THR   A 50  ? 0.96223 1.03417 0.86034 -0.05076 -0.03485 0.02477  47  THR   A CG2 
414  N N   . ALA   A 51  ? 0.73053 0.83819 0.66300 0.01154  -0.08783 -0.01429 48  ALA   A N   
415  C CA  . ALA   A 51  ? 0.73159 0.87441 0.69388 0.02729  -0.09708 -0.03006 48  ALA   A CA  
416  C C   . ALA   A 51  ? 0.77270 0.92998 0.74941 0.03960  -0.10223 -0.03937 48  ALA   A C   
417  O O   . ALA   A 51  ? 0.69805 0.90006 0.71136 0.04294  -0.09605 -0.04950 48  ALA   A O   
418  C CB  . ALA   A 51  ? 0.73623 0.85891 0.67895 0.04179  -0.11863 -0.03784 48  ALA   A CB  
419  N N   . ILE   A 52  ? 0.80800 0.92648 0.75433 0.04534  -0.11285 -0.03650 49  ILE   A N   
420  C CA  . ILE   A 52  ? 0.80022 0.92840 0.75668 0.05821  -0.11865 -0.04622 49  ILE   A CA  
421  C C   . ILE   A 52  ? 0.70613 0.86466 0.68742 0.04471  -0.09760 -0.04154 49  ILE   A C   
422  O O   . ILE   A 52  ? 0.69482 0.88660 0.70165 0.05273  -0.09503 -0.05252 49  ILE   A O   
423  C CB  . ILE   A 52  ? 0.79468 0.86653 0.70759 0.06604  -0.13582 -0.04332 49  ILE   A CB  
424  C CG1 . ILE   A 52  ? 0.86986 0.90191 0.74866 0.07728  -0.15701 -0.04477 49  ILE   A CG1 
425  C CG2 . ILE   A 52  ? 0.86862 0.94925 0.79106 0.08442  -0.14592 -0.05716 49  ILE   A CG2 
426  C CD1 . ILE   A 52  ? 0.91915 0.88716 0.74783 0.08468  -0.17577 -0.04131 49  ILE   A CD1 
427  N N   . ARG   A 53  ? 0.76066 0.90863 0.73400 0.02459  -0.08259 -0.02620 50  ARG   A N   
428  C CA  . ARG   A 53  ? 0.72884 0.90232 0.72296 0.01284  -0.06503 -0.02144 50  ARG   A CA  
429  C C   . ARG   A 53  ? 0.67696 0.89750 0.70666 0.01087  -0.05325 -0.02692 50  ARG   A C   
430  O O   . ARG   A 53  ? 0.67692 0.92469 0.72577 0.01283  -0.04675 -0.03265 50  ARG   A O   
431  C CB  . ARG   A 53  ? 0.79485 0.95009 0.77587 -0.00654 -0.05326 -0.00616 50  ARG   A CB  
432  C CG  . ARG   A 53  ? 0.95385 1.06756 0.90331 -0.01098 -0.05964 -0.00009 50  ARG   A CG  
433  C CD  . ARG   A 53  ? 1.05623 1.16380 1.00156 -0.03170 -0.04519 0.01224  50  ARG   A CD  
434  N NE  . ARG   A 53  ? 0.98870 1.05812 0.90476 -0.04045 -0.04920 0.01781  50  ARG   A NE  
435  C CZ  . ARG   A 53  ? 1.06519 1.12809 0.97637 -0.05940 -0.03764 0.02642  50  ARG   A CZ  
436  N NH1 . ARG   A 53  ? 0.87817 0.96911 0.81139 -0.06891 -0.02258 0.03011  50  ARG   A NH1 
437  N NH2 . ARG   A 53  ? 0.98564 1.01316 0.86947 -0.06918 -0.04151 0.03033  50  ARG   A NH2 
438  N N   . GLU   A 54  ? 0.60637 0.83459 0.64240 0.00571  -0.05002 -0.02529 51  GLU   A N   
439  C CA  . GLU   A 54  ? 0.65452 0.92210 0.72095 -0.00010 -0.03791 -0.02902 51  GLU   A CA  
440  C C   . GLU   A 54  ? 0.64184 0.94243 0.73143 0.01237  -0.04281 -0.04597 51  GLU   A C   
441  O O   . GLU   A 54  ? 0.63693 0.96974 0.74886 0.00658  -0.03012 -0.04944 51  GLU   A O   
442  C CB  . GLU   A 54  ? 0.69982 0.96486 0.76567 -0.00696 -0.03617 -0.02565 51  GLU   A CB  
443  C CG  . GLU   A 54  ? 0.65641 0.95707 0.75079 -0.01448 -0.02495 -0.02981 51  GLU   A CG  
444  C CD  . GLU   A 54  ? 0.75048 1.04482 0.84204 -0.02265 -0.02239 -0.02560 51  GLU   A CD  
445  O OE1 . GLU   A 54  ? 0.90197 1.16935 0.97132 -0.01897 -0.03211 -0.02339 51  GLU   A OE1 
446  O OE2 . GLU   A 54  ? 0.81573 1.12909 0.92414 -0.03314 -0.01072 -0.02450 51  GLU   A OE2 
447  N N   . ILE   A 55  ? 0.64198 0.93493 0.72561 0.02956  -0.06122 -0.05749 52  ILE   A N   
448  C CA  . ILE   A 55  ? 0.67062 1.00031 0.78052 0.04343  -0.06679 -0.07708 52  ILE   A CA  
449  C C   . ILE   A 55  ? 0.65741 1.00068 0.77384 0.04708  -0.06054 -0.08174 52  ILE   A C   
450  O O   . ILE   A 55  ? 0.60481 0.98924 0.74822 0.04432  -0.04886 -0.09119 52  ILE   A O   
451  C CB  . ILE   A 55  ? 0.64712 0.96146 0.74654 0.06477  -0.09162 -0.08941 52  ILE   A CB  
452  C CG1 . ILE   A 55  ? 0.60339 0.91191 0.69985 0.06147  -0.09760 -0.08785 52  ILE   A CG1 
453  C CG2 . ILE   A 55  ? 0.69046 1.04473 0.81880 0.08247  -0.09866 -0.11248 52  ILE   A CG2 
454  C CD1 . ILE   A 55  ? 0.66545 0.95004 0.74358 0.08269  -0.12463 -0.09786 52  ILE   A CD1 
455  N N   . SER   A 56  ? 0.61083 0.91839 0.70052 0.05194  -0.06771 -0.07548 53  SER   A N   
456  C CA  . SER   A 56  ? 0.67242 0.98857 0.76447 0.05714  -0.06424 -0.08102 53  SER   A CA  
457  C C   . SER   A 56  ? 0.67034 1.00618 0.77303 0.03887  -0.04239 -0.07175 53  SER   A C   
458  O O   . SER   A 56  ? 0.67181 1.03599 0.78878 0.04054  -0.03386 -0.08058 53  SER   A O   
459  C CB  . SER   A 56  ? 0.76335 1.03171 0.82158 0.06404  -0.07769 -0.07558 53  SER   A CB  
460  O OG  . SER   A 56  ? 0.82963 1.06913 0.86854 0.04609  -0.07039 -0.05634 53  SER   A OG  
461  N N   . LEU   A 57  ? 0.62511 0.94548 0.71929 0.02208  -0.03355 -0.05477 54  LEU   A N   
462  C CA  . LEU   A 57  ? 0.66294 0.99692 0.76391 0.00666  -0.01583 -0.04567 54  LEU   A CA  
463  C C   . LEU   A 57  ? 0.62169 0.99460 0.74767 0.00004  -0.00312 -0.05217 54  LEU   A C   
464  O O   . LEU   A 57  ? 0.61569 1.00789 0.74814 -0.00558 0.00893  -0.05369 54  LEU   A O   
465  C CB  . LEU   A 57  ? 0.52537 0.83521 0.61362 -0.00706 -0.01127 -0.02853 54  LEU   A CB  
466  C CG  . LEU   A 57  ? 0.68393 0.95842 0.74860 -0.00744 -0.01861 -0.02049 54  LEU   A CG  
467  C CD1 . LEU   A 57  ? 0.63596 0.89644 0.69468 -0.02166 -0.01168 -0.00662 54  LEU   A CD1 
468  C CD2 . LEU   A 57  ? 0.61533 0.89048 0.67605 -0.00537 -0.01753 -0.02215 54  LEU   A CD2 
469  N N   . LEU   A 58  ? 0.58865 0.97175 0.72653 -0.00078 -0.00557 -0.05619 55  LEU   A N   
470  C CA  . LEU   A 58  ? 0.59490 1.01300 0.75617 -0.01085 0.00700  -0.06199 55  LEU   A CA  
471  C C   . LEU   A 58  ? 0.61380 1.07008 0.79629 -0.00233 0.00843  -0.08161 55  LEU   A C   
472  O O   . LEU   A 58  ? 0.66662 1.15334 0.86534 -0.01424 0.02385  -0.08604 55  LEU   A O   
473  C CB  . LEU   A 58  ? 0.54978 0.96713 0.71762 -0.01452 0.00265  -0.06185 55  LEU   A CB  
474  C CG  . LEU   A 58  ? 0.61268 1.00204 0.76491 -0.02676 0.00723  -0.04424 55  LEU   A CG  
475  C CD1 . LEU   A 58  ? 0.53740 0.92885 0.69641 -0.03034 0.00371  -0.04650 55  LEU   A CD1 
476  C CD2 . LEU   A 58  ? 0.62778 1.02031 0.77943 -0.04161 0.02382  -0.03409 55  LEU   A CD2 
477  N N   . LYS   A 59  ? 0.58327 1.03795 0.76487 0.01781  -0.00709 -0.09429 56  LYS   A N   
478  C CA  . LYS   A 59  ? 0.61913 1.11289 0.82247 0.02845  -0.00575 -0.11547 56  LYS   A CA  
479  C C   . LYS   A 59  ? 0.70775 1.20851 0.90472 0.02412  0.00779  -0.11453 56  LYS   A C   
480  O O   . LYS   A 59  ? 0.81090 1.34832 1.02584 0.02946  0.01408  -0.13211 56  LYS   A O   
481  C CB  . LYS   A 59  ? 0.70034 1.18642 0.90217 0.05452  -0.02893 -0.13046 56  LYS   A CB  
482  C CG  . LYS   A 59  ? 0.66890 1.17092 0.88919 0.06273  -0.04176 -0.14265 56  LYS   A CG  
483  C CD  . LYS   A 59  ? 0.77587 1.28200 1.00083 0.09157  -0.06415 -0.16358 56  LYS   A CD  
484  C CE  . LYS   A 59  ? 0.68925 1.21993 0.93785 0.10090  -0.07757 -0.17939 56  LYS   A CE  
485  N NZ  . LYS   A 59  ? 0.68437 1.27462 0.97381 0.08585  -0.05910 -0.19135 56  LYS   A NZ  
486  N N   . GLU   A 60  ? 0.70898 1.17737 0.88127 0.01488  0.01223  -0.09586 57  GLU   A N   
487  C CA  . GLU   A 60  ? 0.71768 1.18900 0.87997 0.00930  0.02438  -0.09318 57  GLU   A CA  
488  C C   . GLU   A 60  ? 0.65296 1.11588 0.80590 -0.01224 0.03978  -0.07537 57  GLU   A C   
489  O O   . GLU   A 60  ? 0.70599 1.16319 0.84431 -0.01762 0.04798  -0.06985 57  GLU   A O   
490  C CB  . GLU   A 60  ? 0.82117 1.25980 0.96025 0.02185  0.01161  -0.09040 57  GLU   A CB  
491  C CG  . GLU   A 60  ? 0.87923 1.31886 1.02170 0.04524  -0.00561 -0.10832 57  GLU   A CG  
492  C CD  . GLU   A 60  ? 1.04533 1.45053 1.16232 0.05571  -0.01720 -0.10643 57  GLU   A CD  
493  O OE1 . GLU   A 60  ? 1.07237 1.45372 1.17113 0.04401  -0.01285 -0.09068 57  GLU   A OE1 
494  O OE2 . GLU   A 60  ? 1.02521 1.42683 1.14062 0.07612  -0.03176 -0.12173 57  GLU   A OE2 
495  N N   . LEU   A 61  ? 0.58644 1.04592 0.74517 -0.02342 0.04239  -0.06684 58  LEU   A N   
496  C CA  . LEU   A 61  ? 0.62886 1.07815 0.77824 -0.04200 0.05518  -0.05129 58  LEU   A CA  
497  C C   . LEU   A 61  ? 0.67305 1.14941 0.83957 -0.05638 0.06830  -0.05622 58  LEU   A C   
498  O O   . LEU   A 61  ? 0.73324 1.20077 0.90216 -0.06554 0.06889  -0.04870 58  LEU   A O   
499  C CB  . LEU   A 61  ? 0.69218 1.10816 0.82963 -0.04411 0.04745  -0.03575 58  LEU   A CB  
500  C CG  . LEU   A 61  ? 0.60676 0.99365 0.72530 -0.03728 0.03831  -0.02742 58  LEU   A CG  
501  C CD1 . LEU   A 61  ? 0.54545 0.90744 0.65674 -0.04243 0.03457  -0.01413 58  LEU   A CD1 
502  C CD2 . LEU   A 61  ? 0.55666 0.94134 0.66226 -0.04117 0.04549  -0.02328 58  LEU   A CD2 
503  N N   . ASN   A 62  ? 0.60977 1.11943 0.78801 -0.05949 0.07950  -0.06978 59  ASN   A N   
504  C CA  . ASN   A 62  ? 0.63486 1.17291 0.82963 -0.07689 0.09434  -0.07585 59  ASN   A CA  
505  C C   . ASN   A 62  ? 0.52542 1.04570 0.69691 -0.09709 0.11011  -0.06054 59  ASN   A C   
506  O O   . ASN   A 62  ? 0.59000 1.10964 0.74520 -0.09923 0.11870  -0.05964 59  ASN   A O   
507  C CB  . ASN   A 62  ? 0.64507 1.23075 0.86464 -0.07237 0.10070  -0.09935 59  ASN   A CB  
508  C CG  . ASN   A 62  ? 0.76276 1.38407 1.00804 -0.08942 0.11280  -0.10984 59  ASN   A CG  
509  O OD1 . ASN   A 62  ? 0.89027 1.52622 1.15881 -0.08395 0.10242  -0.11917 59  ASN   A OD1 
510  N ND2 . ASN   A 62  ? 0.77866 1.41267 1.01792 -0.11121 0.13452  -0.10869 59  ASN   A ND2 
511  N N   . HIS   A 63  ? 0.53520 1.03790 0.70203 -0.11097 0.11271  -0.04886 60  HIS   A N   
512  C CA  . HIS   A 63  ? 0.61543 1.09203 0.75567 -0.12816 0.12378  -0.03297 60  HIS   A CA  
513  C C   . HIS   A 63  ? 0.51738 0.99117 0.66336 -0.14573 0.12963  -0.02967 60  HIS   A C   
514  O O   . HIS   A 63  ? 0.50344 0.98101 0.66733 -0.14065 0.11998  -0.03345 60  HIS   A O   
515  C CB  . HIS   A 63  ? 0.57722 1.01327 0.69312 -0.11917 0.11295  -0.01624 60  HIS   A CB  
516  C CG  . HIS   A 63  ? 0.58721 0.99477 0.67270 -0.13194 0.12084  -0.00143 60  HIS   A CG  
517  N ND1 . HIS   A 63  ? 0.58198 0.96238 0.65614 -0.14146 0.12052  0.01089  60  HIS   A ND1 
518  C CD2 . HIS   A 63  ? 0.59112 0.99001 0.65203 -0.13556 0.12777  0.00258  60  HIS   A CD2 
519  C CE1 . HIS   A 63  ? 0.69246 1.04707 0.73595 -0.14958 0.12572  0.02211  60  HIS   A CE1 
520  N NE2 . HIS   A 63  ? 0.62486 0.98987 0.65883 -0.14673 0.13032  0.01775  60  HIS   A NE2 
521  N N   . PRO   A 64  ? 0.58469 1.04870 0.71265 -0.16703 0.14481  -0.02279 61  PRO   A N   
522  C CA  . PRO   A 64  ? 0.51112 0.96845 0.64197 -0.18572 0.15031  -0.01995 61  PRO   A CA  
523  C C   . PRO   A 64  ? 0.65663 1.07757 0.77871 -0.17974 0.13709  -0.00712 61  PRO   A C   
524  O O   . PRO   A 64  ? 0.56998 0.98924 0.70119 -0.18971 0.13709  -0.00852 61  PRO   A O   
525  C CB  . PRO   A 64  ? 0.59974 1.04190 0.70145 -0.20892 0.16821  -0.01201 61  PRO   A CB  
526  C CG  . PRO   A 64  ? 0.56252 1.02694 0.66073 -0.20459 0.17638  -0.01969 61  PRO   A CG  
527  C CD  . PRO   A 64  ? 0.50583 0.96768 0.60992 -0.17670 0.15883  -0.02019 61  PRO   A CD  
528  N N   . ASN   A 65  ? 0.62056 1.01413 0.72623 -0.16436 0.12620  0.00393  62  ASN   A N   
529  C CA  . ASN   A 65  ? 0.58261 0.94551 0.68147 -0.15797 0.11504  0.01427  62  ASN   A CA  
530  C C   . ASN   A 65  ? 0.55141 0.92139 0.66676 -0.13853 0.10094  0.00980  62  ASN   A C   
531  O O   . ASN   A 65  ? 0.53902 0.88534 0.64637 -0.13011 0.09221  0.01830  62  ASN   A O   
532  C CB  . ASN   A 65  ? 0.57398 0.89911 0.64152 -0.15702 0.11331  0.02980  62  ASN   A CB  
533  C CG  . ASN   A 65  ? 0.65521 0.96276 0.69739 -0.17686 0.12580  0.03636  62  ASN   A CG  
534  O OD1 . ASN   A 65  ? 0.73211 1.03880 0.75637 -0.18080 0.13284  0.03836  62  ASN   A OD1 
535  N ND2 . ASN   A 65  ? 0.63632 0.92677 0.67351 -0.19034 0.12863  0.03965  62  ASN   A ND2 
536  N N   . ILE   A 66  ? 0.58760 0.98889 0.72452 -0.13138 0.09848  -0.00407 63  ILE   A N   
537  C CA  . ILE   A 66  ? 0.52713 0.93099 0.67519 -0.11446 0.08448  -0.00879 63  ILE   A CA  
538  C C   . ILE   A 66  ? 0.49286 0.92337 0.66502 -0.11524 0.08181  -0.02322 63  ILE   A C   
539  O O   . ILE   A 66  ? 0.58297 1.04524 0.77120 -0.12056 0.08884  -0.03575 63  ILE   A O   
540  C CB  . ILE   A 66  ? 0.49109 0.90023 0.63681 -0.09984 0.07885  -0.01211 63  ILE   A CB  
541  C CG1 . ILE   A 66  ? 0.52101 0.90553 0.64415 -0.09931 0.07999  0.00092  63  ILE   A CG1 
542  C CG2 . ILE   A 66  ? 0.47654 0.88206 0.62832 -0.08435 0.06406  -0.01638 63  ILE   A CG2 
543  C CD1 . ILE   A 66  ? 0.63689 1.02308 0.75560 -0.08638 0.07383  -0.00215 63  ILE   A CD1 
544  N N   . VAL   A 67  ? 0.52416 0.94336 0.69901 -0.11006 0.07172  -0.02267 64  VAL   A N   
545  C CA  . VAL   A 67  ? 0.49853 0.94040 0.69457 -0.10935 0.06599  -0.03670 64  VAL   A CA  
546  C C   . VAL   A 67  ? 0.55382 1.02185 0.76473 -0.09415 0.05802  -0.05119 64  VAL   A C   
547  O O   . VAL   A 67  ? 0.58809 1.04167 0.78871 -0.07843 0.04745  -0.04888 64  VAL   A O   
548  C CB  . VAL   A 67  ? 0.53414 0.95370 0.72372 -0.10476 0.05540  -0.03267 64  VAL   A CB  
549  C CG1 . VAL   A 67  ? 0.51157 0.95339 0.72128 -0.10322 0.04713  -0.04793 64  VAL   A CG1 
550  C CG2 . VAL   A 67  ? 0.49880 0.89207 0.67379 -0.11733 0.06261  -0.02007 64  VAL   A CG2 
551  N N   . LYS   A 68  ? 0.49239 0.99893 0.72760 -0.09903 0.06291  -0.06723 65  LYS   A N   
552  C CA  . LYS   A 68  ? 0.55815 1.09390 0.80954 -0.08378 0.05688  -0.08350 65  LYS   A CA  
553  C C   . LYS   A 68  ? 0.50113 1.03857 0.76129 -0.06511 0.03609  -0.09413 65  LYS   A C   
554  O O   . LYS   A 68  ? 0.55172 1.09063 0.81998 -0.06872 0.02994  -0.09766 65  LYS   A O   
555  C CB  . LYS   A 68  ? 0.60406 1.18603 0.88140 -0.09601 0.07094  -0.09947 65  LYS   A CB  
556  C CG  . LYS   A 68  ? 0.66722 1.24505 0.93082 -0.11702 0.09236  -0.08932 65  LYS   A CG  
557  C CD  . LYS   A 68  ? 0.69370 1.31255 0.97277 -0.11997 0.10538  -0.10470 65  LYS   A CD  
558  C CE  . LYS   A 68  ? 0.81014 1.48165 1.12979 -0.11876 0.10375  -0.13011 65  LYS   A CE  
559  N NZ  . LYS   A 68  ? 0.89219 1.58194 1.22744 -0.08982 0.08601  -0.14650 65  LYS   A NZ  
560  N N   . LEU   A 69  ? 0.50715 1.04072 0.76228 -0.04484 0.02410  -0.09931 66  LEU   A N   
561  C CA  . LEU   A 69  ? 0.55963 1.09691 0.82195 -0.02442 0.00277  -0.11287 66  LEU   A CA  
562  C C   . LEU   A 69  ? 0.57273 1.16241 0.87017 -0.01786 0.00240  -0.13785 66  LEU   A C   
563  O O   . LEU   A 69  ? 0.57953 1.18803 0.88299 -0.01348 0.00958  -0.14497 66  LEU   A O   
564  C CB  . LEU   A 69  ? 0.58822 1.08956 0.82372 -0.00619 -0.01113 -0.10615 66  LEU   A CB  
565  C CG  . LEU   A 69  ? 0.56369 1.06058 0.79868 0.01763  -0.03553 -0.11982 66  LEU   A CG  
566  C CD1 . LEU   A 69  ? 0.53708 1.01990 0.76728 0.01727  -0.04729 -0.11864 66  LEU   A CD1 
567  C CD2 . LEU   A 69  ? 0.63447 1.09186 0.83894 0.03205  -0.04670 -0.11225 66  LEU   A CD2 
568  N N   . LEU   A 70  ? 0.56189 1.17715 0.88343 -0.01706 -0.00594 -0.15260 67  LEU   A N   
569  C CA  . LEU   A 70  ? 0.51285 1.18652 0.87489 -0.01377 -0.00450 -0.17892 67  LEU   A CA  
570  C C   . LEU   A 70  ? 0.49617 1.18000 0.86742 0.01759  -0.02890 -0.19821 67  LEU   A C   
571  O O   . LEU   A 70  ? 0.59387 1.31749 0.98916 0.02749  -0.02656 -0.21766 67  LEU   A O   
572  C CB  . LEU   A 70  ? 0.59881 1.30071 0.98696 -0.03101 -0.00072 -0.18765 67  LEU   A CB  
573  C CG  . LEU   A 70  ? 0.55302 1.24395 0.93200 -0.06253 0.02238  -0.17080 67  LEU   A CG  
574  C CD1 . LEU   A 70  ? 0.50810 1.22684 0.91360 -0.07954 0.02433  -0.18204 67  LEU   A CD1 
575  C CD2 . LEU   A 70  ? 0.61228 1.31986 0.99180 -0.07652 0.04623  -0.16845 67  LEU   A CD2 
576  N N   . ASP   A 71  ? 0.55262 1.19944 0.90281 0.03400  -0.05255 -0.19388 68  ASP   A N   
577  C CA  . ASP   A 71  ? 0.63142 1.28039 0.98504 0.06515  -0.07929 -0.21194 68  ASP   A CA  
578  C C   . ASP   A 71  ? 0.63141 1.21636 0.94064 0.07766  -0.10012 -0.19611 68  ASP   A C   
579  O O   . ASP   A 71  ? 0.62818 1.18009 0.91447 0.06234  -0.09500 -0.17671 68  ASP   A O   
580  C CB  . ASP   A 71  ? 0.66615 1.36869 1.06331 0.07221  -0.09029 -0.23984 68  ASP   A CB  
581  C CG  . ASP   A 71  ? 0.69635 1.41602 1.10691 0.10634  -0.11506 -0.26454 68  ASP   A CG  
582  O OD1 . ASP   A 71  ? 0.66161 1.35539 1.04974 0.12237  -0.12019 -0.26095 68  ASP   A OD1 
583  O OD2 . ASP   A 71  ? 0.73477 1.49324 1.17834 0.11790  -0.13073 -0.28858 68  ASP   A OD2 
584  N N   . VAL   A 72  ? 0.62492 1.19126 0.92035 0.10555  -0.12340 -0.20523 69  VAL   A N   
585  C CA  . VAL   A 72  ? 0.64873 1.15211 0.89833 0.11884  -0.14555 -0.19284 69  VAL   A CA  
586  C C   . VAL   A 72  ? 0.74924 1.26103 1.00751 0.14825  -0.17697 -0.21618 69  VAL   A C   
587  O O   . VAL   A 72  ? 0.69353 1.21206 0.95669 0.17199  -0.19067 -0.23180 69  VAL   A O   
588  C CB  . VAL   A 72  ? 0.69794 1.15405 0.90949 0.12305  -0.14468 -0.17712 69  VAL   A CB  
589  C CG1 . VAL   A 72  ? 0.64432 1.03396 0.80592 0.13314  -0.16610 -0.16447 69  VAL   A CG1 
590  C CG2 . VAL   A 72  ? 0.62517 1.07820 0.83220 0.09614  -0.11554 -0.15675 69  VAL   A CG2 
591  N N   . ILE   A 73  ? 0.75697 1.26744 1.01631 0.14827  -0.18997 -0.21973 70  ILE   A N   
592  C CA  . ILE   A 73  ? 0.71852 1.23815 0.98688 0.17638  -0.22234 -0.24284 70  ILE   A CA  
593  C C   . ILE   A 73  ? 0.79244 1.23659 1.00105 0.18983  -0.24727 -0.22877 70  ILE   A C   
594  O O   . ILE   A 73  ? 0.85002 1.25543 1.02638 0.17166  -0.23956 -0.20709 70  ILE   A O   
595  C CB  . ILE   A 73  ? 0.80811 1.38128 1.12014 0.16771  -0.22215 -0.25974 70  ILE   A CB  
596  C CG1 . ILE   A 73  ? 0.71429 1.35394 1.07715 0.14499  -0.19098 -0.26790 70  ILE   A CG1 
597  C CG2 . ILE   A 73  ? 0.68296 1.27830 1.01443 0.19967  -0.25647 -0.28903 70  ILE   A CG2 
598  C CD1 . ILE   A 73  ? 0.83169 1.52462 1.23842 0.13127  -0.18773 -0.28426 70  ILE   A CD1 
599  N N   . HIS   A 74  ? 0.77900 1.20067 0.97071 0.22162  -0.27704 -0.24166 71  HIS   A N   
600  C CA  . HIS   A 74  ? 0.99150 1.33682 1.12116 0.23647  -0.30389 -0.23023 71  HIS   A CA  
601  C C   . HIS   A 74  ? 1.00616 1.36084 1.14387 0.26467  -0.33970 -0.25406 71  HIS   A C   
602  O O   . HIS   A 74  ? 1.04405 1.43917 1.21711 0.29019  -0.35599 -0.28131 71  HIS   A O   
603  C CB  . HIS   A 74  ? 0.89584 1.19122 0.98670 0.25022  -0.31161 -0.22255 71  HIS   A CB  
604  C CG  . HIS   A 74  ? 1.00368 1.22109 1.03080 0.26994  -0.34402 -0.21608 71  HIS   A CG  
605  N ND1 . HIS   A 74  ? 1.06454 1.25581 1.07378 0.30335  -0.37430 -0.23063 71  HIS   A ND1 
606  C CD2 . HIS   A 74  ? 1.05971 1.21664 1.03315 0.26071  -0.35095 -0.19684 71  HIS   A CD2 
607  C CE1 . HIS   A 74  ? 1.11799 1.23197 1.06229 0.31308  -0.39920 -0.21927 71  HIS   A CE1 
608  N NE2 . HIS   A 74  ? 1.16625 1.25925 1.08762 0.28677  -0.38462 -0.19869 71  HIS   A NE2 
609  N N   . THR   A 75  ? 1.07667 1.39505 1.18169 0.26107  -0.35251 -0.24516 72  THR   A N   
610  C CA  . THR   A 75  ? 1.14242 1.46610 1.25120 0.28715  -0.38850 -0.26691 72  THR   A CA  
611  C C   . THR   A 75  ? 1.17176 1.42557 1.21717 0.28285  -0.40260 -0.24849 72  THR   A C   
612  O O   . THR   A 75  ? 1.13132 1.37148 1.16187 0.25318  -0.37822 -0.22745 72  THR   A O   
613  C CB  . THR   A 75  ? 1.12762 1.53955 1.31004 0.28137  -0.38192 -0.29159 72  THR   A CB  
614  O OG1 . THR   A 75  ? 1.25070 1.66386 1.43315 0.30372  -0.41754 -0.31075 72  THR   A OG1 
615  C CG2 . THR   A 75  ? 0.98450 1.41627 1.18169 0.24152  -0.34591 -0.27443 72  THR   A CG2 
616  N N   . GLU   A 76  ? 1.27334 1.48125 1.27917 0.31360  -0.44252 -0.25717 73  GLU   A N   
617  C CA  . GLU   A 76  ? 1.43885 1.58211 1.38298 0.31414  -0.46178 -0.24473 73  GLU   A CA  
618  C C   . GLU   A 76  ? 1.42557 1.49741 1.30463 0.28842  -0.44035 -0.20970 73  GLU   A C   
619  O O   . GLU   A 76  ? 1.41249 1.46076 1.26398 0.26851  -0.43067 -0.19483 73  GLU   A O   
620  C CB  . GLU   A 76  ? 1.48058 1.66932 1.45919 0.30300  -0.46029 -0.25512 73  GLU   A CB  
621  C CG  . GLU   A 76  ? 1.50687 1.77060 1.55548 0.32154  -0.47378 -0.28959 73  GLU   A CG  
622  C CD  . GLU   A 76  ? 1.57048 1.88759 1.66186 0.30199  -0.46361 -0.29843 73  GLU   A CD  
623  O OE1 . GLU   A 76  ? 1.57100 1.87169 1.64246 0.27388  -0.44343 -0.27803 73  GLU   A OE1 
624  O OE2 . GLU   A 76  ? 1.60435 1.97213 1.74659 0.31079  -0.46770 -0.32335 73  GLU   A OE2 
625  N N   . ASN   A 77  ? 1.27244 1.31084 1.12742 0.28876  -0.43297 -0.19790 74  ASN   A N   
626  C CA  . ASN   A 77  ? 1.37032 1.34807 1.17028 0.26277  -0.41053 -0.16670 74  ASN   A CA  
627  C C   . ASN   A 77  ? 1.23050 1.24696 1.06112 0.22672  -0.36986 -0.15317 74  ASN   A C   
628  O O   . ASN   A 77  ? 1.20677 1.18144 0.99564 0.20378  -0.35298 -0.13055 74  ASN   A O   
629  C CB  . ASN   A 77  ? 1.37200 1.26194 1.08810 0.26699  -0.43276 -0.15274 74  ASN   A CB  
630  C CG  . ASN   A 77  ? 1.57183 1.39234 1.23216 0.29064  -0.46116 -0.15141 74  ASN   A CG  
631  O OD1 . ASN   A 77  ? 1.63194 1.43953 1.28308 0.32448  -0.49964 -0.17005 74  ASN   A OD1 
632  N ND2 . ASN   A 77  ? 1.38127 1.15514 1.00325 0.27310  -0.44351 -0.13004 74  ASN   A ND2 
633  N N   . LYS   A 78  ? 1.16937 1.26565 1.07235 0.22166  -0.35414 -0.16799 75  LYS   A N   
634  C CA  . LYS   A 78  ? 1.12358 1.25834 1.05908 0.18978  -0.31690 -0.15709 75  LYS   A CA  
635  C C   . LYS   A 78  ? 1.09493 1.28099 1.08028 0.18468  -0.29569 -0.16226 75  LYS   A C   
636  O O   . LYS   A 78  ? 1.02512 1.24736 1.04454 0.20558  -0.30897 -0.18353 75  LYS   A O   
637  C CB  . LYS   A 78  ? 1.17015 1.34882 1.14050 0.18308  -0.31667 -0.16895 75  LYS   A CB  
638  C CG  . LYS   A 78  ? 1.06422 1.19732 0.98769 0.17055  -0.31728 -0.15441 75  LYS   A CG  
639  C CD  . LYS   A 78  ? 1.29151 1.38826 1.17812 0.19539  -0.35612 -0.16514 75  LYS   A CD  
640  C CE  . LYS   A 78  ? 1.32812 1.48721 1.27098 0.21184  -0.37553 -0.19464 75  LYS   A CE  
641  N NZ  . LYS   A 78  ? 1.24044 1.44865 1.22537 0.18835  -0.35474 -0.19777 75  LYS   A NZ  
642  N N   . LEU   A 79  ? 1.05408 1.24285 1.04226 0.15778  -0.26328 -0.14371 76  LEU   A N   
643  C CA  . LEU   A 79  ? 0.94152 1.17423 0.97082 0.14923  -0.24049 -0.14552 76  LEU   A CA  
644  C C   . LEU   A 79  ? 0.85979 1.13932 0.92831 0.12414  -0.21350 -0.14306 76  LEU   A C   
645  O O   . LEU   A 79  ? 0.91362 1.17092 0.96216 0.10321  -0.19636 -0.12445 76  LEU   A O   
646  C CB  . LEU   A 79  ? 0.87383 1.06389 0.86864 0.14096  -0.22853 -0.12600 76  LEU   A CB  
647  C CG  . LEU   A 79  ? 0.88653 1.11169 0.91404 0.13913  -0.21246 -0.12987 76  LEU   A CG  
648  C CD1 . LEU   A 79  ? 0.85008 1.09894 0.89919 0.16805  -0.23406 -0.15419 76  LEU   A CD1 
649  C CD2 . LEU   A 79  ? 0.83478 1.01589 0.82677 0.12772  -0.20068 -0.10957 76  LEU   A CD2 
650  N N   . TYR   A 80  ? 0.82215 1.16539 0.94527 0.12601  -0.20984 -0.16265 77  TYR   A N   
651  C CA  . TYR   A 80  ? 0.78363 1.17031 0.94352 0.10195  -0.18591 -0.16226 77  TYR   A CA  
652  C C   . TYR   A 80  ? 0.76318 1.17841 0.94732 0.08823  -0.15934 -0.15756 77  TYR   A C   
653  O O   . TYR   A 80  ? 0.75988 1.20426 0.96721 0.10059  -0.16158 -0.17158 77  TYR   A O   
654  C CB  . TYR   A 80  ? 0.78455 1.22371 0.98826 0.10820  -0.19751 -0.18738 77  TYR   A CB  
655  C CG  . TYR   A 80  ? 0.88258 1.29777 1.06513 0.11510  -0.21971 -0.19063 77  TYR   A CG  
656  C CD1 . TYR   A 80  ? 0.90748 1.31587 1.08428 0.09394  -0.20809 -0.18081 77  TYR   A CD1 
657  C CD2 . TYR   A 80  ? 1.00777 1.40439 1.17335 0.14393  -0.25368 -0.20415 77  TYR   A CD2 
658  C CE1 . TYR   A 80  ? 0.92802 1.31338 1.08286 0.10019  -0.22843 -0.18438 77  TYR   A CE1 
659  C CE2 . TYR   A 80  ? 1.00952 1.38129 1.15145 0.15072  -0.27541 -0.20713 77  TYR   A CE2 
660  C CZ  . TYR   A 80  ? 1.01841 1.38552 1.15517 0.12821  -0.26204 -0.19724 77  TYR   A CZ  
661  O OH  . TYR   A 80  ? 1.16177 1.50310 1.27252 0.13496  -0.28372 -0.20080 77  TYR   A OH  
662  N N   . LEU   A 81  ? 0.72713 1.13305 0.90434 0.06400  -0.13521 -0.13881 78  LEU   A N   
663  C CA  . LEU   A 81  ? 0.69922 1.12854 0.89536 0.04874  -0.10989 -0.13265 78  LEU   A CA  
664  C C   . LEU   A 81  ? 0.67106 1.14227 0.90221 0.02878  -0.09322 -0.13797 78  LEU   A C   
665  O O   . LEU   A 81  ? 0.67212 1.12871 0.89388 0.01465  -0.08776 -0.12864 78  LEU   A O   
666  C CB  . LEU   A 81  ? 0.71725 1.10383 0.87913 0.03698  -0.09640 -0.10829 78  LEU   A CB  
667  C CG  . LEU   A 81  ? 0.73653 1.08490 0.86651 0.04929  -0.10486 -0.10072 78  LEU   A CG  
668  C CD1 . LEU   A 81  ? 0.67927 0.98463 0.77337 0.06512  -0.12949 -0.10104 78  LEU   A CD1 
669  C CD2 . LEU   A 81  ? 0.75315 1.07722 0.86408 0.03248  -0.08600 -0.07974 78  LEU   A CD2 
670  N N   . VAL   A 82  ? 0.52330 1.04492 0.79282 0.02688  -0.08475 -0.15351 79  VAL   A N   
671  C CA  . VAL   A 82  ? 0.49324 1.05640 0.79645 0.00594  -0.06858 -0.16071 79  VAL   A CA  
672  C C   . VAL   A 82  ? 0.58205 1.14242 0.88080 -0.01525 -0.04156 -0.14469 79  VAL   A C   
673  O O   . VAL   A 82  ? 0.55777 1.12931 0.86002 -0.01228 -0.03296 -0.14544 79  VAL   A O   
674  C CB  . VAL   A 82  ? 0.57902 1.20250 0.92769 0.01374  -0.07366 -0.18903 79  VAL   A CB  
675  C CG1 . VAL   A 82  ? 0.44102 1.10469 0.82252 -0.01128 -0.05785 -0.19699 79  VAL   A CG1 
676  C CG2 . VAL   A 82  ? 0.56332 1.18548 0.91306 0.04100  -0.10509 -0.20579 79  VAL   A CG2 
677  N N   . PHE   A 83  ? 0.53724 1.08084 0.82636 -0.03538 -0.02953 -0.13098 80  PHE   A N   
678  C CA  . PHE   A 83  ? 0.50898 1.04232 0.78863 -0.05437 -0.00698 -0.11465 80  PHE   A CA  
679  C C   . PHE   A 83  ? 0.50538 1.06768 0.80809 -0.07807 0.00913  -0.11990 80  PHE   A C   
680  O O   . PHE   A 83  ? 0.53718 1.12008 0.85977 -0.08295 0.00317  -0.13278 80  PHE   A O   
681  C CB  . PHE   A 83  ? 0.56134 1.04486 0.80610 -0.05783 -0.00593 -0.09312 80  PHE   A CB  
682  C CG  . PHE   A 83  ? 0.54582 0.99754 0.76402 -0.04161 -0.01537 -0.08422 80  PHE   A CG  
683  C CD1 . PHE   A 83  ? 0.60462 1.04733 0.81255 -0.04234 -0.00562 -0.07423 80  PHE   A CD1 
684  C CD2 . PHE   A 83  ? 0.64495 1.07285 0.84538 -0.02704 -0.03423 -0.08566 80  PHE   A CD2 
685  C CE1 . PHE   A 83  ? 0.57715 0.99012 0.76097 -0.03001 -0.01407 -0.06662 80  PHE   A CE1 
686  C CE2 . PHE   A 83  ? 0.62680 1.02161 0.79932 -0.01543 -0.04185 -0.07690 80  PHE   A CE2 
687  C CZ  . PHE   A 83  ? 0.58395 0.97239 0.74977 -0.01756 -0.03151 -0.06771 80  PHE   A CZ  
688  N N   . GLU   A 84  ? 0.55267 1.11359 0.84987 -0.09363 0.02908  -0.10967 81  GLU   A N   
689  C CA  . GLU   A 84  ? 0.43046 1.00108 0.73568 -0.11987 0.04597  -0.10809 81  GLU   A CA  
690  C C   . GLU   A 84  ? 0.53612 1.07043 0.82277 -0.12771 0.04270  -0.09615 81  GLU   A C   
691  O O   . GLU   A 84  ? 0.50585 1.00229 0.76644 -0.11757 0.03607  -0.08234 81  GLU   A O   
692  C CB  . GLU   A 84  ? 0.50802 1.07282 0.80026 -0.13243 0.06559  -0.09667 81  GLU   A CB  
693  C CG  . GLU   A 84  ? 0.65694 1.21789 0.94561 -0.16074 0.08335  -0.09066 81  GLU   A CG  
694  C CD  . GLU   A 84  ? 0.64332 1.18363 0.90715 -0.16979 0.09874  -0.07528 81  GLU   A CD  
695  O OE1 . GLU   A 84  ? 0.56992 1.09409 0.81821 -0.15376 0.09418  -0.06719 81  GLU   A OE1 
696  O OE2 . GLU   A 84  ? 0.74651 1.28436 1.00411 -0.19346 0.11458  -0.07137 81  GLU   A OE2 
697  N N   . PHE   A 85  ? 0.47216 1.01889 0.77260 -0.14651 0.04780  -0.10270 82  PHE   A N   
698  C CA  . PHE   A 85  ? 0.51733 1.03181 0.80204 -0.15360 0.04363  -0.09483 82  PHE   A CA  
699  C C   . PHE   A 85  ? 0.51937 1.00758 0.78559 -0.17501 0.06052  -0.08001 82  PHE   A C   
700  O O   . PHE   A 85  ? 0.55438 1.06066 0.82994 -0.19435 0.07555  -0.08289 82  PHE   A O   
701  C CB  . PHE   A 85  ? 0.50711 1.04673 0.81635 -0.15882 0.03386  -0.11293 82  PHE   A CB  
702  C CG  . PHE   A 85  ? 0.53552 1.04225 0.82814 -0.16788 0.03038  -0.10653 82  PHE   A CG  
703  C CD1 . PHE   A 85  ? 0.48988 0.96356 0.75944 -0.15144 0.01646  -0.09982 82  PHE   A CD1 
704  C CD2 . PHE   A 85  ? 0.48576 0.99248 0.78321 -0.19371 0.04164  -0.10757 82  PHE   A CD2 
705  C CE1 . PHE   A 85  ? 0.61221 1.05627 0.86565 -0.15867 0.01384  -0.09545 82  PHE   A CE1 
706  C CE2 . PHE   A 85  ? 0.57664 1.05036 0.85720 -0.20086 0.03748  -0.10271 82  PHE   A CE2 
707  C CZ  . PHE   A 85  ? 0.51643 0.96021 0.77588 -0.18236 0.02358  -0.09722 82  PHE   A CZ  
708  N N   . LEU   A 86  ? 0.53139 0.97595 0.76976 -0.17125 0.05780  -0.06486 83  LEU   A N   
709  C CA  . LEU   A 86  ? 0.53955 0.95141 0.75699 -0.18753 0.06867  -0.05166 83  LEU   A CA  
710  C C   . LEU   A 86  ? 0.54688 0.93054 0.75256 -0.18660 0.05973  -0.05012 83  LEU   A C   
711  O O   . LEU   A 86  ? 0.52404 0.90076 0.72541 -0.16951 0.04723  -0.05158 83  LEU   A O   
712  C CB  . LEU   A 86  ? 0.59810 0.98389 0.79173 -0.18089 0.07476  -0.03484 83  LEU   A CB  
713  C CG  . LEU   A 86  ? 0.69445 1.10174 0.89311 -0.18242 0.08449  -0.03483 83  LEU   A CG  
714  C CD1 . LEU   A 86  ? 0.59224 1.01844 0.80059 -0.16084 0.07525  -0.04027 83  LEU   A CD1 
715  C CD2 . LEU   A 86  ? 0.44697 0.82249 0.61825 -0.18761 0.09362  -0.01818 83  LEU   A CD2 
716  N N   . HIS   A 87  ? 0.59586 0.96018 0.79295 -0.20567 0.06638  -0.04725 84  HIS   A N   
717  C CA  . HIS   A 87  ? 0.59929 0.94456 0.79091 -0.20802 0.05775  -0.05128 84  HIS   A CA  
718  C C   . HIS   A 87  ? 0.65629 0.95853 0.81962 -0.19557 0.05385  -0.03901 84  HIS   A C   
719  O O   . HIS   A 87  ? 0.69166 0.97834 0.84847 -0.19280 0.04550  -0.04328 84  HIS   A O   
720  C CB  . HIS   A 87  ? 0.53768 0.87908 0.73202 -0.23516 0.06556  -0.05539 84  HIS   A CB  
721  C CG  . HIS   A 87  ? 0.65034 0.94588 0.81415 -0.24524 0.07394  -0.04018 84  HIS   A CG  
722  N ND1 . HIS   A 87  ? 0.69733 0.98098 0.84591 -0.24601 0.08399  -0.02731 84  HIS   A ND1 
723  C CD2 . HIS   A 87  ? 0.76199 1.01789 0.90552 -0.25339 0.07188  -0.03653 84  HIS   A CD2 
724  C CE1 . HIS   A 87  ? 0.72170 0.95969 0.84150 -0.25343 0.08675  -0.01615 84  HIS   A CE1 
725  N NE2 . HIS   A 87  ? 0.87941 1.09942 0.99585 -0.25779 0.07970  -0.02162 84  HIS   A NE2 
726  N N   . GLN   A 88  ? 0.65519 0.93986 0.80259 -0.18766 0.05930  -0.02559 85  GLN   A N   
727  C CA  . GLN   A 88  ? 0.61891 0.86740 0.74358 -0.17667 0.05656  -0.01637 85  GLN   A CA  
728  C C   . GLN   A 88  ? 0.63080 0.87610 0.74796 -0.16309 0.05928  -0.00587 85  GLN   A C   
729  O O   . GLN   A 88  ? 0.60806 0.86532 0.72876 -0.16704 0.06573  -0.00192 85  GLN   A O   
730  C CB  . GLN   A 88  ? 0.67806 0.89173 0.78502 -0.18996 0.06059  -0.01142 85  GLN   A CB  
731  C CG  . GLN   A 88  ? 0.75681 0.93571 0.84376 -0.17734 0.05591  -0.00676 85  GLN   A CG  
732  C CD  . GLN   A 88  ? 0.90204 1.04405 0.97109 -0.18942 0.05653  -0.00513 85  GLN   A CD  
733  O OE1 . GLN   A 88  ? 1.03016 1.15869 1.09499 -0.19069 0.05079  -0.01239 85  GLN   A OE1 
734  N NE2 . GLN   A 88  ? 0.87277 0.99443 0.92758 -0.19824 0.06260  0.00439  85  GLN   A NE2 
735  N N   . ASP   A 89  ? 0.60305 0.83336 0.70980 -0.14798 0.05475  -0.00249 86  ASP   A N   
736  C CA  . ASP   A 89  ? 0.61371 0.83902 0.71370 -0.13620 0.05686  0.00657  86  ASP   A CA  
737  C C   . ASP   A 89  ? 0.70367 0.89867 0.78746 -0.13625 0.05965  0.01459  86  ASP   A C   
738  O O   . ASP   A 89  ? 0.68482 0.85793 0.75939 -0.14301 0.05896  0.01318  86  ASP   A O   
739  C CB  . ASP   A 89  ? 0.65725 0.88541 0.75553 -0.12174 0.05175  0.00480  86  ASP   A CB  
740  C CG  . ASP   A 89  ? 0.72954 0.93782 0.81674 -0.11817 0.04902  0.00154  86  ASP   A CG  
741  O OD1 . ASP   A 89  ? 0.72220 0.91179 0.79991 -0.11326 0.05164  0.00587  86  ASP   A OD1 
742  O OD2 . ASP   A 89  ? 1.05630 1.26801 1.14398 -0.11913 0.04344  -0.00653 86  ASP   A OD2 
743  N N   . LEU   A 90  ? 0.64675 0.83902 0.72630 -0.12769 0.06120  0.02226  87  LEU   A N   
744  C CA  . LEU   A 90  ? 0.71954 0.88341 0.78357 -0.12518 0.06126  0.02925  87  LEU   A CA  
745  C C   . LEU   A 90  ? 0.67441 0.81972 0.73210 -0.11496 0.05732  0.02594  87  LEU   A C   
746  O O   . LEU   A 90  ? 0.75438 0.87059 0.79803 -0.11600 0.05529  0.02729  87  LEU   A O   
747  C CB  . LEU   A 90  ? 0.59968 0.76817 0.66253 -0.11701 0.06172  0.03641  87  LEU   A CB  
748  C CG  . LEU   A 90  ? 0.59582 0.73476 0.64148 -0.11198 0.05888  0.04330  87  LEU   A CG  
749  C CD1 . LEU   A 90  ? 0.71743 0.83231 0.74505 -0.12755 0.06140  0.04807  87  LEU   A CD1 
750  C CD2 . LEU   A 90  ? 0.66902 0.81654 0.71635 -0.10166 0.05702  0.04824  87  LEU   A CD2 
751  N N   . LYS   A 91  ? 0.68271 0.84230 0.74804 -0.10528 0.05639  0.02111  88  LYS   A N   
752  C CA  . LYS   A 91  ? 0.64755 0.79362 0.70724 -0.09536 0.05483  0.01635  88  LYS   A CA  
753  C C   . LYS   A 91  ? 0.70536 0.83110 0.75583 -0.10210 0.05241  0.01071  88  LYS   A C   
754  O O   . LYS   A 91  ? 0.73577 0.83697 0.77562 -0.09640 0.05021  0.00884  88  LYS   A O   
755  C CB  . LYS   A 91  ? 0.73045 0.89511 0.79609 -0.08820 0.05640  0.01208  88  LYS   A CB  
756  C CG  . LYS   A 91  ? 0.62461 0.78010 0.68497 -0.07825 0.05766  0.00598  88  LYS   A CG  
757  C CD  . LYS   A 91  ? 0.91165 1.07114 0.96644 -0.07943 0.05829  -0.00091 88  LYS   A CD  
758  C CE  . LYS   A 91  ? 1.00573 1.18201 1.06241 -0.07523 0.06280  -0.00066 88  LYS   A CE  
759  N NZ  . LYS   A 91  ? 0.95294 1.12715 0.99687 -0.07683 0.06279  -0.00625 88  LYS   A NZ  
760  N N   . LYS   A 92  ? 0.67471 0.81053 0.72972 -0.11342 0.05158  0.00657  89  LYS   A N   
761  C CA  . LYS   A 92  ? 0.69389 0.81168 0.74146 -0.12238 0.04851  0.00035  89  LYS   A CA  
762  C C   . LYS   A 92  ? 0.78147 0.87250 0.81786 -0.13271 0.04901  0.00537  89  LYS   A C   
763  O O   . LYS   A 92  ? 0.72750 0.78993 0.75068 -0.13572 0.04576  0.00185  89  LYS   A O   
764  C CB  . LYS   A 92  ? 0.84865 0.98809 0.90736 -0.13241 0.04614  -0.00642 89  LYS   A CB  
765  C CG  . LYS   A 92  ? 0.93988 1.06543 0.99321 -0.14095 0.04128  -0.01545 89  LYS   A CG  
766  C CD  . LYS   A 92  ? 0.96397 1.11648 1.03264 -0.14975 0.03712  -0.02350 89  LYS   A CD  
767  C CE  . LYS   A 92  ? 1.07435 1.21584 1.13865 -0.15682 0.03014  -0.03438 89  LYS   A CE  
768  N NZ  . LYS   A 92  ? 1.10213 1.27362 1.18467 -0.16385 0.02388  -0.04414 89  LYS   A NZ  
769  N N   . PHE   A 93  ? 0.75439 0.85061 0.79211 -0.13856 0.05281  0.01363  90  PHE   A N   
770  C CA  . PHE   A 93  ? 0.74798 0.81357 0.76826 -0.14969 0.05375  0.02015  90  PHE   A CA  
771  C C   . PHE   A 93  ? 0.77907 0.81128 0.78147 -0.13463 0.04874  0.02445  90  PHE   A C   
772  O O   . PHE   A 93  ? 0.79677 0.78990 0.77828 -0.13932 0.04511  0.02591  90  PHE   A O   
773  C CB  . PHE   A 93  ? 0.78671 0.86819 0.81054 -0.16034 0.06010  0.02714  90  PHE   A CB  
774  C CG  . PHE   A 93  ? 0.77172 0.81848 0.77130 -0.17303 0.06218  0.03569  90  PHE   A CG  
775  C CD1 . PHE   A 93  ? 0.78366 0.81430 0.77427 -0.19553 0.06545  0.03384  90  PHE   A CD1 
776  C CD2 . PHE   A 93  ? 0.78269 0.81126 0.76631 -0.16354 0.06035  0.04542  90  PHE   A CD2 
777  C CE1 . PHE   A 93  ? 0.79308 0.78598 0.75527 -0.20979 0.06808  0.04280  90  PHE   A CE1 
778  C CE2 . PHE   A 93  ? 0.91544 0.90565 0.86979 -0.17516 0.06107  0.05428  90  PHE   A CE2 
779  C CZ  . PHE   A 93  ? 0.86300 0.83342 0.80468 -0.19909 0.06559  0.05362  90  PHE   A CZ  
780  N N   . MET   A 94  ? 0.74984 0.79643 0.76022 -0.11636 0.04765  0.02551  91  MET   A N   
781  C CA  . MET   A 94  ? 0.80041 0.82237 0.79951 -0.09913 0.04160  0.02640  91  MET   A CA  
782  C C   . MET   A 94  ? 0.75587 0.76047 0.74991 -0.09075 0.03772  0.01660  91  MET   A C   
783  O O   . MET   A 94  ? 0.81359 0.78304 0.79072 -0.08212 0.03095  0.01583  91  MET   A O   
784  C CB  . MET   A 94  ? 0.75610 0.80492 0.77023 -0.08354 0.04210  0.02739  91  MET   A CB  
785  C CG  . MET   A 94  ? 0.86289 0.92888 0.88119 -0.09023 0.04526  0.03588  91  MET   A CG  
786  S SD  . MET   A 94  ? 1.02788 1.13151 1.06764 -0.07667 0.04678  0.03479  91  MET   A SD  
787  C CE  . MET   A 94  ? 0.79623 0.88049 0.82891 -0.05800 0.03793  0.03592  91  MET   A CE  
788  N N   . ASP   A 95  ? 0.74951 0.77581 0.75532 -0.09208 0.04091  0.00847  92  ASP   A N   
789  C CA  . ASP   A 95  ? 0.86469 0.87477 0.86330 -0.08509 0.03800  -0.00187 92  ASP   A CA  
790  C C   . ASP   A 95  ? 0.82029 0.79310 0.80025 -0.09811 0.03337  -0.00291 92  ASP   A C   
791  O O   . ASP   A 95  ? 0.85256 0.79285 0.81721 -0.08938 0.02766  -0.00823 92  ASP   A O   
792  C CB  . ASP   A 95  ? 0.82485 0.86326 0.83468 -0.08536 0.04196  -0.00940 92  ASP   A CB  
793  C CG  . ASP   A 95  ? 0.86629 0.93434 0.88944 -0.07310 0.04696  -0.00954 92  ASP   A CG  
794  O OD1 . ASP   A 95  ? 0.89246 0.96245 0.92002 -0.06327 0.04687  -0.00558 92  ASP   A OD1 
795  O OD2 . ASP   A 95  ? 0.87314 0.96081 0.90065 -0.07396 0.05030  -0.01382 92  ASP   A OD2 
796  N N   . ALA   A 96  ? 0.77108 0.74840 0.75243 -0.11941 0.03583  0.00096  93  ALA   A N   
797  C CA  . ALA   A 96  ? 0.85957 0.80213 0.82347 -0.13652 0.03277  0.00037  93  ALA   A CA  
798  C C   . ALA   A 96  ? 0.87336 0.77214 0.81235 -0.13646 0.02887  0.00926  93  ALA   A C   
799  O O   . ALA   A 96  ? 0.97098 0.82729 0.88765 -0.14537 0.02403  0.00813  93  ALA   A O   
800  C CB  . ALA   A 96  ? 0.72898 0.69460 0.70498 -0.16060 0.03792  0.00071  93  ALA   A CB  
801  N N   . SER   A 97  ? 0.87978 0.78451 0.81921 -0.12676 0.02957  0.01795  94  SER   A N   
802  C CA  . SER   A 97  ? 0.89496 0.75592 0.80695 -0.12420 0.02365  0.02700  94  SER   A CA  
803  C C   . SER   A 97  ? 0.99716 0.84180 0.90401 -0.09518 0.01405  0.02319  94  SER   A C   
804  O O   . SER   A 97  ? 1.02028 0.83146 0.90577 -0.08710 0.00625  0.03009  94  SER   A O   
805  C CB  . SER   A 97  ? 0.94159 0.81664 0.85370 -0.13303 0.02917  0.03868  94  SER   A CB  
806  O OG  . SER   A 97  ? 0.92383 0.82184 0.84569 -0.15833 0.03913  0.03960  94  SER   A OG  
807  N N   . ALA   A 98  ? 0.92936 0.79698 0.85438 -0.07920 0.01423  0.01144  95  ALA   A N   
808  C CA  . ALA   A 98  ? 1.02324 0.88854 0.95150 -0.05115 0.00744  0.00507  95  ALA   A CA  
809  C C   . ALA   A 98  ? 1.10694 0.91487 1.00594 -0.04049 -0.00540 0.00242  95  ALA   A C   
810  O O   . ALA   A 98  ? 1.11584 0.91009 1.00985 -0.01885 -0.01488 0.00150  95  ALA   A O   
811  C CB  . ALA   A 98  ? 0.97511 0.87740 0.92651 -0.04022 0.01329  -0.00788 95  ALA   A CB  
812  N N   . LEU   A 99  ? 1.03310 0.80587 0.91219 -0.05467 -0.00737 0.00024  96  LEU   A N   
813  C CA  . LEU   A 99  ? 1.22030 0.93206 1.06759 -0.04487 -0.02075 -0.00289 96  LEU   A CA  
814  C C   . LEU   A 99  ? 1.27373 0.93832 1.08854 -0.05218 -0.02847 0.01171  96  LEU   A C   
815  O O   . LEU   A 99  ? 1.28536 0.91748 1.08291 -0.03018 -0.04186 0.01187  96  LEU   A O   
816  C CB  . LEU   A 99  ? 1.19727 0.88418 1.03187 -0.05974 -0.02074 -0.01027 96  LEU   A CB  
817  C CG  . LEU   A 99  ? 1.19666 0.91775 1.05328 -0.05083 -0.01563 -0.02587 96  LEU   A CG  
818  C CD1 . LEU   A 99  ? 1.20312 0.89038 1.04137 -0.06495 -0.01898 -0.03322 96  LEU   A CD1 
819  C CD2 . LEU   A 99  ? 1.20805 0.93811 1.07397 -0.01729 -0.02021 -0.03773 96  LEU   A CD2 
820  N N   . THR   A 100 ? 1.28966 0.95009 1.09477 -0.08267 -0.02041 0.02325  97  THR   A N   
821  C CA  . THR   A 100 ? 1.33080 0.94246 1.09867 -0.09440 -0.02538 0.03790  97  THR   A CA  
822  C C   . THR   A 100 ? 1.29217 0.92848 1.06726 -0.08711 -0.02388 0.04765  97  THR   A C   
823  O O   . THR   A 100 ? 1.27046 0.86277 1.01073 -0.08889 -0.03126 0.05917  97  THR   A O   
824  C CB  . THR   A 100 ? 1.36521 0.96261 1.11862 -0.13313 -0.01528 0.04473  97  THR   A CB  
825  O OG1 . THR   A 100 ? 1.33429 0.99714 1.12440 -0.14806 0.00015  0.04423  97  THR   A OG1 
826  C CG2 . THR   A 100 ? 1.42222 0.98771 1.16399 -0.14186 -0.01907 0.03508  97  THR   A CG2 
827  N N   . GLY   A 101 ? 1.26662 0.96806 1.08226 -0.07952 -0.01531 0.04346  98  GLY   A N   
828  C CA  . GLY   A 101 ? 1.16921 0.89608 0.99301 -0.07450 -0.01361 0.05176  98  GLY   A CA  
829  C C   . GLY   A 101 ? 1.10697 0.84649 0.92685 -0.10416 -0.00069 0.06269  98  GLY   A C   
830  O O   . GLY   A 101 ? 1.15300 0.86458 0.95193 -0.12954 0.00420  0.06681  98  GLY   A O   
831  N N   . ILE   A 102 ? 1.17019 0.95352 1.01128 -0.10186 0.00545  0.06603  99  ILE   A N   
832  C CA  . ILE   A 102 ? 1.07442 0.87126 0.91124 -0.12676 0.01744  0.07528  99  ILE   A CA  
833  C C   . ILE   A 102 ? 1.12467 0.87129 0.91772 -0.13009 0.01102  0.08851  99  ILE   A C   
834  O O   . ILE   A 102 ? 1.19109 0.92344 0.97505 -0.10638 -0.00197 0.09045  99  ILE   A O   
835  C CB  . ILE   A 102 ? 1.05533 0.91432 0.92857 -0.12182 0.02528  0.07294  99  ILE   A CB  
836  C CG1 . ILE   A 102 ? 0.94514 0.84617 0.85460 -0.11704 0.02973  0.06064  99  ILE   A CG1 
837  C CG2 . ILE   A 102 ? 0.97638 0.85221 0.84708 -0.14614 0.03807  0.07987  99  ILE   A CG2 
838  C CD1 . ILE   A 102 ? 0.84079 0.79723 0.78214 -0.11332 0.03663  0.05843  99  ILE   A CD1 
839  N N   . PRO   A 103 ? 1.15775 0.87643 0.92218 -0.15902 0.01932  0.09695  100 PRO   A N   
840  C CA  . PRO   A 103 ? 1.09423 0.76032 0.80975 -0.16452 0.01417  0.11083  100 PRO   A CA  
841  C C   . PRO   A 103 ? 1.09678 0.79023 0.81870 -0.15241 0.01362  0.11575  100 PRO   A C   
842  O O   . PRO   A 103 ? 1.07269 0.82447 0.82966 -0.15668 0.02536  0.11198  100 PRO   A O   
843  C CB  . PRO   A 103 ? 1.28823 0.93941 0.98308 -0.20389 0.03009  0.11659  100 PRO   A CB  
844  C CG  . PRO   A 103 ? 1.16908 0.84092 0.89215 -0.21381 0.03543  0.10483  100 PRO   A CG  
845  C CD  . PRO   A 103 ? 1.10543 0.83611 0.87843 -0.18880 0.03309  0.09327  100 PRO   A CD  
846  N N   . LEU   A 104 ? 1.12712 0.77532 0.81317 -0.13599 -0.00203 0.12350  101 LEU   A N   
847  C CA  . LEU   A 104 ? 1.15949 0.82870 0.84832 -0.12261 -0.00576 0.12754  101 LEU   A CA  
848  C C   . LEU   A 104 ? 1.17270 0.86328 0.85530 -0.14864 0.01220  0.13479  101 LEU   A C   
849  O O   . LEU   A 104 ? 1.03938 0.77994 0.75128 -0.14098 0.01633  0.13166  101 LEU   A O   
850  C CB  . LEU   A 104 ? 1.19502 0.80384 0.83943 -0.10173 -0.02805 0.13463  101 LEU   A CB  
851  C CG  . LEU   A 104 ? 1.35610 0.97852 0.99709 -0.08654 -0.03581 0.13872  101 LEU   A CG  
852  C CD1 . LEU   A 104 ? 1.18305 0.87621 0.88402 -0.06583 -0.03608 0.12599  101 LEU   A CD1 
853  C CD2 . LEU   A 104 ? 1.39295 0.94952 0.98585 -0.06537 -0.06082 0.14500  101 LEU   A CD2 
854  N N   . PRO   A 105 ? 1.19944 0.85615 0.84554 -0.17953 0.02379  0.14336  102 PRO   A N   
855  C CA  . PRO   A 105 ? 1.20867 0.89719 0.85657 -0.20410 0.04370  0.14667  102 PRO   A CA  
856  C C   . PRO   A 105 ? 1.08203 0.84703 0.78944 -0.20887 0.05814  0.13419  102 PRO   A C   
857  O O   . PRO   A 105 ? 1.03347 0.83881 0.75535 -0.21471 0.06921  0.13322  102 PRO   A O   
858  C CB  . PRO   A 105 ? 1.12998 0.76832 0.73155 -0.23864 0.05458  0.15539  102 PRO   A CB  
859  C CG  . PRO   A 105 ? 1.25882 0.82047 0.81439 -0.22637 0.03443  0.16252  102 PRO   A CG  
860  C CD  . PRO   A 105 ? 1.11702 0.70025 0.71270 -0.19353 0.01877  0.15092  102 PRO   A CD  
861  N N   . LEU   A 106 ? 1.00860 0.79223 0.74833 -0.20541 0.05718  0.12408  103 LEU   A N   
862  C CA  . LEU   A 106 ? 0.95063 0.80186 0.74306 -0.20731 0.06768  0.11217  103 LEU   A CA  
863  C C   . LEU   A 106 ? 0.99238 0.88281 0.81789 -0.17864 0.05943  0.10674  103 LEU   A C   
864  O O   . LEU   A 106 ? 0.91961 0.86160 0.77725 -0.17948 0.06779  0.10080  103 LEU   A O   
865  C CB  . LEU   A 106 ? 0.93243 0.78612 0.74272 -0.21518 0.06897  0.10332  103 LEU   A CB  
866  C CG  . LEU   A 106 ? 0.91310 0.83011 0.77220 -0.21967 0.07845  0.09072  103 LEU   A CG  
867  C CD1 . LEU   A 106 ? 0.93650 0.88636 0.80275 -0.24255 0.09521  0.08999  103 LEU   A CD1 
868  C CD2 . LEU   A 106 ? 0.89928 0.81062 0.76890 -0.22758 0.07735  0.08235  103 LEU   A CD2 
869  N N   . ILE   A 107 ? 0.98299 0.84996 0.80142 -0.15352 0.04291  0.10763  104 ILE   A N   
870  C CA  . ILE   A 107 ? 0.98713 0.89011 0.83483 -0.12892 0.03575  0.10253  104 ILE   A CA  
871  C C   . ILE   A 107 ? 0.92306 0.83851 0.76246 -0.12943 0.03804  0.10843  104 ILE   A C   
872  O O   . ILE   A 107 ? 0.82604 0.78753 0.69575 -0.12374 0.04194  0.10329  104 ILE   A O   
873  C CB  . ILE   A 107 ? 0.95393 0.83066 0.79635 -0.10263 0.01774  0.10033  104 ILE   A CB  
874  C CG1 . ILE   A 107 ? 0.97546 0.84444 0.82863 -0.10047 0.01633  0.09222  104 ILE   A CG1 
875  C CG2 . ILE   A 107 ? 0.85196 0.76741 0.72444 -0.08032 0.01140  0.09460  104 ILE   A CG2 
876  C CD1 . ILE   A 107 ? 0.97520 0.82268 0.82649 -0.07327 -0.00039 0.08697  104 ILE   A CD1 
877  N N   . LYS   A 108 ? 0.89517 0.76602 0.68956 -0.13658 0.03518  0.11932  105 LYS   A N   
878  C CA  . LYS   A 108 ? 1.00682 0.88461 0.78685 -0.13798 0.03737  0.12500  105 LYS   A CA  
879  C C   . LYS   A 108 ? 0.94577 0.86494 0.74273 -0.15944 0.05744  0.12188  105 LYS   A C   
880  O O   . LYS   A 108 ? 0.95817 0.91181 0.77085 -0.15402 0.06016  0.11922  105 LYS   A O   
881  C CB  . LYS   A 108 ? 0.94715 0.76134 0.66778 -0.14291 0.03018  0.13791  105 LYS   A CB  
882  C CG  . LYS   A 108 ? 1.06941 0.88356 0.76765 -0.14253 0.03023  0.14412  105 LYS   A CG  
883  C CD  . LYS   A 108 ? 1.32620 1.07003 0.95825 -0.14782 0.02201  0.15777  105 LYS   A CD  
884  C CE  . LYS   A 108 ? 1.35161 1.05120 0.96724 -0.12187 -0.00329 0.15914  105 LYS   A CE  
885  N NZ  . LYS   A 108 ? 1.47007 1.09554 1.01581 -0.12384 -0.01501 0.17288  105 LYS   A NZ  
886  N N   . SER   A 109 ? 0.94019 0.85743 0.73534 -0.18344 0.07089  0.12067  106 SER   A N   
887  C CA  . SER   A 109 ? 0.87185 0.83329 0.68779 -0.20275 0.08946  0.11465  106 SER   A CA  
888  C C   . SER   A 109 ? 0.88593 0.90472 0.75384 -0.18958 0.08950  0.10250  106 SER   A C   
889  O O   . SER   A 109 ? 0.82113 0.87866 0.70668 -0.19104 0.09730  0.09752  106 SER   A O   
890  C CB  . SER   A 109 ? 0.89940 0.84921 0.70655 -0.23149 0.10256  0.11379  106 SER   A CB  
891  O OG  . SER   A 109 ? 1.00324 1.00524 0.84111 -0.24715 0.11901  0.10380  106 SER   A OG  
892  N N   . TYR   A 110 ? 0.79444 0.81655 0.68418 -0.17636 0.08059  0.09733  107 TYR   A N   
893  C CA  . TYR   A 110 ? 0.74249 0.81192 0.67492 -0.16502 0.08018  0.08686  107 TYR   A CA  
894  C C   . TYR   A 110 ? 0.74474 0.83112 0.68631 -0.14554 0.07280  0.08715  107 TYR   A C   
895  O O   . TYR   A 110 ? 0.67416 0.79829 0.63853 -0.14356 0.07706  0.08121  107 TYR   A O   
896  C CB  . TYR   A 110 ? 0.71128 0.77561 0.65851 -0.15709 0.07345  0.08160  107 TYR   A CB  
897  C CG  . TYR   A 110 ? 0.78065 0.85050 0.73632 -0.17563 0.08141  0.07568  107 TYR   A CG  
898  C CD1 . TYR   A 110 ? 0.76312 0.85290 0.72229 -0.19688 0.09445  0.07297  107 TYR   A CD1 
899  C CD2 . TYR   A 110 ? 0.77232 0.83017 0.73401 -0.17179 0.07584  0.07107  107 TYR   A CD2 
900  C CE1 . TYR   A 110 ? 0.78002 0.87910 0.75076 -0.21441 0.10082  0.06561  107 TYR   A CE1 
901  C CE2 . TYR   A 110 ? 0.79180 0.85482 0.76149 -0.18887 0.08152  0.06463  107 TYR   A CE2 
902  C CZ  . TYR   A 110 ? 0.78823 0.87273 0.76365 -0.21041 0.09355  0.06180  107 TYR   A CZ  
903  O OH  . TYR   A 110 ? 0.82044 0.91400 0.80742 -0.22799 0.09832  0.05355  107 TYR   A OH  
904  N N   . LEU   A 111 ? 0.73218 0.79047 0.65638 -0.13052 0.06042  0.09297  108 LEU   A N   
905  C CA  . LEU   A 111 ? 0.77716 0.85161 0.71063 -0.11340 0.05247  0.09235  108 LEU   A CA  
906  C C   . LEU   A 111 ? 0.80288 0.88746 0.72438 -0.12089 0.05886  0.09516  108 LEU   A C   
907  O O   . LEU   A 111 ? 0.78705 0.90152 0.72726 -0.11320 0.05813  0.09066  108 LEU   A O   
908  C CB  . LEU   A 111 ? 0.74523 0.78781 0.66191 -0.09618 0.03673  0.09650  108 LEU   A CB  
909  C CG  . LEU   A 111 ? 0.71746 0.77708 0.64567 -0.07848 0.02655  0.09441  108 LEU   A CG  
910  C CD1 . LEU   A 111 ? 0.65332 0.75239 0.62214 -0.07002 0.02734  0.08469  108 LEU   A CD1 
911  C CD2 . LEU   A 111 ? 0.78135 0.80688 0.68852 -0.06216 0.00955  0.09798  108 LEU   A CD2 
912  N N   . PHE   A 112 ? 0.71363 0.77165 0.60153 -0.13682 0.06571  0.10225  109 PHE   A N   
913  C CA  . PHE   A 112 ? 0.80012 0.86717 0.67306 -0.14543 0.07402  0.10406  109 PHE   A CA  
914  C C   . PHE   A 112 ? 0.74901 0.86487 0.65451 -0.15270 0.08662  0.09362  109 PHE   A C   
915  O O   . PHE   A 112 ? 0.75991 0.89930 0.67280 -0.14713 0.08767  0.08989  109 PHE   A O   
916  C CB  . PHE   A 112 ? 0.82464 0.85190 0.65240 -0.16494 0.08168  0.11343  109 PHE   A CB  
917  C CG  . PHE   A 112 ? 0.87035 0.90052 0.67438 -0.17380 0.09053  0.11601  109 PHE   A CG  
918  C CD1 . PHE   A 112 ? 0.83379 0.84313 0.61173 -0.16033 0.07865  0.12207  109 PHE   A CD1 
919  C CD2 . PHE   A 112 ? 0.89514 0.95020 0.70305 -0.19538 0.11056  0.11095  109 PHE   A CD2 
920  C CE1 . PHE   A 112 ? 0.98917 0.99918 0.74160 -0.16834 0.08686  0.12398  109 PHE   A CE1 
921  C CE2 . PHE   A 112 ? 0.97052 1.02965 0.75555 -0.20351 0.12032  0.11188  109 PHE   A CE2 
922  C CZ  . PHE   A 112 ? 0.94611 0.98086 0.70134 -0.19009 0.10861  0.11892  109 PHE   A CZ  
923  N N   . GLN   A 113 ? 0.71826 0.84882 0.64317 -0.16389 0.09458  0.08773  110 GLN   A N   
924  C CA  . GLN   A 113 ? 0.75205 0.92889 0.70942 -0.16799 0.10352  0.07603  110 GLN   A CA  
925  C C   . GLN   A 113 ? 0.70352 0.90540 0.69001 -0.14820 0.09372  0.06989  110 GLN   A C   
926  O O   . GLN   A 113 ? 0.68861 0.92087 0.69113 -0.14454 0.09637  0.06251  110 GLN   A O   
927  C CB  . GLN   A 113 ? 0.76412 0.94944 0.73547 -0.18357 0.11142  0.07028  110 GLN   A CB  
928  C CG  . GLN   A 113 ? 0.75985 0.92384 0.70396 -0.20840 0.12399  0.07487  110 GLN   A CG  
929  C CD  . GLN   A 113 ? 0.81159 0.98558 0.77260 -0.22471 0.13056  0.06773  110 GLN   A CD  
930  O OE1 . GLN   A 113 ? 0.75114 0.96745 0.74711 -0.22472 0.13371  0.05504  110 GLN   A OE1 
931  N NE2 . GLN   A 113 ? 0.85740 0.99029 0.79244 -0.23793 0.13090  0.07524  110 GLN   A NE2 
932  N N   . LEU   A 114 ? 0.63620 0.82466 0.62845 -0.13580 0.08275  0.07213  111 LEU   A N   
933  C CA  . LEU   A 114 ? 0.66725 0.87619 0.68336 -0.12012 0.07497  0.06699  111 LEU   A CA  
934  C C   . LEU   A 114 ? 0.62801 0.84131 0.63867 -0.11051 0.06996  0.06860  111 LEU   A C   
935  O O   . LEU   A 114 ? 0.61236 0.84912 0.63993 -0.10418 0.06849  0.06256  111 LEU   A O   
936  C CB  . LEU   A 114 ? 0.67249 0.86670 0.69373 -0.11045 0.06646  0.06831  111 LEU   A CB  
937  C CG  . LEU   A 114 ? 0.67934 0.87099 0.70910 -0.11666 0.06914  0.06465  111 LEU   A CG  
938  C CD1 . LEU   A 114 ? 0.56184 0.73468 0.59086 -0.10573 0.06101  0.06588  111 LEU   A CD1 
939  C CD2 . LEU   A 114 ? 0.61434 0.83688 0.66845 -0.11721 0.07185  0.05552  111 LEU   A CD2 
940  N N   . LEU   A 115 ? 0.61785 0.80551 0.60238 -0.10900 0.06581  0.07648  112 LEU   A N   
941  C CA  . LEU   A 115 ? 0.71409 0.90425 0.69107 -0.10029 0.05977  0.07748  112 LEU   A CA  
942  C C   . LEU   A 115 ? 0.66802 0.87696 0.64175 -0.10768 0.06931  0.07328  112 LEU   A C   
943  O O   . LEU   A 115 ? 0.65431 0.87725 0.63387 -0.09958 0.06516  0.06941  112 LEU   A O   
944  C CB  . LEU   A 115 ? 0.64105 0.79641 0.58713 -0.09614 0.05115  0.08642  112 LEU   A CB  
945  C CG  . LEU   A 115 ? 0.68445 0.82465 0.63595 -0.08271 0.03797  0.08789  112 LEU   A CG  
946  C CD1 . LEU   A 115 ? 0.73458 0.83438 0.65021 -0.07904 0.02859  0.09646  112 LEU   A CD1 
947  C CD2 . LEU   A 115 ? 0.60225 0.76591 0.57916 -0.06908 0.02922  0.08183  112 LEU   A CD2 
948  N N   . GLN   A 116 ? 0.62566 0.83593 0.59057 -0.12341 0.08233  0.07274  113 GLN   A N   
949  C CA  . GLN   A 116 ? 0.64424 0.87853 0.61016 -0.13026 0.09323  0.06573  113 GLN   A CA  
950  C C   . GLN   A 116 ? 0.64540 0.91511 0.64559 -0.12290 0.09248  0.05385  113 GLN   A C   
951  O O   . GLN   A 116 ? 0.56000 0.84653 0.56420 -0.11633 0.09191  0.04750  113 GLN   A O   
952  C CB  . GLN   A 116 ? 0.68780 0.91969 0.64023 -0.15115 0.10898  0.06608  113 GLN   A CB  
953  C CG  . GLN   A 116 ? 0.69970 0.89363 0.60777 -0.16077 0.11181  0.07763  113 GLN   A CG  
954  C CD  . GLN   A 116 ? 0.87174 1.06075 0.76492 -0.18549 0.12904  0.07831  113 GLN   A CD  
955  O OE1 . GLN   A 116 ? 0.89192 1.08501 0.80101 -0.19457 0.13269  0.07587  113 GLN   A OE1 
956  N NE2 . GLN   A 116 ? 0.86059 1.04075 0.72197 -0.19796 0.14031  0.08103  113 GLN   A NE2 
957  N N   . GLY   A 117 ? 0.59942 0.87740 0.62139 -0.12314 0.09124  0.05043  114 GLY   A N   
958  C CA  . GLY   A 117 ? 0.61412 0.91849 0.66314 -0.11464 0.08759  0.04015  114 GLY   A CA  
959  C C   . GLY   A 117 ? 0.56949 0.87010 0.62229 -0.09971 0.07559  0.04115  114 GLY   A C   
960  O O   . GLY   A 117 ? 0.58507 0.90195 0.64955 -0.09217 0.07215  0.03334  114 GLY   A O   
961  N N   . LEU   A 118 ? 0.61965 0.89863 0.66280 -0.09538 0.06855  0.04971  115 LEU   A N   
962  C CA  . LEU   A 118 ? 0.66752 0.94572 0.71618 -0.08404 0.05828  0.04965  115 LEU   A CA  
963  C C   . LEU   A 118 ? 0.57407 0.85260 0.61013 -0.08019 0.05566  0.04902  115 LEU   A C   
964  O O   . LEU   A 118 ? 0.63608 0.92194 0.67916 -0.07318 0.04959  0.04448  115 LEU   A O   
965  C CB  . LEU   A 118 ? 0.55698 0.81846 0.60457 -0.08002 0.05168  0.05593  115 LEU   A CB  
966  C CG  . LEU   A 118 ? 0.64056 0.90665 0.70064 -0.07154 0.04323  0.05393  115 LEU   A CG  
967  C CD1 . LEU   A 118 ? 0.55954 0.83768 0.63499 -0.07168 0.04454  0.04825  115 LEU   A CD1 
968  C CD2 . LEU   A 118 ? 0.55768 0.81265 0.61944 -0.06695 0.03768  0.05761  115 LEU   A CD2 
969  N N   . ALA   A 119 ? 0.55720 0.82450 0.57109 -0.08543 0.05991  0.05357  116 ALA   A N   
970  C CA  . ALA   A 119 ? 0.72616 0.99301 0.72418 -0.08228 0.05820  0.05217  116 ALA   A CA  
971  C C   . ALA   A 119 ? 0.62925 0.91965 0.63646 -0.08193 0.06428  0.04134  116 ALA   A C   
972  O O   . ALA   A 119 ? 0.58818 0.88239 0.59229 -0.07461 0.05904  0.03658  116 ALA   A O   
973  C CB  . ALA   A 119 ? 0.57201 0.81826 0.53849 -0.08951 0.06266  0.05969  116 ALA   A CB  
974  N N   . PHE   A 120 ? 0.63512 0.94189 0.65437 -0.08902 0.07429  0.03591  117 PHE   A N   
975  C CA  . PHE   A 120 ? 0.59634 0.92915 0.62924 -0.08581 0.07824  0.02288  117 PHE   A CA  
976  C C   . PHE   A 120 ? 0.62184 0.95870 0.67163 -0.07351 0.06643  0.01764  117 PHE   A C   
977  O O   . PHE   A 120 ? 0.70100 1.04747 0.75305 -0.06513 0.06292  0.00850  117 PHE   A O   
978  C CB  . PHE   A 120 ? 0.68672 1.03912 0.73256 -0.09635 0.09023  0.01681  117 PHE   A CB  
979  C CG  . PHE   A 120 ? 0.60287 0.98690 0.66494 -0.09218 0.09459  0.00076  117 PHE   A CG  
980  C CD1 . PHE   A 120 ? 0.66663 1.06485 0.71856 -0.09689 0.10595  -0.00593 117 PHE   A CD1 
981  C CD2 . PHE   A 120 ? 0.59356 0.99262 0.67951 -0.08279 0.08693  -0.00862 117 PHE   A CD2 
982  C CE1 . PHE   A 120 ? 0.66066 1.09191 0.73051 -0.09115 0.10994  -0.02337 117 PHE   A CE1 
983  C CE2 . PHE   A 120 ? 0.62081 1.04913 0.72263 -0.07588 0.08846  -0.02526 117 PHE   A CE2 
984  C CZ  . PHE   A 120 ? 0.56460 1.01131 0.66072 -0.07954 0.10017  -0.03350 117 PHE   A CZ  
985  N N   . CYS   A 121 ? 0.57965 0.90676 0.63852 -0.07260 0.06035  0.02299  118 CYS   A N   
986  C CA  . CYS   A 121 ? 0.58125 0.90650 0.65003 -0.06377 0.05007  0.01967  118 CYS   A CA  
987  C C   . CYS   A 121 ? 0.60674 0.92016 0.66558 -0.05798 0.04151  0.02157  118 CYS   A C   
988  O O   . CYS   A 121 ? 0.64926 0.96275 0.70877 -0.05092 0.03478  0.01509  118 CYS   A O   
989  C CB  . CYS   A 121 ? 0.61973 0.93680 0.69701 -0.06611 0.04781  0.02501  118 CYS   A CB  
990  S SG  . CYS   A 121 ? 0.60420 0.93438 0.69558 -0.07079 0.05330  0.01984  118 CYS   A SG  
991  N N   . HIS   A 122 ? 0.58533 0.88686 0.63402 -0.06051 0.04016  0.02970  119 HIS   A N   
992  C CA  . HIS   A 122 ? 0.63327 0.92552 0.67544 -0.05593 0.03066  0.03067  119 HIS   A CA  
993  C C   . HIS   A 122 ? 0.55553 0.84994 0.58404 -0.05200 0.02986  0.02474  119 HIS   A C   
994  O O   . HIS   A 122 ? 0.61322 0.90254 0.63928 -0.04703 0.02112  0.02095  119 HIS   A O   
995  C CB  . HIS   A 122 ? 0.58491 0.86625 0.62204 -0.05754 0.02734  0.03904  119 HIS   A CB  
996  C CG  . HIS   A 122 ? 0.64066 0.92057 0.69217 -0.05930 0.02691  0.04271  119 HIS   A CG  
997  N ND1 . HIS   A 122 ? 0.68649 0.95863 0.73745 -0.05855 0.02359  0.04822  119 HIS   A ND1 
998  C CD2 . HIS   A 122 ? 0.58411 0.86855 0.64915 -0.06075 0.02891  0.04068  119 HIS   A CD2 
999  C CE1 . HIS   A 122 ? 0.70680 0.98132 0.77232 -0.05964 0.02495  0.04861  119 HIS   A CE1 
1000 N NE2 . HIS   A 122 ? 0.57980 0.86085 0.65252 -0.06183 0.02858  0.04468  119 HIS   A NE2 
1001 N N   . SER   A 123 ? 0.53834 0.83938 0.55636 -0.05527 0.03949  0.02327  120 SER   A N   
1002 C CA  . SER   A 123 ? 0.61741 0.92306 0.62188 -0.05129 0.04074  0.01563  120 SER   A CA  
1003 C C   . SER   A 123 ? 0.66453 0.98270 0.68099 -0.04340 0.03852  0.00326  120 SER   A C   
1004 O O   . SER   A 123 ? 0.70587 1.02276 0.71333 -0.03619 0.03377  -0.00437 120 SER   A O   
1005 C CB  . SER   A 123 ? 0.66456 0.97581 0.65381 -0.05913 0.05442  0.01623  120 SER   A CB  
1006 O OG  . SER   A 123 ? 0.75692 1.08863 0.76162 -0.06382 0.06546  0.01001  120 SER   A OG  
1007 N N   . HIS   A 124 ? 0.57757 0.90559 0.61228 -0.04340 0.04030  0.00042  121 HIS   A N   
1008 C CA  . HIS   A 124 ? 0.62469 0.95885 0.66942 -0.03355 0.03394  -0.01072 121 HIS   A CA  
1009 C C   . HIS   A 124 ? 0.60170 0.91526 0.64608 -0.02990 0.02076  -0.00726 121 HIS   A C   
1010 O O   . HIS   A 124 ? 0.61808 0.92826 0.66599 -0.02206 0.01330  -0.01447 121 HIS   A O   
1011 C CB  . HIS   A 124 ? 0.58298 0.93636 0.64572 -0.03461 0.03990  -0.01639 121 HIS   A CB  
1012 C CG  . HIS   A 124 ? 0.64631 1.02603 0.71313 -0.03726 0.05270  -0.02588 121 HIS   A CG  
1013 N ND1 . HIS   A 124 ? 0.69471 1.07688 0.74992 -0.04913 0.06536  -0.01989 121 HIS   A ND1 
1014 C CD2 . HIS   A 124 ? 0.63773 1.04305 0.71844 -0.03011 0.05513  -0.04194 121 HIS   A CD2 
1015 C CE1 . HIS   A 124 ? 0.67056 1.07945 0.73184 -0.05182 0.07731  -0.03137 121 HIS   A CE1 
1016 N NE2 . HIS   A 124 ? 0.76210 1.18877 0.84189 -0.03972 0.07139  -0.04592 121 HIS   A NE2 
1017 N N   . ARG   A 125 ? 0.60610 0.90562 0.64556 -0.03574 0.01761  0.00288  122 ARG   A N   
1018 C CA  . ARG   A 125 ? 0.64015 0.92238 0.67941 -0.03624 0.00758  0.00590  122 ARG   A CA  
1019 C C   . ARG   A 125 ? 0.69368 0.97269 0.74221 -0.03772 0.00704  0.00731  122 ARG   A C   
1020 O O   . ARG   A 125 ? 0.68107 0.94621 0.72493 -0.03438 -0.00093 0.00404  122 ARG   A O   
1021 C CB  . ARG   A 125 ? 0.68061 0.95096 0.70837 -0.02927 -0.00229 -0.00177 122 ARG   A CB  
1022 C CG  . ARG   A 125 ? 0.71629 0.98481 0.73210 -0.02893 -0.00425 -0.00222 122 ARG   A CG  
1023 C CD  . ARG   A 125 ? 0.81492 1.07877 0.81834 -0.01914 -0.01006 -0.01375 122 ARG   A CD  
1024 N NE  . ARG   A 125 ? 0.79673 1.03990 0.79571 -0.01607 -0.02190 -0.01750 122 ARG   A NE  
1025 C CZ  . ARG   A 125 ? 0.92002 1.15810 0.91851 -0.00733 -0.02615 -0.02520 122 ARG   A CZ  
1026 N NH1 . ARG   A 125 ? 0.91796 1.17624 0.92565 -0.00032 -0.01945 -0.03171 122 ARG   A NH1 
1027 N NH2 . ARG   A 125 ? 1.01028 1.22142 0.99799 -0.00580 -0.03820 -0.02706 122 ARG   A NH2 
1028 N N   . VAL   A 126 ? 0.56194 0.85003 0.61996 -0.04303 0.01491  0.01240  123 VAL   A N   
1029 C CA  . VAL   A 126 ? 0.52459 0.80983 0.58961 -0.04492 0.01506  0.01387  123 VAL   A CA  
1030 C C   . VAL   A 126 ? 0.55218 0.83598 0.62289 -0.05297 0.01983  0.02282  123 VAL   A C   
1031 O O   . VAL   A 126 ? 0.56793 0.85907 0.64111 -0.05591 0.02602  0.02646  123 VAL   A O   
1032 C CB  . VAL   A 126 ? 0.52269 0.82330 0.59586 -0.04157 0.01912  0.00732  123 VAL   A CB  
1033 C CG1 . VAL   A 126 ? 0.58129 0.87765 0.65976 -0.04417 0.01875  0.00962  123 VAL   A CG1 
1034 C CG2 . VAL   A 126 ? 0.66812 0.97222 0.73866 -0.03053 0.01259  -0.00438 123 VAL   A CG2 
1035 N N   . LEU   A 127 ? 0.58748 0.86036 0.65833 -0.05659 0.01708  0.02574  124 LEU   A N   
1036 C CA  . LEU   A 127 ? 0.58685 0.86096 0.66532 -0.06258 0.02198  0.03145  124 LEU   A CA  
1037 C C   . LEU   A 127 ? 0.57940 0.85372 0.66051 -0.06334 0.02553  0.03102  124 LEU   A C   
1038 O O   . LEU   A 127 ? 0.61268 0.87959 0.68760 -0.06081 0.02136  0.02745  124 LEU   A O   
1039 C CB  . LEU   A 127 ? 0.56937 0.83566 0.64783 -0.06804 0.01940  0.03310  124 LEU   A CB  
1040 C CG  . LEU   A 127 ? 0.71901 0.98329 0.79468 -0.06834 0.01335  0.03174  124 LEU   A CG  
1041 C CD1 . LEU   A 127 ? 0.66478 0.92418 0.74324 -0.07719 0.01241  0.03204  124 LEU   A CD1 
1042 C CD2 . LEU   A 127 ? 0.60827 0.88276 0.68844 -0.06528 0.01356  0.03346  124 LEU   A CD2 
1043 N N   . HIS   A 128 ? 0.54865 0.82866 0.63675 -0.06604 0.03159  0.03419  125 HIS   A N   
1044 C CA  . HIS   A 128 ? 0.48882 0.76822 0.57900 -0.06739 0.03438  0.03320  125 HIS   A CA  
1045 C C   . HIS   A 128 ? 0.53443 0.80435 0.62199 -0.07099 0.03499  0.03488  125 HIS   A C   
1046 O O   . HIS   A 128 ? 0.54654 0.80769 0.62618 -0.07089 0.03256  0.03283  125 HIS   A O   
1047 C CB  . HIS   A 128 ? 0.47689 0.76215 0.57264 -0.06981 0.04036  0.03534  125 HIS   A CB  
1048 C CG  . HIS   A 128 ? 0.57492 0.86054 0.67317 -0.07167 0.04241  0.03286  125 HIS   A CG  
1049 N ND1 . HIS   A 128 ? 0.53765 0.81562 0.63498 -0.07332 0.04350  0.03384  125 HIS   A ND1 
1050 C CD2 . HIS   A 128 ? 0.53915 0.83343 0.64135 -0.07256 0.04344  0.02811  125 HIS   A CD2 
1051 C CE1 . HIS   A 128 ? 0.57307 0.85204 0.67148 -0.07447 0.04385  0.03045  125 HIS   A CE1 
1052 N NE2 . HIS   A 128 ? 0.58470 0.87472 0.68777 -0.07434 0.04349  0.02667  125 HIS   A NE2 
1053 N N   . ARG   A 129 ? 0.48445 0.75644 0.57778 -0.07395 0.03809  0.03768  126 ARG   A N   
1054 C CA  . ARG   A 129 ? 0.57179 0.84003 0.66501 -0.07922 0.04118  0.03782  126 ARG   A CA  
1055 C C   . ARG   A 129 ? 0.49349 0.75852 0.58506 -0.08079 0.04626  0.03718  126 ARG   A C   
1056 O O   . ARG   A 129 ? 0.55264 0.81268 0.63920 -0.08618 0.05016  0.03650  126 ARG   A O   
1057 C CB  . ARG   A 129 ? 0.57991 0.83587 0.66059 -0.08335 0.03748  0.03715  126 ARG   A CB  
1058 C CG  . ARG   A 129 ? 0.58725 0.84357 0.66758 -0.08220 0.03156  0.03665  126 ARG   A CG  
1059 C CD  . ARG   A 129 ? 0.66621 0.90614 0.73274 -0.08901 0.02839  0.03626  126 ARG   A CD  
1060 N NE  . ARG   A 129 ? 0.68163 0.90177 0.72892 -0.08716 0.02431  0.03587  126 ARG   A NE  
1061 C CZ  . ARG   A 129 ? 0.77347 0.96978 0.80018 -0.09263 0.02016  0.03643  126 ARG   A CZ  
1062 N NH1 . ARG   A 129 ? 0.67246 0.86341 0.69669 -0.10294 0.02125  0.03721  126 ARG   A NH1 
1063 N NH2 . ARG   A 129 ? 0.75730 0.93300 0.76410 -0.08802 0.01380  0.03577  126 ARG   A NH2 
1064 N N   . ASP   A 130 ? 0.51768 0.78465 0.61173 -0.07765 0.04696  0.03689  127 ASP   A N   
1065 C CA  . ASP   A 130 ? 0.54414 0.80743 0.63681 -0.07883 0.05110  0.03550  127 ASP   A CA  
1066 C C   . ASP   A 130 ? 0.55561 0.82169 0.65436 -0.07683 0.05213  0.03583  127 ASP   A C   
1067 O O   . ASP   A 130 ? 0.60481 0.86794 0.70086 -0.07769 0.05188  0.03368  127 ASP   A O   
1068 C CB  . ASP   A 130 ? 0.54572 0.79820 0.62454 -0.07980 0.04817  0.03334  127 ASP   A CB  
1069 C CG  . ASP   A 130 ? 0.71181 0.95718 0.78368 -0.08266 0.05313  0.03179  127 ASP   A CG  
1070 O OD1 . ASP   A 130 ? 0.64315 0.89386 0.72214 -0.08428 0.05990  0.03151  127 ASP   A OD1 
1071 O OD2 . ASP   A 130 ? 0.77355 1.00864 0.83270 -0.08230 0.04962  0.02968  127 ASP   A OD2 
1072 N N   . LEU   A 131 ? 0.53886 0.80841 0.64389 -0.07476 0.05240  0.03834  128 LEU   A N   
1073 C CA  . LEU   A 131 ? 0.50944 0.77462 0.61442 -0.07440 0.05324  0.03999  128 LEU   A CA  
1074 C C   . LEU   A 131 ? 0.61435 0.87301 0.72077 -0.07270 0.05582  0.03814  128 LEU   A C   
1075 O O   . LEU   A 131 ? 0.61977 0.88083 0.73211 -0.06824 0.05600  0.03714  128 LEU   A O   
1076 C CB  . LEU   A 131 ? 0.49975 0.76477 0.60410 -0.07195 0.05072  0.04389  128 LEU   A CB  
1077 C CG  . LEU   A 131 ? 0.62212 0.89275 0.72273 -0.07338 0.04909  0.04478  128 LEU   A CG  
1078 C CD1 . LEU   A 131 ? 0.58927 0.85618 0.68444 -0.07090 0.04632  0.04882  128 LEU   A CD1 
1079 C CD2 . LEU   A 131 ? 0.53335 0.80657 0.63184 -0.07828 0.05199  0.04268  128 LEU   A CD2 
1080 N N   . LYS   A 132 ? 0.56889 0.82101 0.67120 -0.07564 0.05728  0.03605  129 LYS   A N   
1081 C CA  . LYS   A 132 ? 0.62747 0.87052 0.72852 -0.07373 0.05928  0.03318  129 LYS   A CA  
1082 C C   . LYS   A 132 ? 0.55462 0.78752 0.65020 -0.07879 0.05882  0.03282  129 LYS   A C   
1083 O O   . LYS   A 132 ? 0.61389 0.85249 0.70957 -0.08438 0.05809  0.03271  129 LYS   A O   
1084 C CB  . LYS   A 132 ? 0.57892 0.82433 0.67817 -0.07375 0.06252  0.02853  129 LYS   A CB  
1085 C CG  . LYS   A 132 ? 0.58114 0.82664 0.67283 -0.07805 0.06072  0.02742  129 LYS   A CG  
1086 C CD  . LYS   A 132 ? 0.58229 0.82381 0.66475 -0.07904 0.06406  0.02407  129 LYS   A CD  
1087 C CE  . LYS   A 132 ? 0.68602 0.92181 0.75582 -0.08132 0.05912  0.02330  129 LYS   A CE  
1088 N NZ  . LYS   A 132 ? 0.73393 0.95946 0.78699 -0.08361 0.06237  0.02103  129 LYS   A NZ  
1089 N N   . PRO   A 133 ? 0.60683 0.82525 0.69835 -0.07720 0.05898  0.03140  130 PRO   A N   
1090 C CA  . PRO   A 133 ? 0.57878 0.78471 0.66386 -0.08475 0.05857  0.03100  130 PRO   A CA  
1091 C C   . PRO   A 133 ? 0.58033 0.79438 0.66719 -0.09115 0.05837  0.02599  130 PRO   A C   
1092 O O   . PRO   A 133 ? 0.64088 0.85519 0.72821 -0.10008 0.05833  0.02506  130 PRO   A O   
1093 C CB  . PRO   A 133 ? 0.58805 0.77465 0.66696 -0.07950 0.05760  0.02841  130 PRO   A CB  
1094 C CG  . PRO   A 133 ? 0.68205 0.87192 0.76574 -0.06841 0.05647  0.02928  130 PRO   A CG  
1095 C CD  . PRO   A 133 ? 0.60519 0.81784 0.69838 -0.06817 0.05891  0.02912  130 PRO   A CD  
1096 N N   . GLN   A 134 ? 0.56434 0.78470 0.65115 -0.08737 0.05791  0.02213  131 GLN   A N   
1097 C CA  . GLN   A 134 ? 0.60118 0.82701 0.68702 -0.09092 0.05452  0.01692  131 GLN   A CA  
1098 C C   . GLN   A 134 ? 0.56649 0.80853 0.65989 -0.09322 0.05194  0.01707  131 GLN   A C   
1099 O O   . GLN   A 134 ? 0.57564 0.82535 0.67285 -0.09647 0.04781  0.01117  131 GLN   A O   
1100 C CB  . GLN   A 134 ? 0.66731 0.89033 0.74425 -0.08631 0.05405  0.01396  131 GLN   A CB  
1101 C CG  . GLN   A 134 ? 0.73063 0.94092 0.80000 -0.08362 0.05768  0.01079  131 GLN   A CG  
1102 C CD  . GLN   A 134 ? 0.86671 1.08001 0.93880 -0.07824 0.06363  0.01275  131 GLN   A CD  
1103 O OE1 . GLN   A 134 ? 0.61274 0.83076 0.69401 -0.07606 0.06415  0.01690  131 GLN   A OE1 
1104 N NE2 . GLN   A 134 ? 0.86071 1.07226 0.92445 -0.07653 0.06818  0.00885  131 GLN   A NE2 
1105 N N   . ASN   A 135 ? 0.50034 0.74908 0.59689 -0.09071 0.05350  0.02206  132 ASN   A N   
1106 C CA  . ASN   A 135 ? 0.55201 0.81600 0.65491 -0.09115 0.05138  0.02101  132 ASN   A CA  
1107 C C   . ASN   A 135 ? 0.60634 0.87598 0.71404 -0.09792 0.05557  0.02300  132 ASN   A C   
1108 O O   . ASN   A 135 ? 0.51744 0.80154 0.63049 -0.09812 0.05569  0.02155  132 ASN   A O   
1109 C CB  . ASN   A 135 ? 0.58918 0.85516 0.68947 -0.08499 0.05002  0.02426  132 ASN   A CB  
1110 C CG  . ASN   A 135 ? 0.55919 0.81832 0.65034 -0.08130 0.04627  0.02210  132 ASN   A CG  
1111 O OD1 . ASN   A 135 ? 0.70036 0.95667 0.78730 -0.08121 0.04200  0.01703  132 ASN   A OD1 
1112 N ND2 . ASN   A 135 ? 0.58459 0.83972 0.67074 -0.07929 0.04758  0.02568  132 ASN   A ND2 
1113 N N   . LEU   A 136 ? 0.62036 0.87653 0.72337 -0.10366 0.05909  0.02596  133 LEU   A N   
1114 C CA  . LEU   A 136 ? 0.57995 0.83450 0.68051 -0.11308 0.06401  0.02898  133 LEU   A CA  
1115 C C   . LEU   A 136 ? 0.62101 0.87600 0.72483 -0.12493 0.06584  0.02337  133 LEU   A C   
1116 O O   . LEU   A 136 ? 0.60481 0.84221 0.70262 -0.12658 0.06441  0.02290  133 LEU   A O   
1117 C CB  . LEU   A 136 ? 0.55897 0.79107 0.64636 -0.11093 0.06485  0.03737  133 LEU   A CB  
1118 C CG  . LEU   A 136 ? 0.59391 0.82713 0.68141 -0.09898 0.06168  0.04093  133 LEU   A CG  
1119 C CD1 . LEU   A 136 ? 0.66470 0.87744 0.74077 -0.09498 0.05988  0.04726  133 LEU   A CD1 
1120 C CD2 . LEU   A 136 ? 0.51818 0.76953 0.61055 -0.09771 0.06184  0.04072  133 LEU   A CD2 
1121 N N   . LEU   A 137 ? 0.55209 0.82874 0.66661 -0.13322 0.06897  0.01762  134 LEU   A N   
1122 C CA  . LEU   A 137 ? 0.59918 0.88494 0.72293 -0.14566 0.07030  0.00923  134 LEU   A CA  
1123 C C   . LEU   A 137 ? 0.61418 0.89580 0.73216 -0.16346 0.08022  0.01202  134 LEU   A C   
1124 O O   . LEU   A 137 ? 0.64537 0.93348 0.75953 -0.16588 0.08635  0.01582  134 LEU   A O   
1125 C CB  . LEU   A 137 ? 0.51123 0.82973 0.65519 -0.14199 0.06578  -0.00290 134 LEU   A CB  
1126 C CG  . LEU   A 137 ? 0.49820 0.81548 0.64150 -0.12568 0.05519  -0.00514 134 LEU   A CG  
1127 C CD1 . LEU   A 137 ? 0.63183 0.97724 0.79186 -0.12007 0.04803  -0.01751 134 LEU   A CD1 
1128 C CD2 . LEU   A 137 ? 0.60365 0.89989 0.73762 -0.12497 0.05088  -0.00497 134 LEU   A CD2 
1129 N N   . ILE   A 138 ? 0.55618 0.82457 0.67062 -0.17703 0.08193  0.00999  135 ILE   A N   
1130 C CA  . ILE   A 138 ? 0.54037 0.79780 0.64413 -0.19790 0.09189  0.01315  135 ILE   A CA  
1131 C C   . ILE   A 138 ? 0.69698 0.98062 0.82104 -0.21493 0.09543  0.00001  135 ILE   A C   
1132 O O   . ILE   A 138 ? 0.68345 0.98109 0.82387 -0.20964 0.08715  -0.00999 135 ILE   A O   
1133 C CB  . ILE   A 138 ? 0.67322 0.88304 0.74942 -0.20105 0.09036  0.02327  135 ILE   A CB  
1134 C CG1 . ILE   A 138 ? 0.76669 0.96510 0.84611 -0.20041 0.08316  0.01699  135 ILE   A CG1 
1135 C CG2 . ILE   A 138 ? 0.71640 0.90599 0.77754 -0.18253 0.08533  0.03352  135 ILE   A CG2 
1136 C CD1 . ILE   A 138 ? 0.82127 0.97199 0.87417 -0.20126 0.08013  0.02445  135 ILE   A CD1 
1137 N N   . ASN   A 139 ? 0.65439 0.94513 0.77660 -0.23618 0.10782  -0.00066 136 ASN   A N   
1138 C CA  . ASN   A 139 ? 0.69105 1.00769 0.83331 -0.25725 0.11356  -0.01386 136 ASN   A CA  
1139 C C   . ASN   A 139 ? 0.73113 1.01082 0.84901 -0.28222 0.12143  -0.00705 136 ASN   A C   
1140 O O   . ASN   A 139 ? 0.73043 0.96315 0.81509 -0.28011 0.12048  0.00757  136 ASN   A O   
1141 C CB  . ASN   A 139 ? 0.79454 1.15976 0.96024 -0.26368 0.12353  -0.02445 136 ASN   A CB  
1142 C CG  . ASN   A 139 ? 0.73980 1.09339 0.88269 -0.27442 0.13785  -0.01404 136 ASN   A CG  
1143 O OD1 . ASN   A 139 ? 0.76661 1.07373 0.87479 -0.27627 0.13869  0.00182  136 ASN   A OD1 
1144 N ND2 . ASN   A 139 ? 0.75515 1.15094 0.91645 -0.28053 0.14845  -0.02409 136 ASN   A ND2 
1145 N N   . THR   A 140 ? 0.76183 1.06233 0.89611 -0.30616 0.12836  -0.01866 137 THR   A N   
1146 C CA  . THR   A 140 ? 0.81930 1.08408 0.93015 -0.33419 0.13626  -0.01367 137 THR   A CA  
1147 C C   . THR   A 140 ? 0.82036 1.07684 0.90965 -0.35644 0.15428  -0.00575 137 THR   A C   
1148 O O   . THR   A 140 ? 0.90477 1.13730 0.97571 -0.38581 0.16399  -0.00349 137 THR   A O   
1149 C CB  . THR   A 140 ? 0.81219 1.10282 0.95033 -0.35314 0.13583  -0.03066 137 THR   A CB  
1150 O OG1 . THR   A 140 ? 0.87385 1.22806 1.05027 -0.36082 0.14413  -0.04699 137 THR   A OG1 
1151 C CG2 . THR   A 140 ? 0.66786 0.95604 0.81770 -0.33248 0.11720  -0.03706 137 THR   A CG2 
1152 N N   . GLU   A 141 ? 0.88806 1.16040 0.97559 -0.34428 0.15901  -0.00137 138 GLU   A N   
1153 C CA  . GLU   A 141 ? 0.83821 1.10226 0.90130 -0.36376 0.17627  0.00612  138 GLU   A CA  
1154 C C   . GLU   A 141 ? 0.83763 1.05735 0.86152 -0.34686 0.17152  0.02482  138 GLU   A C   
1155 O O   . GLU   A 141 ? 0.81147 1.03146 0.81737 -0.35340 0.18275  0.03034  138 GLU   A O   
1156 C CB  . GLU   A 141 ? 0.80638 1.13576 0.90377 -0.36837 0.18863  -0.00918 138 GLU   A CB  
1157 C CG  . GLU   A 141 ? 0.83089 1.21026 0.97089 -0.38539 0.19300  -0.03041 138 GLU   A CG  
1158 C CD  . GLU   A 141 ? 0.99089 1.43240 1.16514 -0.38180 0.20150  -0.04770 138 GLU   A CD  
1159 O OE1 . GLU   A 141 ? 0.90208 1.35357 1.07142 -0.36619 0.20377  -0.04414 138 GLU   A OE1 
1160 O OE2 . GLU   A 141 ? 0.88671 1.36262 1.09082 -0.39036 0.20326  -0.06542 138 GLU   A OE2 
1161 N N   . GLY   A 142 ? 0.89294 1.07657 0.90393 -0.32494 0.15491  0.03329  139 GLY   A N   
1162 C CA  . GLY   A 142 ? 0.74511 0.88656 0.72121 -0.30850 0.14807  0.04927  139 GLY   A CA  
1163 C C   . GLY   A 142 ? 0.69916 0.86756 0.68903 -0.28288 0.14306  0.04915  139 GLY   A C   
1164 O O   . GLY   A 142 ? 0.81873 0.95767 0.78145 -0.27085 0.13815  0.06105  139 GLY   A O   
1165 N N   . ALA   A 143 ? 0.73761 0.95854 0.76725 -0.27369 0.14256  0.03567  140 ALA   A N   
1166 C CA  . ALA   A 143 ? 0.73681 0.98182 0.77848 -0.25120 0.13782  0.03465  140 ALA   A CA  
1167 C C   . ALA   A 143 ? 0.72784 0.97288 0.78428 -0.22605 0.12185  0.03344  140 ALA   A C   
1168 O O   . ALA   A 143 ? 0.68400 0.92759 0.75210 -0.22584 0.11593  0.02819  140 ALA   A O   
1169 C CB  . ALA   A 143 ? 0.68942 0.98969 0.76148 -0.25588 0.14709  0.01996  140 ALA   A CB  
1170 N N   . ILE   A 144 ? 0.64448 0.89047 0.69859 -0.20618 0.11546  0.03798  141 ILE   A N   
1171 C CA  . ILE   A 144 ? 0.61825 0.86695 0.68504 -0.18411 0.10273  0.03677  141 ILE   A CA  
1172 C C   . ILE   A 144 ? 0.69463 0.97252 0.77539 -0.17078 0.10100  0.03252  141 ILE   A C   
1173 O O   . ILE   A 144 ? 0.66132 0.94152 0.73144 -0.17228 0.10628  0.03590  141 ILE   A O   
1174 C CB  . ILE   A 144 ? 0.62875 0.83757 0.67353 -0.17326 0.09455  0.04792  141 ILE   A CB  
1175 C CG1 . ILE   A 144 ? 0.60899 0.82415 0.66833 -0.15404 0.08439  0.04494  141 ILE   A CG1 
1176 C CG2 . ILE   A 144 ? 0.65372 0.84606 0.67587 -0.16986 0.09520  0.05768  141 ILE   A CG2 
1177 C CD1 . ILE   A 144 ? 0.56072 0.74395 0.60514 -0.14298 0.07694  0.05189  141 ILE   A CD1 
1178 N N   . LYS   A 145 ? 0.61410 0.91107 0.71528 -0.15803 0.09312  0.02492  142 LYS   A N   
1179 C CA  . LYS   A 145 ? 0.58308 0.90648 0.69754 -0.14652 0.09040  0.01873  142 LYS   A CA  
1180 C C   . LYS   A 145 ? 0.61466 0.93176 0.73173 -0.12918 0.07915  0.02002  142 LYS   A C   
1181 O O   . LYS   A 145 ? 0.56339 0.86916 0.68121 -0.12674 0.07418  0.02012  142 LYS   A O   
1182 C CB  . LYS   A 145 ? 0.51156 0.87154 0.64992 -0.15143 0.09301  0.00381  142 LYS   A CB  
1183 C CG  . LYS   A 145 ? 0.50653 0.87792 0.64600 -0.17279 0.10661  0.00014  142 LYS   A CG  
1184 C CD  . LYS   A 145 ? 0.52946 0.94620 0.69748 -0.17542 0.10981  -0.01744 142 LYS   A CD  
1185 C CE  . LYS   A 145 ? 0.46776 0.89862 0.63797 -0.20044 0.12608  -0.02198 142 LYS   A CE  
1186 N NZ  . LYS   A 145 ? 0.55914 1.04107 0.75906 -0.20197 0.13162  -0.04090 142 LYS   A NZ  
1187 N N   . LEU   A 146 ? 0.54638 0.86996 0.66298 -0.11845 0.07589  0.02056  143 LEU   A N   
1188 C CA  . LEU   A 146 ? 0.53760 0.85563 0.65500 -0.10492 0.06666  0.02141  143 LEU   A CA  
1189 C C   . LEU   A 146 ? 0.54171 0.87591 0.67224 -0.09924 0.06021  0.01093  143 LEU   A C   
1190 O O   . LEU   A 146 ? 0.53417 0.89112 0.67621 -0.09931 0.06081  0.00152  143 LEU   A O   
1191 C CB  . LEU   A 146 ? 0.53420 0.85084 0.64483 -0.09727 0.06468  0.02519  143 LEU   A CB  
1192 C CG  . LEU   A 146 ? 0.62770 0.92864 0.72343 -0.09967 0.06777  0.03460  143 LEU   A CG  
1193 C CD1 . LEU   A 146 ? 0.53136 0.83440 0.62278 -0.09151 0.06379  0.03563  143 LEU   A CD1 
1194 C CD2 . LEU   A 146 ? 0.62066 0.90036 0.71035 -0.09835 0.06517  0.04134  143 LEU   A CD2 
1195 N N   . ALA   A 147 ? 0.52719 0.84938 0.65472 -0.09351 0.05356  0.01168  144 ALA   A N   
1196 C CA  . ALA   A 147 ? 0.49728 0.82717 0.63068 -0.08712 0.04491  0.00276  144 ALA   A CA  
1197 C C   . ALA   A 147 ? 0.64990 0.96271 0.77074 -0.07802 0.03795  0.00658  144 ALA   A C   
1198 O O   . ALA   A 147 ? 0.51879 0.81809 0.63106 -0.07821 0.04105  0.01488  144 ALA   A O   
1199 C CB  . ALA   A 147 ? 0.55143 0.88173 0.68988 -0.09331 0.04408  -0.00205 144 ALA   A CB  
1200 N N   . ASP   A 148 ? 0.60757 0.92082 0.72667 -0.07044 0.02800  -0.00037 145 ASP   A N   
1201 C CA  . ASP   A 148 ? 0.63838 0.93103 0.74010 -0.06394 0.02101  0.00277  145 ASP   A CA  
1202 C C   . ASP   A 148 ? 0.62496 0.91162 0.72024 -0.06126 0.02179  0.00805  145 ASP   A C   
1203 O O   . ASP   A 148 ? 0.61482 0.89311 0.70580 -0.06575 0.02815  0.01596  145 ASP   A O   
1204 C CB  . ASP   A 148 ? 0.59106 0.86629 0.68187 -0.06876 0.02480  0.00840  145 ASP   A CB  
1205 C CG  . ASP   A 148 ? 0.79401 1.04797 0.86371 -0.06465 0.01793  0.00930  145 ASP   A CG  
1206 O OD1 . ASP   A 148 ? 0.71984 0.96763 0.78096 -0.05797 0.00935  0.00736  145 ASP   A OD1 
1207 O OD2 . ASP   A 148 ? 0.77730 1.01831 0.83623 -0.06826 0.02113  0.01166  145 ASP   A OD2 
1208 N N   . PHE   A 149 ? 0.64673 0.93824 0.74214 -0.05314 0.01427  0.00224  146 PHE   A N   
1209 C CA  . PHE   A 149 ? 0.61344 0.89648 0.70054 -0.05002 0.01268  0.00561  146 PHE   A CA  
1210 C C   . PHE   A 149 ? 0.63960 0.89660 0.70524 -0.04495 0.00249  0.00651  146 PHE   A C   
1211 O O   . PHE   A 149 ? 0.64775 0.89574 0.70494 -0.04009 -0.00309 0.00583  146 PHE   A O   
1212 C CB  . PHE   A 149 ? 0.55382 0.85651 0.65213 -0.04429 0.01164  -0.00198 146 PHE   A CB  
1213 C CG  . PHE   A 149 ? 0.57581 0.89517 0.68527 -0.05206 0.02354  0.00083  146 PHE   A CG  
1214 C CD1 . PHE   A 149 ? 0.58029 0.91407 0.70156 -0.05965 0.03086  -0.00076 146 PHE   A CD1 
1215 C CD2 . PHE   A 149 ? 0.50408 0.82131 0.60887 -0.05248 0.02655  0.00507  146 PHE   A CD2 
1216 C CE1 . PHE   A 149 ? 0.54629 0.88842 0.67103 -0.06808 0.04144  0.00298  146 PHE   A CE1 
1217 C CE2 . PHE   A 149 ? 0.45709 0.78430 0.56585 -0.05924 0.03616  0.00834  146 PHE   A CE2 
1218 C CZ  . PHE   A 149 ? 0.54783 0.88573 0.66485 -0.06732 0.04384  0.00784  146 PHE   A CZ  
1219 N N   . GLY   A 150 ? 0.63846 0.87986 0.69156 -0.04671 -0.00015 0.00804  147 GLY   A N   
1220 C CA  . GLY   A 150 ? 0.70784 0.91854 0.73360 -0.04417 -0.00915 0.01009  147 GLY   A CA  
1221 C C   . GLY   A 150 ? 0.70153 0.89638 0.71517 -0.05303 -0.00282 0.01872  147 GLY   A C   
1222 O O   . GLY   A 150 ? 0.71902 0.88836 0.71028 -0.05212 -0.01014 0.02025  147 GLY   A O   
1223 N N   . LEU   A 151 ? 0.66813 0.87684 0.69588 -0.06175 0.00986  0.02360  148 LEU   A N   
1224 C CA  . LEU   A 151 ? 0.68838 0.89071 0.71233 -0.07033 0.01614  0.02941  148 LEU   A CA  
1225 C C   . LEU   A 151 ? 0.64022 0.85610 0.67761 -0.06835 0.01624  0.02910  148 LEU   A C   
1226 O O   . LEU   A 151 ? 0.67161 0.88774 0.71120 -0.07507 0.02066  0.03256  148 LEU   A O   
1227 C CB  . LEU   A 151 ? 0.65378 0.86379 0.68540 -0.07882 0.02812  0.03280  148 LEU   A CB  
1228 C CG  . LEU   A 151 ? 0.83132 1.02524 0.84499 -0.08291 0.03014  0.03326  148 LEU   A CG  
1229 C CD1 . LEU   A 151 ? 0.86401 1.06982 0.88883 -0.08901 0.04244  0.03414  148 LEU   A CD1 
1230 C CD2 . LEU   A 151 ? 0.78222 0.94783 0.76727 -0.08889 0.02705  0.03602  148 LEU   A CD2 
1231 N N   . ALA   A 152 ? 0.61857 0.84726 0.66514 -0.05965 0.01165  0.02390  149 ALA   A N   
1232 C CA  . ALA   A 152 ? 0.62058 0.86076 0.67585 -0.05738 0.01199  0.02292  149 ALA   A CA  
1233 C C   . ALA   A 152 ? 0.58441 0.80624 0.62424 -0.05423 0.00299  0.02124  149 ALA   A C   
1234 O O   . ALA   A 152 ? 0.63793 0.83809 0.65988 -0.05082 -0.00563 0.01943  149 ALA   A O   
1235 C CB  . ALA   A 152 ? 0.50685 0.76837 0.57573 -0.05102 0.01263  0.01676  149 ALA   A CB  
1236 N N   . ARG   A 153 ? 0.64427 0.87140 0.68813 -0.05514 0.00374  0.02175  150 ARG   A N   
1237 C CA  . ARG   A 153 ? 0.66724 0.87611 0.69644 -0.05256 -0.00517 0.01938  150 ARG   A CA  
1238 C C   . ARG   A 153 ? 0.70643 0.92937 0.74332 -0.04831 -0.00521 0.01612  150 ARG   A C   
1239 O O   . ARG   A 153 ? 0.69014 0.92846 0.73861 -0.05298 0.00181  0.01969  150 ARG   A O   
1240 C CB  . ARG   A 153 ? 0.72428 0.91348 0.74179 -0.06488 -0.00433 0.02509  150 ARG   A CB  
1241 C CG  . ARG   A 153 ? 0.91324 1.07705 0.91149 -0.06449 -0.01443 0.02287  150 ARG   A CG  
1242 C CD  . ARG   A 153 ? 0.99537 1.14480 0.98579 -0.08090 -0.01117 0.02786  150 ARG   A CD  
1243 N NE  . ARG   A 153 ? 1.04216 1.16195 1.01070 -0.08247 -0.02149 0.02588  150 ARG   A NE  
1244 C CZ  . ARG   A 153 ? 1.06839 1.15073 1.00725 -0.08460 -0.02896 0.02704  150 ARG   A CZ  
1245 N NH1 . ARG   A 153 ? 1.16258 1.23312 1.08922 -0.08549 -0.02733 0.03023  150 ARG   A NH1 
1246 N NH2 . ARG   A 153 ? 1.15251 1.20482 1.07002 -0.08572 -0.03939 0.02493  150 ARG   A NH2 
1247 N N   . ALA   A 154 ? 0.70044 0.91587 0.72833 -0.03831 -0.01412 0.00871  151 ALA   A N   
1248 C CA  . ALA   A 154 ? 0.75209 0.97607 0.78155 -0.03423 -0.01498 0.00462  151 ALA   A CA  
1249 C C   . ALA   A 154 ? 0.76996 0.97625 0.78950 -0.04205 -0.01903 0.00825  151 ALA   A C   
1250 O O   . ALA   A 154 ? 0.89117 1.07069 0.89458 -0.04483 -0.02649 0.00863  151 ALA   A O   
1251 C CB  . ALA   A 154 ? 0.64532 0.86935 0.66967 -0.01934 -0.02298 -0.00706 151 ALA   A CB  
1252 N N   . PHE   A 155 ? 0.73831 0.95780 0.76584 -0.04638 -0.01485 0.01067  152 PHE   A N   
1253 C CA  . PHE   A 155 ? 0.74019 0.94869 0.76296 -0.05430 -0.01927 0.01234  152 PHE   A CA  
1254 C C   . PHE   A 155 ? 0.80462 1.00881 0.81765 -0.04681 -0.02663 0.00542  152 PHE   A C   
1255 O O   . PHE   A 155 ? 0.82993 1.04938 0.84509 -0.03827 -0.02378 0.00148  152 PHE   A O   
1256 C CB  . PHE   A 155 ? 0.76234 0.98761 0.80073 -0.06284 -0.01278 0.01814  152 PHE   A CB  
1257 C CG  . PHE   A 155 ? 0.74643 0.98999 0.79101 -0.05718 -0.00945 0.01835  152 PHE   A CG  
1258 C CD1 . PHE   A 155 ? 0.71307 0.95706 0.75235 -0.05511 -0.01497 0.01576  152 PHE   A CD1 
1259 C CD2 . PHE   A 155 ? 0.67571 0.93265 0.72802 -0.05520 -0.00115 0.02140  152 PHE   A CD2 
1260 C CE1 . PHE   A 155 ? 0.78292 1.03834 0.82116 -0.05079 -0.01207 0.01694  152 PHE   A CE1 
1261 C CE2 . PHE   A 155 ? 0.74612 1.01378 0.79820 -0.05237 0.00233  0.02278  152 PHE   A CE2 
1262 C CZ  . PHE   A 155 ? 0.71384 0.97974 0.75724 -0.05002 -0.00302 0.02094  152 PHE   A CZ  
1263 N N   . GLY   A 156 ? 0.81697 0.99915 0.81749 -0.05132 -0.03544 0.00347  153 GLY   A N   
1264 C CA  . GLY   A 156 ? 0.97665 1.15113 0.96573 -0.04472 -0.04373 -0.00386 153 GLY   A CA  
1265 C C   . GLY   A 156 ? 0.99670 1.18416 0.99281 -0.05005 -0.04356 -0.00251 153 GLY   A C   
1266 O O   . GLY   A 156 ? 0.96156 1.16385 0.97275 -0.05820 -0.03812 0.00363  153 GLY   A O   
1267 N N   . VAL   A 157 ? 1.11476 1.29581 1.09873 -0.04373 -0.05095 -0.00953 154 VAL   A N   
1268 C CA  . VAL   A 157 ? 1.13417 1.32334 1.11962 -0.04669 -0.05435 -0.00993 154 VAL   A CA  
1269 C C   . VAL   A 157 ? 1.14837 1.31457 1.12117 -0.05144 -0.06688 -0.01577 154 VAL   A C   
1270 O O   . VAL   A 157 ? 1.20102 1.35225 1.15606 -0.04220 -0.07387 -0.02398 154 VAL   A O   
1271 C CB  . VAL   A 157 ? 1.13005 1.33293 1.10859 -0.03548 -0.05076 -0.01321 154 VAL   A CB  
1272 C CG1 . VAL   A 157 ? 1.09529 1.30238 1.07071 -0.03776 -0.05639 -0.01293 154 VAL   A CG1 
1273 C CG2 . VAL   A 157 ? 1.00943 1.23168 0.99857 -0.03346 -0.03789 -0.00772 154 VAL   A CG2 
1274 N N   . PRO   A 158 ? 1.11399 1.27747 1.09603 -0.06650 -0.06981 -0.01298 155 PRO   A N   
1275 C CA  . PRO   A 158 ? 1.07034 1.25343 1.07521 -0.07732 -0.06216 -0.00596 155 PRO   A CA  
1276 C C   . PRO   A 158 ? 1.06104 1.23702 1.06800 -0.08330 -0.05418 -0.00068 155 PRO   A C   
1277 O O   . PRO   A 158 ? 0.99945 1.15142 0.98873 -0.08023 -0.05693 -0.00214 155 PRO   A O   
1278 C CB  . PRO   A 158 ? 1.08169 1.26421 1.09385 -0.09103 -0.07003 -0.00949 155 PRO   A CB  
1279 C CG  . PRO   A 158 ? 1.12752 1.27668 1.11656 -0.09401 -0.07920 -0.01496 155 PRO   A CG  
1280 C CD  . PRO   A 158 ? 1.17094 1.31084 1.14096 -0.07483 -0.08150 -0.01873 155 PRO   A CD  
1281 N N   . VAL   A 159 ? 0.98837 1.18346 1.01497 -0.09059 -0.04531 0.00475  156 VAL   A N   
1282 C CA  . VAL   A 159 ? 0.93751 1.12624 0.96434 -0.09701 -0.03712 0.00965  156 VAL   A CA  
1283 C C   . VAL   A 159 ? 0.96562 1.13799 0.98810 -0.11574 -0.03804 0.00926  156 VAL   A C   
1284 O O   . VAL   A 159 ? 0.99446 1.16811 1.02142 -0.12480 -0.04388 0.00490  156 VAL   A O   
1285 C CB  . VAL   A 159 ? 0.85281 1.06801 0.90067 -0.09633 -0.02658 0.01448  156 VAL   A CB  
1286 C CG1 . VAL   A 159 ? 0.79238 1.02245 0.84321 -0.08190 -0.02594 0.01504  156 VAL   A CG1 
1287 C CG2 . VAL   A 159 ? 0.83632 1.07056 0.90578 -0.10842 -0.02440 0.01341  156 VAL   A CG2 
1288 N N   . ARG   A 160 ? 0.96263 1.11848 0.97454 -0.12289 -0.03231 0.01349  157 ARG   A N   
1289 C CA  . ARG   A 160 ? 1.00257 1.14287 1.00800 -0.14439 -0.02908 0.01455  157 ARG   A CA  
1290 C C   . ARG   A 160 ? 0.94261 1.09772 0.95940 -0.15213 -0.01512 0.01928  157 ARG   A C   
1291 O O   . ARG   A 160 ? 0.91279 1.08883 0.94310 -0.14026 -0.00983 0.02137  157 ARG   A O   
1292 C CB  . ARG   A 160 ? 0.99159 1.08392 0.96029 -0.14734 -0.03758 0.01498  157 ARG   A CB  
1293 C CG  . ARG   A 160 ? 0.98709 1.05774 0.93514 -0.13835 -0.03670 0.01954  157 ARG   A CG  
1294 C CD  . ARG   A 160 ? 1.04525 1.06287 0.95341 -0.14167 -0.04756 0.01974  157 ARG   A CD  
1295 N NE  . ARG   A 160 ? 1.17744 1.17059 1.06304 -0.13864 -0.04669 0.02486  157 ARG   A NE  
1296 C CZ  . ARG   A 160 ? 1.08959 1.07196 0.96370 -0.11695 -0.05544 0.02273  157 ARG   A CZ  
1297 N NH1 . ARG   A 160 ? 1.04771 1.04308 0.93105 -0.09707 -0.06351 0.01534  157 ARG   A NH1 
1298 N NH2 . ARG   A 160 ? 1.01808 0.97740 0.87089 -0.11526 -0.05613 0.02702  157 ARG   A NH2 
1299 N N   . THR   A 161 ? 0.87589 1.01883 0.88536 -0.17341 -0.00848 0.02049  158 THR   A N   
1300 C CA  . THR   A 161 ? 0.92808 1.08521 0.94651 -0.18260 0.00620  0.02353  158 THR   A CA  
1301 C C   . THR   A 161 ? 0.99262 1.12989 0.98990 -0.17104 0.00713  0.02933  158 THR   A C   
1302 O O   . THR   A 161 ? 1.01660 1.11318 0.97973 -0.17196 0.00085  0.03235  158 THR   A O   
1303 C CB  . THR   A 161 ? 0.84354 0.98872 0.85330 -0.21051 0.01454  0.02305  158 THR   A CB  
1304 O OG1 . THR   A 161 ? 0.96725 1.13646 1.00186 -0.22161 0.01291  0.01557  158 THR   A OG1 
1305 C CG2 . THR   A 161 ? 0.94841 1.11075 0.96684 -0.22005 0.03156  0.02474  158 THR   A CG2 
1306 N N   . TYR   A 162 ? 0.93786 1.10209 0.95445 -0.15963 0.01338  0.03020  159 TYR   A N   
1307 C CA  . TYR   A 162 ? 0.93383 1.08500 0.93530 -0.14853 0.01384  0.03419  159 TYR   A CA  
1308 C C   . TYR   A 162 ? 0.88934 1.04208 0.88793 -0.16032 0.02712  0.03691  159 TYR   A C   
1309 O O   . TYR   A 162 ? 0.85239 1.01522 0.85914 -0.17825 0.03696  0.03531  159 TYR   A O   
1310 C CB  . TYR   A 162 ? 0.95585 1.13149 0.97641 -0.12881 0.01155  0.03305  159 TYR   A CB  
1311 C CG  . TYR   A 162 ? 0.87176 1.04426 0.89007 -0.11644 0.00001  0.02988  159 TYR   A CG  
1312 C CD1 . TYR   A 162 ? 0.85535 0.99617 0.84880 -0.11628 -0.01037 0.02830  159 TYR   A CD1 
1313 C CD2 . TYR   A 162 ? 0.86847 1.06675 0.90610 -0.10501 -0.00055 0.02811  159 TYR   A CD2 
1314 C CE1 . TYR   A 162 ? 0.94814 1.08708 0.93907 -0.10404 -0.02032 0.02366  159 TYR   A CE1 
1315 C CE2 . TYR   A 162 ? 0.77812 0.97383 0.81092 -0.09465 -0.00934 0.02455  159 TYR   A CE2 
1316 C CZ  . TYR   A 162 ? 0.90795 1.07599 0.91893 -0.09372 -0.01886 0.02164  159 TYR   A CZ  
1317 O OH  . TYR   A 162 ? 0.85802 1.02439 0.86378 -0.08245 -0.02708 0.01639  159 TYR   A OH  
1318 N N   . TPO   A 163 ? 0.88119 1.02575 0.86876 -0.15055 0.02757  0.03971  160 TPO   A N   
1319 C CA  . TPO   A 163 ? 0.92280 1.06412 0.90154 -0.15996 0.03918  0.04205  160 TPO   A CA  
1320 C CB  . TPO   A 163 ? 0.97946 1.10856 0.94403 -0.14559 0.03464  0.04413  160 TPO   A CB  
1321 C CG2 . TPO   A 163 ? 0.88057 1.00576 0.83399 -0.15459 0.04634  0.04594  160 TPO   A CG2 
1322 O OG1 . TPO   A 163 ? 1.00725 1.09925 0.94087 -0.13975 0.02093  0.04568  160 TPO   A OG1 
1323 P P   . TPO   A 163 ? 0.92349 1.02038 0.86407 -0.11527 0.00642  0.04184  160 TPO   A P   
1324 O O1P . TPO   A 163 ? 1.00501 1.05699 0.90819 -0.11233 -0.00780 0.04224  160 TPO   A O1P 
1325 O O2P . TPO   A 163 ? 0.84203 0.96779 0.81141 -0.11172 0.00676  0.03866  160 TPO   A O2P 
1326 O O3P . TPO   A 163 ? 0.92865 1.04111 0.87865 -0.10653 0.00994  0.04127  160 TPO   A O3P 
1327 C C   . TPO   A 163 ? 0.87457 1.05605 0.88679 -0.16508 0.05268  0.03836  160 TPO   A C   
1328 O O   . TPO   A 163 ? 0.90884 1.11832 0.94815 -0.15225 0.05134  0.03588  160 TPO   A O   
1329 N N   . HIS   A 164 ? 0.86774 1.05054 0.87621 -0.18401 0.06561  0.03733  161 HIS   A N   
1330 C CA  . HIS   A 164 ? 0.99816 1.22091 1.03943 -0.18872 0.07873  0.03111  161 HIS   A CA  
1331 C C   . HIS   A 164 ? 1.02084 1.25087 1.06297 -0.18058 0.08614  0.03107  161 HIS   A C   
1332 O O   . HIS   A 164 ? 0.97390 1.17551 0.98668 -0.17754 0.08379  0.03606  161 HIS   A O   
1333 C CB  . HIS   A 164 ? 1.04174 1.26810 1.08152 -0.21425 0.09156  0.02758  161 HIS   A CB  
1334 C CG  . HIS   A 164 ? 1.06922 1.25768 1.06637 -0.23008 0.09914  0.03308  161 HIS   A CG  
1335 N ND1 . HIS   A 164 ? 1.16580 1.36023 1.15692 -0.23733 0.11457  0.03157  161 HIS   A ND1 
1336 C CD2 . HIS   A 164 ? 1.12763 1.26781 1.08193 -0.23928 0.09238  0.04001  161 HIS   A CD2 
1337 C CE1 . HIS   A 164 ? 1.22245 1.37342 1.16703 -0.25144 0.11751  0.03809  161 HIS   A CE1 
1338 N NE2 . HIS   A 164 ? 1.34552 1.46148 1.26650 -0.25253 0.10345  0.04356  161 HIS   A NE2 
1339 N N   . GLU   A 165 ? 0.97090 1.23809 1.04637 -0.17593 0.09337  0.02442  162 GLU   A N   
1340 C CA  . GLU   A 165 ? 0.95308 1.22950 1.03206 -0.16916 0.10144  0.02228  162 GLU   A CA  
1341 C C   . GLU   A 165 ? 0.87262 1.13191 0.93932 -0.15207 0.09115  0.02764  162 GLU   A C   
1342 O O   . GLU   A 165 ? 1.00805 1.25089 1.05442 -0.15113 0.09394  0.02958  162 GLU   A O   
1343 C CB  . GLU   A 165 ? 0.95962 1.22404 1.01566 -0.18659 0.11637  0.02158  162 GLU   A CB  
1344 C CG  . GLU   A 165 ? 1.00705 1.29039 1.07508 -0.20769 0.12929  0.01517  162 GLU   A CG  
1345 C CD  . GLU   A 165 ? 1.17775 1.44532 1.21665 -0.22793 0.14604  0.01523  162 GLU   A CD  
1346 O OE1 . GLU   A 165 ? 1.21805 1.47283 1.23816 -0.22210 0.14981  0.01690  162 GLU   A OE1 
1347 O OE2 . GLU   A 165 ? 1.17412 1.44063 1.20677 -0.25093 0.15564  0.01345  162 GLU   A OE2 
1348 N N   . VAL   A 166 ? 0.81956 1.08377 0.89851 -0.13940 0.07938  0.02921  163 VAL   A N   
1349 C CA  . VAL   A 166 ? 0.84928 1.10355 0.92177 -0.12505 0.07095  0.03262  163 VAL   A CA  
1350 C C   . VAL   A 166 ? 0.75431 1.02885 0.84807 -0.11495 0.07378  0.02955  163 VAL   A C   
1351 O O   . VAL   A 166 ? 0.76409 1.06013 0.87803 -0.11623 0.08022  0.02424  163 VAL   A O   
1352 C CB  . VAL   A 166 ? 0.82119 1.06913 0.89233 -0.11790 0.05861  0.03521  163 VAL   A CB  
1353 C CG1 . VAL   A 166 ? 0.87835 1.09845 0.92283 -0.12481 0.05327  0.03784  163 VAL   A CG1 
1354 C CG2 . VAL   A 166 ? 0.61500 0.88463 0.70980 -0.11628 0.05651  0.03259  163 VAL   A CG2 
1355 N N   . VAL   A 167 ? 0.68267 0.95004 0.77194 -0.10497 0.06841  0.03183  164 VAL   A N   
1356 C CA  . VAL   A 167 ? 0.67342 0.95131 0.77651 -0.09583 0.06916  0.03014  164 VAL   A CA  
1357 C C   . VAL   A 167 ? 0.64550 0.92574 0.74794 -0.09795 0.07857  0.02583  164 VAL   A C   
1358 O O   . VAL   A 167 ? 0.63069 0.91817 0.73472 -0.10626 0.08721  0.02208  164 VAL   A O   
1359 C CB  . VAL   A 167 ? 0.62717 0.92223 0.75139 -0.08992 0.06592  0.02876  164 VAL   A CB  
1360 C CG1 . VAL   A 167 ? 0.62807 0.92432 0.75886 -0.08019 0.06431  0.02851  164 VAL   A CG1 
1361 C CG2 . VAL   A 167 ? 0.64377 0.93589 0.76549 -0.08888 0.05751  0.03219  164 VAL   A CG2 
1362 N N   . THR   A 168 ? 0.61647 0.89090 0.71598 -0.09159 0.07768  0.02543  165 THR   A N   
1363 C CA  . THR   A 168 ? 0.56191 0.83811 0.66092 -0.09134 0.08576  0.02006  165 THR   A CA  
1364 C C   . THR   A 168 ? 0.63814 0.93613 0.76025 -0.08773 0.09072  0.01359  165 THR   A C   
1365 O O   . THR   A 168 ? 0.57997 0.88776 0.71795 -0.08138 0.08456  0.01409  165 THR   A O   
1366 C CB  . THR   A 168 ? 0.64391 0.90932 0.73765 -0.08472 0.08174  0.02021  165 THR   A CB  
1367 O OG1 . THR   A 168 ? 0.67754 0.92918 0.75631 -0.08643 0.07490  0.02431  165 THR   A OG1 
1368 C CG2 . THR   A 168 ? 0.52963 0.79154 0.61636 -0.08484 0.08924  0.01417  165 THR   A CG2 
1369 N N   . LEU   A 169 ? 0.45886 0.76488 0.58205 -0.09108 0.10153  0.00636  166 LEU   A N   
1370 C CA  . LEU   A 169 ? 0.55874 0.89191 0.70677 -0.08940 0.10768  -0.00279 166 LEU   A CA  
1371 C C   . LEU   A 169 ? 0.59573 0.93699 0.76334 -0.07325 0.09932  -0.00625 166 LEU   A C   
1372 O O   . LEU   A 169 ? 0.52769 0.88800 0.71676 -0.06860 0.09527  -0.01009 166 LEU   A O   
1373 C CB  . LEU   A 169 ? 0.49299 0.83417 0.63723 -0.09553 0.12252  -0.01162 166 LEU   A CB  
1374 C CG  . LEU   A 169 ? 0.55225 0.92835 0.72487 -0.09658 0.13183  -0.02409 166 LEU   A CG  
1375 C CD1 . LEU   A 169 ? 0.54244 0.93123 0.72442 -0.10863 0.13202  -0.02213 166 LEU   A CD1 
1376 C CD2 . LEU   A 169 ? 0.47623 0.86031 0.64191 -0.10397 0.14901  -0.03357 166 LEU   A CD2 
1377 N N   . TRP   A 170 ? 0.55971 0.88409 0.71816 -0.06473 0.09535  -0.00517 167 TRP   A N   
1378 C CA  . TRP   A 170 ? 0.53864 0.86241 0.70882 -0.04972 0.08681  -0.00802 167 TRP   A CA  
1379 C C   . TRP   A 170 ? 0.56200 0.88158 0.73512 -0.04592 0.07498  -0.00041 167 TRP   A C   
1380 O O   . TRP   A 170 ? 0.50172 0.82401 0.68573 -0.03375 0.06686  -0.00340 167 TRP   A O   
1381 C CB  . TRP   A 170 ? 0.54586 0.84618 0.70050 -0.04480 0.08481  -0.00725 167 TRP   A CB  
1382 C CG  . TRP   A 170 ? 0.59736 0.90138 0.75045 -0.04330 0.09439  -0.01749 167 TRP   A CG  
1383 C CD1 . TRP   A 170 ? 0.60157 0.92823 0.76400 -0.04772 0.10652  -0.02669 167 TRP   A CD1 
1384 C CD2 . TRP   A 170 ? 0.63028 0.91465 0.77045 -0.03796 0.09351  -0.02058 167 TRP   A CD2 
1385 N NE1 . TRP   A 170 ? 0.62409 0.94702 0.77926 -0.04447 0.11386  -0.03553 167 TRP   A NE1 
1386 C CE2 . TRP   A 170 ? 0.63303 0.92913 0.77441 -0.03774 0.10509  -0.03203 167 TRP   A CE2 
1387 C CE3 . TRP   A 170 ? 0.61450 0.87227 0.74141 -0.03490 0.08469  -0.01538 167 TRP   A CE3 
1388 C CZ2 . TRP   A 170 ? 0.71372 0.99456 0.84270 -0.03254 0.10680  -0.03862 167 TRP   A CZ2 
1389 C CZ3 . TRP   A 170 ? 0.73181 0.97393 0.84752 -0.03113 0.08591  -0.02162 167 TRP   A CZ3 
1390 C CH2 . TRP   A 170 ? 0.70478 0.95780 0.82120 -0.02895 0.09622  -0.03323 167 TRP   A CH2 
1391 N N   . TYR   A 171 ? 0.46104 0.77263 0.62271 -0.05490 0.07304  0.00857  168 TYR   A N   
1392 C CA  . TYR   A 171 ? 0.50657 0.81259 0.66676 -0.05224 0.06321  0.01559  168 TYR   A CA  
1393 C C   . TYR   A 171 ? 0.45066 0.77059 0.61787 -0.05859 0.06246  0.01642  168 TYR   A C   
1394 O O   . TYR   A 171 ? 0.49237 0.80600 0.65325 -0.05920 0.05586  0.02260  168 TYR   A O   
1395 C CB  . TYR   A 171 ? 0.54111 0.82642 0.68260 -0.05593 0.06083  0.02363  168 TYR   A CB  
1396 C CG  . TYR   A 171 ? 0.56449 0.83477 0.69808 -0.05288 0.06196  0.02217  168 TYR   A CG  
1397 C CD1 . TYR   A 171 ? 0.52220 0.77841 0.65256 -0.04505 0.05569  0.02347  168 TYR   A CD1 
1398 C CD2 . TYR   A 171 ? 0.54129 0.80780 0.66739 -0.05800 0.06829  0.01930  168 TYR   A CD2 
1399 C CE1 . TYR   A 171 ? 0.56354 0.80246 0.68493 -0.04333 0.05609  0.02172  168 TYR   A CE1 
1400 C CE2 . TYR   A 171 ? 0.49237 0.74444 0.61091 -0.05555 0.06848  0.01690  168 TYR   A CE2 
1401 C CZ  . TYR   A 171 ? 0.58071 0.81918 0.69778 -0.04863 0.06258  0.01794  168 TYR   A CZ  
1402 O OH  . TYR   A 171 ? 0.61765 0.83811 0.72532 -0.04727 0.06212  0.01527  168 TYR   A OH  
1403 N N   . ARG   A 172 ? 0.45496 0.79354 0.63439 -0.06430 0.06971  0.00949  169 ARG   A N   
1404 C CA  . ARG   A 172 ? 0.46946 0.81905 0.65406 -0.07361 0.06998  0.00950  169 ARG   A CA  
1405 C C   . ARG   A 172 ? 0.44461 0.81413 0.65161 -0.06625 0.06230  0.00391  169 ARG   A C   
1406 O O   . ARG   A 172 ? 0.42575 0.81332 0.65222 -0.05830 0.06303  -0.00556 169 ARG   A O   
1407 C CB  . ARG   A 172 ? 0.46445 0.82225 0.64818 -0.08698 0.08282  0.00477  169 ARG   A CB  
1408 C CG  . ARG   A 172 ? 0.53951 0.90081 0.72182 -0.10046 0.08390  0.00591  169 ARG   A CG  
1409 C CD  . ARG   A 172 ? 0.50616 0.86931 0.68062 -0.11627 0.09808  0.00240  169 ARG   A CD  
1410 N NE  . ARG   A 172 ? 0.55861 0.89692 0.70575 -0.11807 0.10204  0.00750  169 ARG   A NE  
1411 C CZ  . ARG   A 172 ? 0.67244 1.00368 0.80291 -0.13057 0.11386  0.00605  169 ARG   A CZ  
1412 N NH1 . ARG   A 172 ? 0.47390 0.82214 0.61254 -0.14476 0.12548  -0.00035 169 ARG   A NH1 
1413 N NH2 . ARG   A 172 ? 0.56570 0.87226 0.66963 -0.12976 0.11412  0.01056  169 ARG   A NH2 
1414 N N   . ALA   A 173 ? 0.45367 0.82031 0.65781 -0.06769 0.05393  0.00841  170 ALA   A N   
1415 C CA  . ALA   A 173 ? 0.41793 0.80060 0.64001 -0.05996 0.04365  0.00341  170 ALA   A CA  
1416 C C   . ALA   A 173 ? 0.43297 0.84751 0.68193 -0.06665 0.04926  -0.00864 170 ALA   A C   
1417 O O   . ALA   A 173 ? 0.49261 0.91160 0.73968 -0.08200 0.06137  -0.01011 170 ALA   A O   
1418 C CB  . ALA   A 173 ? 0.49176 0.86299 0.70138 -0.06185 0.03453  0.01029  170 ALA   A CB  
1419 N N   . PRO   A 174 ? 0.47079 0.90790 0.74437 -0.05585 0.04045  -0.01816 171 PRO   A N   
1420 C CA  . PRO   A 174 ? 0.41656 0.89134 0.72164 -0.06286 0.04683  -0.03259 171 PRO   A CA  
1421 C C   . PRO   A 174 ? 0.44075 0.92322 0.74813 -0.08144 0.04909  -0.03262 171 PRO   A C   
1422 O O   . PRO   A 174 ? 0.44787 0.95467 0.77225 -0.09636 0.06116  -0.04176 171 PRO   A O   
1423 C CB  . PRO   A 174 ? 0.45712 0.95174 0.78699 -0.04280 0.03201  -0.04309 171 PRO   A CB  
1424 C CG  . PRO   A 174 ? 0.39644 0.85966 0.70209 -0.03109 0.01606  -0.03129 171 PRO   A CG  
1425 C CD  . PRO   A 174 ? 0.41428 0.84349 0.68739 -0.03667 0.02406  -0.01734 171 PRO   A CD  
1426 N N   . GLU   A 175 ? 0.47564 0.93722 0.76500 -0.08204 0.03855  -0.02336 172 GLU   A N   
1427 C CA  . GLU   A 175 ? 0.52801 0.99153 0.81608 -0.09960 0.03956  -0.02358 172 GLU   A CA  
1428 C C   . GLU   A 175 ? 0.53343 0.97913 0.80007 -0.11829 0.05450  -0.01769 172 GLU   A C   
1429 O O   . GLU   A 175 ? 0.51104 0.96290 0.78031 -0.13715 0.06082  -0.02120 172 GLU   A O   
1430 C CB  . GLU   A 175 ? 0.46628 0.90947 0.73733 -0.09387 0.02442  -0.01606 172 GLU   A CB  
1431 C CG  . GLU   A 175 ? 0.53298 0.94099 0.77091 -0.08807 0.02350  -0.00260 172 GLU   A CG  
1432 C CD  . GLU   A 175 ? 0.48102 0.88142 0.71459 -0.06920 0.01547  0.00071  172 GLU   A CD  
1433 O OE1 . GLU   A 175 ? 0.51136 0.92926 0.76470 -0.05918 0.01297  -0.00671 172 GLU   A OE1 
1434 O OE2 . GLU   A 175 ? 0.42520 0.80134 0.63465 -0.06465 0.01168  0.01006  172 GLU   A OE2 
1435 N N   . ILE   A 176 ? 0.50630 0.92790 0.74985 -0.11395 0.05936  -0.00907 173 ILE   A N   
1436 C CA  . ILE   A 176 ? 0.49453 0.89739 0.71539 -0.12918 0.07178  -0.00427 173 ILE   A CA  
1437 C C   . ILE   A 176 ? 0.52571 0.95184 0.76174 -0.14039 0.08774  -0.01386 173 ILE   A C   
1438 O O   . ILE   A 176 ? 0.56207 0.98350 0.78750 -0.16058 0.09846  -0.01423 173 ILE   A O   
1439 C CB  . ILE   A 176 ? 0.51393 0.88849 0.70914 -0.12007 0.07081  0.00542  173 ILE   A CB  
1440 C CG1 . ILE   A 176 ? 0.55281 0.91001 0.73584 -0.10994 0.05726  0.01283  173 ILE   A CG1 
1441 C CG2 . ILE   A 176 ? 0.50920 0.86093 0.67748 -0.13369 0.08018  0.01014  173 ILE   A CG2 
1442 C CD1 . ILE   A 176 ? 0.59350 0.93458 0.76080 -0.11954 0.05263  0.01628  173 ILE   A CD1 
1443 N N   . LEU   A 177 ? 0.48240 0.93233 0.74130 -0.12772 0.08979  -0.02232 174 LEU   A N   
1444 C CA  . LEU   A 177 ? 0.51791 0.99463 0.79372 -0.13628 0.10613  -0.03399 174 LEU   A CA  
1445 C C   . LEU   A 177 ? 0.56376 1.07446 0.86695 -0.15212 0.11154  -0.04573 174 LEU   A C   
1446 O O   . LEU   A 177 ? 0.55940 1.08651 0.86744 -0.16975 0.12934  -0.05330 174 LEU   A O   
1447 C CB  . LEU   A 177 ? 0.51931 1.01368 0.81504 -0.11548 0.10416  -0.04233 174 LEU   A CB  
1448 C CG  . LEU   A 177 ? 0.52357 0.98705 0.79423 -0.10290 0.10172  -0.03316 174 LEU   A CG  
1449 C CD1 . LEU   A 177 ? 0.35637 0.83091 0.64542 -0.07999 0.09338  -0.04039 174 LEU   A CD1 
1450 C CD2 . LEU   A 177 ? 0.50454 0.95647 0.75419 -0.11526 0.11837  -0.03217 174 LEU   A CD2 
1451 N N   . LEU   A 178 ? 0.58422 1.10604 0.90446 -0.14758 0.09702  -0.04805 175 LEU   A N   
1452 C CA  . LEU   A 178 ? 0.58527 1.14123 0.93443 -0.16301 0.09980  -0.06042 175 LEU   A CA  
1453 C C   . LEU   A 178 ? 0.59066 1.12247 0.91596 -0.18714 0.10219  -0.05262 175 LEU   A C   
1454 O O   . LEU   A 178 ? 0.63485 1.19088 0.98075 -0.20432 0.10506  -0.06219 175 LEU   A O   
1455 C CB  . LEU   A 178 ? 0.53313 1.11492 0.91415 -0.14459 0.08059  -0.06921 175 LEU   A CB  
1456 C CG  . LEU   A 178 ? 0.56902 1.18308 0.98171 -0.12260 0.07765  -0.08259 175 LEU   A CG  
1457 C CD1 . LEU   A 178 ? 0.51664 1.14634 0.95211 -0.10228 0.05455  -0.08923 175 LEU   A CD1 
1458 C CD2 . LEU   A 178 ? 0.48470 1.14373 0.92929 -0.13590 0.09675  -0.10055 175 LEU   A CD2 
1459 N N   . GLY   A 179 ? 0.64115 1.12593 0.92421 -0.18857 0.10016  -0.03674 176 GLY   A N   
1460 C CA  . GLY   A 179 ? 0.63122 1.08590 0.88549 -0.21031 0.10242  -0.02940 176 GLY   A CA  
1461 C C   . GLY   A 179 ? 0.61307 1.05793 0.86642 -0.20879 0.08531  -0.02719 176 GLY   A C   
1462 O O   . GLY   A 179 ? 0.72410 1.16854 0.97730 -0.22955 0.08698  -0.03051 176 GLY   A O   
1463 N N   . CYS   A 180 ? 0.50365 0.93872 0.75390 -0.18580 0.06938  -0.02184 177 CYS   A N   
1464 C CA  . CYS   A 180 ? 0.65692 1.08104 0.90270 -0.18260 0.05309  -0.02007 177 CYS   A CA  
1465 C C   . CYS   A 180 ? 0.71597 1.09569 0.92214 -0.19393 0.05181  -0.01009 177 CYS   A C   
1466 O O   . CYS   A 180 ? 0.63279 0.98423 0.81079 -0.19305 0.05721  -0.00133 177 CYS   A O   
1467 C CB  . CYS   A 180 ? 0.63119 1.05370 0.87852 -0.15625 0.03854  -0.01655 177 CYS   A CB  
1468 S SG  . CYS   A 180 ? 0.74601 1.13373 0.96028 -0.14217 0.03981  -0.00285 177 CYS   A SG  
1469 N N   . LYS   A 181 ? 0.76609 1.13866 0.96967 -0.20369 0.04305  -0.01254 178 LYS   A N   
1470 C CA  . LYS   A 181 ? 0.81004 1.13714 0.97481 -0.21198 0.03877  -0.00447 178 LYS   A CA  
1471 C C   . LYS   A 181 ? 0.82116 1.12349 0.96424 -0.18941 0.02749  0.00377  178 LYS   A C   
1472 O O   . LYS   A 181 ? 0.89032 1.16150 1.00405 -0.18696 0.02937  0.01156  178 LYS   A O   
1473 C CB  . LYS   A 181 ? 0.86314 1.18828 1.03110 -0.22733 0.03096  -0.01052 178 LYS   A CB  
1474 C CG  . LYS   A 181 ? 0.95228 1.28360 1.12491 -0.25835 0.04427  -0.01608 178 LYS   A CG  
1475 C CD  . LYS   A 181 ? 1.11749 1.44533 1.29331 -0.27396 0.03475  -0.02261 178 LYS   A CD  
1476 C CE  . LYS   A 181 ? 1.14227 1.42037 1.27903 -0.26614 0.01952  -0.01480 178 LYS   A CE  
1477 N NZ  . LYS   A 181 ? 1.15348 1.38128 1.24473 -0.27325 0.02496  -0.00394 178 LYS   A NZ  
1478 N N   . TYR   A 182 ? 0.76140 1.07787 0.91805 -0.17297 0.01561  0.00131  179 TYR   A N   
1479 C CA  . TYR   A 182 ? 0.79903 1.09693 0.93721 -0.15363 0.00653  0.00737  179 TYR   A CA  
1480 C C   . TYR   A 182 ? 0.79814 1.11504 0.95024 -0.13645 0.00833  0.00909  179 TYR   A C   
1481 O O   . TYR   A 182 ? 0.81354 1.15956 0.99245 -0.13448 0.01000  0.00368  179 TYR   A O   
1482 C CB  . TYR   A 182 ? 0.71577 1.00855 0.85022 -0.14881 -0.00808 0.00397  179 TYR   A CB  
1483 C CG  . TYR   A 182 ? 0.80742 1.08021 0.92886 -0.16625 -0.01195 0.00090  179 TYR   A CG  
1484 C CD1 . TYR   A 182 ? 0.82482 1.06180 0.91653 -0.17533 -0.00864 0.00588  179 TYR   A CD1 
1485 C CD2 . TYR   A 182 ? 0.83678 1.12376 0.97375 -0.17371 -0.02039 -0.00739 179 TYR   A CD2 
1486 C CE1 . TYR   A 182 ? 0.89456 1.10643 0.96951 -0.19215 -0.01309 0.00360  179 TYR   A CE1 
1487 C CE2 . TYR   A 182 ? 0.88570 1.15176 1.00952 -0.19168 -0.02418 -0.01053 179 TYR   A CE2 
1488 C CZ  . TYR   A 182 ? 0.95450 1.18111 1.04597 -0.20130 -0.02018 -0.00456 179 TYR   A CZ  
1489 O OH  . TYR   A 182 ? 0.98309 1.18236 1.05682 -0.22001 -0.02480 -0.00717 179 TYR   A OH  
1490 N N   . TYR   A 183 ? 0.72720 1.02698 0.86088 -0.12405 0.00741  0.01567  180 TYR   A N   
1491 C CA  . TYR   A 183 ? 0.75224 1.06307 0.89316 -0.10915 0.00819  0.01823  180 TYR   A CA  
1492 C C   . TYR   A 183 ? 0.65424 0.94662 0.77388 -0.09824 0.00413  0.02314  180 TYR   A C   
1493 O O   . TYR   A 183 ? 0.73588 1.00817 0.83688 -0.10049 0.00205  0.02403  180 TYR   A O   
1494 C CB  . TYR   A 183 ? 0.77988 1.09857 0.92870 -0.11104 0.01990  0.01940  180 TYR   A CB  
1495 C CG  . TYR   A 183 ? 0.74302 1.03951 0.87049 -0.11568 0.02638  0.02425  180 TYR   A CG  
1496 C CD1 . TYR   A 183 ? 0.67755 0.96254 0.79216 -0.10512 0.02573  0.02889  180 TYR   A CD1 
1497 C CD2 . TYR   A 183 ? 0.77476 1.06127 0.89375 -0.13130 0.03277  0.02362  180 TYR   A CD2 
1498 C CE1 . TYR   A 183 ? 0.73711 1.00309 0.83337 -0.10744 0.02893  0.03179  180 TYR   A CE1 
1499 C CE2 . TYR   A 183 ? 0.66087 0.92271 0.75576 -0.13402 0.03621  0.02817  180 TYR   A CE2 
1500 C CZ  . TYR   A 183 ? 0.66456 0.91718 0.74940 -0.12077 0.03315  0.03175  180 TYR   A CZ  
1501 O OH  . TYR   A 183 ? 0.78132 1.01059 0.84329 -0.12166 0.03396  0.03481  180 TYR   A OH  
1502 N N   . SER   A 184 ? 0.65249 0.95145 0.77442 -0.08651 0.00297  0.02547  181 SER   A N   
1503 C CA  . SER   A 184 ? 0.75332 1.04046 0.85796 -0.07801 0.00180  0.02879  181 SER   A CA  
1504 C C   . SER   A 184 ? 0.66938 0.96132 0.77608 -0.07086 0.00633  0.03273  181 SER   A C   
1505 O O   . SER   A 184 ? 0.67423 0.96950 0.78821 -0.07268 0.01322  0.03409  181 SER   A O   
1506 C CB  . SER   A 184 ? 0.72370 1.00661 0.81850 -0.07346 -0.00761 0.02649  181 SER   A CB  
1507 O OG  . SER   A 184 ? 0.81781 1.11129 0.92056 -0.06880 -0.01342 0.02585  181 SER   A OG  
1508 N N   . THR   A 185 ? 0.62789 0.91754 0.72517 -0.06372 0.00264  0.03449  182 THR   A N   
1509 C CA  . THR   A 185 ? 0.64936 0.93675 0.74130 -0.05952 0.00761  0.03897  182 THR   A CA  
1510 C C   . THR   A 185 ? 0.54978 0.84179 0.65284 -0.05684 0.00745  0.04049  182 THR   A C   
1511 O O   . THR   A 185 ? 0.57742 0.86433 0.67669 -0.05540 0.01243  0.04408  182 THR   A O   
1512 C CB  . THR   A 185 ? 0.57676 0.85768 0.65087 -0.05508 0.00486  0.04056  182 THR   A CB  
1513 O OG1 . THR   A 185 ? 0.60163 0.88232 0.67403 -0.05124 -0.00520 0.03965  182 THR   A OG1 
1514 C CG2 . THR   A 185 ? 0.63974 0.91831 0.70399 -0.05548 0.00580  0.03684  182 THR   A CG2 
1515 N N   . ALA   A 186 ? 0.53061 0.83273 0.64818 -0.05590 0.00132  0.03650  183 ALA   A N   
1516 C CA  . ALA   A 186 ? 0.52791 0.83584 0.65713 -0.04966 -0.00123 0.03556  183 ALA   A CA  
1517 C C   . ALA   A 186 ? 0.50869 0.82038 0.64799 -0.05235 0.00852  0.03511  183 ALA   A C   
1518 O O   . ALA   A 186 ? 0.51951 0.82886 0.66151 -0.04575 0.00803  0.03556  183 ALA   A O   
1519 C CB  . ALA   A 186 ? 0.48202 0.80650 0.62985 -0.04764 -0.01040 0.02823  183 ALA   A CB  
1520 N N   . VAL   A 187 ? 0.48407 0.79800 0.62558 -0.06136 0.01637  0.03404  184 VAL   A N   
1521 C CA  . VAL   A 187 ? 0.50954 0.82609 0.65776 -0.06430 0.02539  0.03294  184 VAL   A CA  
1522 C C   . VAL   A 187 ? 0.48375 0.78699 0.61972 -0.06117 0.02899  0.03787  184 VAL   A C   
1523 O O   . VAL   A 187 ? 0.52318 0.82624 0.66382 -0.05935 0.03330  0.03682  184 VAL   A O   
1524 C CB  . VAL   A 187 ? 0.57220 0.88877 0.71908 -0.07534 0.03164  0.03130  184 VAL   A CB  
1525 C CG1 . VAL   A 187 ? 0.52810 0.85724 0.68713 -0.08189 0.02917  0.02598  184 VAL   A CG1 
1526 C CG2 . VAL   A 187 ? 0.61101 0.91207 0.73912 -0.07704 0.03076  0.03520  184 VAL   A CG2 
1527 N N   . ASP   A 188 ? 0.56088 0.85402 0.68171 -0.06114 0.02774  0.04206  185 ASP   A N   
1528 C CA  . ASP   A 188 ? 0.52651 0.80976 0.63759 -0.06096 0.03193  0.04564  185 ASP   A CA  
1529 C C   . ASP   A 188 ? 0.57599 0.85007 0.68205 -0.05512 0.02842  0.04864  185 ASP   A C   
1530 O O   . ASP   A 188 ? 0.58470 0.84971 0.68700 -0.05541 0.03194  0.05026  185 ASP   A O   
1531 C CB  . ASP   A 188 ? 0.57751 0.85771 0.67672 -0.06361 0.03306  0.04694  185 ASP   A CB  
1532 C CG  . ASP   A 188 ? 0.59249 0.87571 0.69296 -0.06700 0.03475  0.04361  185 ASP   A CG  
1533 O OD1 . ASP   A 188 ? 0.55433 0.83766 0.65999 -0.06949 0.03747  0.04216  185 ASP   A OD1 
1534 O OD2 . ASP   A 188 ? 0.58437 0.86790 0.67822 -0.06647 0.03287  0.04197  185 ASP   A OD2 
1535 N N   . ILE   A 189 ? 0.55934 0.83236 0.66268 -0.04955 0.02006  0.04919  186 ILE   A N   
1536 C CA  . ILE   A 189 ? 0.54285 0.80098 0.63585 -0.04225 0.01372  0.05240  186 ILE   A CA  
1537 C C   . ILE   A 189 ? 0.56138 0.82270 0.66910 -0.03536 0.01191  0.04799  186 ILE   A C   
1538 O O   . ILE   A 189 ? 0.56652 0.81026 0.66431 -0.03109 0.01036  0.05046  186 ILE   A O   
1539 C CB  . ILE   A 189 ? 0.50321 0.75853 0.58775 -0.03643 0.00278  0.05310  186 ILE   A CB  
1540 C CG1 . ILE   A 189 ? 0.58515 0.83436 0.65048 -0.04256 0.00592  0.05699  186 ILE   A CG1 
1541 C CG2 . ILE   A 189 ? 0.59753 0.83394 0.66946 -0.02627 -0.00728 0.05576  186 ILE   A CG2 
1542 C CD1 . ILE   A 189 ? 0.58212 0.81216 0.62452 -0.04754 0.01219  0.06357  186 ILE   A CD1 
1543 N N   . TRP   A 190 ? 0.44957 0.73261 0.58009 -0.03478 0.01252  0.04058  187 TRP   A N   
1544 C CA  . TRP   A 190 ? 0.53273 0.82448 0.68013 -0.02850 0.01321  0.03377  187 TRP   A CA  
1545 C C   . TRP   A 190 ? 0.51869 0.79988 0.66003 -0.03228 0.02238  0.03529  187 TRP   A C   
1546 O O   . TRP   A 190 ? 0.51301 0.78515 0.65422 -0.02448 0.02040  0.03303  187 TRP   A O   
1547 C CB  . TRP   A 190 ? 0.45421 0.77413 0.62643 -0.03216 0.01643  0.02498  187 TRP   A CB  
1548 C CG  . TRP   A 190 ? 0.42827 0.76306 0.62018 -0.02681 0.01999  0.01562  187 TRP   A CG  
1549 C CD1 . TRP   A 190 ? 0.46095 0.79708 0.65455 -0.03178 0.03149  0.01331  187 TRP   A CD1 
1550 C CD2 . TRP   A 190 ? 0.46073 0.81278 0.67370 -0.01432 0.01162  0.00555  187 TRP   A CD2 
1551 N NE1 . TRP   A 190 ? 0.44032 0.79380 0.65413 -0.02375 0.03253  0.00232  187 TRP   A NE1 
1552 C CE2 . TRP   A 190 ? 0.44873 0.81401 0.67684 -0.01238 0.02021  -0.00329 187 TRP   A CE2 
1553 C CE3 . TRP   A 190 ? 0.50384 0.86218 0.72431 -0.00349 -0.00334 0.00190  187 TRP   A CE3 
1554 C CZ2 . TRP   A 190 ? 0.42099 0.80870 0.67451 0.00053  0.01520  -0.01678 187 TRP   A CZ2 
1555 C CZ3 . TRP   A 190 ? 0.49938 0.87911 0.74524 0.00990  -0.01029 -0.01119 187 TRP   A CZ3 
1556 C CH2 . TRP   A 190 ? 0.46646 0.86226 0.73015 0.01206  -0.00060 -0.02096 187 TRP   A CH2 
1557 N N   . SER   A 191 ? 0.47875 0.75983 0.61442 -0.04314 0.03091  0.03810  188 SER   A N   
1558 C CA  . SER   A 191 ? 0.51581 0.78737 0.64530 -0.04712 0.03805  0.03878  188 SER   A CA  
1559 C C   . SER   A 191 ? 0.54786 0.79639 0.66040 -0.04538 0.03530  0.04416  188 SER   A C   
1560 O O   . SER   A 191 ? 0.57575 0.81303 0.68552 -0.04328 0.03673  0.04262  188 SER   A O   
1561 C CB  . SER   A 191 ? 0.47611 0.75092 0.60128 -0.05710 0.04419  0.04015  188 SER   A CB  
1562 O OG  . SER   A 191 ? 0.50056 0.78939 0.63531 -0.06067 0.04687  0.03617  188 SER   A OG  
1563 N N   . LEU   A 192 ? 0.44072 0.67997 0.53930 -0.04732 0.03181  0.05023  189 LEU   A N   
1564 C CA  . LEU   A 192 ? 0.57835 0.79254 0.65632 -0.04903 0.03058  0.05613  189 LEU   A CA  
1565 C C   . LEU   A 192 ? 0.59066 0.78692 0.66267 -0.03716 0.02111  0.05596  189 LEU   A C   
1566 O O   . LEU   A 192 ? 0.60571 0.77707 0.66234 -0.03776 0.02044  0.05875  189 LEU   A O   
1567 C CB  . LEU   A 192 ? 0.54510 0.75427 0.60691 -0.05505 0.03082  0.06197  189 LEU   A CB  
1568 C CG  . LEU   A 192 ? 0.71644 0.93821 0.77995 -0.06608 0.03981  0.06133  189 LEU   A CG  
1569 C CD1 . LEU   A 192 ? 0.60489 0.81851 0.64909 -0.07244 0.04200  0.06614  189 LEU   A CD1 
1570 C CD2 . LEU   A 192 ? 0.64441 0.86513 0.71212 -0.07264 0.04632  0.05900  189 LEU   A CD2 
1571 N N   . GLY   A 193 ? 0.59646 0.80417 0.68034 -0.02601 0.01257  0.05174  190 GLY   A N   
1572 C CA  . GLY   A 193 ? 0.58292 0.77725 0.66539 -0.01104 0.00132  0.04857  190 GLY   A CA  
1573 C C   . GLY   A 193 ? 0.57542 0.77098 0.66955 -0.00644 0.00492  0.04141  190 GLY   A C   
1574 O O   . GLY   A 193 ? 0.60181 0.77161 0.68309 0.00215  -0.00181 0.04130  190 GLY   A O   
1575 N N   . CYS   A 194 ? 0.49455 0.71667 0.60965 -0.01200 0.01518  0.03519  191 CYS   A N   
1576 C CA  . CYS   A 194 ? 0.57587 0.79893 0.69873 -0.00919 0.02052  0.02804  191 CYS   A CA  
1577 C C   . CYS   A 194 ? 0.56955 0.76458 0.67110 -0.01695 0.02413  0.03375  191 CYS   A C   
1578 O O   . CYS   A 194 ? 0.54138 0.71814 0.63681 -0.01015 0.02146  0.03022  191 CYS   A O   
1579 C CB  . CYS   A 194 ? 0.51586 0.76904 0.65852 -0.01635 0.03171  0.02163  191 CYS   A CB  
1580 S SG  . CYS   A 194 ? 0.54494 0.83401 0.71548 -0.01178 0.02991  0.01293  191 CYS   A SG  
1581 N N   . ILE   A 195 ? 0.59612 0.78832 0.68718 -0.03108 0.02978  0.04120  192 ILE   A N   
1582 C CA  . ILE   A 195 ? 0.70184 0.87205 0.77584 -0.04105 0.03359  0.04538  192 ILE   A CA  
1583 C C   . ILE   A 195 ? 0.72862 0.86328 0.77832 -0.03845 0.02573  0.05152  192 ILE   A C   
1584 O O   . ILE   A 195 ? 0.71732 0.82659 0.75308 -0.04164 0.02567  0.05203  192 ILE   A O   
1585 C CB  . ILE   A 195 ? 0.65754 0.83962 0.73063 -0.05555 0.04100  0.04928  192 ILE   A CB  
1586 C CG1 . ILE   A 195 ? 0.60971 0.81789 0.70017 -0.05733 0.04665  0.04361  192 ILE   A CG1 
1587 C CG2 . ILE   A 195 ? 0.69881 0.86313 0.75790 -0.06755 0.04497  0.05198  192 ILE   A CG2 
1588 C CD1 . ILE   A 195 ? 0.65584 0.87692 0.74697 -0.06681 0.05054  0.04570  192 ILE   A CD1 
1589 N N   . PHE   A 196 ? 0.67328 0.80200 0.71419 -0.03313 0.01817  0.05633  193 PHE   A N   
1590 C CA  . PHE   A 196 ? 0.69320 0.78211 0.70451 -0.02961 0.00881  0.06304  193 PHE   A CA  
1591 C C   . PHE   A 196 ? 0.76376 0.83200 0.77293 -0.01397 -0.00072 0.05711  193 PHE   A C   
1592 O O   . PHE   A 196 ? 0.71062 0.74190 0.69616 -0.01717 -0.00298 0.06043  193 PHE   A O   
1593 C CB  . PHE   A 196 ? 0.67676 0.76497 0.67938 -0.02348 0.00025  0.06757  193 PHE   A CB  
1594 C CG  . PHE   A 196 ? 0.72861 0.77080 0.69319 -0.02053 -0.01036 0.07604  193 PHE   A CG  
1595 C CD1 . PHE   A 196 ? 0.79386 0.79790 0.73046 -0.03104 -0.00763 0.08201  193 PHE   A CD1 
1596 C CD2 . PHE   A 196 ? 0.79311 0.82734 0.74709 -0.00795 -0.02398 0.07798  193 PHE   A CD2 
1597 C CE1 . PHE   A 196 ? 0.81103 0.76603 0.70624 -0.02991 -0.01753 0.09092  193 PHE   A CE1 
1598 C CE2 . PHE   A 196 ? 0.79738 0.78345 0.71001 -0.00466 -0.03533 0.08653  193 PHE   A CE2 
1599 C CZ  . PHE   A 196 ? 0.80352 0.74794 0.68486 -0.01612 -0.03170 0.09362  193 PHE   A CZ  
1600 N N   . ALA   A 197 ? 0.69950 0.79159 0.73355 0.00276  -0.00629 0.04710  194 ALA   A N   
1601 C CA  . ALA   A 197 ? 0.72350 0.80145 0.75966 0.02065  -0.01557 0.03829  194 ALA   A CA  
1602 C C   . ALA   A 197 ? 0.73273 0.80594 0.77099 0.01498  -0.00665 0.03336  194 ALA   A C   
1603 O O   . ALA   A 197 ? 0.77877 0.82118 0.80317 0.02448  -0.01402 0.02992  194 ALA   A O   
1604 C CB  . ALA   A 197 ? 0.66854 0.78322 0.73732 0.03791  -0.02078 0.02579  194 ALA   A CB  
1605 N N   . GLU   A 198 ? 0.64476 0.74500 0.69766 0.00057  0.00759  0.03246  195 GLU   A N   
1606 C CA  . GLU   A 198 ? 0.74537 0.84122 0.79862 -0.00479 0.01497  0.02721  195 GLU   A CA  
1607 C C   . GLU   A 198 ? 0.80034 0.85549 0.82447 -0.01666 0.01390  0.03482  195 GLU   A C   
1608 O O   . GLU   A 198 ? 0.81621 0.85074 0.83225 -0.01510 0.01301  0.02984  195 GLU   A O   
1609 C CB  . GLU   A 198 ? 0.66423 0.79459 0.73535 -0.01685 0.02800  0.02508  195 GLU   A CB  
1610 C CG  . GLU   A 198 ? 0.69626 0.82836 0.77065 -0.01860 0.03464  0.01681  195 GLU   A CG  
1611 C CD  . GLU   A 198 ? 0.79309 0.95461 0.87997 -0.02883 0.04522  0.01511  195 GLU   A CD  
1612 O OE1 . GLU   A 198 ? 0.72241 0.90791 0.82158 -0.03005 0.04747  0.01689  195 GLU   A OE1 
1613 O OE2 . GLU   A 198 ? 0.69109 0.84867 0.77295 -0.03556 0.05002  0.01190  195 GLU   A OE2 
1614 N N   . MET   A 199 ? 0.73469 0.77811 0.74225 -0.02991 0.01478  0.04606  196 MET   A N   
1615 C CA  . MET   A 199 ? 0.79036 0.79410 0.76850 -0.04392 0.01470  0.05334  196 MET   A CA  
1616 C C   . MET   A 199 ? 0.88104 0.83698 0.83212 -0.03134 0.00082  0.05498  196 MET   A C   
1617 O O   . MET   A 199 ? 0.89813 0.81618 0.82627 -0.03910 -0.00066 0.05669  196 MET   A O   
1618 C CB  . MET   A 199 ? 0.80168 0.80787 0.76872 -0.06150 0.02084  0.06363  196 MET   A CB  
1619 C CG  . MET   A 199 ? 0.81139 0.85502 0.79910 -0.07621 0.03347  0.06137  196 MET   A CG  
1620 S SD  . MET   A 199 ? 0.86014 0.90548 0.83409 -0.09739 0.04192  0.07037  196 MET   A SD  
1621 C CE  . MET   A 199 ? 0.62779 0.67886 0.59787 -0.08430 0.03515  0.07560  196 MET   A CE  
1622 N N   . VAL   A 200 ? 0.87221 0.82771 0.82490 -0.01158 -0.01083 0.05367  197 VAL   A N   
1623 C CA  . VAL   A 200 ? 0.96454 0.87205 0.88948 0.00418  -0.02760 0.05458  197 VAL   A CA  
1624 C C   . VAL   A 200 ? 0.96794 0.87029 0.90348 0.02168  -0.03314 0.04104  197 VAL   A C   
1625 O O   . VAL   A 200 ? 0.98692 0.84133 0.89486 0.02403  -0.04097 0.04139  197 VAL   A O   
1626 C CB  . VAL   A 200 ? 0.87487 0.78566 0.79865 0.02086  -0.04055 0.05642  197 VAL   A CB  
1627 C CG1 . VAL   A 200 ? 0.99296 0.85402 0.88887 0.04209  -0.06149 0.05524  197 VAL   A CG1 
1628 C CG2 . VAL   A 200 ? 0.82186 0.73033 0.72777 0.00333  -0.03531 0.06983  197 VAL   A CG2 
1629 N N   . THR   A 201 ? 0.90908 0.85910 0.88270 0.03332  -0.02858 0.02840  198 THR   A N   
1630 C CA  . THR   A 201 ? 0.95159 0.90404 0.93844 0.05204  -0.03250 0.01299  198 THR   A CA  
1631 C C   . THR   A 201 ? 0.88131 0.84026 0.87342 0.03958  -0.01949 0.00779  198 THR   A C   
1632 O O   . THR   A 201 ? 0.92115 0.87738 0.91926 0.05356  -0.02163 -0.00531 198 THR   A O   
1633 C CB  . THR   A 201 ? 0.92947 0.93195 0.95460 0.07026  -0.03308 0.00009  198 THR   A CB  
1634 O OG1 . THR   A 201 ? 0.86691 0.91651 0.91682 0.05456  -0.01676 0.00123  198 THR   A OG1 
1635 C CG2 . THR   A 201 ? 0.78612 0.78176 0.80726 0.08605  -0.04958 0.00245  198 THR   A CG2 
1636 N N   . ARG   A 202 ? 0.96275 0.93106 0.95288 0.01508  -0.00703 0.01626  199 ARG   A N   
1637 C CA  . ARG   A 202 ? 0.96650 0.94242 0.96101 0.00230  0.00375  0.01153  199 ARG   A CA  
1638 C C   . ARG   A 202 ? 0.92335 0.94132 0.94682 0.01163  0.01173  -0.00174 199 ARG   A C   
1639 O O   . ARG   A 202 ? 0.92363 0.94170 0.94706 0.00817  0.01741  -0.00916 199 ARG   A O   
1640 C CB  . ARG   A 202 ? 1.05824 0.98492 1.02577 0.00118  -0.00269 0.00957  199 ARG   A CB  
1641 C CG  . ARG   A 202 ? 1.15689 1.04698 1.09549 -0.02108 -0.00300 0.02284  199 ARG   A CG  
1642 C CD  . ARG   A 202 ? 1.09796 0.93763 1.00445 -0.01330 -0.01719 0.03043  199 ARG   A CD  
1643 N NE  . ARG   A 202 ? 1.13757 0.92749 1.01981 -0.00459 -0.02777 0.02474  199 ARG   A NE  
1644 C CZ  . ARG   A 202 ? 1.24175 1.01812 1.12403 0.02352  -0.04070 0.01441  199 ARG   A CZ  
1645 N NH1 . ARG   A 202 ? 1.27345 1.08505 1.18106 0.04489  -0.04440 0.00810  199 ARG   A NH1 
1646 N NH2 . ARG   A 202 ? 1.34173 1.06865 1.19892 0.03051  -0.05066 0.00897  199 ARG   A NH2 
1647 N N   . ARG   A 203 ? 0.83926 0.89233 0.88576 0.02193  0.01265  -0.00516 200 ARG   A N   
1648 C CA  . ARG   A 203 ? 0.86952 0.96455 0.94206 0.02595  0.02306  -0.01656 200 ARG   A CA  
1649 C C   . ARG   A 203 ? 0.76882 0.90071 0.86166 0.02326  0.02682  -0.01303 200 ARG   A C   
1650 O O   . ARG   A 203 ? 0.78152 0.90767 0.87164 0.02641  0.01829  -0.00584 200 ARG   A O   
1651 C CB  . ARG   A 203 ? 0.90211 0.99977 0.98456 0.04817  0.01914  -0.03313 200 ARG   A CB  
1652 C CG  . ARG   A 203 ? 0.92656 1.02834 1.01997 0.06873  0.00646  -0.03754 200 ARG   A CG  
1653 C CD  . ARG   A 203 ? 1.08207 1.19337 1.19022 0.09206  0.00331  -0.05735 200 ARG   A CD  
1654 N NE  . ARG   A 203 ? 1.08590 1.20597 1.20871 0.11409  -0.01083 -0.06422 200 ARG   A NE  
1655 C CZ  . ARG   A 203 ? 1.20681 1.28499 1.30954 0.13093  -0.03053 -0.06290 200 ARG   A CZ  
1656 N NH1 . ARG   A 203 ? 1.28030 1.30302 1.34637 0.12624  -0.03713 -0.05434 200 ARG   A NH1 
1657 N NH2 . ARG   A 203 ? 1.24476 1.33523 1.36306 0.15257  -0.04487 -0.07070 200 ARG   A NH2 
1658 N N   . ALA   A 204 ? 0.72628 0.89271 0.83598 0.01658  0.03931  -0.01805 201 ALA   A N   
1659 C CA  . ALA   A 204 ? 0.71138 0.91051 0.83845 0.01123  0.04371  -0.01504 201 ALA   A CA  
1660 C C   . ALA   A 204 ? 0.58019 0.79634 0.72644 0.02789  0.03594  -0.02226 201 ALA   A C   
1661 O O   . ALA   A 204 ? 0.56688 0.78612 0.72266 0.04442  0.03250  -0.03516 201 ALA   A O   
1662 C CB  . ALA   A 204 ? 0.65600 0.88244 0.79253 0.00123  0.05815  -0.02012 201 ALA   A CB  
1663 N N   . LEU   A 205 ? 0.54920 0.77756 0.70189 0.02452  0.03220  -0.01536 202 LEU   A N   
1664 C CA  . LEU   A 205 ? 0.52691 0.77094 0.69747 0.04027  0.02184  -0.02208 202 LEU   A CA  
1665 C C   . LEU   A 205 ? 0.54182 0.83182 0.74500 0.04273  0.03110  -0.03686 202 LEU   A C   
1666 O O   . LEU   A 205 ? 0.59115 0.89651 0.81346 0.06037  0.02587  -0.05140 202 LEU   A O   
1667 C CB  . LEU   A 205 ? 0.54780 0.78772 0.71160 0.03510  0.01425  -0.01024 202 LEU   A CB  
1668 C CG  . LEU   A 205 ? 0.59594 0.84525 0.77243 0.05173  -0.00075 -0.01539 202 LEU   A CG  
1669 C CD1 . LEU   A 205 ? 0.61283 0.83375 0.77900 0.07318  -0.01596 -0.02090 202 LEU   A CD1 
1670 C CD2 . LEU   A 205 ? 0.53493 0.77405 0.69708 0.04442  -0.00728 -0.00235 202 LEU   A CD2 
1671 N N   . PHE   A 206 ? 0.50916 0.82115 0.71844 0.02500  0.04474  -0.03422 203 PHE   A N   
1672 C CA  . PHE   A 206 ? 0.49690 0.85046 0.73284 0.02136  0.05674  -0.04695 203 PHE   A CA  
1673 C C   . PHE   A 206 ? 0.54110 0.89404 0.76499 0.00548  0.07347  -0.04588 203 PHE   A C   
1674 O O   . PHE   A 206 ? 0.51145 0.86748 0.72813 -0.01154 0.08058  -0.03771 203 PHE   A O   
1675 C CB  . PHE   A 206 ? 0.51198 0.89037 0.76402 0.01378  0.05542  -0.04480 203 PHE   A CB  
1676 C CG  . PHE   A 206 ? 0.52588 0.89825 0.78188 0.02749  0.03684  -0.04263 203 PHE   A CG  
1677 C CD1 . PHE   A 206 ? 0.51422 0.89689 0.78840 0.04907  0.02536  -0.05585 203 PHE   A CD1 
1678 C CD2 . PHE   A 206 ? 0.54273 0.89887 0.78293 0.01989  0.03009  -0.02843 203 PHE   A CD2 
1679 C CE1 . PHE   A 206 ? 0.56783 0.94087 0.84112 0.06279  0.00595  -0.05367 203 PHE   A CE1 
1680 C CE2 . PHE   A 206 ? 0.56729 0.91495 0.80604 0.03202  0.01290  -0.02614 203 PHE   A CE2 
1681 C CZ  . PHE   A 206 ? 0.60215 0.95652 0.85596 0.05343  0.00008  -0.03816 203 PHE   A CZ  
1682 N N   . PRO   A 207 ? 0.53020 0.87599 0.74864 0.01154  0.07871  -0.05436 204 PRO   A N   
1683 C CA  . PRO   A 207 ? 0.56893 0.91043 0.77115 -0.00257 0.09326  -0.05378 204 PRO   A CA  
1684 C C   . PRO   A 207 ? 0.67675 1.05380 0.89500 -0.00975 0.11010  -0.06631 204 PRO   A C   
1685 O O   . PRO   A 207 ? 0.62603 1.01307 0.84823 -0.00396 0.11907  -0.08003 204 PRO   A O   
1686 C CB  . PRO   A 207 ? 0.60319 0.91705 0.78993 0.00822  0.08907  -0.05757 204 PRO   A CB  
1687 C CG  . PRO   A 207 ? 0.59939 0.92046 0.80498 0.03006  0.07917  -0.06926 204 PRO   A CG  
1688 C CD  . PRO   A 207 ? 0.50162 0.83456 0.72211 0.03259  0.06897  -0.06376 204 PRO   A CD  
1689 N N   . GLY   A 208 ? 0.55585 0.95174 0.78201 -0.02385 0.11543  -0.06217 205 GLY   A N   
1690 C CA  . GLY   A 208 ? 0.58354 1.01177 0.82258 -0.03546 0.13287  -0.07288 205 GLY   A CA  
1691 C C   . GLY   A 208 ? 0.59702 1.00946 0.80598 -0.05362 0.14665  -0.06739 205 GLY   A C   
1692 O O   . GLY   A 208 ? 0.60278 0.98324 0.78441 -0.05924 0.14088  -0.05370 205 GLY   A O   
1693 N N   . ASP   A 209 ? 0.61905 1.05496 0.83262 -0.06270 0.16502  -0.07940 206 ASP   A N   
1694 C CA  . ASP   A 209 ? 0.72661 1.14611 0.90714 -0.08071 0.17907  -0.07521 206 ASP   A CA  
1695 C C   . ASP   A 209 ? 0.64929 1.08231 0.82745 -0.10368 0.19167  -0.07277 206 ASP   A C   
1696 O O   . ASP   A 209 ? 0.72557 1.14152 0.87161 -0.12036 0.20348  -0.06871 206 ASP   A O   
1697 C CB  . ASP   A 209 ? 0.69322 1.11961 0.86861 -0.07585 0.19246  -0.09007 206 ASP   A CB  
1698 C CG  . ASP   A 209 ? 0.69434 1.16889 0.90748 -0.07080 0.20448  -0.11078 206 ASP   A CG  
1699 O OD1 . ASP   A 209 ? 0.78521 1.28880 1.02872 -0.07296 0.20254  -0.11354 206 ASP   A OD1 
1700 O OD2 . ASP   A 209 ? 0.94492 1.42997 1.15846 -0.06403 0.21546  -0.12582 206 ASP   A OD2 
1701 N N   . SER   A 210 ? 0.66737 1.12745 0.87574 -0.10553 0.18863  -0.07519 207 SER   A N   
1702 C CA  . SER   A 210 ? 0.65589 1.12518 0.86171 -0.12884 0.19849  -0.07210 207 SER   A CA  
1703 C C   . SER   A 210 ? 0.60465 1.08630 0.83613 -0.12495 0.18387  -0.06839 207 SER   A C   
1704 O O   . SER   A 210 ? 0.66400 1.14967 0.91493 -0.10442 0.16809  -0.06948 207 SER   A O   
1705 C CB  . SER   A 210 ? 0.62051 1.12768 0.84193 -0.14249 0.22198  -0.08912 207 SER   A CB  
1706 O OG  . SER   A 210 ? 0.62627 1.18080 0.89727 -0.12895 0.22068  -0.10668 207 SER   A OG  
1707 N N   . GLU   A 211 ? 0.59441 1.07820 0.82191 -0.14551 0.18869  -0.06377 208 GLU   A N   
1708 C CA  . GLU   A 211 ? 0.56872 1.06293 0.81787 -0.14339 0.17482  -0.06081 208 GLU   A CA  
1709 C C   . GLU   A 211 ? 0.53947 1.08294 0.83792 -0.13235 0.17352  -0.07866 208 GLU   A C   
1710 O O   . GLU   A 211 ? 0.56696 1.11556 0.88447 -0.11573 0.15542  -0.07812 208 GLU   A O   
1711 C CB  . GLU   A 211 ? 0.61108 1.09431 0.84325 -0.16891 0.18036  -0.05335 208 GLU   A CB  
1712 C CG  . GLU   A 211 ? 0.64056 1.07228 0.82526 -0.17523 0.17472  -0.03548 208 GLU   A CG  
1713 C CD  . GLU   A 211 ? 0.97549 1.39138 1.14330 -0.19663 0.17519  -0.02808 208 GLU   A CD  
1714 O OE1 . GLU   A 211 ? 0.91993 1.34073 1.10323 -0.19331 0.16225  -0.02579 208 GLU   A OE1 
1715 O OE2 . GLU   A 211 ? 1.11192 1.50721 1.24771 -0.21695 0.18800  -0.02462 208 GLU   A OE2 
1716 N N   . ILE   A 212 ? 0.53108 1.11166 0.85003 -0.14094 0.19220  -0.09558 209 ILE   A N   
1717 C CA  . ILE   A 212 ? 0.55484 1.18787 0.92515 -0.12910 0.19025  -0.11580 209 ILE   A CA  
1718 C C   . ILE   A 212 ? 0.57160 1.20697 0.95500 -0.09768 0.17876  -0.12358 209 ILE   A C   
1719 O O   . ILE   A 212 ? 0.50096 1.16075 0.91833 -0.07800 0.16384  -0.13372 209 ILE   A O   
1720 C CB  . ILE   A 212 ? 0.48012 1.15762 0.87148 -0.15030 0.21568  -0.13371 209 ILE   A CB  
1721 C CG1 . ILE   A 212 ? 0.58877 1.32525 1.03843 -0.13921 0.21118  -0.15604 209 ILE   A CG1 
1722 C CG2 . ILE   A 212 ? 0.55261 1.22723 0.92623 -0.15096 0.23452  -0.14033 209 ILE   A CG2 
1723 C CD1 . ILE   A 212 ? 0.56852 1.31248 1.03668 -0.14147 0.19392  -0.15200 209 ILE   A CD1 
1724 N N   . ASP   A 213 ? 0.51866 1.12542 0.87309 -0.09198 0.18361  -0.11911 210 ASP   A N   
1725 C CA  . ASP   A 213 ? 0.47219 1.07318 0.83350 -0.06328 0.17179  -0.12550 210 ASP   A CA  
1726 C C   . ASP   A 213 ? 0.49120 1.05671 0.83995 -0.04772 0.14707  -0.10991 210 ASP   A C   
1727 O O   . ASP   A 213 ? 0.48371 1.05186 0.84884 -0.02365 0.13132  -0.11623 210 ASP   A O   
1728 C CB  . ASP   A 213 ? 0.47558 1.05490 0.80780 -0.06383 0.18425  -0.12588 210 ASP   A CB  
1729 C CG  . ASP   A 213 ? 0.60917 1.17738 0.94486 -0.03553 0.17201  -0.13272 210 ASP   A CG  
1730 O OD1 . ASP   A 213 ? 0.56613 1.16995 0.93573 -0.01913 0.17245  -0.15334 210 ASP   A OD1 
1731 O OD2 . ASP   A 213 ? 0.58329 1.10702 0.88799 -0.02975 0.16147  -0.11846 210 ASP   A OD2 
1732 N N   . GLN   A 214 ? 0.46912 0.99976 0.78678 -0.06097 0.14339  -0.09008 211 GLN   A N   
1733 C CA  . GLN   A 214 ? 0.41242 0.91368 0.71879 -0.04969 0.12266  -0.07600 211 GLN   A CA  
1734 C C   . GLN   A 214 ? 0.48291 1.00813 0.81912 -0.04114 0.10904  -0.08120 211 GLN   A C   
1735 O O   . GLN   A 214 ? 0.44134 0.95404 0.77950 -0.02183 0.09101  -0.07900 211 GLN   A O   
1736 C CB  . GLN   A 214 ? 0.45995 0.92752 0.73232 -0.06618 0.12290  -0.05727 211 GLN   A CB  
1737 C CG  . GLN   A 214 ? 0.48520 0.92492 0.74478 -0.05723 0.10466  -0.04350 211 GLN   A CG  
1738 C CD  . GLN   A 214 ? 0.58020 0.99126 0.82226 -0.04395 0.09800  -0.03899 211 GLN   A CD  
1739 O OE1 . GLN   A 214 ? 0.54922 0.95336 0.78076 -0.04431 0.10686  -0.04286 211 GLN   A OE1 
1740 N NE2 . GLN   A 214 ? 0.49130 0.88384 0.72779 -0.03356 0.08266  -0.03096 211 GLN   A NE2 
1741 N N   . LEU   A 215 ? 0.49650 1.05425 0.85388 -0.05625 0.11695  -0.08832 212 LEU   A N   
1742 C CA  . LEU   A 215 ? 0.49950 1.08320 0.88705 -0.04925 0.10329  -0.09511 212 LEU   A CA  
1743 C C   . LEU   A 215 ? 0.50184 1.11667 0.92425 -0.02499 0.09516  -0.11448 212 LEU   A C   
1744 O O   . LEU   A 215 ? 0.51135 1.12732 0.94608 -0.00684 0.07453  -0.11627 212 LEU   A O   
1745 C CB  . LEU   A 215 ? 0.44873 1.06092 0.85148 -0.07396 0.11509  -0.09995 212 LEU   A CB  
1746 C CG  . LEU   A 215 ? 0.52349 1.15740 0.95164 -0.07292 0.10063  -0.10421 212 LEU   A CG  
1747 C CD1 . LEU   A 215 ? 0.41164 1.00452 0.81019 -0.07136 0.08461  -0.08478 212 LEU   A CD1 
1748 C CD2 . LEU   A 215 ? 0.54868 1.21747 0.99729 -0.09930 0.11598  -0.11395 212 LEU   A CD2 
1749 N N   . PHE   A 216 ? 0.42586 1.06456 0.86241 -0.02309 0.11024  -0.12989 213 PHE   A N   
1750 C CA  . PHE   A 216 ? 0.40550 1.07562 0.87689 0.00248  0.10211  -0.15116 213 PHE   A CA  
1751 C C   . PHE   A 216 ? 0.49898 1.12853 0.94953 0.02922  0.08360  -0.14494 213 PHE   A C   
1752 O O   . PHE   A 216 ? 0.48851 1.12804 0.95959 0.05489  0.06536  -0.15646 213 PHE   A O   
1753 C CB  . PHE   A 216 ? 0.45679 1.16632 0.94925 -0.00352 0.12543  -0.17136 213 PHE   A CB  
1754 C CG  . PHE   A 216 ? 0.40338 1.16588 0.92944 -0.02568 0.14158  -0.18511 213 PHE   A CG  
1755 C CD1 . PHE   A 216 ? 0.45292 1.22122 0.98618 -0.03964 0.13420  -0.17804 213 PHE   A CD1 
1756 C CD2 . PHE   A 216 ? 0.38962 1.19642 0.93961 -0.03365 0.16480  -0.20616 213 PHE   A CD2 
1757 C CE1 . PHE   A 216 ? 0.56769 1.38312 1.13131 -0.06263 0.14907  -0.19103 213 PHE   A CE1 
1758 C CE2 . PHE   A 216 ? 0.43567 1.27913 1.00776 -0.05662 0.17883  -0.21591 213 PHE   A CE2 
1759 C CZ  . PHE   A 216 ? 0.54269 1.38586 1.11914 -0.07119 0.16996  -0.20722 213 PHE   A CZ  
1760 N N   . ARG   A 217 ? 0.41211 0.99468 0.82124 0.02353  0.08704  -0.12757 214 ARG   A N   
1761 C CA  . ARG   A 217 ? 0.45562 0.99492 0.84113 0.04425  0.06981  -0.11965 214 ARG   A CA  
1762 C C   . ARG   A 217 ? 0.49350 1.01088 0.87039 0.05207  0.04769  -0.10738 214 ARG   A C   
1763 O O   . ARG   A 217 ? 0.54836 1.04352 0.91888 0.07454  0.02875  -0.10790 214 ARG   A O   
1764 C CB  . ARG   A 217 ? 0.45000 0.94822 0.79584 0.03302  0.07912  -0.10488 214 ARG   A CB  
1765 C CG  . ARG   A 217 ? 0.47710 0.98676 0.82358 0.03098  0.09717  -0.11731 214 ARG   A CG  
1766 C CD  . ARG   A 217 ? 0.63028 1.09646 0.93657 0.02247  0.10195  -0.10326 214 ARG   A CD  
1767 N NE  . ARG   A 217 ? 0.68066 1.15528 0.98333 0.02017  0.11886  -0.11514 214 ARG   A NE  
1768 C CZ  . ARG   A 217 ? 0.73590 1.20329 1.03883 0.03903  0.11583  -0.12721 214 ARG   A CZ  
1769 N NH1 . ARG   A 217 ? 0.81061 1.25896 1.11566 0.06175  0.09577  -0.12851 214 ARG   A NH1 
1770 N NH2 . ARG   A 217 ? 0.73331 1.20941 1.03075 0.03508  0.13288  -0.13835 214 ARG   A NH2 
1771 N N   . ILE   A 218 ? 0.45768 0.97750 0.83055 0.03375  0.04948  -0.09632 215 ILE   A N   
1772 C CA  . ILE   A 218 ? 0.49206 0.99594 0.85786 0.04030  0.02971  -0.08675 215 ILE   A CA  
1773 C C   . ILE   A 218 ? 0.43553 0.97405 0.83753 0.05863  0.01474  -0.10425 215 ILE   A C   
1774 O O   . ILE   A 218 ? 0.53106 1.04945 0.92522 0.07796  -0.00734 -0.10187 215 ILE   A O   
1775 C CB  . ILE   A 218 ? 0.44615 0.94557 0.79939 0.01677  0.03582  -0.07297 215 ILE   A CB  
1776 C CG1 . ILE   A 218 ? 0.48427 0.94795 0.80159 0.00276  0.04654  -0.05673 215 ILE   A CG1 
1777 C CG2 . ILE   A 218 ? 0.50507 0.99213 0.85215 0.02352  0.01623  -0.06546 215 ILE   A CG2 
1778 C CD1 . ILE   A 218 ? 0.36091 0.82021 0.66575 -0.01885 0.05320  -0.04559 215 ILE   A CD1 
1779 N N   . PHE   A 219 ? 0.47012 1.06111 0.91137 0.05249  0.02618  -0.12280 216 PHE   A N   
1780 C CA  . PHE   A 219 ? 0.42775 1.06010 0.91033 0.07001  0.01189  -0.14306 216 PHE   A CA  
1781 C C   . PHE   A 219 ? 0.55075 1.17643 1.03940 0.10243  -0.00322 -0.15556 216 PHE   A C   
1782 O O   . PHE   A 219 ? 0.52633 1.15494 1.02715 0.12562  -0.02742 -0.16332 216 PHE   A O   
1783 C CB  . PHE   A 219 ? 0.43175 1.12568 0.95716 0.05351  0.03094  -0.16227 216 PHE   A CB  
1784 C CG  . PHE   A 219 ? 0.36751 1.06975 0.89097 0.02375  0.04068  -0.15317 216 PHE   A CG  
1785 C CD1 . PHE   A 219 ? 0.36117 1.02064 0.84890 0.01590  0.03179  -0.13074 216 PHE   A CD1 
1786 C CD2 . PHE   A 219 ? 0.35725 1.10988 0.91407 0.00308  0.05910  -0.16823 216 PHE   A CD2 
1787 C CE1 . PHE   A 219 ? 0.37041 1.03448 0.85482 -0.00965 0.03936  -0.12363 216 PHE   A CE1 
1788 C CE2 . PHE   A 219 ? 0.38104 1.13584 0.93265 -0.02499 0.06707  -0.15993 216 PHE   A CE2 
1789 C CZ  . PHE   A 219 ? 0.38747 1.09672 0.90256 -0.03009 0.05615  -0.13772 216 PHE   A CZ  
1790 N N   . ARG   A 220 ? 0.50522 1.11907 0.98315 0.10547  0.00921  -0.15822 217 ARG   A N   
1791 C CA  . ARG   A 220 ? 0.54845 1.15366 1.03085 0.13665  -0.00457 -0.17175 217 ARG   A CA  
1792 C C   . ARG   A 220 ? 0.54464 1.08902 0.98824 0.15499  -0.03021 -0.15606 217 ARG   A C   
1793 O O   . ARG   A 220 ? 0.61160 1.14693 1.05985 0.18479  -0.05053 -0.16767 217 ARG   A O   
1794 C CB  . ARG   A 220 ? 0.54258 1.14392 1.01685 0.13333  0.01542  -0.17700 217 ARG   A CB  
1795 C CG  . ARG   A 220 ? 0.69369 1.35907 1.21116 0.12691  0.03680  -0.20156 217 ARG   A CG  
1796 C CD  . ARG   A 220 ? 0.73457 1.39092 1.23720 0.12355  0.05645  -0.20584 217 ARG   A CD  
1797 N NE  . ARG   A 220 ? 0.82834 1.43085 1.29871 0.14517  0.04111  -0.19963 217 ARG   A NE  
1798 C CZ  . ARG   A 220 ? 0.86858 1.46881 1.35103 0.17816  0.02244  -0.21592 217 ARG   A CZ  
1799 N NH1 . ARG   A 220 ? 0.77235 1.42472 1.30198 0.19650  0.01483  -0.24075 217 ARG   A NH1 
1800 N NH2 . ARG   A 220 ? 0.95071 1.49415 1.39691 0.19330  0.01000  -0.20791 217 ARG   A NH2 
1801 N N   . THR   A 221 ? 0.46795 0.96984 0.87229 0.13795  -0.02982 -0.13080 218 THR   A N   
1802 C CA  . THR   A 221 ? 0.65301 1.09527 1.01575 0.14990  -0.05037 -0.11436 218 THR   A CA  
1803 C C   . THR   A 221 ? 0.58311 1.02181 0.94310 0.15413  -0.06992 -0.10834 218 THR   A C   
1804 O O   . THR   A 221 ? 0.69448 1.10385 1.03888 0.17703  -0.09450 -0.10820 218 THR   A O   
1805 C CB  . THR   A 221 ? 0.62332 1.02147 0.94384 0.12889  -0.03747 -0.09189 218 THR   A CB  
1806 O OG1 . THR   A 221 ? 0.62586 1.02651 0.94731 0.12509  -0.02057 -0.09812 218 THR   A OG1 
1807 C CG2 . THR   A 221 ? 0.73521 1.07163 1.01161 0.13848  -0.05576 -0.07604 218 THR   A CG2 
1808 N N   . LEU   A 222 ? 0.57952 1.04398 0.95096 0.13275  -0.06047 -0.10350 219 LEU   A N   
1809 C CA  . LEU   A 222 ? 0.59306 1.05299 0.95881 0.13395  -0.07752 -0.09716 219 LEU   A CA  
1810 C C   . LEU   A 222 ? 0.58326 1.09955 0.99756 0.14227  -0.08629 -0.11845 219 LEU   A C   
1811 O O   . LEU   A 222 ? 0.62188 1.13898 1.03504 0.14390  -0.10185 -0.11588 219 LEU   A O   
1812 C CB  . LEU   A 222 ? 0.53773 0.98444 0.88095 0.10576  -0.06409 -0.07792 219 LEU   A CB  
1813 C CG  . LEU   A 222 ? 0.60845 1.00436 0.90641 0.09524  -0.05580 -0.05740 219 LEU   A CG  
1814 C CD1 . LEU   A 222 ? 0.56078 0.95575 0.84651 0.06888  -0.04114 -0.04376 219 LEU   A CD1 
1815 C CD2 . LEU   A 222 ? 0.73327 1.07796 0.99304 0.11079  -0.07639 -0.04654 219 LEU   A CD2 
1816 N N   . GLY   A 223 ? 0.54221 1.10688 0.99920 0.14692  -0.07652 -0.14041 220 GLY   A N   
1817 C CA  . GLY   A 223 ? 0.48071 1.10602 0.98930 0.15246  -0.08309 -0.16315 220 GLY   A CA  
1818 C C   . GLY   A 223 ? 0.42004 1.08313 0.94914 0.12001  -0.06200 -0.16302 220 GLY   A C   
1819 O O   . GLY   A 223 ? 0.50020 1.13562 0.99874 0.09775  -0.05298 -0.14267 220 GLY   A O   
1820 N N   . THR   A 224 ? 0.40920 1.13646 0.99075 0.11707  -0.05394 -0.18724 221 THR   A N   
1821 C CA  . THR   A 224 ? 0.45469 1.21927 1.05747 0.08491  -0.03443 -0.18960 221 THR   A CA  
1822 C C   . THR   A 224 ? 0.38570 1.14525 0.98458 0.08010  -0.05230 -0.18279 221 THR   A C   
1823 O O   . THR   A 224 ? 0.39617 1.18110 1.02298 0.09963  -0.07532 -0.19833 221 THR   A O   
1824 C CB  . THR   A 224 ? 0.37973 1.21740 1.04171 0.08244  -0.02165 -0.21952 221 THR   A CB  
1825 O OG1 . THR   A 224 ? 0.45235 1.29315 1.11500 0.08824  -0.00482 -0.22673 221 THR   A OG1 
1826 C CG2 . THR   A 224 ? 0.36228 1.23286 1.04078 0.04492  0.00047  -0.22071 221 THR   A CG2 
1827 N N   . PRO   A 225 ? 0.37723 1.10513 0.94246 0.05639  -0.04410 -0.16156 222 PRO   A N   
1828 C CA  . PRO   A 225 ? 0.49982 1.21668 1.05547 0.05403  -0.06236 -0.15461 222 PRO   A CA  
1829 C C   . PRO   A 225 ? 0.43172 1.20658 1.03519 0.04103  -0.06234 -0.17426 222 PRO   A C   
1830 O O   . PRO   A 225 ? 0.39592 1.21338 1.03115 0.02180  -0.04046 -0.18723 222 PRO   A O   
1831 C CB  . PRO   A 225 ? 0.48165 1.15277 0.99093 0.03124  -0.04912 -0.12920 222 PRO   A CB  
1832 C CG  . PRO   A 225 ? 0.48785 1.16827 0.99955 0.01210  -0.02031 -0.12904 222 PRO   A CG  
1833 C CD  . PRO   A 225 ? 0.41917 1.11854 0.95213 0.03254  -0.01931 -0.14394 222 PRO   A CD  
1834 N N   . ASP   A 226 ? 0.44774 1.22310 1.05442 0.05054  -0.08715 -0.17675 223 ASP   A N   
1835 C CA  . ASP   A 226 ? 0.41867 1.24576 1.06877 0.03782  -0.09114 -0.19502 223 ASP   A CA  
1836 C C   . ASP   A 226 ? 0.47819 1.27325 1.09788 0.02860  -0.10460 -0.18041 223 ASP   A C   
1837 O O   . ASP   A 226 ? 0.42029 1.15820 0.98804 0.02949  -0.10622 -0.15703 223 ASP   A O   
1838 C CB  . ASP   A 226 ? 0.38664 1.26324 1.08674 0.06535  -0.11247 -0.22288 223 ASP   A CB  
1839 C CG  . ASP   A 226 ? 0.42533 1.26260 1.09847 0.10186  -0.14574 -0.21747 223 ASP   A CG  
1840 O OD1 . ASP   A 226 ? 0.65080 1.42426 1.26695 0.10354  -0.14988 -0.19205 223 ASP   A OD1 
1841 O OD2 . ASP   A 226 ? 0.54263 1.41257 1.25082 0.12888  -0.16804 -0.23943 223 ASP   A OD2 
1842 N N   . GLU   A 227 ? 0.38785 1.22194 1.04129 0.01947  -0.11422 -0.19584 224 GLU   A N   
1843 C CA  . GLU   A 227 ? 0.47801 1.28492 1.10459 0.00784  -0.12527 -0.18435 224 GLU   A CA  
1844 C C   . GLU   A 227 ? 0.51611 1.27841 1.10477 0.03590  -0.15448 -0.17345 224 GLU   A C   
1845 O O   . GLU   A 227 ? 0.51300 1.23372 1.06025 0.02875  -0.15919 -0.15655 224 GLU   A O   
1846 C CB  . GLU   A 227 ? 0.38691 1.24751 1.06060 -0.00833 -0.13040 -0.20570 224 GLU   A CB  
1847 C CG  . GLU   A 227 ? 0.40811 1.29546 1.10109 -0.04662 -0.09952 -0.20962 224 GLU   A CG  
1848 C CD  . GLU   A 227 ? 0.56498 1.39880 1.20661 -0.07056 -0.08571 -0.18503 224 GLU   A CD  
1849 O OE1 . GLU   A 227 ? 0.53035 1.32050 1.13329 -0.06178 -0.10253 -0.17058 224 GLU   A OE1 
1850 O OE2 . GLU   A 227 ? 0.55247 1.38706 1.19084 -0.09747 -0.05846 -0.18085 224 GLU   A OE2 
1851 N N   . VAL   A 228 ? 0.49299 1.26073 1.09209 0.06795  -0.17429 -0.18315 225 VAL   A N   
1852 C CA  . VAL   A 228 ? 0.54303 1.26399 1.10103 0.09421  -0.20308 -0.17275 225 VAL   A CA  
1853 C C   . VAL   A 228 ? 0.58903 1.24415 1.08578 0.09377  -0.19249 -0.14496 225 VAL   A C   
1854 O O   . VAL   A 228 ? 0.63171 1.24187 1.08222 0.09249  -0.20061 -0.12804 225 VAL   A O   
1855 C CB  . VAL   A 228 ? 0.60531 1.34649 1.18911 0.12976  -0.22923 -0.19167 225 VAL   A CB  
1856 C CG1 . VAL   A 228 ? 0.66068 1.33973 1.18920 0.15623  -0.25614 -0.17675 225 VAL   A CG1 
1857 C CG2 . VAL   A 228 ? 0.47464 1.28052 1.11738 0.13198  -0.24550 -0.22006 225 VAL   A CG2 
1858 N N   . VAL   A 229 ? 0.61726 1.26754 1.11346 0.09435  -0.17390 -0.14118 226 VAL   A N   
1859 C CA  . VAL   A 229 ? 0.60008 1.19206 1.04261 0.09321  -0.16377 -0.11692 226 VAL   A CA  
1860 C C   . VAL   A 229 ? 0.60222 1.17982 1.02463 0.06274  -0.13910 -0.10145 226 VAL   A C   
1861 O O   . VAL   A 229 ? 0.62737 1.15761 1.00386 0.05975  -0.13350 -0.08145 226 VAL   A O   
1862 C CB  . VAL   A 229 ? 0.61546 1.20430 1.06261 0.10610  -0.15516 -0.11924 226 VAL   A CB  
1863 C CG1 . VAL   A 229 ? 0.64501 1.25827 1.12258 0.13695  -0.17886 -0.14007 226 VAL   A CG1 
1864 C CG2 . VAL   A 229 ? 0.64784 1.26801 1.12123 0.08350  -0.12419 -0.12362 226 VAL   A CG2 
1865 N N   . TRP   A 230 ? 0.56682 1.18305 1.02141 0.03996  -0.12479 -0.11084 227 TRP   A N   
1866 C CA  . TRP   A 230 ? 0.47727 1.07878 0.91305 0.01200  -0.10299 -0.09793 227 TRP   A CA  
1867 C C   . TRP   A 230 ? 0.52685 1.16291 0.99128 -0.00891 -0.10105 -0.10953 227 TRP   A C   
1868 O O   . TRP   A 230 ? 0.44568 1.12107 0.94576 -0.02454 -0.08517 -0.12205 227 TRP   A O   
1869 C CB  . TRP   A 230 ? 0.51558 1.11784 0.95274 0.00240  -0.07766 -0.09421 227 TRP   A CB  
1870 C CG  . TRP   A 230 ? 0.55582 1.13543 0.96738 -0.02238 -0.05751 -0.07980 227 TRP   A CG  
1871 C CD1 . TRP   A 230 ? 0.54403 1.10425 0.93394 -0.03620 -0.05919 -0.07107 227 TRP   A CD1 
1872 C CD2 . TRP   A 230 ? 0.53231 1.10444 0.93562 -0.03431 -0.03455 -0.07357 227 TRP   A CD2 
1873 N NE1 . TRP   A 230 ? 0.54064 1.08157 0.91011 -0.05478 -0.03965 -0.06011 227 TRP   A NE1 
1874 C CE2 . TRP   A 230 ? 0.48603 1.03353 0.86255 -0.05428 -0.02463 -0.06105 227 TRP   A CE2 
1875 C CE3 . TRP   A 230 ? 0.56329 1.14574 0.97769 -0.02891 -0.02263 -0.07820 227 TRP   A CE3 
1876 C CZ2 . TRP   A 230 ? 0.50421 1.03663 0.86426 -0.06839 -0.00472 -0.05274 227 TRP   A CZ2 
1877 C CZ3 . TRP   A 230 ? 0.48531 1.05322 0.88271 -0.04441 -0.00155 -0.06966 227 TRP   A CZ3 
1878 C CH2 . TRP   A 230 ? 0.54541 1.08828 0.91565 -0.06370 0.00653  -0.05687 227 TRP   A CH2 
1879 N N   . PRO   A 231 ? 0.57942 1.20175 1.02845 -0.01081 -0.11644 -0.10664 228 PRO   A N   
1880 C CA  . PRO   A 231 ? 0.52750 1.18127 1.00397 -0.03134 -0.11653 -0.11896 228 PRO   A CA  
1881 C C   . PRO   A 231 ? 0.44509 1.09554 0.91670 -0.06219 -0.09003 -0.11284 228 PRO   A C   
1882 O O   . PRO   A 231 ? 0.51259 1.12090 0.94352 -0.06890 -0.08029 -0.09481 228 PRO   A O   
1883 C CB  . PRO   A 231 ? 0.53014 1.15526 0.97694 -0.02528 -0.13789 -0.11281 228 PRO   A CB  
1884 C CG  . PRO   A 231 ? 0.56881 1.16300 0.98658 0.00328  -0.15417 -0.10425 228 PRO   A CG  
1885 C CD  . PRO   A 231 ? 0.61117 1.18965 1.01706 0.00579  -0.13536 -0.09375 228 PRO   A CD  
1886 N N   . GLY   A 232 ? 0.51530 1.21059 1.02815 -0.08124 -0.07890 -0.12894 229 GLY   A N   
1887 C CA  . GLY   A 232 ? 0.50633 1.19801 1.01358 -0.11250 -0.05445 -0.12465 229 GLY   A CA  
1888 C C   . GLY   A 232 ? 0.49736 1.19486 1.00761 -0.11776 -0.03049 -0.12255 229 GLY   A C   
1889 O O   . GLY   A 232 ? 0.65746 1.34411 1.15462 -0.14313 -0.01008 -0.11678 229 GLY   A O   
1890 N N   . VAL   A 233 ? 0.46798 1.17905 0.99197 -0.09433 -0.03324 -0.12735 230 VAL   A N   
1891 C CA  . VAL   A 233 ? 0.56352 1.27647 1.08642 -0.09756 -0.01124 -0.12534 230 VAL   A CA  
1892 C C   . VAL   A 233 ? 0.54105 1.30497 1.10491 -0.11953 0.00810  -0.14373 230 VAL   A C   
1893 O O   . VAL   A 233 ? 0.43147 1.18998 0.98436 -0.13695 0.03193  -0.13948 230 VAL   A O   
1894 C CB  . VAL   A 233 ? 0.46631 1.17512 0.98962 -0.06564 -0.02103 -0.12590 230 VAL   A CB  
1895 C CG1 . VAL   A 233 ? 0.46251 1.21995 1.03350 -0.04659 -0.03751 -0.14889 230 VAL   A CG1 
1896 C CG2 . VAL   A 233 ? 0.45961 1.16258 0.97468 -0.06863 0.00085  -0.12213 230 VAL   A CG2 
1897 N N   . THR   A 234 ? 0.44478 1.25924 1.05534 -0.12023 -0.00135 -0.16502 231 THR   A N   
1898 C CA  . THR   A 234 ? 0.41819 1.27909 1.06595 -0.14160 0.01821  -0.18294 231 THR   A CA  
1899 C C   . THR   A 234 ? 0.47493 1.31731 1.10222 -0.17998 0.03588  -0.17531 231 THR   A C   
1900 O O   . THR   A 234 ? 0.58899 1.44362 1.22399 -0.19946 0.05647  -0.18211 231 THR   A O   
1901 C CB  . THR   A 234 ? 0.56194 1.46269 1.25222 -0.12742 0.00114  -0.20396 231 THR   A CB  
1902 O OG1 . THR   A 234 ? 0.50543 1.40219 1.19576 -0.13247 -0.01888 -0.20381 231 THR   A OG1 
1903 C CG2 . THR   A 234 ? 0.50994 1.42374 1.21668 -0.08785 -0.01760 -0.21220 231 THR   A CG2 
1904 N N   . SER   A 235 ? 0.57584 1.38239 1.17146 -0.18983 0.02764  -0.16065 232 SER   A N   
1905 C CA  . SER   A 235 ? 0.61852 1.40281 1.19140 -0.22560 0.04123  -0.15346 232 SER   A CA  
1906 C C   . SER   A 235 ? 0.67923 1.40680 1.19761 -0.23378 0.05646  -0.13111 232 SER   A C   
1907 O O   . SER   A 235 ? 0.77885 1.47708 1.26927 -0.26117 0.06613  -0.12283 232 SER   A O   
1908 C CB  . SER   A 235 ? 0.60565 1.37157 1.16877 -0.22814 0.01963  -0.15092 232 SER   A CB  
1909 O OG  . SER   A 235 ? 0.64462 1.46077 1.25631 -0.22127 0.00374  -0.17212 232 SER   A OG  
1910 N N   . MET   A 236 ? 0.56858 1.27840 1.07032 -0.21066 0.05743  -0.12184 233 MET   A N   
1911 C CA  . MET   A 236 ? 0.58163 1.23953 1.03359 -0.21572 0.06891  -0.10197 233 MET   A CA  
1912 C C   . MET   A 236 ? 0.61474 1.28132 1.06417 -0.24234 0.09670  -0.10513 233 MET   A C   
1913 O O   . MET   A 236 ? 0.65647 1.37363 1.14552 -0.24814 0.10889  -0.12295 233 MET   A O   
1914 C CB  . MET   A 236 ? 0.57929 1.21796 1.01643 -0.18463 0.06120  -0.09266 233 MET   A CB  
1915 C CG  . MET   A 236 ? 0.62917 1.25510 1.06245 -0.15984 0.03542  -0.08849 233 MET   A CG  
1916 S SD  . MET   A 236 ? 0.64882 1.23821 1.05160 -0.13066 0.02844  -0.07330 233 MET   A SD  
1917 C CE  . MET   A 236 ? 0.64393 1.18037 0.99558 -0.14643 0.03996  -0.05360 233 MET   A CE  
1918 N N   . PRO   A 237 ? 0.61622 1.23360 1.01789 -0.25848 0.10683  -0.08887 234 PRO   A N   
1919 C CA  . PRO   A 237 ? 0.69765 1.31618 1.08869 -0.28877 0.13284  -0.09089 234 PRO   A CA  
1920 C C   . PRO   A 237 ? 0.59931 1.24666 1.00689 -0.28143 0.14964  -0.09943 234 PRO   A C   
1921 O O   . PRO   A 237 ? 0.67751 1.33859 1.09240 -0.29520 0.16556  -0.10883 234 PRO   A O   
1922 C CB  . PRO   A 237 ? 0.70137 1.25145 1.03087 -0.29709 0.13326  -0.06960 234 PRO   A CB  
1923 C CG  . PRO   A 237 ? 0.69227 1.21604 1.01018 -0.28164 0.10890  -0.06143 234 PRO   A CG  
1924 C CD  . PRO   A 237 ? 0.66555 1.22438 1.02029 -0.25143 0.09421  -0.06951 234 PRO   A CD  
1925 N N   . ASP   A 238 ? 0.62054 1.25865 1.02222 -0.25285 0.14266  -0.09386 235 ASP   A N   
1926 C CA  . ASP   A 238 ? 0.67686 1.33815 1.09072 -0.24479 0.15772  -0.10210 235 ASP   A CA  
1927 C C   . ASP   A 238 ? 0.61319 1.32604 1.07882 -0.22083 0.14938  -0.12125 235 ASP   A C   
1928 O O   . ASP   A 238 ? 0.62426 1.35180 1.09922 -0.20764 0.15787  -0.12892 235 ASP   A O   
1929 C CB  . ASP   A 238 ? 0.63059 1.24571 1.00406 -0.22704 0.15452  -0.08549 235 ASP   A CB  
1930 C CG  . ASP   A 238 ? 0.77333 1.33643 1.09337 -0.24764 0.16389  -0.06891 235 ASP   A CG  
1931 O OD1 . ASP   A 238 ? 0.86847 1.43438 1.17989 -0.27705 0.18231  -0.07226 235 ASP   A OD1 
1932 O OD2 . ASP   A 238 ? 0.83788 1.35683 1.12367 -0.23462 0.15250  -0.05318 235 ASP   A OD2 
1933 N N   . TYR   A 239 ? 0.61175 1.34892 1.10837 -0.21333 0.13131  -0.12954 236 TYR   A N   
1934 C CA  . TYR   A 239 ? 0.63079 1.41279 1.17372 -0.18905 0.12052  -0.14848 236 TYR   A CA  
1935 C C   . TYR   A 239 ? 0.51678 1.32927 1.08242 -0.20146 0.13651  -0.16510 236 TYR   A C   
1936 O O   . TYR   A 239 ? 0.53090 1.33849 1.08830 -0.22965 0.14748  -0.16475 236 TYR   A O   
1937 C CB  . TYR   A 239 ? 0.57466 1.37143 1.14069 -0.17707 0.09447  -0.15280 236 TYR   A CB  
1938 C CG  . TYR   A 239 ? 0.50911 1.34798 1.11985 -0.14949 0.07935  -0.17247 236 TYR   A CG  
1939 C CD1 . TYR   A 239 ? 0.51363 1.35476 1.13092 -0.11677 0.06385  -0.17359 236 TYR   A CD1 
1940 C CD2 . TYR   A 239 ? 0.45192 1.32636 1.09647 -0.15578 0.07966  -0.19028 236 TYR   A CD2 
1941 C CE1 . TYR   A 239 ? 0.38251 1.25691 1.03681 -0.08952 0.04749  -0.19181 236 TYR   A CE1 
1942 C CE2 . TYR   A 239 ? 0.50750 1.41922 1.19161 -0.12900 0.06414  -0.20912 236 TYR   A CE2 
1943 C CZ  . TYR   A 239 ? 0.45812 1.36756 1.14556 -0.09511 0.04732  -0.20963 236 TYR   A CZ  
1944 O OH  . TYR   A 239 ? 0.39955 1.34040 1.12211 -0.06656 0.02948  -0.22843 236 TYR   A OH  
1945 N N   . LYS   A 240 ? 0.49256 1.33663 1.08623 -0.18031 0.13760  -0.18049 237 LYS   A N   
1946 C CA  . LYS   A 240 ? 0.56179 1.44204 1.18163 -0.18827 0.15206  -0.19929 237 LYS   A CA  
1947 C C   . LYS   A 240 ? 0.59725 1.52249 1.26621 -0.15945 0.13323  -0.22013 237 LYS   A C   
1948 O O   . LYS   A 240 ? 0.53631 1.46198 1.21242 -0.12854 0.11804  -0.22156 237 LYS   A O   
1949 C CB  . LYS   A 240 ? 0.60945 1.48279 1.21050 -0.19198 0.17536  -0.19972 237 LYS   A CB  
1950 C CG  . LYS   A 240 ? 0.66301 1.48991 1.21208 -0.22014 0.19364  -0.18042 237 LYS   A CG  
1951 C CD  . LYS   A 240 ? 0.76029 1.58830 1.30280 -0.25425 0.20859  -0.18271 237 LYS   A CD  
1952 C CE  . LYS   A 240 ? 0.78129 1.55724 1.26697 -0.28073 0.22442  -0.16345 237 LYS   A CE  
1953 N NZ  . LYS   A 240 ? 0.81628 1.55062 1.27299 -0.28155 0.20998  -0.14362 237 LYS   A NZ  
1954 N N   . PRO   A 241 ? 0.60020 1.56212 1.30233 -0.16786 0.13235  -0.23693 238 PRO   A N   
1955 C CA  . PRO   A 241 ? 0.59266 1.59822 1.34123 -0.13900 0.11407  -0.25898 238 PRO   A CA  
1956 C C   . PRO   A 241 ? 0.63707 1.66378 1.40001 -0.11865 0.12235  -0.27341 238 PRO   A C   
1957 O O   . PRO   A 241 ? 0.50153 1.55613 1.29709 -0.08827 0.10398  -0.29029 238 PRO   A O   
1958 C CB  . PRO   A 241 ? 0.51050 1.55034 1.28765 -0.15986 0.11750  -0.27373 238 PRO   A CB  
1959 C CG  . PRO   A 241 ? 0.59262 1.59823 1.33622 -0.19476 0.12759  -0.25552 238 PRO   A CG  
1960 C CD  . PRO   A 241 ? 0.59863 1.56157 1.29633 -0.20349 0.14521  -0.23651 238 PRO   A CD  
1961 N N   . SER   A 242 ? 0.60126 1.61334 1.33878 -0.13352 0.14801  -0.26785 239 SER   A N   
1962 C CA  . SER   A 242 ? 0.62269 1.65246 1.37017 -0.11599 0.15767  -0.28164 239 SER   A CA  
1963 C C   . SER   A 242 ? 0.56027 1.56346 1.29143 -0.08679 0.14558  -0.27286 239 SER   A C   
1964 O O   . SER   A 242 ? 0.60166 1.61284 1.33577 -0.07157 0.15330  -0.28276 239 SER   A O   
1965 C CB  . SER   A 242 ? 0.77233 1.79644 1.49634 -0.14546 0.19040  -0.27993 239 SER   A CB  
1966 O OG  . SER   A 242 ? 0.78335 1.75602 1.45724 -0.16364 0.19972  -0.25456 239 SER   A OG  
1967 N N   . PHE   A 243 ? 0.49636 1.46875 1.21011 -0.07919 0.12730  -0.25554 240 PHE   A N   
1968 C CA  . PHE   A 243 ? 0.56040 1.50809 1.25904 -0.05235 0.11518  -0.24754 240 PHE   A CA  
1969 C C   . PHE   A 243 ? 0.57725 1.55149 1.30948 -0.01418 0.09600  -0.26823 240 PHE   A C   
1970 O O   . PHE   A 243 ? 0.63259 1.63237 1.39544 -0.00202 0.07705  -0.28109 240 PHE   A O   
1971 C CB  . PHE   A 243 ? 0.53508 1.45099 1.21330 -0.05094 0.09700  -0.22774 240 PHE   A CB  
1972 C CG  . PHE   A 243 ? 0.57059 1.44995 1.20751 -0.08149 0.11353  -0.20553 240 PHE   A CG  
1973 C CD1 . PHE   A 243 ? 0.52650 1.39494 1.14048 -0.10363 0.14089  -0.20195 240 PHE   A CD1 
1974 C CD2 . PHE   A 243 ? 0.58887 1.44280 1.20723 -0.08694 0.10037  -0.18871 240 PHE   A CD2 
1975 C CE1 . PHE   A 243 ? 0.48391 1.31381 1.05602 -0.12959 0.15329  -0.18162 240 PHE   A CE1 
1976 C CE2 . PHE   A 243 ? 0.54071 1.35928 1.11986 -0.11318 0.11380  -0.16927 240 PHE   A CE2 
1977 C CZ  . PHE   A 243 ? 0.62695 1.43194 1.18234 -0.13394 0.13949  -0.16553 240 PHE   A CZ  
1978 N N   . PRO   A 244 ? 0.54999 1.51704 1.27607 0.00610  0.09894  -0.27270 241 PRO   A N   
1979 C CA  . PRO   A 244 ? 0.48518 1.47020 1.23870 0.04521  0.07780  -0.29218 241 PRO   A CA  
1980 C C   . PRO   A 244 ? 0.55661 1.52225 1.30907 0.07168  0.04373  -0.28532 241 PRO   A C   
1981 O O   . PRO   A 244 ? 0.43941 1.37278 1.16486 0.06499  0.03843  -0.26430 241 PRO   A O   
1982 C CB  . PRO   A 244 ? 0.50405 1.47469 1.24120 0.05715  0.09022  -0.29418 241 PRO   A CB  
1983 C CG  . PRO   A 244 ? 0.53846 1.49872 1.24856 0.02014  0.12288  -0.28249 241 PRO   A CG  
1984 C CD  . PRO   A 244 ? 0.53423 1.47647 1.22735 -0.00616 0.12218  -0.26232 241 PRO   A CD  
1985 N N   . LYS   A 245 ? 0.42132 1.40589 1.20150 0.10241  0.01967  -0.30383 242 LYS   A N   
1986 C CA  . LYS   A 245 ? 0.42258 1.38621 1.19914 0.13081  -0.01619 -0.29933 242 LYS   A CA  
1987 C C   . LYS   A 245 ? 0.45651 1.38936 1.21672 0.16590  -0.03135 -0.29924 242 LYS   A C   
1988 O O   . LYS   A 245 ? 0.59996 1.54461 1.37654 0.19164  -0.03874 -0.31883 242 LYS   A O   
1989 C CB  . LYS   A 245 ? 0.44432 1.43957 1.25478 0.14474  -0.03685 -0.31882 242 LYS   A CB  
1990 C CG  . LYS   A 245 ? 0.43968 1.46529 1.26791 0.11106  -0.02381 -0.32068 242 LYS   A CG  
1991 C CD  . LYS   A 245 ? 0.41712 1.41470 1.21940 0.09047  -0.02688 -0.29669 242 LYS   A CD  
1992 C CE  . LYS   A 245 ? 0.42480 1.44837 1.24347 0.05898  -0.01706 -0.29959 242 LYS   A CE  
1993 N NZ  . LYS   A 245 ? 0.52840 1.52330 1.32090 0.04008  -0.02144 -0.27771 242 LYS   A NZ  
1994 N N   . TRP   A 246 ? 0.42331 1.30150 1.13868 0.16431  -0.03582 -0.27366 243 TRP   A N   
1995 C CA  . TRP   A 246 ? 0.49751 1.31577 1.17309 0.19147  -0.05203 -0.26362 243 TRP   A CA  
1996 C C   . TRP   A 246 ? 0.53144 1.30315 1.17838 0.21052  -0.08630 -0.24955 243 TRP   A C   
1997 O O   . TRP   A 246 ? 0.55147 1.31339 1.18574 0.19319  -0.09016 -0.23455 243 TRP   A O   
1998 C CB  . TRP   A 246 ? 0.54499 1.31241 1.17084 0.17093  -0.03053 -0.23932 243 TRP   A CB  
1999 C CG  . TRP   A 246 ? 0.59847 1.39632 1.24002 0.16005  -0.00097 -0.25269 243 TRP   A CG  
2000 C CD1 . TRP   A 246 ? 0.50986 1.31933 1.16544 0.18363  -0.00019 -0.27254 243 TRP   A CD1 
2001 C CD2 . TRP   A 246 ? 0.51545 1.33167 1.15532 0.12318  0.03166  -0.24716 243 TRP   A CD2 
2002 N NE1 . TRP   A 246 ? 0.58983 1.42647 1.25328 0.16300  0.03221  -0.28010 243 TRP   A NE1 
2003 C CE2 . TRP   A 246 ? 0.54934 1.38891 1.20168 0.12542  0.05194  -0.26411 243 TRP   A CE2 
2004 C CE3 . TRP   A 246 ? 0.47952 1.29145 1.10551 0.08926  0.04477  -0.22987 243 TRP   A CE3 
2005 C CZ2 . TRP   A 246 ? 0.51893 1.37609 1.16745 0.09377  0.08507  -0.26321 243 TRP   A CZ2 
2006 C CZ3 . TRP   A 246 ? 0.62475 1.45195 1.24706 0.05884  0.07618  -0.22889 243 TRP   A CZ3 
2007 C CH2 . TRP   A 246 ? 0.56816 1.41702 1.20032 0.06068  0.09617  -0.24490 243 TRP   A CH2 
2008 N N   . ALA   A 247 ? 0.53286 1.27274 1.16617 0.24609  -0.11132 -0.25457 244 ALA   A N   
2009 C CA  . ALA   A 247 ? 0.58861 1.27589 1.18630 0.26552  -0.14456 -0.24070 244 ALA   A CA  
2010 C C   . ALA   A 247 ? 0.55622 1.16421 1.08571 0.25288  -0.14071 -0.20744 244 ALA   A C   
2011 O O   . ALA   A 247 ? 0.64145 1.22549 1.15064 0.24699  -0.12397 -0.20102 244 ALA   A O   
2012 C CB  . ALA   A 247 ? 0.57159 1.25451 1.18064 0.31019  -0.17568 -0.26112 244 ALA   A CB  
2013 N N   . ARG   A 248 ? 0.56709 1.13658 1.06209 0.24816  -0.15599 -0.18760 245 ARG   A N   
2014 C CA  . ARG   A 248 ? 0.58364 1.08107 1.01560 0.23620  -0.15331 -0.15761 245 ARG   A CA  
2015 C C   . ARG   A 248 ? 0.66743 1.10928 1.06489 0.26230  -0.16990 -0.15540 245 ARG   A C   
2016 O O   . ARG   A 248 ? 0.87860 1.31254 1.27986 0.29457  -0.19836 -0.16828 245 ARG   A O   
2017 C CB  . ARG   A 248 ? 0.71723 1.18794 1.12046 0.22878  -0.16772 -0.14024 245 ARG   A CB  
2018 C CG  . ARG   A 248 ? 0.68444 1.08755 1.02554 0.21321  -0.16227 -0.11054 245 ARG   A CG  
2019 C CD  . ARG   A 248 ? 0.84069 1.21804 1.15247 0.20978  -0.17822 -0.09637 245 ARG   A CD  
2020 N NE  . ARG   A 248 ? 0.82521 1.14410 1.08060 0.19311  -0.17050 -0.06993 245 ARG   A NE  
2021 C CZ  . ARG   A 248 ? 0.79755 1.11951 1.04412 0.16435  -0.14948 -0.05621 245 ARG   A CZ  
2022 N NH1 . ARG   A 248 ? 0.71978 1.09321 1.00440 0.14776  -0.13433 -0.06407 245 ARG   A NH1 
2023 N NH2 . ARG   A 248 ? 0.85417 1.12573 1.05196 0.15173  -0.14383 -0.03488 245 ARG   A NH2 
2024 N N   . GLN   A 249 ? 0.85191 1.25350 1.21471 0.24849  -0.15329 -0.13969 246 GLN   A N   
2025 C CA  . GLN   A 249 ? 0.91052 1.25553 1.23775 0.26860  -0.16601 -0.13679 246 GLN   A CA  
2026 C C   . GLN   A 249 ? 0.95233 1.22344 1.21805 0.26886  -0.18393 -0.11241 246 GLN   A C   
2027 O O   . GLN   A 249 ? 0.94459 1.20194 1.18728 0.24415  -0.17466 -0.09256 246 GLN   A O   
2028 C CB  . GLN   A 249 ? 0.88188 1.21920 1.20154 0.25299  -0.14012 -0.13335 246 GLN   A CB  
2029 C CG  . GLN   A 249 ? 0.87448 1.27713 1.24710 0.25473  -0.12207 -0.15833 246 GLN   A CG  
2030 C CD  . GLN   A 249 ? 0.97884 1.36882 1.33804 0.24022  -0.09822 -0.15464 246 GLN   A CD  
2031 O OE1 . GLN   A 249 ? 1.01441 1.35242 1.32922 0.22532  -0.09349 -0.13298 246 GLN   A OE1 
2032 N NE2 . GLN   A 249 ? 1.03273 1.47184 1.43050 0.24404  -0.08287 -0.17696 246 GLN   A NE2 
2033 N N   . ASP   A 250 ? 1.02140 1.24353 1.25879 0.29728  -0.20980 -0.11486 247 ASP   A N   
2034 C CA  . ASP   A 250 ? 1.08604 1.23066 1.25824 0.29744  -0.22687 -0.09195 247 ASP   A CA  
2035 C C   . ASP   A 250 ? 1.10196 1.20531 1.23440 0.26769  -0.20407 -0.06945 247 ASP   A C   
2036 O O   . ASP   A 250 ? 1.14840 1.24503 1.28205 0.26561  -0.19154 -0.07330 247 ASP   A O   
2037 C CB  . ASP   A 250 ? 1.16568 1.26134 1.31284 0.33448  -0.25934 -0.10033 247 ASP   A CB  
2038 C CG  . ASP   A 250 ? 1.27635 1.29925 1.35986 0.33946  -0.28383 -0.08054 247 ASP   A CG  
2039 O OD1 . ASP   A 250 ? 1.38700 1.37974 1.43245 0.31037  -0.27023 -0.05644 247 ASP   A OD1 
2040 O OD2 . ASP   A 250 ? 1.32260 1.31806 1.39287 0.37306  -0.31706 -0.08991 247 ASP   A OD2 
2041 N N   . PHE   A 251 ? 1.09613 1.17380 1.19428 0.24488  -0.19890 -0.04738 248 PHE   A N   
2042 C CA  . PHE   A 251 ? 1.13961 1.18404 1.20383 0.21570  -0.17745 -0.02751 248 PHE   A CA  
2043 C C   . PHE   A 251 ? 1.25111 1.22310 1.26560 0.22239  -0.18708 -0.01915 248 PHE   A C   
2044 O O   . PHE   A 251 ? 1.24200 1.19001 1.23423 0.19943  -0.16913 -0.00673 248 PHE   A O   
2045 C CB  . PHE   A 251 ? 1.12106 1.15542 1.16000 0.19238  -0.17119 -0.00822 248 PHE   A CB  
2046 C CG  . PHE   A 251 ? 0.99563 1.09136 1.07451 0.17156  -0.14934 -0.01052 248 PHE   A CG  
2047 C CD1 . PHE   A 251 ? 0.96296 1.12129 1.09773 0.17782  -0.14280 -0.03015 248 PHE   A CD1 
2048 C CD2 . PHE   A 251 ? 0.94497 1.03435 1.00390 0.14523  -0.13490 0.00625  248 PHE   A CD2 
2049 C CE1 . PHE   A 251 ? 0.93604 1.14358 1.10167 0.15715  -0.12326 -0.03128 248 PHE   A CE1 
2050 C CE2 . PHE   A 251 ? 0.84241 0.98210 0.93418 0.12762  -0.11693 0.00399  248 PHE   A CE2 
2051 C CZ  . PHE   A 251 ? 0.91479 1.11058 1.05772 0.13298  -0.11150 -0.01389 248 PHE   A CZ  
2052 N N   . SER   A 252 ? 1.31402 1.24922 1.30980 0.25310  -0.21599 -0.02626 249 SER   A N   
2053 C CA  . SER   A 252 ? 1.36026 1.22620 1.31149 0.26171  -0.22605 -0.02161 249 SER   A CA  
2054 C C   . SER   A 252 ? 1.34461 1.23226 1.32447 0.26288  -0.21083 -0.03543 249 SER   A C   
2055 O O   . SER   A 252 ? 1.43312 1.26761 1.37712 0.25798  -0.20956 -0.02859 249 SER   A O   
2056 C CB  . SER   A 252 ? 1.45629 1.27967 1.38378 0.29883  -0.26317 -0.02922 249 SER   A CB  
2057 O OG  . SER   A 252 ? 1.59862 1.39464 1.49179 0.29789  -0.27873 -0.01558 249 SER   A OG  
2058 N N   . LYS   A 253 ? 1.28660 1.24968 1.32802 0.26790  -0.19890 -0.05497 250 LYS   A N   
2059 C CA  . LYS   A 253 ? 1.26873 1.25848 1.33791 0.26660  -0.18123 -0.06864 250 LYS   A CA  
2060 C C   . LYS   A 253 ? 1.23487 1.26137 1.32081 0.23169  -0.14862 -0.06046 250 LYS   A C   
2061 O O   . LYS   A 253 ? 1.31175 1.33437 1.39684 0.22230  -0.13334 -0.06258 250 LYS   A O   
2062 C CB  . LYS   A 253 ? 1.26103 1.31021 1.38599 0.29526  -0.18782 -0.09819 250 LYS   A CB  
2063 C CG  . LYS   A 253 ? 1.37482 1.39665 1.49129 0.33495  -0.22307 -0.11084 250 LYS   A CG  
2064 C CD  . LYS   A 253 ? 1.41240 1.49498 1.58687 0.36361  -0.22668 -0.14381 250 LYS   A CD  
2065 C CE  . LYS   A 253 ? 1.35367 1.52564 1.58920 0.35155  -0.20901 -0.15552 250 LYS   A CE  
2066 N NZ  . LYS   A 253 ? 1.20811 1.38938 1.44594 0.35427  -0.22616 -0.15001 250 LYS   A NZ  
2067 N N   . VAL   A 254 ? 1.08078 1.14044 1.18003 0.21346  -0.13923 -0.05186 251 VAL   A N   
2068 C CA  . VAL   A 254 ? 1.04327 1.13387 1.15539 0.18220  -0.11101 -0.04408 251 VAL   A CA  
2069 C C   . VAL   A 254 ? 1.07183 1.11048 1.13808 0.15923  -0.10295 -0.02325 251 VAL   A C   
2070 O O   . VAL   A 254 ? 1.08313 1.12440 1.15016 0.14339  -0.08528 -0.02208 251 VAL   A O   
2071 C CB  . VAL   A 254 ? 0.98079 1.11743 1.11805 0.17097  -0.10556 -0.04185 251 VAL   A CB  
2072 C CG1 . VAL   A 254 ? 0.88577 1.04558 1.02963 0.14009  -0.07922 -0.03270 251 VAL   A CG1 
2073 C CG2 . VAL   A 254 ? 0.99566 1.18996 1.18343 0.19001  -0.11101 -0.06464 251 VAL   A CG2 
2074 N N   . VAL   A 255 ? 1.08990 1.08159 1.11518 0.15636  -0.11563 -0.00739 252 VAL   A N   
2075 C CA  . VAL   A 255 ? 1.10829 1.04988 1.08886 0.13357  -0.10832 0.01134  252 VAL   A CA  
2076 C C   . VAL   A 255 ? 1.17887 1.04832 1.11027 0.14761  -0.13045 0.01748  252 VAL   A C   
2077 O O   . VAL   A 255 ? 1.27309 1.10809 1.16919 0.14485  -0.14117 0.03074  252 VAL   A O   
2078 C CB  . VAL   A 255 ? 1.05720 1.01026 1.02987 0.10910  -0.09697 0.02659  252 VAL   A CB  
2079 C CG1 . VAL   A 255 ? 1.02551 1.02812 1.03076 0.08879  -0.07269 0.02449  252 VAL   A CG1 
2080 C CG2 . VAL   A 255 ? 1.06308 1.03483 1.04490 0.12192  -0.11084 0.02495  252 VAL   A CG2 
2081 N N   . PRO   A 256 ? 1.23358 1.07491 1.15748 0.16282  -0.13832 0.00821  253 PRO   A N   
2082 C CA  . PRO   A 256 ? 1.25765 1.02362 1.13112 0.17868  -0.16227 0.01315  253 PRO   A CA  
2083 C C   . PRO   A 256 ? 1.28612 0.99109 1.10214 0.15175  -0.15853 0.03638  253 PRO   A C   
2084 O O   . PRO   A 256 ? 1.39090 1.04327 1.16235 0.15881  -0.17724 0.04656  253 PRO   A O   
2085 C CB  . PRO   A 256 ? 1.22247 0.97597 1.10281 0.19372  -0.16470 -0.00185 253 PRO   A CB  
2086 C CG  . PRO   A 256 ? 1.22198 1.05539 1.16526 0.19974  -0.15026 -0.02062 253 PRO   A CG  
2087 C CD  . PRO   A 256 ? 1.12426 1.00348 1.08695 0.17099  -0.12832 -0.01015 253 PRO   A CD  
2088 N N   . PRO   A 257 ? 1.30371 1.01213 1.11676 0.12049  -0.13539 0.04476  254 PRO   A N   
2089 C CA  . PRO   A 257 ? 1.30035 0.95245 1.05978 0.09341  -0.13088 0.06493  254 PRO   A CA  
2090 C C   . PRO   A 257 ? 1.41025 1.06558 1.15326 0.08188  -0.12961 0.07851  254 PRO   A C   
2091 O O   . PRO   A 257 ? 1.39675 0.99758 1.08752 0.06440  -0.13030 0.09461  254 PRO   A O   
2092 C CB  . PRO   A 257 ? 1.30592 0.98014 1.08093 0.06454  -0.10573 0.06602  254 PRO   A CB  
2093 C CG  . PRO   A 257 ? 1.19981 0.91310 1.01801 0.08136  -0.10345 0.04725  254 PRO   A CG  
2094 C CD  . PRO   A 257 ? 1.13291 0.89028 0.98601 0.10787  -0.11348 0.03594  254 PRO   A CD  
2095 N N   . LEU   A 258 ? 1.36825 1.08368 1.15167 0.08985  -0.12730 0.07222  255 LEU   A N   
2096 C CA  . LEU   A 258 ? 1.36472 1.08801 1.13522 0.07772  -0.12420 0.08373  255 LEU   A CA  
2097 C C   . LEU   A 258 ? 1.41255 1.08693 1.14149 0.09751  -0.15063 0.08900  255 LEU   A C   
2098 O O   . LEU   A 258 ? 1.42382 1.09493 1.16296 0.12913  -0.17280 0.07706  255 LEU   A O   
2099 C CB  . LEU   A 258 ? 1.24158 1.04266 1.06811 0.07893  -0.11370 0.07448  255 LEU   A CB  
2100 C CG  . LEU   A 258 ? 1.21185 1.03964 1.04110 0.05074  -0.09297 0.08436  255 LEU   A CG  
2101 C CD1 . LEU   A 258 ? 1.13666 0.94443 0.94740 0.02287  -0.07463 0.09270  255 LEU   A CD1 
2102 C CD2 . LEU   A 258 ? 1.07773 0.97783 0.96303 0.05164  -0.08201 0.07354  255 LEU   A CD2 
2103 N N   . ASP   A 259 ? 1.41477 1.05158 1.09593 0.07916  -0.14849 0.10601  256 ASP   A N   
2104 C CA  . ASP   A 259 ? 1.52109 1.10290 1.15177 0.09470  -0.17334 0.11370  256 ASP   A CA  
2105 C C   . ASP   A 259 ? 1.45823 1.08661 1.11652 0.10963  -0.18219 0.10769  256 ASP   A C   
2106 O O   . ASP   A 259 ? 1.45298 1.15312 1.17161 0.11240  -0.17224 0.09540  256 ASP   A O   
2107 C CB  . ASP   A 259 ? 1.54537 1.06359 1.10780 0.06613  -0.16547 0.13449  256 ASP   A CB  
2108 C CG  . ASP   A 259 ? 1.59665 1.15609 1.17126 0.03380  -0.13697 0.14165  256 ASP   A CG  
2109 O OD1 . ASP   A 259 ? 1.56424 1.14910 1.14319 0.03606  -0.13831 0.14303  256 ASP   A OD1 
2110 O OD2 . ASP   A 259 ? 1.72399 1.29086 1.30442 0.00706  -0.11426 0.14459  256 ASP   A OD2 
2111 N N   . GLU   A 260 ? 1.49143 1.07597 1.10215 0.11837  -0.20160 0.11651  257 GLU   A N   
2112 C CA  . GLU   A 260 ? 1.45584 1.07880 1.08886 0.13470  -0.21432 0.10978  257 GLU   A CA  
2113 C C   . GLU   A 260 ? 1.33209 1.00856 0.99003 0.10930  -0.18909 0.11333  257 GLU   A C   
2114 O O   . GLU   A 260 ? 1.24855 0.98947 0.96006 0.11705  -0.18741 0.10105  257 GLU   A O   
2115 C CB  . GLU   A 260 ? 1.49087 1.04710 1.05935 0.14962  -0.24244 0.11917  257 GLU   A CB  
2116 C CG  . GLU   A 260 ? 1.58514 1.17549 1.16903 0.16372  -0.25646 0.11351  257 GLU   A CG  
2117 C CD  . GLU   A 260 ? 1.76351 1.28286 1.27696 0.17810  -0.28534 0.12356  257 GLU   A CD  
2118 O OE1 . GLU   A 260 ? 1.78437 1.22903 1.24362 0.18597  -0.30085 0.13120  257 GLU   A OE1 
2119 O OE2 . GLU   A 260 ? 1.90186 1.43654 1.41082 0.18149  -0.29344 0.12387  257 GLU   A OE2 
2120 N N   . ASP   A 261 ? 1.28047 0.93085 0.89978 0.07853  -0.16932 0.12912  258 ASP   A N   
2121 C CA  . ASP   A 261 ? 1.22545 0.92474 0.86676 0.05602  -0.14598 0.13118  258 ASP   A CA  
2122 C C   . ASP   A 261 ? 1.18220 0.94720 0.88831 0.04791  -0.12537 0.12017  258 ASP   A C   
2123 O O   . ASP   A 261 ? 1.03739 0.85593 0.77904 0.04145  -0.11395 0.11533  258 ASP   A O   
2124 C CB  . ASP   A 261 ? 1.31549 0.97433 0.90230 0.02516  -0.12855 0.14822  258 ASP   A CB  
2125 C CG  . ASP   A 261 ? 1.39096 0.99332 0.91218 0.02916  -0.14513 0.15979  258 ASP   A CG  
2126 O OD1 . ASP   A 261 ? 1.48253 1.10055 1.01179 0.04955  -0.16330 0.15421  258 ASP   A OD1 
2127 O OD2 . ASP   A 261 ? 1.47235 1.01348 0.93216 0.01081  -0.14003 0.17427  258 ASP   A OD2 
2128 N N   . GLY   A 262 ? 1.22304 0.98144 0.94184 0.04848  -0.12139 0.11599  259 GLY   A N   
2129 C CA  . GLY   A 262 ? 1.09876 0.91456 0.87354 0.04150  -0.10316 0.10571  259 GLY   A CA  
2130 C C   . GLY   A 262 ? 1.02308 0.89244 0.85197 0.06382  -0.11193 0.08930  259 GLY   A C   
2131 O O   . GLY   A 262 ? 0.89143 0.81575 0.76201 0.05580  -0.09757 0.08310  259 GLY   A O   
2132 N N   . ARG   A 263 ? 1.07833 0.93205 0.90684 0.09183  -0.13581 0.08120  260 ARG   A N   
2133 C CA  . ARG   A 263 ? 1.03550 0.94371 0.91762 0.11243  -0.14406 0.06348  260 ARG   A CA  
2134 C C   . ARG   A 263 ? 1.01557 0.95891 0.91248 0.11058  -0.14576 0.06263  260 ARG   A C   
2135 O O   . ARG   A 263 ? 0.99774 0.99923 0.94476 0.11197  -0.13948 0.05059  260 ARG   A O   
2136 C CB  . ARG   A 263 ? 1.17365 1.05774 1.05137 0.14480  -0.17157 0.05327  260 ARG   A CB  
2137 C CG  . ARG   A 263 ? 1.19648 1.04198 1.05831 0.15034  -0.17310 0.05205  260 ARG   A CG  
2138 C CD  . ARG   A 263 ? 1.30888 1.13944 1.17467 0.18677  -0.20164 0.03779  260 ARG   A CD  
2139 N NE  . ARG   A 263 ? 1.36727 1.17315 1.20621 0.20394  -0.22759 0.04058  260 ARG   A NE  
2140 C CZ  . ARG   A 263 ? 1.43043 1.16019 1.20432 0.20959  -0.24623 0.05364  260 ARG   A CZ  
2141 N NH1 . ARG   A 263 ? 1.48535 1.15483 1.21435 0.19821  -0.24157 0.06523  260 ARG   A NH1 
2142 N NH2 . ARG   A 263 ? 1.44279 1.15403 1.19352 0.22611  -0.27064 0.05509  260 ARG   A NH2 
2143 N N   . SER   A 264 ? 1.00729 0.91395 0.85861 0.10641  -0.15397 0.07506  261 SER   A N   
2144 C CA  . SER   A 264 ? 1.00437 0.93980 0.86486 0.10461  -0.15658 0.07416  261 SER   A CA  
2145 C C   . SER   A 264 ? 0.92677 0.90516 0.81335 0.07990  -0.12993 0.07567  261 SER   A C   
2146 O O   . SER   A 264 ? 0.87156 0.89907 0.79779 0.08085  -0.12778 0.06621  261 SER   A O   
2147 C CB  . SER   A 264 ? 0.97639 0.85750 0.77492 0.10432  -0.16983 0.08778  261 SER   A CB  
2148 O OG  . SER   A 264 ? 1.01829 0.92540 0.82188 0.09943  -0.16958 0.08752  261 SER   A OG  
2149 N N   . LEU   A 265 ? 0.90769 0.86738 0.77212 0.05755  -0.11028 0.08670  262 LEU   A N   
2150 C CA  . LEU   A 265 ? 0.77969 0.77769 0.66727 0.03638  -0.08696 0.08713  262 LEU   A CA  
2151 C C   . LEU   A 265 ? 0.83599 0.88266 0.77770 0.03840  -0.07822 0.07457  262 LEU   A C   
2152 O O   . LEU   A 265 ? 0.71434 0.80225 0.68569 0.03184  -0.06958 0.06947  262 LEU   A O   
2153 C CB  . LEU   A 265 ? 0.89816 0.86884 0.75455 0.01350  -0.06911 0.09885  262 LEU   A CB  
2154 C CG  . LEU   A 265 ? 0.86006 0.86881 0.74044 -0.00656 -0.04623 0.09781  262 LEU   A CG  
2155 C CD1 . LEU   A 265 ? 0.79452 0.82676 0.67825 -0.00919 -0.04528 0.09710  262 LEU   A CD1 
2156 C CD2 . LEU   A 265 ? 0.81101 0.79552 0.66468 -0.02809 -0.03011 0.10668  262 LEU   A CD2 
2157 N N   . LEU   A 266 ? 0.80601 0.84551 0.75784 0.04712  -0.08037 0.06930  263 LEU   A N   
2158 C CA  . LEU   A 266 ? 0.77965 0.86271 0.77830 0.04855  -0.07103 0.05709  263 LEU   A CA  
2159 C C   . LEU   A 266 ? 0.70298 0.82802 0.73907 0.06185  -0.08021 0.04419  263 LEU   A C   
2160 O O   . LEU   A 266 ? 0.64198 0.80942 0.71303 0.05411  -0.06815 0.03706  263 LEU   A O   
2161 C CB  . LEU   A 266 ? 0.72485 0.78877 0.72317 0.05778  -0.07340 0.05257  263 LEU   A CB  
2162 C CG  . LEU   A 266 ? 0.70952 0.81430 0.75077 0.05914  -0.06260 0.03955  263 LEU   A CG  
2163 C CD1 . LEU   A 266 ? 0.68573 0.80996 0.73535 0.03618  -0.04089 0.04382  263 LEU   A CD1 
2164 C CD2 . LEU   A 266 ? 0.68246 0.76479 0.72000 0.07228  -0.06817 0.03336  263 LEU   A CD2 
2165 N N   . SER   A 267 ? 0.73203 0.84472 0.76005 0.08123  -0.10223 0.04061  264 SER   A N   
2166 C CA  . SER   A 267 ? 0.74174 0.89706 0.80750 0.09312  -0.11238 0.02672  264 SER   A CA  
2167 C C   . SER   A 267 ? 0.70677 0.88725 0.78010 0.07756  -0.10434 0.02957  264 SER   A C   
2168 O O   . SER   A 267 ? 0.72336 0.94911 0.83622 0.07389  -0.09861 0.01902  264 SER   A O   
2169 C CB  . SER   A 267 ? 0.76383 0.89735 0.81542 0.11812  -0.14068 0.02232  264 SER   A CB  
2170 O OG  . SER   A 267 ? 1.01729 1.12728 1.06353 0.13553  -0.15028 0.01743  264 SER   A OG  
2171 N N   . GLN   A 268 ? 0.64882 0.79921 0.68293 0.06737  -0.10307 0.04323  265 GLN   A N   
2172 C CA  . GLN   A 268 ? 0.67509 0.84547 0.71273 0.05461  -0.09683 0.04509  265 GLN   A CA  
2173 C C   . GLN   A 268 ? 0.60490 0.80064 0.66249 0.03545  -0.07369 0.04553  265 GLN   A C   
2174 O O   . GLN   A 268 ? 0.63467 0.85760 0.70980 0.02740  -0.06893 0.04186  265 GLN   A O   
2175 C CB  . GLN   A 268 ? 0.70723 0.83844 0.69533 0.05000  -0.10111 0.05809  265 GLN   A CB  
2176 C CG  . GLN   A 268 ? 0.71160 0.80940 0.67085 0.06921  -0.12611 0.05916  265 GLN   A CG  
2177 C CD  . GLN   A 268 ? 0.82194 0.87754 0.72589 0.06250  -0.12860 0.07270  265 GLN   A CD  
2178 O OE1 . GLN   A 268 ? 0.96728 0.97427 0.82807 0.06831  -0.13835 0.08130  265 GLN   A OE1 
2179 N NE2 . GLN   A 268 ? 0.82939 0.90105 0.73158 0.05002  -0.11980 0.07427  265 GLN   A NE2 
2180 N N   . MET   A 269 ? 0.65407 0.83867 0.70720 0.02837  -0.06074 0.04960  266 MET   A N   
2181 C CA  . MET   A 269 ? 0.64254 0.85013 0.71465 0.01298  -0.04158 0.04863  266 MET   A CA  
2182 C C   . MET   A 269 ? 0.61843 0.86182 0.73092 0.01622  -0.03816 0.03622  266 MET   A C   
2183 O O   . MET   A 269 ? 0.58014 0.84473 0.70835 0.00392  -0.02491 0.03436  266 MET   A O   
2184 C CB  . MET   A 269 ? 0.64303 0.82679 0.69589 0.00373  -0.03005 0.05626  266 MET   A CB  
2185 C CG  . MET   A 269 ? 0.61226 0.76345 0.62551 -0.00444 -0.02880 0.06798  266 MET   A CG  
2186 S SD  . MET   A 269 ? 0.73126 0.85745 0.72569 -0.01783 -0.01538 0.07489  266 MET   A SD  
2187 C CE  . MET   A 269 ? 0.53739 0.69950 0.55771 -0.03256 0.00231  0.07107  266 MET   A CE  
2188 N N   . LEU   A 270 ? 0.55685 0.80673 0.68491 0.03259  -0.04987 0.02700  267 LEU   A N   
2189 C CA  . LEU   A 270 ? 0.45435 0.74185 0.62201 0.03561  -0.04548 0.01302  267 LEU   A CA  
2190 C C   . LEU   A 270 ? 0.52739 0.84521 0.72148 0.04392  -0.05783 0.00159  267 LEU   A C   
2191 O O   . LEU   A 270 ? 0.47616 0.82463 0.70361 0.05179  -0.05901 -0.01282 267 LEU   A O   
2192 C CB  . LEU   A 270 ? 0.50027 0.77886 0.67179 0.04812  -0.04696 0.00728  267 LEU   A CB  
2193 C CG  . LEU   A 270 ? 0.59025 0.84384 0.74149 0.03851  -0.03402 0.01565  267 LEU   A CG  
2194 C CD1 . LEU   A 270 ? 0.52407 0.76903 0.68008 0.05237  -0.03706 0.00774  267 LEU   A CD1 
2195 C CD2 . LEU   A 270 ? 0.49669 0.77160 0.65947 0.01969  -0.01517 0.01654  267 LEU   A CD2 
2196 N N   . HIS   A 271 ? 0.58158 0.89326 0.76224 0.04203  -0.06688 0.00637  268 HIS   A N   
2197 C CA  . HIS   A 271 ? 0.56103 0.90276 0.76735 0.04738  -0.07894 -0.00503 268 HIS   A CA  
2198 C C   . HIS   A 271 ? 0.60977 0.99164 0.85032 0.03160  -0.06402 -0.01363 268 HIS   A C   
2199 O O   . HIS   A 271 ? 0.52422 0.90205 0.75604 0.01437  -0.04806 -0.00627 268 HIS   A O   
2200 C CB  . HIS   A 271 ? 0.59453 0.91728 0.77390 0.04643  -0.09033 0.00273  268 HIS   A CB  
2201 C CG  . HIS   A 271 ? 0.67131 1.01305 0.86791 0.05884  -0.11088 -0.00861 268 HIS   A CG  
2202 N ND1 . HIS   A 271 ? 0.65017 1.03732 0.88935 0.05395  -0.11002 -0.02327 268 HIS   A ND1 
2203 C CD2 . HIS   A 271 ? 0.69368 1.01443 0.86936 0.07521  -0.13356 -0.00795 268 HIS   A CD2 
2204 C CE1 . HIS   A 271 ? 0.82232 1.21958 1.07043 0.06728  -0.13182 -0.03238 268 HIS   A CE1 
2205 N NE2 . HIS   A 271 ? 0.88970 1.24595 1.09850 0.08152  -0.14737 -0.02315 268 HIS   A NE2 
2206 N N   . TYR   A 272 ? 0.48695 0.90724 0.76587 0.03733  -0.06961 -0.03005 269 TYR   A N   
2207 C CA  . TYR   A 272 ? 0.50463 0.96227 0.81447 0.01968  -0.05446 -0.03886 269 TYR   A CA  
2208 C C   . TYR   A 272 ? 0.53235 0.98746 0.83229 0.00300  -0.05286 -0.03303 269 TYR   A C   
2209 O O   . TYR   A 272 ? 0.51067 0.96523 0.80631 -0.01563 -0.03655 -0.02833 269 TYR   A O   
2210 C CB  . TYR   A 272 ? 0.43751 0.94097 0.79287 0.02826  -0.06088 -0.05970 269 TYR   A CB  
2211 C CG  . TYR   A 272 ? 0.44841 0.96729 0.82317 0.03698  -0.05244 -0.06956 269 TYR   A CG  
2212 C CD1 . TYR   A 272 ? 0.50190 1.02585 0.87794 0.02097  -0.02906 -0.06785 269 TYR   A CD1 
2213 C CD2 . TYR   A 272 ? 0.49784 1.02469 0.88778 0.06248  -0.06902 -0.08158 269 TYR   A CD2 
2214 C CE1 . TYR   A 272 ? 0.44437 0.98212 0.83622 0.02909  -0.02082 -0.07793 269 TYR   A CE1 
2215 C CE2 . TYR   A 272 ? 0.42550 0.96648 0.83316 0.07210  -0.06162 -0.09245 269 TYR   A CE2 
2216 C CZ  . TYR   A 272 ? 0.55478 1.10201 0.96349 0.05477  -0.03668 -0.09068 269 TYR   A CZ  
2217 O OH  . TYR   A 272 ? 0.48631 1.04709 0.91060 0.06450  -0.02882 -0.10241 269 TYR   A OH  
2218 N N   . ASP   A 273 ? 0.46731 0.91805 0.76097 0.01045  -0.07098 -0.03377 270 ASP   A N   
2219 C CA  . ASP   A 273 ? 0.54439 0.99188 0.82824 -0.00337 -0.07179 -0.03019 270 ASP   A CA  
2220 C C   . ASP   A 273 ? 0.56566 0.97615 0.80998 -0.01105 -0.06244 -0.01352 270 ASP   A C   
2221 O O   . ASP   A 273 ? 0.52742 0.90828 0.74228 -0.00066 -0.06865 -0.00412 270 ASP   A O   
2222 C CB  . ASP   A 273 ? 0.57592 1.02436 0.85844 0.00890  -0.09524 -0.03536 270 ASP   A CB  
2223 C CG  . ASP   A 273 ? 0.60108 1.05477 0.88271 -0.00549 -0.09755 -0.03692 270 ASP   A CG  
2224 O OD1 . ASP   A 273 ? 0.57068 1.01156 0.83727 -0.02189 -0.08323 -0.02894 270 ASP   A OD1 
2225 O OD2 . ASP   A 273 ? 0.66159 1.13083 0.95678 0.00066  -0.11539 -0.04698 270 ASP   A OD2 
2226 N N   . PRO   A 274 ? 0.55980 0.97011 0.80128 -0.02902 -0.04794 -0.01014 271 PRO   A N   
2227 C CA  . PRO   A 274 ? 0.57912 0.95856 0.78654 -0.03410 -0.04101 0.00294  271 PRO   A CA  
2228 C C   . PRO   A 274 ? 0.62669 0.98779 0.80932 -0.02953 -0.05318 0.00728  271 PRO   A C   
2229 O O   . PRO   A 274 ? 0.60751 0.94383 0.76097 -0.02859 -0.04962 0.01702  271 PRO   A O   
2230 C CB  . PRO   A 274 ? 0.52895 0.91394 0.74138 -0.05226 -0.02721 0.00245  271 PRO   A CB  
2231 C CG  . PRO   A 274 ? 0.53673 0.95218 0.78231 -0.05795 -0.02145 -0.00835 271 PRO   A CG  
2232 C CD  . PRO   A 274 ? 0.49891 0.93532 0.76610 -0.04563 -0.03698 -0.01846 271 PRO   A CD  
2233 N N   . ASN   A 275 ? 0.63379 1.00788 0.82737 -0.02725 -0.06714 -0.00080 272 ASN   A N   
2234 C CA  . ASN   A 275 ? 0.64966 1.00500 0.81665 -0.02216 -0.07960 0.00246  272 ASN   A CA  
2235 C C   . ASN   A 275 ? 0.64951 0.98492 0.79443 -0.00548 -0.09108 0.00763  272 ASN   A C   
2236 O O   . ASN   A 275 ? 0.75167 1.06187 0.86231 -0.00256 -0.09533 0.01477  272 ASN   A O   
2237 C CB  . ASN   A 275 ? 0.64971 1.02401 0.83442 -0.02556 -0.09236 -0.00870 272 ASN   A CB  
2238 C CG  . ASN   A 275 ? 0.81815 1.20601 1.01959 -0.04459 -0.08134 -0.01321 272 ASN   A CG  
2239 O OD1 . ASN   A 275 ? 0.81683 1.18820 1.00135 -0.05354 -0.06892 -0.00610 272 ASN   A OD1 
2240 N ND2 . ASN   A 275 ? 0.83536 1.25266 1.06942 -0.05117 -0.08631 -0.02572 272 ASN   A ND2 
2241 N N   . LYS   A 276 ? 0.62405 0.96804 0.78530 0.00548  -0.09606 0.00378  273 LYS   A N   
2242 C CA  . LYS   A 276 ? 0.62462 0.94336 0.76140 0.02200  -0.10864 0.00892  273 LYS   A CA  
2243 C C   . LYS   A 276 ? 0.66512 0.95970 0.78161 0.02129  -0.09580 0.01988  273 LYS   A C   
2244 O O   . LYS   A 276 ? 0.66949 0.93246 0.75375 0.03041  -0.10336 0.02764  273 LYS   A O   
2245 C CB  . LYS   A 276 ? 0.57826 0.91716 0.74293 0.03810  -0.12570 -0.00349 273 LYS   A CB  
2246 C CG  . LYS   A 276 ? 0.76421 1.12806 0.94993 0.04060  -0.14231 -0.01614 273 LYS   A CG  
2247 C CD  . LYS   A 276 ? 0.78558 1.11973 0.93224 0.04871  -0.15990 -0.01067 273 LYS   A CD  
2248 C CE  . LYS   A 276 ? 0.82227 1.18145 0.99138 0.05450  -0.18081 -0.02527 273 LYS   A CE  
2249 N NZ  . LYS   A 276 ? 0.97802 1.30568 1.10551 0.06488  -0.20058 -0.02070 273 LYS   A NZ  
2250 N N   . ARG   A 277 ? 0.57340 0.87974 0.70556 0.00993  -0.07736 0.02055  274 ARG   A N   
2251 C CA  . ARG   A 277 ? 0.58341 0.86945 0.69941 0.00808  -0.06555 0.02936  274 ARG   A CA  
2252 C C   . ARG   A 277 ? 0.61958 0.87537 0.69563 0.00282  -0.06148 0.04111  274 ARG   A C   
2253 O O   . ARG   A 277 ? 0.60442 0.86274 0.67281 -0.00555 -0.05744 0.04217  274 ARG   A O   
2254 C CB  . ARG   A 277 ? 0.54065 0.84515 0.67846 -0.00408 -0.04767 0.02719  274 ARG   A CB  
2255 C CG  . ARG   A 277 ? 0.49234 0.78361 0.62417 -0.00376 -0.03795 0.03184  274 ARG   A CG  
2256 C CD  . ARG   A 277 ? 0.53098 0.84220 0.68488 -0.01415 -0.02298 0.02771  274 ARG   A CD  
2257 N NE  . ARG   A 277 ? 0.51590 0.85810 0.70291 -0.01271 -0.02505 0.01567  274 ARG   A NE  
2258 C CZ  . ARG   A 277 ? 0.50033 0.86259 0.70535 -0.02491 -0.01354 0.01086  274 ARG   A CZ  
2259 N NH1 . ARG   A 277 ? 0.45461 0.80719 0.64697 -0.03701 -0.00169 0.01706  274 ARG   A NH1 
2260 N NH2 . ARG   A 277 ? 0.42528 0.81771 0.66076 -0.02525 -0.01428 -0.00113 274 ARG   A NH2 
2261 N N   . ILE   A 278 ? 0.59199 0.81862 0.64179 0.00725  -0.06220 0.04905  275 ILE   A N   
2262 C CA  . ILE   A 278 ? 0.62464 0.82266 0.63448 0.00097  -0.05773 0.05945  275 ILE   A CA  
2263 C C   . ILE   A 278 ? 0.66646 0.87460 0.67934 -0.01435 -0.03870 0.06149  275 ILE   A C   
2264 O O   . ILE   A 278 ? 0.57865 0.80238 0.61447 -0.01955 -0.02843 0.05879  275 ILE   A O   
2265 C CB  . ILE   A 278 ? 0.72235 0.88449 0.70274 0.00566  -0.06090 0.06759  275 ILE   A CB  
2266 C CG1 . ILE   A 278 ? 0.72350 0.85425 0.65780 -0.00190 -0.05749 0.07790  275 ILE   A CG1 
2267 C CG2 . ILE   A 278 ? 0.67487 0.83862 0.66809 -0.00024 -0.04769 0.06853  275 ILE   A CG2 
2268 C CD1 . ILE   A 278 ? 0.71229 0.79946 0.60907 0.00131  -0.06292 0.08699  275 ILE   A CD1 
2269 N N   . SER   A 279 ? 0.69851 0.89822 0.68760 -0.02052 -0.03478 0.06506  276 SER   A N   
2270 C CA  . SER   A 279 ? 0.71559 0.92559 0.70706 -0.03236 -0.01874 0.06507  276 SER   A CA  
2271 C C   . SER   A 279 ? 0.68578 0.87965 0.65952 -0.04046 -0.00656 0.07191  276 SER   A C   
2272 O O   . SER   A 279 ? 0.67501 0.84310 0.62610 -0.03851 -0.01037 0.07835  276 SER   A O   
2273 C CB  . SER   A 279 ? 0.68743 0.89913 0.66384 -0.03443 -0.01934 0.06310  276 SER   A CB  
2274 O OG  . SER   A 279 ? 0.72942 0.91625 0.66802 -0.03402 -0.02174 0.06927  276 SER   A OG  
2275 N N   . ALA   A 280 ? 0.57706 0.78513 0.56064 -0.04984 0.00725  0.06981  277 ALA   A N   
2276 C CA  . ALA   A 280 ? 0.70163 0.90010 0.67286 -0.05994 0.01972  0.07416  277 ALA   A CA  
2277 C C   . ALA   A 280 ? 0.76152 0.94058 0.69627 -0.06606 0.02365  0.07955  277 ALA   A C   
2278 O O   . ALA   A 280 ? 0.73683 0.89275 0.64921 -0.07292 0.02800  0.08639  277 ALA   A O   
2279 C CB  . ALA   A 280 ? 0.61847 0.84028 0.61065 -0.06685 0.03126  0.06832  277 ALA   A CB  
2280 N N   . LYS   A 281 ? 0.77520 0.96077 0.70045 -0.06460 0.02244  0.07643  278 LYS   A N   
2281 C CA  . LYS   A 281 ? 0.78644 0.95395 0.67363 -0.07102 0.02752  0.08080  278 LYS   A CA  
2282 C C   . LYS   A 281 ? 0.84298 0.97431 0.69751 -0.06561 0.01483  0.08970  278 LYS   A C   
2283 O O   . LYS   A 281 ? 0.78473 0.88851 0.60335 -0.07472 0.02083  0.09749  278 LYS   A O   
2284 C CB  . LYS   A 281 ? 0.90369 1.08600 0.78799 -0.06830 0.02745  0.07380  278 LYS   A CB  
2285 C CG  . LYS   A 281 ? 0.88986 1.05720 0.73404 -0.07580 0.03545  0.07647  278 LYS   A CG  
2286 C CD  . LYS   A 281 ? 1.09424 1.27379 0.93450 -0.06998 0.03238  0.06836  278 LYS   A CD  
2287 C CE  . LYS   A 281 ? 1.22313 1.39051 1.02240 -0.07834 0.04319  0.06946  278 LYS   A CE  
2288 N NZ  . LYS   A 281 ? 1.23456 1.42071 1.03912 -0.09254 0.06558  0.06527  278 LYS   A NZ  
2289 N N   . ALA   A 282 ? 0.77177 0.90189 0.63728 -0.05108 -0.00332 0.08802  279 ALA   A N   
2290 C CA  . ALA   A 282 ? 0.81277 0.90910 0.64945 -0.04192 -0.01942 0.09456  279 ALA   A CA  
2291 C C   . ALA   A 282 ? 0.80818 0.88193 0.63956 -0.04278 -0.01946 0.10074  279 ALA   A C   
2292 O O   . ALA   A 282 ? 0.89010 0.92374 0.68191 -0.04126 -0.02691 0.10915  279 ALA   A O   
2293 C CB  . ALA   A 282 ? 0.69951 0.80789 0.55683 -0.02555 -0.03943 0.08796  279 ALA   A CB  
2294 N N   . ALA   A 283 ? 0.79471 0.88964 0.66166 -0.04494 -0.01221 0.09666  280 ALA   A N   
2295 C CA  . ALA   A 283 ? 0.88722 0.96049 0.74956 -0.04578 -0.01203 0.10118  280 ALA   A CA  
2296 C C   . ALA   A 283 ? 0.86722 0.91332 0.69389 -0.06346 0.00188  0.10974  280 ALA   A C   
2297 O O   . ALA   A 283 ? 0.87043 0.87869 0.67011 -0.06448 -0.00238 0.11700  280 ALA   A O   
2298 C CB  . ALA   A 283 ? 0.77608 0.87904 0.68211 -0.04550 -0.00594 0.09407  280 ALA   A CB  
2299 N N   . LEU   A 284 ? 0.87506 0.94008 0.70134 -0.07795 0.01866  0.10795  281 LEU   A N   
2300 C CA  . LEU   A 284 ? 0.84632 0.89161 0.64055 -0.09775 0.03439  0.11422  281 LEU   A CA  
2301 C C   . LEU   A 284 ? 0.97888 0.97754 0.71695 -0.09920 0.02767  0.12457  281 LEU   A C   
2302 O O   . LEU   A 284 ? 0.98147 0.94664 0.68398 -0.11459 0.03600  0.13287  281 LEU   A O   
2303 C CB  . LEU   A 284 ? 0.91301 0.99496 0.72239 -0.10992 0.05252  0.10686  281 LEU   A CB  
2304 C CG  . LEU   A 284 ? 0.84837 0.96975 0.70466 -0.11200 0.06083  0.09744  281 LEU   A CG  
2305 C CD1 . LEU   A 284 ? 0.77037 0.92686 0.64015 -0.11848 0.07400  0.08829  281 LEU   A CD1 
2306 C CD2 . LEU   A 284 ? 0.79119 0.90100 0.64795 -0.12471 0.06899  0.10031  281 LEU   A CD2 
2307 N N   . ALA   A 285 ? 1.00916 1.00252 0.73591 -0.08439 0.01219  0.12422  282 ALA   A N   
2308 C CA  . ALA   A 285 ? 0.96455 0.91074 0.63427 -0.08297 0.00232  0.13378  282 ALA   A CA  
2309 C C   . ALA   A 285 ? 1.01434 0.92129 0.66788 -0.06613 -0.02099 0.13917  282 ALA   A C   
2310 O O   . ALA   A 285 ? 1.09620 0.95888 0.70009 -0.06090 -0.03435 0.14704  282 ALA   A O   
2311 C CB  . ALA   A 285 ? 0.98432 0.94329 0.64657 -0.07499 -0.00418 0.12947  282 ALA   A CB  
2312 N N   . HIS   A 286 ? 1.00562 0.92666 0.69783 -0.05649 -0.02684 0.13428  283 HIS   A N   
2313 C CA  . HIS   A 286 ? 1.08808 0.97628 0.76989 -0.03779 -0.04940 0.13640  283 HIS   A CA  
2314 C C   . HIS   A 286 ? 1.09900 0.92532 0.72482 -0.04801 -0.04899 0.14919  283 HIS   A C   
2315 O O   . HIS   A 286 ? 1.17664 0.99734 0.79154 -0.07127 -0.02805 0.15384  283 HIS   A O   
2316 C CB  . HIS   A 286 ? 0.99110 0.91170 0.72751 -0.02729 -0.05181 0.12671  283 HIS   A CB  
2317 C CG  . HIS   A 286 ? 1.06048 0.96258 0.79933 -0.00289 -0.07657 0.12349  283 HIS   A CG  
2318 N ND1 . HIS   A 286 ? 1.05797 0.91730 0.77387 0.00149  -0.08408 0.12823  283 HIS   A ND1 
2319 C CD2 . HIS   A 286 ? 1.09451 1.01644 0.85748 0.01899  -0.09616 0.11433  283 HIS   A CD2 
2320 C CE1 . HIS   A 286 ? 1.09446 0.94875 0.82070 0.02724  -0.10778 0.12150  283 HIS   A CE1 
2321 N NE2 . HIS   A 286 ? 1.10229 0.99670 0.85890 0.03769  -0.11509 0.11261  283 HIS   A NE2 
2322 N N   . PRO   A 287 ? 1.18666 0.96431 0.77495 -0.03128 -0.07282 0.15451  284 PRO   A N   
2323 C CA  . PRO   A 287 ? 1.34524 1.05451 0.87363 -0.04071 -0.07474 0.16760  284 PRO   A CA  
2324 C C   . PRO   A 287 ? 1.28143 0.98451 0.82643 -0.04838 -0.06632 0.16714  284 PRO   A C   
2325 O O   . PRO   A 287 ? 1.32106 0.96647 0.81694 -0.05999 -0.06568 0.17784  284 PRO   A O   
2326 C CB  . PRO   A 287 ? 1.38058 1.04548 0.87619 -0.01330 -0.10791 0.16968  284 PRO   A CB  
2327 C CG  . PRO   A 287 ? 1.34982 1.05561 0.87099 0.00132  -0.11783 0.16095  284 PRO   A CG  
2328 C CD  . PRO   A 287 ? 1.21146 0.99072 0.80331 -0.00457 -0.09966 0.14904  284 PRO   A CD  
2329 N N   . PHE   A 288 ? 1.19030 0.94702 0.79894 -0.04310 -0.06027 0.15526  285 PHE   A N   
2330 C CA  . PHE   A 288 ? 1.21766 0.97026 0.84112 -0.05204 -0.05089 0.15405  285 PHE   A CA  
2331 C C   . PHE   A 288 ? 1.18761 0.94216 0.79905 -0.08531 -0.02358 0.15949  285 PHE   A C   
2332 O O   . PHE   A 288 ? 1.19352 0.92086 0.79160 -0.09884 -0.01689 0.16309  285 PHE   A O   
2333 C CB  . PHE   A 288 ? 1.05834 0.86767 0.74935 -0.03836 -0.05092 0.13970  285 PHE   A CB  
2334 C CG  . PHE   A 288 ? 1.15012 0.95519 0.85661 -0.04402 -0.04402 0.13683  285 PHE   A CG  
2335 C CD1 . PHE   A 288 ? 1.22785 0.98509 0.91122 -0.03133 -0.06005 0.13848  285 PHE   A CD1 
2336 C CD2 . PHE   A 288 ? 0.99175 0.83897 0.73462 -0.06045 -0.02331 0.13151  285 PHE   A CD2 
2337 C CE1 . PHE   A 288 ? 1.14342 0.89494 0.83933 -0.03626 -0.05428 0.13492  285 PHE   A CE1 
2338 C CE2 . PHE   A 288 ? 1.10172 0.94420 0.85723 -0.06545 -0.01819 0.12816  285 PHE   A CE2 
2339 C CZ  . PHE   A 288 ? 1.12449 0.91926 0.85651 -0.05394 -0.03308 0.12985  285 PHE   A CZ  
2340 N N   . PHE   A 289 ? 1.26803 1.05544 0.88501 -0.09861 -0.00804 0.15867  286 PHE   A N   
2341 C CA  . PHE   A 289 ? 1.28954 1.08629 0.89843 -0.12950 0.01832  0.16112  286 PHE   A CA  
2342 C C   . PHE   A 289 ? 1.51319 1.26862 1.05910 -0.14650 0.02483  0.17256  286 PHE   A C   
2343 O O   . PHE   A 289 ? 1.61210 1.38520 1.15347 -0.17178 0.04840  0.17233  286 PHE   A O   
2344 C CB  . PHE   A 289 ? 1.15809 1.02529 0.82088 -0.13290 0.03336  0.14943  286 PHE   A CB  
2345 C CG  . PHE   A 289 ? 1.06089 0.96793 0.78115 -0.11801 0.02832  0.13866  286 PHE   A CG  
2346 C CD1 . PHE   A 289 ? 0.97011 0.87992 0.70901 -0.12642 0.03526  0.13582  286 PHE   A CD1 
2347 C CD2 . PHE   A 289 ? 0.89335 0.83415 0.64685 -0.09732 0.01726  0.13106  286 PHE   A CD2 
2348 C CE1 . PHE   A 289 ? 0.94284 0.88681 0.72950 -0.11344 0.03140  0.12607  286 PHE   A CE1 
2349 C CE2 . PHE   A 289 ? 0.91879 0.89404 0.72061 -0.08629 0.01460  0.12158  286 PHE   A CE2 
2350 C CZ  . PHE   A 289 ? 0.92821 0.90451 0.74529 -0.09392 0.02184  0.11929  286 PHE   A CZ  
2351 N N   . GLN   A 290 ? 1.60408 1.30533 1.10047 -0.13296 0.00432  0.18161  287 GLN   A N   
2352 C CA  . GLN   A 290 ? 1.73427 1.39060 1.16321 -0.14879 0.00954  0.19336  287 GLN   A CA  
2353 C C   . GLN   A 290 ? 1.91887 1.53551 1.30658 -0.18195 0.02888  0.20277  287 GLN   A C   
2354 O O   . GLN   A 290 ? 2.01758 1.61439 1.35914 -0.20503 0.04472  0.21000  287 GLN   A O   
2355 C CB  . GLN   A 290 ? 1.78159 1.38147 1.16261 -0.12505 -0.02053 0.20111  287 GLN   A CB  
2356 C CG  . GLN   A 290 ? 1.86474 1.40104 1.21406 -0.11665 -0.03889 0.20839  287 GLN   A CG  
2357 C CD  . GLN   A 290 ? 1.97265 1.46714 1.29224 -0.08425 -0.07390 0.21086  287 GLN   A CD  
2358 O OE1 . GLN   A 290 ? 2.07554 1.57592 1.38213 -0.07347 -0.08337 0.21051  287 GLN   A OE1 
2359 N NE2 . GLN   A 290 ? 1.94656 1.39932 1.25614 -0.06726 -0.09460 0.21188  287 GLN   A NE2 
2360 N N   . ASP   A 291 ? 1.89477 1.49938 1.29704 -0.18612 0.02867  0.20215  288 ASP   A N   
2361 C CA  . ASP   A 291 ? 1.95094 1.52262 1.32092 -0.22018 0.04782  0.20923  288 ASP   A CA  
2362 C C   . ASP   A 291 ? 1.95116 1.58859 1.37148 -0.24438 0.07687  0.19842  288 ASP   A C   
2363 O O   . ASP   A 291 ? 2.04772 1.67085 1.44352 -0.27811 0.09827  0.20227  288 ASP   A O   
2364 C CB  . ASP   A 291 ? 1.98210 1.50305 1.33894 -0.21327 0.03184  0.21318  288 ASP   A CB  
2365 C CG  . ASP   A 291 ? 1.93309 1.50182 1.36011 -0.18922 0.02191  0.19954  288 ASP   A CG  
2366 O OD1 . ASP   A 291 ? 1.86951 1.49361 1.34341 -0.16867 0.01713  0.18992  288 ASP   A OD1 
2367 O OD2 . ASP   A 291 ? 1.93328 1.48229 1.36615 -0.19186 0.01922  0.19827  288 ASP   A OD2 
2368 N N   . VAL   A 292 ? 1.89037 1.59817 1.37906 -0.22843 0.07750  0.18447  289 VAL   A N   
2369 C CA  . VAL   A 292 ? 1.80913 1.58054 1.34759 -0.24671 0.10121  0.17253  289 VAL   A CA  
2370 C C   . VAL   A 292 ? 1.84022 1.64986 1.37966 -0.25701 0.11867  0.16807  289 VAL   A C   
2371 O O   . VAL   A 292 ? 1.91096 1.74540 1.45525 -0.28462 0.14326  0.16336  289 VAL   A O   
2372 C CB  . VAL   A 292 ? 1.66243 1.48433 1.26909 -0.22471 0.09234  0.15989  289 VAL   A CB  
2373 C CG1 . VAL   A 292 ? 1.47905 1.36712 1.13610 -0.23901 0.11305  0.14661  289 VAL   A CG1 
2374 C CG2 . VAL   A 292 ? 1.65278 1.44008 1.25888 -0.21813 0.07926  0.16215  289 VAL   A CG2 
2375 N N   . THR   A 293 ? 1.75301 1.56945 1.28886 -0.23519 0.10627  0.16797  290 THR   A N   
2376 C CA  . THR   A 293 ? 1.75460 1.60687 1.29181 -0.24076 0.12036  0.16223  290 THR   A CA  
2377 C C   . THR   A 293 ? 1.91948 1.72084 1.38941 -0.23980 0.11341  0.17408  290 THR   A C   
2378 O O   . THR   A 293 ? 1.95809 1.70471 1.39130 -0.22496 0.09095  0.18471  290 THR   A O   
2379 C CB  . THR   A 293 ? 1.59863 1.51032 1.19467 -0.21632 0.11259  0.14905  290 THR   A CB  
2380 O OG1 . THR   A 293 ? 1.62285 1.56858 1.21986 -0.22226 0.12702  0.14191  290 THR   A OG1 
2381 C CG2 . THR   A 293 ? 1.54249 1.43294 1.13507 -0.18571 0.08410  0.15287  290 THR   A CG2 
2382 N N   . LYS   A 294 ? 1.93791 1.75795 1.39103 -0.25489 0.13240  0.17101  291 LYS   A N   
2383 C CA  . LYS   A 294 ? 1.99494 1.77384 1.38474 -0.25442 0.12807  0.18019  291 LYS   A CA  
2384 C C   . LYS   A 294 ? 2.00524 1.83198 1.42007 -0.23882 0.12778  0.16882  291 LYS   A C   
2385 O O   . LYS   A 294 ? 1.94187 1.83102 1.40676 -0.24326 0.14425  0.15438  291 LYS   A O   
2386 C CB  . LYS   A 294 ? 2.11340 1.86012 1.44476 -0.29134 0.15374  0.18805  291 LYS   A CB  
2387 C CG  . LYS   A 294 ? 2.11006 1.76593 1.35803 -0.29635 0.14050  0.20774  291 LYS   A CG  
2388 C CD  . LYS   A 294 ? 2.15734 1.77546 1.41115 -0.28374 0.11862  0.21442  291 LYS   A CD  
2389 C CE  . LYS   A 294 ? 2.23218 1.75513 1.40108 -0.28321 0.10034  0.23322  291 LYS   A CE  
2390 N NZ  . LYS   A 294 ? 2.18842 1.67440 1.36374 -0.26714 0.07706  0.23766  291 LYS   A NZ  
2391 N N   . PRO   A 295 ? 2.08553 1.88339 1.46631 -0.21966 0.10780  0.17403  292 PRO   A N   
2392 C CA  . PRO   A 295 ? 2.03469 1.87572 1.44156 -0.20266 0.10391  0.16247  292 PRO   A CA  
2393 C C   . PRO   A 295 ? 2.06460 1.92933 1.45374 -0.22284 0.13115  0.15587  292 PRO   A C   
2394 O O   . PRO   A 295 ? 2.04790 1.88045 1.38349 -0.24842 0.14913  0.16374  292 PRO   A O   
2395 C CB  . PRO   A 295 ? 2.05375 1.84840 1.42005 -0.17973 0.07410  0.17086  292 PRO   A CB  
2396 C CG  . PRO   A 295 ? 2.16767 1.88829 1.46181 -0.19359 0.07187  0.18802  292 PRO   A CG  
2397 C CD  . PRO   A 295 ? 2.13355 1.85566 1.44887 -0.21171 0.08577  0.18994  292 PRO   A CD  
2398 N N   . VAL   A 296 ? 2.02662 1.94767 1.46052 -0.21133 0.13438  0.14047  293 VAL   A N   
2399 C CA  . VAL   A 296 ? 1.98846 1.93936 1.41242 -0.22457 0.15801  0.13023  293 VAL   A CA  
2400 C C   . VAL   A 296 ? 1.96321 1.88678 1.34019 -0.21127 0.14450  0.13303  293 VAL   A C   
2401 O O   . VAL   A 296 ? 2.02612 1.93080 1.40450 -0.18684 0.11550  0.13691  293 VAL   A O   
2402 C CB  . VAL   A 296 ? 1.84924 1.87345 1.34536 -0.21809 0.16781  0.11046  293 VAL   A CB  
2403 C CG1 . VAL   A 296 ? 1.77355 1.82156 1.31697 -0.22691 0.17497  0.10788  293 VAL   A CG1 
2404 C CG2 . VAL   A 296 ? 1.81988 1.86173 1.34817 -0.18758 0.14349  0.10374  293 VAL   A CG2 
2405 N N   . PRO   A 297 ? 1.90478 1.82594 1.23918 -0.22675 0.16432  0.13029  294 PRO   A N   
2406 C CA  . PRO   A 297 ? 1.91725 1.81493 1.20755 -0.21293 0.15088  0.13103  294 PRO   A CA  
2407 C C   . PRO   A 297 ? 1.85169 1.79820 1.19551 -0.18799 0.13861  0.11469  294 PRO   A C   
2408 O O   . PRO   A 297 ? 1.86182 1.86504 1.25617 -0.18978 0.15464  0.09880  294 PRO   A O   
2409 C CB  . PRO   A 297 ? 1.90878 1.80067 1.14645 -0.23953 0.18151  0.12948  294 PRO   A CB  
2410 C CG  . PRO   A 297 ? 1.84769 1.79109 1.13147 -0.26109 0.21183  0.11863  294 PRO   A CG  
2411 C CD  . PRO   A 297 ? 1.91701 1.85532 1.23849 -0.25897 0.20031  0.12598  294 PRO   A CD  
2412 N N   . HIS   A 298 ? 1.86804 1.79079 1.19977 -0.16463 0.10885  0.11801  295 HIS   A N   
2413 C CA  . HIS   A 298 ? 1.85875 1.81930 1.23692 -0.14165 0.09358  0.10409  295 HIS   A CA  
2414 C C   . HIS   A 298 ? 1.78601 1.74316 1.12527 -0.13820 0.09543  0.09655  295 HIS   A C   
2415 O O   . HIS   A 298 ? 1.93101 1.83976 1.20831 -0.13600 0.08306  0.10609  295 HIS   A O   
2416 C CB  . HIS   A 298 ? 1.94325 1.88698 1.34077 -0.11900 0.05973  0.10967  295 HIS   A CB  
2417 C CG  . HIS   A 298 ? 1.92974 1.89003 1.37937 -0.11784 0.05739  0.11183  295 HIS   A CG  
2418 N ND1 . HIS   A 298 ? 1.96118 1.95650 1.44759 -0.13249 0.08082  0.10653  295 HIS   A ND1 
2419 C CD2 . HIS   A 298 ? 1.99198 1.93983 1.46298 -0.10329 0.03426  0.11736  295 HIS   A CD2 
2420 C CE1 . HIS   A 298 ? 1.93922 1.93972 1.46410 -0.12736 0.07202  0.10971  295 HIS   A CE1 
2421 N NE2 . HIS   A 298 ? 1.97216 1.94497 1.48884 -0.10984 0.04484  0.11607  295 HIS   A NE2 
2422 N N   . LEU   A 299 ? 1.74155 1.74790 1.11516 -0.13644 0.10948  0.07879  296 LEU   A N   
2423 C CA  . LEU   A 299 ? 1.76073 1.76865 1.10369 -0.13056 0.11061  0.06845  296 LEU   A CA  
2424 C C   . LEU   A 299 ? 1.91762 1.91122 1.26410 -0.10587 0.07642  0.06751  296 LEU   A C   
2425 O O   . LEU   A 299 ? 1.89300 1.91361 1.29679 -0.09148 0.06183  0.06109  296 LEU   A O   
2426 C CB  . LEU   A 299 ? 1.57754 1.64310 0.96174 -0.13223 0.13251  0.04766  296 LEU   A CB  
2427 C CG  . LEU   A 299 ? 1.69784 1.77253 1.06104 -0.12257 0.13309  0.03266  296 LEU   A CG  
2428 C CD1 . LEU   A 299 ? 1.62781 1.66984 0.91417 -0.13850 0.14940  0.03756  296 LEU   A CD1 
2429 C CD2 . LEU   A 299 ? 1.50810 1.64156 0.92372 -0.11862 0.14925  0.01054  296 LEU   A CD2 
2430 N N   . ARG   A 300 ? 2.26338 2.21400 1.54736 -0.10203 0.06354  0.07349  297 ARG   A N   
2431 C CA  . ARG   A 300 ? 2.28581 2.22202 1.56954 -0.07966 0.02976  0.07152  297 ARG   A CA  
2432 C C   . ARG   A 300 ? 2.26466 2.22934 1.55950 -0.07024 0.03046  0.05273  297 ARG   A C   
2433 O O   . ARG   A 300 ? 2.25865 2.19986 1.50905 -0.06291 0.01834  0.04972  297 ARG   A O   
2434 C CB  . ARG   A 300 ? 2.32490 2.19953 1.53565 -0.07765 0.01168  0.08583  297 ARG   A CB  
2435 C CG  . ARG   A 300 ? 2.34617 2.18231 1.52305 -0.09261 0.01913  0.10434  297 ARG   A CG  
2436 C CD  . ARG   A 300 ? 2.43220 2.27887 1.66428 -0.08613 0.00703  0.10989  297 ARG   A CD  
2437 N NE  . ARG   A 300 ? 2.56873 2.38966 1.79989 -0.06447 -0.03027 0.11448  297 ARG   A NE  
2438 C CZ  . ARG   A 300 ? 2.56733 2.41925 1.85301 -0.04592 -0.05111 0.10403  297 ARG   A CZ  
2439 N NH1 . ARG   A 300 ? 2.46657 2.37007 1.80790 -0.04552 -0.04012 0.08989  297 ARG   A NH1 
2440 N NH2 . ARG   A 300 ? 2.60038 2.43032 1.88404 -0.02757 -0.08417 0.10716  297 ARG   A NH2 
2441 N N   . LEU   A 301 ? 2.00806 2.02177 1.36165 -0.06969 0.04367  0.03947  298 LEU   A N   
2442 C CA  . LEU   A 301 ? 2.01831 2.05994 1.38647 -0.06034 0.04571  0.02012  298 LEU   A CA  
2443 C C   . LEU   A 301 ? 1.99546 2.08058 1.43720 -0.05278 0.04491  0.00928  298 LEU   A C   
2444 O O   . LEU   A 301 ? 2.03303 2.12279 1.50224 -0.03835 0.02273  0.00342  298 LEU   A O   
2445 C CB  . LEU   A 301 ? 1.93910 1.99041 1.27167 -0.07317 0.07623  0.01123  298 LEU   A CB  
2446 C CG  . LEU   A 301 ? 1.91489 1.99842 1.26311 -0.06314 0.08237  -0.01156 298 LEU   A CG  
2447 C CD1 . LEU   A 301 ? 1.99813 2.05795 1.32271 -0.04630 0.05470  -0.01641 298 LEU   A CD1 
2448 C CD2 . LEU   A 301 ? 1.83310 1.93115 1.14906 -0.07743 0.11599  -0.02113 298 LEU   A CD2 
2449 N N   . GLY   B 9   ? 1.25620 1.52396 0.98330 0.05403  0.01633  -0.13908 102 GLY   B N   
2450 C CA  . GLY   B 9   ? 1.37188 1.61651 1.08828 0.04149  0.00659  -0.11798 102 GLY   B CA  
2451 C C   . GLY   B 9   ? 1.33750 1.57938 1.08856 0.03615  -0.00276 -0.10437 102 GLY   B C   
2452 O O   . GLY   B 9   ? 1.28186 1.53384 1.06163 0.04244  -0.00443 -0.11058 102 GLY   B O   
2453 N N   . SER   B 10  ? 1.33759 1.56499 1.08433 0.02545  -0.00952 -0.08660 103 SER   B N   
2454 C CA  . SER   B 10  ? 1.25831 1.48394 1.03587 0.01927  -0.01709 -0.07363 103 SER   B CA  
2455 C C   . SER   B 10  ? 1.29620 1.49797 1.06960 0.01760  -0.03891 -0.06744 103 SER   B C   
2456 O O   . SER   B 10  ? 1.33312 1.52293 1.08260 0.01423  -0.04405 -0.06101 103 SER   B O   
2457 C CB  . SER   B 10  ? 1.34406 1.58096 1.12746 0.00750  -0.00263 -0.05915 103 SER   B CB  
2458 O OG  . SER   B 10  ? 1.27200 1.50735 1.08395 0.00245  -0.00980 -0.04780 103 SER   B OG  
2459 N N   . PRO   B 11  ? 1.25957 1.45323 1.05408 0.01919  -0.05255 -0.06969 104 PRO   B N   
2460 C CA  . PRO   B 11  ? 1.19682 1.37242 0.99181 0.01503  -0.07227 -0.06579 104 PRO   B CA  
2461 C C   . PRO   B 11  ? 1.19106 1.37143 1.01057 0.00491  -0.07505 -0.05131 104 PRO   B C   
2462 O O   . PRO   B 11  ? 1.22332 1.39477 1.04914 0.00054  -0.09057 -0.04956 104 PRO   B O   
2463 C CB  . PRO   B 11  ? 1.13032 1.29294 0.93275 0.01988  -0.08324 -0.07696 104 PRO   B CB  
2464 C CG  . PRO   B 11  ? 1.22670 1.40274 1.04822 0.02345  -0.07104 -0.07860 104 PRO   B CG  
2465 C CD  . PRO   B 11  ? 1.19579 1.39415 1.01037 0.02547  -0.05148 -0.07838 104 PRO   B CD  
2466 N N   . LEU   B 12  ? 1.20223 1.39785 1.03686 0.00101  -0.06068 -0.04249 105 LEU   B N   
2467 C CA  . LEU   B 12  ? 1.18333 1.38368 1.04113 -0.00708 -0.06284 -0.03027 105 LEU   B CA  
2468 C C   . LEU   B 12  ? 1.19066 1.38593 1.03314 -0.00871 -0.06852 -0.02232 105 LEU   B C   
2469 O O   . LEU   B 12  ? 1.25462 1.44574 1.06845 -0.00645 -0.06183 -0.02116 105 LEU   B O   
2470 C CB  . LEU   B 12  ? 1.17158 1.38722 1.04802 -0.01012 -0.04679 -0.02430 105 LEU   B CB  
2471 C CG  . LEU   B 12  ? 0.98063 1.20056 0.87504 -0.00770 -0.04365 -0.03067 105 LEU   B CG  
2472 C CD1 . LEU   B 12  ? 0.90967 1.14660 0.81913 -0.00999 -0.02808 -0.02599 105 LEU   B CD1 
2473 C CD2 . LEU   B 12  ? 1.10287 1.31271 1.01453 -0.01269 -0.05603 -0.02922 105 LEU   B CD2 
2474 N N   . PRO   B 13  ? 1.16180 1.35682 1.02152 -0.01246 -0.08108 -0.01752 106 PRO   B N   
2475 C CA  . PRO   B 13  ? 1.21230 1.40179 1.05887 -0.01110 -0.08934 -0.01066 106 PRO   B CA  
2476 C C   . PRO   B 13  ? 1.21171 1.40494 1.05904 -0.01331 -0.07669 0.00091  106 PRO   B C   
2477 O O   . PRO   B 13  ? 1.25016 1.45285 1.10844 -0.01671 -0.06058 0.00287  106 PRO   B O   
2478 C CB  . PRO   B 13  ? 1.35283 1.54751 1.22628 -0.01390 -0.10636 -0.01265 106 PRO   B CB  
2479 C CG  . PRO   B 13  ? 1.31110 1.51639 1.21571 -0.02075 -0.09889 -0.01372 106 PRO   B CG  
2480 C CD  . PRO   B 13  ? 1.24371 1.44342 1.13467 -0.01820 -0.08854 -0.01927 106 PRO   B CD  
2481 N N   . VAL   B 14  ? 1.27111 1.45511 1.10583 -0.01088 -0.08539 0.00797  107 VAL   B N   
2482 C CA  . VAL   B 14  ? 1.22125 1.40297 1.05396 -0.01313 -0.07560 0.01917  107 VAL   B CA  
2483 C C   . VAL   B 14  ? 1.18971 1.38879 1.06446 -0.01703 -0.07178 0.02134  107 VAL   B C   
2484 O O   . VAL   B 14  ? 1.13184 1.34021 1.03309 -0.01633 -0.08395 0.01798  107 VAL   B O   
2485 C CB  . VAL   B 14  ? 1.19265 1.35476 0.99934 -0.00733 -0.08977 0.02556  107 VAL   B CB  
2486 C CG1 . VAL   B 14  ? 1.24363 1.38371 0.99896 -0.00614 -0.08714 0.02655  107 VAL   B CG1 
2487 C CG2 . VAL   B 14  ? 1.31459 1.48184 1.13999 -0.00118 -0.11320 0.01931  107 VAL   B CG2 
2488 N N   . LEU   B 15  ? 1.11634 1.32129 0.99739 -0.02211 -0.05423 0.02590  108 LEU   B N   
2489 C CA  . LEU   B 15  ? 1.15095 1.37033 1.06705 -0.02603 -0.04880 0.02792  108 LEU   B CA  
2490 C C   . LEU   B 15  ? 1.12498 1.33823 1.04055 -0.02588 -0.04754 0.03743  108 LEU   B C   
2491 O O   . LEU   B 15  ? 1.20795 1.40811 1.09773 -0.02792 -0.03904 0.04389  108 LEU   B O   
2492 C CB  . LEU   B 15  ? 1.11770 1.34743 1.04263 -0.03045 -0.03277 0.02507  108 LEU   B CB  
2493 C CG  . LEU   B 15  ? 1.17223 1.40408 1.09375 -0.02823 -0.03409 0.01466  108 LEU   B CG  
2494 C CD1 . LEU   B 15  ? 1.03106 1.27388 0.96350 -0.02969 -0.02065 0.01084  108 LEU   B CD1 
2495 C CD2 . LEU   B 15  ? 1.13855 1.37030 1.07657 -0.02813 -0.04861 0.00961  108 LEU   B CD2 
2496 N N   . SER   B 16  ? 1.08250 1.30441 1.02546 -0.02408 -0.05567 0.03747  109 SER   B N   
2497 C CA  . SER   B 16  ? 1.15436 1.36930 1.09815 -0.02148 -0.05648 0.04476  109 SER   B CA  
2498 C C   . SER   B 16  ? 1.17748 1.39558 1.12881 -0.02839 -0.03904 0.04960  109 SER   B C   
2499 O O   . SER   B 16  ? 1.20147 1.40565 1.14016 -0.02835 -0.03603 0.05692  109 SER   B O   
2500 C CB  . SER   B 16  ? 1.15579 1.38417 1.13018 -0.01634 -0.06970 0.04038  109 SER   B CB  
2501 O OG  . SER   B 16  ? 1.19334 1.44276 1.20113 -0.02303 -0.06238 0.03565  109 SER   B OG  
2502 N N   . TRP   B 17  ? 1.10319 1.33657 1.07266 -0.03410 -0.02891 0.04529  110 TRP   B N   
2503 C CA  . TRP   B 17  ? 1.01618 1.25556 0.99737 -0.03989 -0.01488 0.04801  110 TRP   B CA  
2504 C C   . TRP   B 17  ? 1.02070 1.25732 0.98301 -0.04524 -0.00109 0.04914  110 TRP   B C   
2505 O O   . TRP   B 17  ? 1.09642 1.33669 1.06548 -0.05068 0.00988  0.05156  110 TRP   B O   
2506 C CB  . TRP   B 17  ? 0.94122 1.19676 0.95100 -0.04260 -0.01280 0.04252  110 TRP   B CB  
2507 C CG  . TRP   B 17  ? 1.02525 1.28428 1.03600 -0.04201 -0.01875 0.03522  110 TRP   B CG  
2508 C CD1 . TRP   B 17  ? 1.06985 1.32958 1.08517 -0.04003 -0.03160 0.03117  110 TRP   B CD1 
2509 C CD2 . TRP   B 17  ? 0.99311 1.25437 1.00053 -0.04309 -0.01333 0.02987  110 TRP   B CD2 
2510 N NE1 . TRP   B 17  ? 0.97216 1.23086 0.98436 -0.04122 -0.03406 0.02461  110 TRP   B NE1 
2511 C CE2 . TRP   B 17  ? 0.96423 1.22277 0.97082 -0.04179 -0.02350 0.02363  110 TRP   B CE2 
2512 C CE3 . TRP   B 17  ? 0.88335 1.14930 0.88936 -0.04428 -0.00203 0.02838  110 TRP   B CE3 
2513 C CZ2 . TRP   B 17  ? 0.89456 1.15038 0.89568 -0.04044 -0.02327 0.01662  110 TRP   B CZ2 
2514 C CZ3 . TRP   B 17  ? 0.86074 1.12834 0.86452 -0.04152 -0.00223 0.02032  110 TRP   B CZ3 
2515 C CH2 . TRP   B 17  ? 0.83590 1.09625 0.83566 -0.03904 -0.01303 0.01486  110 TRP   B CH2 
2516 N N   . ALA   B 18  ? 1.08182 1.31396 1.02157 -0.04433 -0.00096 0.04618  111 ALA   B N   
2517 C CA  . ALA   B 18  ? 1.12755 1.36184 1.05057 -0.05023 0.01390  0.04502  111 ALA   B CA  
2518 C C   . ALA   B 18  ? 1.24500 1.46969 1.13708 -0.04781 0.01131  0.04239  111 ALA   B C   
2519 O O   . ALA   B 18  ? 1.24104 1.45919 1.12833 -0.04096 -0.00306 0.04017  111 ALA   B O   
2520 C CB  . ALA   B 18  ? 1.10774 1.36323 1.05336 -0.05152 0.02264  0.03665  111 ALA   B CB  
2521 N N   . ASN   B 19  ? 1.34832 1.57331 1.21925 -0.05454 0.02593  0.04173  112 ASN   B N   
2522 C CA  . ASN   B 19  ? 1.42850 1.64655 1.26790 -0.05316 0.02693  0.03751  112 ASN   B CA  
2523 C C   . ASN   B 19  ? 1.44458 1.67762 1.29832 -0.04493 0.02170  0.02475  112 ASN   B C   
2524 O O   . ASN   B 19  ? 1.39555 1.64891 1.27295 -0.04438 0.02894  0.01671  112 ASN   B O   
2525 C CB  . ASN   B 19  ? 1.48527 1.70635 1.30312 -0.06459 0.04759  0.03736  112 ASN   B CB  
2526 C CG  . ASN   B 19  ? 1.65213 1.86464 1.43206 -0.06447 0.05101  0.03308  112 ASN   B CG  
2527 O OD1 . ASN   B 19  ? 1.72925 1.92354 1.48932 -0.05657 0.03565  0.03439  112 ASN   B OD1 
2528 N ND2 . ASN   B 19  ? 1.68455 1.91199 1.45469 -0.07353 0.07141  0.02665  112 ASN   B ND2 
2529 N N   . ARG   B 20  ? 1.42461 1.64515 1.26266 -0.03790 0.00731  0.02244  113 ARG   B N   
2530 C CA  . ARG   B 20  ? 1.30287 1.53116 1.15185 -0.03037 -0.00057 0.01068  113 ARG   B CA  
2531 C C   . ARG   B 20  ? 1.32424 1.56749 1.16848 -0.02920 0.01321  -0.00103 113 ARG   B C   
2532 O O   . ARG   B 20  ? 1.16661 1.42158 1.03158 -0.02362 0.01149  -0.01080 113 ARG   B O   
2533 C CB  . ARG   B 20  ? 1.35537 1.56643 1.18356 -0.02457 -0.01792 0.00949  113 ARG   B CB  
2534 C CG  . ARG   B 20  ? 1.37359 1.56599 1.15873 -0.02603 -0.01634 0.01479  113 ARG   B CG  
2535 C CD  . ARG   B 20  ? 1.38710 1.56346 1.15098 -0.01871 -0.03529 0.01103  113 ARG   B CD  
2536 N NE  . ARG   B 20  ? 1.41843 1.60130 1.18190 -0.01371 -0.03667 -0.00275 113 ARG   B NE  
2537 C CZ  . ARG   B 20  ? 1.52481 1.70639 1.25939 -0.01250 -0.02661 -0.01027 113 ARG   B CZ  
2538 N NH1 . ARG   B 20  ? 1.59813 1.77256 1.30025 -0.01842 -0.01266 -0.00480 113 ARG   B NH1 
2539 N NH2 . ARG   B 20  ? 1.51820 1.70441 1.25473 -0.00576 -0.03017 -0.02417 113 ARG   B NH2 
2540 N N   . GLU   B 21  ? 1.60339 1.84585 1.41930 -0.03431 0.02692  -0.00105 114 GLU   B N   
2541 C CA  . GLU   B 21  ? 1.59002 1.85322 1.40496 -0.03347 0.04231  -0.01453 114 GLU   B CA  
2542 C C   . GLU   B 21  ? 1.47627 1.76484 1.32325 -0.03780 0.05539  -0.01753 114 GLU   B C   
2543 O O   . GLU   B 21  ? 1.40646 1.71771 1.26725 -0.03241 0.06256  -0.03214 114 GLU   B O   
2544 C CB  . GLU   B 21  ? 1.61352 1.87010 1.38742 -0.04058 0.05582  -0.01413 114 GLU   B CB  
2545 C CG  . GLU   B 21  ? 1.74458 1.97746 1.48249 -0.03429 0.04291  -0.01491 114 GLU   B CG  
2546 C CD  . GLU   B 21  ? 1.80184 2.04360 1.54376 -0.02185 0.03698  -0.03209 114 GLU   B CD  
2547 O OE1 . GLU   B 21  ? 1.73086 1.99797 1.49650 -0.01796 0.04652  -0.04473 114 GLU   B OE1 
2548 O OE2 . GLU   B 21  ? 1.83853 2.06079 1.55934 -0.01512 0.02132  -0.03385 114 GLU   B OE2 
2549 N N   . GLU   B 22  ? 1.35219 1.63742 1.21140 -0.04608 0.05725  -0.00540 115 GLU   B N   
2550 C CA  . GLU   B 22  ? 1.23592 1.54414 1.12509 -0.05052 0.06799  -0.00845 115 GLU   B CA  
2551 C C   . GLU   B 22  ? 1.10321 1.41952 1.02398 -0.03989 0.05624  -0.01496 115 GLU   B C   
2552 O O   . GLU   B 22  ? 1.02659 1.36539 0.96823 -0.03616 0.06185  -0.02621 115 GLU   B O   
2553 C CB  . GLU   B 22  ? 1.29923 1.59708 1.18823 -0.06243 0.07242  0.00617  115 GLU   B CB  
2554 C CG  . GLU   B 22  ? 1.25244 1.57318 1.16768 -0.06991 0.08511  0.00298  115 GLU   B CG  
2555 C CD  . GLU   B 22  ? 1.28880 1.59444 1.20164 -0.08117 0.08765  0.01715  115 GLU   B CD  
2556 O OE1 . GLU   B 22  ? 1.23666 1.51629 1.13720 -0.07874 0.07549  0.02854  115 GLU   B OE1 
2557 O OE2 . GLU   B 22  ? 1.23003 1.55032 1.15405 -0.09197 0.10103  0.01564  115 GLU   B OE2 
2558 N N   . VAL   B 23  ? 0.97126 1.26902 0.89487 -0.03531 0.03958  -0.00865 116 VAL   B N   
2559 C CA  . VAL   B 23  ? 0.96510 1.26404 0.91180 -0.02784 0.02869  -0.01345 116 VAL   B CA  
2560 C C   . VAL   B 23  ? 0.97916 1.28227 0.92233 -0.01655 0.02452  -0.02875 116 VAL   B C   
2561 O O   . VAL   B 23  ? 0.79253 1.10422 0.75271 -0.00953 0.02226  -0.03753 116 VAL   B O   
2562 C CB  . VAL   B 23  ? 0.88767 1.16769 0.83707 -0.02862 0.01401  -0.00422 116 VAL   B CB  
2563 C CG1 . VAL   B 23  ? 0.86384 1.14056 0.83088 -0.02404 0.00418  -0.00862 116 VAL   B CG1 
2564 C CG2 . VAL   B 23  ? 0.81068 1.08781 0.76562 -0.03683 0.01745  0.00856  116 VAL   B CG2 
2565 N N   . TRP   B 24  ? 0.99009 1.28491 0.90883 -0.01336 0.02217  -0.03285 117 TRP   B N   
2566 C CA  . TRP   B 24  ? 0.94797 1.24408 0.86059 -0.00131 0.01735  -0.04866 117 TRP   B CA  
2567 C C   . TRP   B 24  ? 0.98215 1.30651 0.90288 0.00300  0.03209  -0.06258 117 TRP   B C   
2568 O O   . TRP   B 24  ? 0.84983 1.18089 0.78067 0.01571  0.02693  -0.07698 117 TRP   B O   
2569 C CB  . TRP   B 24  ? 1.03665 1.31663 0.91893 0.00055  0.01141  -0.05005 117 TRP   B CB  
2570 C CG  . TRP   B 24  ? 0.97378 1.24991 0.84673 0.01357  0.00415  -0.06656 117 TRP   B CG  
2571 C CD1 . TRP   B 24  ? 1.17738 1.46531 1.03404 0.02001  0.01353  -0.08045 117 TRP   B CD1 
2572 C CD2 . TRP   B 24  ? 0.94619 1.20340 0.82341 0.02132  -0.01386 -0.07169 117 TRP   B CD2 
2573 N NE1 . TRP   B 24  ? 1.08341 1.36069 0.93471 0.03362  0.00114  -0.09461 117 TRP   B NE1 
2574 C CE2 . TRP   B 24  ? 1.04301 1.29898 0.90540 0.03402  -0.01625 -0.08889 117 TRP   B CE2 
2575 C CE3 . TRP   B 24  ? 0.92897 1.16915 0.81940 0.01757  -0.02734 -0.06388 117 TRP   B CE3 
2576 C CZ2 . TRP   B 24  ? 1.03552 1.26941 0.89412 0.04354  -0.03343 -0.09773 117 TRP   B CZ2 
2577 C CZ3 . TRP   B 24  ? 1.00216 1.22135 0.88821 0.02445  -0.04269 -0.07197 117 TRP   B CZ3 
2578 C CH2 . TRP   B 24  ? 0.90739 1.12141 0.77680 0.03756  -0.04652 -0.08836 117 TRP   B CH2 
2579 N N   . LYS   B 25  ? 1.08023 1.42108 0.99652 -0.00761 0.05006  -0.05943 118 LYS   B N   
2580 C CA  . LYS   B 25  ? 0.95035 1.32470 0.87885 -0.00643 0.06635  -0.07410 118 LYS   B CA  
2581 C C   . LYS   B 25  ? 0.86058 1.25170 0.82392 -0.00112 0.06324  -0.07960 118 LYS   B C   
2582 O O   . LYS   B 25  ? 0.84609 1.25956 0.82471 0.01086  0.06416  -0.09779 118 LYS   B O   
2583 C CB  . LYS   B 25  ? 1.01203 1.39700 0.92751 -0.02382 0.08698  -0.06730 118 LYS   B CB  
2584 C CG  . LYS   B 25  ? 1.20950 1.61596 1.10914 -0.02504 0.10442  -0.08195 118 LYS   B CG  
2585 C CD  . LYS   B 25  ? 1.26318 1.64472 1.12362 -0.02173 0.09904  -0.08052 118 LYS   B CD  
2586 C CE  . LYS   B 25  ? 1.33897 1.74034 1.17801 -0.02596 0.11962  -0.09373 118 LYS   B CE  
2587 N NZ  . LYS   B 25  ? 1.29979 1.67322 1.09460 -0.02404 0.11449  -0.09105 118 LYS   B NZ  
2588 N N   . ILE   B 26  ? 0.76906 1.14929 0.74434 -0.00858 0.05850  -0.06511 119 ILE   B N   
2589 C CA  . ILE   B 26  ? 0.85754 1.24941 0.86155 -0.00417 0.05431  -0.06893 119 ILE   B CA  
2590 C C   . ILE   B 26  ? 0.76793 1.14713 0.77570 0.01323  0.03631  -0.07860 119 ILE   B C   
2591 O O   . ILE   B 26  ? 0.76428 1.15932 0.78998 0.02444  0.03300  -0.09208 119 ILE   B O   
2592 C CB  . ILE   B 26  ? 0.86675 1.24515 0.87754 -0.01576 0.05264  -0.05108 119 ILE   B CB  
2593 C CG1 . ILE   B 26  ? 0.86647 1.25499 0.87275 -0.03230 0.06986  -0.04313 119 ILE   B CG1 
2594 C CG2 . ILE   B 26  ? 0.74133 1.12473 0.77612 -0.01016 0.04522  -0.05426 119 ILE   B CG2 
2595 C CD1 . ILE   B 26  ? 0.87967 1.24840 0.88478 -0.04234 0.06701  -0.02517 119 ILE   B CD1 
2596 N N   . MET   B 27  ? 0.67872 1.02756 0.66851 0.01569  0.02328  -0.07252 120 MET   B N   
2597 C CA  . MET   B 27  ? 0.80571 1.13497 0.79302 0.02981  0.00576  -0.08067 120 MET   B CA  
2598 C C   . MET   B 27  ? 0.79556 1.13886 0.78012 0.04613  0.00559  -0.10195 120 MET   B C   
2599 O O   . MET   B 27  ? 0.74344 1.08303 0.73516 0.06126  -0.00584 -0.11388 120 MET   B O   
2600 C CB  . MET   B 27  ? 0.82695 1.12308 0.79575 0.02563  -0.00648 -0.07075 120 MET   B CB  
2601 C CG  . MET   B 27  ? 0.76777 1.05239 0.74268 0.01176  -0.00773 -0.05268 120 MET   B CG  
2602 S SD  . MET   B 27  ? 0.84274 1.09775 0.80181 0.00565  -0.02108 -0.04427 120 MET   B SD  
2603 C CE  . MET   B 27  ? 0.95269 1.18120 0.90500 0.01573  -0.03804 -0.05411 120 MET   B CE  
2604 N N   . LEU   B 28  ? 0.75591 1.11399 0.72799 0.04411  0.01775  -0.10769 121 LEU   B N   
2605 C CA  . LEU   B 28  ? 0.85235 1.22928 0.82320 0.05965  0.02043  -0.13016 121 LEU   B CA  
2606 C C   . LEU   B 28  ? 0.81047 1.22925 0.81006 0.06377  0.03200  -0.14395 121 LEU   B C   
2607 O O   . LEU   B 28  ? 0.88713 1.31941 0.89824 0.08277  0.02550  -0.16426 121 LEU   B O   
2608 C CB  . LEU   B 28  ? 0.80418 1.18455 0.74994 0.05462  0.03180  -0.13236 121 LEU   B CB  
2609 C CG  . LEU   B 28  ? 0.91970 1.26274 0.83627 0.05282  0.01915  -0.12330 121 LEU   B CG  
2610 C CD1 . LEU   B 28  ? 0.96091 1.30998 0.85047 0.05077  0.03055  -0.12928 121 LEU   B CD1 
2611 C CD2 . LEU   B 28  ? 0.90031 1.21590 0.81320 0.06829  -0.00273 -0.13152 121 LEU   B CD2 
2612 N N   . ASN   B 29  ? 0.84158 1.28104 0.85343 0.04658  0.04803  -0.13435 122 ASN   B N   
2613 C CA  . ASN   B 29  ? 0.99230 1.47502 1.03397 0.04720  0.05996  -0.14802 122 ASN   B CA  
2614 C C   . ASN   B 29  ? 0.92027 1.40170 0.98505 0.06129  0.04310  -0.15397 122 ASN   B C   
2615 O O   . ASN   B 29  ? 0.95228 1.46866 1.04259 0.07223  0.04492  -0.17347 122 ASN   B O   
2616 C CB  . ASN   B 29  ? 1.02694 1.52408 1.07271 0.02310  0.07916  -0.13436 122 ASN   B CB  
2617 C CG  . ASN   B 29  ? 1.17760 1.72540 1.24675 0.01796  0.09905  -0.15138 122 ASN   B CG  
2618 O OD1 . ASN   B 29  ? 1.25305 1.81991 1.31055 0.01043  0.11720  -0.15876 122 ASN   B OD1 
2619 N ND2 . ASN   B 29  ? 0.99530 1.56589 1.09700 0.02100  0.09601  -0.15845 122 ASN   B ND2 
2620 N N   . LYS   B 30  ? 1.00381 1.44582 1.05930 0.06115  0.02645  -0.13835 123 LYS   B N   
2621 C CA  . LYS   B 30  ? 0.99758 1.42977 1.06629 0.07418  0.00908  -0.14250 123 LYS   B CA  
2622 C C   . LYS   B 30  ? 1.03668 1.46125 1.10104 0.09965  -0.00723 -0.16260 123 LYS   B C   
2623 O O   . LYS   B 30  ? 1.05235 1.48885 1.13406 0.11592  -0.01752 -0.17705 123 LYS   B O   
2624 C CB  . LYS   B 30  ? 1.03682 1.42723 1.09222 0.06499  -0.00209 -0.12069 123 LYS   B CB  
2625 C CG  . LYS   B 30  ? 1.02612 1.39271 1.08222 0.07837  -0.02235 -0.12332 123 LYS   B CG  
2626 C CD  . LYS   B 30  ? 1.00893 1.33703 1.05082 0.06591  -0.02958 -0.10222 123 LYS   B CD  
2627 C CE  . LYS   B 30  ? 0.92830 1.27163 0.98402 0.04786  -0.01625 -0.08832 123 LYS   B CE  
2628 N NZ  . LYS   B 30  ? 1.00640 1.31710 1.05177 0.03772  -0.02290 -0.07098 123 LYS   B NZ  
2629 N N   . GLU   B 31  ? 1.07337 1.47664 1.11358 0.10459  -0.01138 -0.16475 124 GLU   B N   
2630 C CA  . GLU   B 31  ? 1.14227 1.53119 1.17372 0.12937  -0.02851 -0.18372 124 GLU   B CA  
2631 C C   . GLU   B 31  ? 1.15716 1.59406 1.21241 0.14673  -0.02190 -0.21147 124 GLU   B C   
2632 O O   . GLU   B 31  ? 1.19896 1.62889 1.25435 0.17187  -0.03880 -0.23048 124 GLU   B O   
2633 C CB  . GLU   B 31  ? 1.26237 1.62129 1.26298 0.12875  -0.03234 -0.18102 124 GLU   B CB  
2634 C CG  . GLU   B 31  ? 1.36220 1.68068 1.34333 0.14919  -0.05655 -0.19120 124 GLU   B CG  
2635 C CD  . GLU   B 31  ? 1.29509 1.56383 1.24688 0.13760  -0.06703 -0.17415 124 GLU   B CD  
2636 O OE1 . GLU   B 31  ? 1.11091 1.36807 1.06316 0.11774  -0.06389 -0.15274 124 GLU   B OE1 
2637 O OE2 . GLU   B 31  ? 1.23724 1.48006 1.16674 0.14823  -0.07842 -0.18347 124 GLU   B OE2 
2638 N N   . LYS   B 32  ? 1.30153 1.78652 1.37641 0.13368  0.00215  -0.21514 125 LYS   B N   
2639 C CA  . LYS   B 32  ? 1.16989 1.70943 1.27459 0.14665  0.01120  -0.24259 125 LYS   B CA  
2640 C C   . LYS   B 32  ? 1.10743 1.66944 1.24491 0.15197  0.00448  -0.24845 125 LYS   B C   
2641 O O   . LYS   B 32  ? 1.16356 1.76322 1.32768 0.17157  0.00107  -0.27498 125 LYS   B O   
2642 C CB  . LYS   B 32  ? 1.20460 1.78568 1.31374 0.12703  0.04177  -0.24473 125 LYS   B CB  
2643 C CG  . LYS   B 32  ? 1.30001 1.86148 1.37441 0.12299  0.04863  -0.24134 125 LYS   B CG  
2644 C CD  . LYS   B 32  ? 1.39420 1.99238 1.46694 0.10230  0.07925  -0.24262 125 LYS   B CD  
2645 C CE  . LYS   B 32  ? 1.46187 2.03773 1.49554 0.09972  0.08436  -0.23987 125 LYS   B CE  
2646 N NZ  . LYS   B 32  ? 1.56864 2.17439 1.59288 0.07859  0.11443  -0.24028 125 LYS   B NZ  
2647 N N   . THR   B 33  ? 1.09932 1.64037 1.23591 0.13598  0.00179  -0.22580 126 THR   B N   
2648 C CA  . THR   B 33  ? 1.01345 1.56924 1.17642 0.14160  -0.00753 -0.23042 126 THR   B CA  
2649 C C   . THR   B 33  ? 0.96329 1.48386 1.11697 0.16886  -0.03811 -0.23847 126 THR   B C   
2650 O O   . THR   B 33  ? 1.00847 1.55244 1.18607 0.18785  -0.04980 -0.25788 126 THR   B O   
2651 C CB  . THR   B 33  ? 0.99609 1.53655 1.15679 0.11672  -0.00119 -0.20414 126 THR   B CB  
2652 O OG1 . THR   B 33  ? 1.01942 1.58810 1.18540 0.09222  0.02566  -0.19713 126 THR   B OG1 
2653 C CG2 . THR   B 33  ? 1.05569 1.60937 1.24096 0.12234  -0.01166 -0.20915 126 THR   B CG2 
2654 N N   . TYR   B 34  ? 1.01321 1.47613 1.13108 0.17074  -0.05223 -0.22428 127 TYR   B N   
2655 C CA  . TYR   B 34  ? 0.95579 1.37335 1.05503 0.19349  -0.08150 -0.22889 127 TYR   B CA  
2656 C C   . TYR   B 34  ? 1.04777 1.46600 1.14023 0.21909  -0.09083 -0.25291 127 TYR   B C   
2657 O O   . TYR   B 34  ? 1.13072 1.52997 1.20049 0.21493  -0.08647 -0.24930 127 TYR   B O   
2658 C CB  . TYR   B 34  ? 0.97994 1.33491 1.04368 0.17930  -0.09057 -0.20210 127 TYR   B CB  
2659 C CG  . TYR   B 34  ? 0.96585 1.31587 1.03478 0.15898  -0.08537 -0.18118 127 TYR   B CG  
2660 C CD1 . TYR   B 34  ? 0.85883 1.23291 0.93879 0.13359  -0.06224 -0.16664 127 TYR   B CD1 
2661 C CD2 . TYR   B 34  ? 0.85863 1.17673 0.91800 0.16591  -0.10431 -0.17641 127 TYR   B CD2 
2662 C CE1 . TYR   B 34  ? 0.92501 1.29381 1.00933 0.11667  -0.05802 -0.14914 127 TYR   B CE1 
2663 C CE2 . TYR   B 34  ? 0.88238 1.19609 0.94494 0.14786  -0.09898 -0.15858 127 TYR   B CE2 
2664 C CZ  . TYR   B 34  ? 0.85816 1.19849 0.93474 0.12378  -0.07574 -0.14562 127 TYR   B CZ  
2665 O OH  . TYR   B 34  ? 0.73353 1.06877 0.81294 0.10738  -0.07093 -0.12939 127 TYR   B OH  
2666 N N   . LEU   B 35  ? 1.01162 1.45175 1.12381 0.24677  -0.10491 -0.27869 128 LEU   B N   
2667 C CA  . LEU   B 35  ? 1.04179 1.48966 1.15279 0.27498  -0.11406 -0.30621 128 LEU   B CA  
2668 C C   . LEU   B 35  ? 1.11027 1.48837 1.18428 0.29719  -0.14674 -0.30657 128 LEU   B C   
2669 O O   . LEU   B 35  ? 1.20127 1.53874 1.26095 0.29921  -0.16579 -0.29470 128 LEU   B O   
2670 C CB  . LEU   B 35  ? 1.07375 1.58852 1.22980 0.29546  -0.11214 -0.33817 128 LEU   B CB  
2671 C CG  . LEU   B 35  ? 1.00330 1.59374 1.19449 0.28036  -0.07871 -0.35037 128 LEU   B CG  
2672 C CD1 . LEU   B 35  ? 1.01706 1.62517 1.22020 0.24518  -0.05702 -0.32676 128 LEU   B CD1 
2673 C CD2 . LEU   B 35  ? 0.87961 1.53357 1.11452 0.30642  -0.08143 -0.38813 128 LEU   B CD2 
2674 N N   . ARG   B 36  ? 1.27469 1.63614 1.32981 0.31310  -0.15296 -0.32043 129 ARG   B N   
2675 C CA  . ARG   B 36  ? 1.33937 1.63500 1.35825 0.33716  -0.18459 -0.32588 129 ARG   B CA  
2676 C C   . ARG   B 36  ? 1.39394 1.71593 1.42747 0.37529  -0.19645 -0.36342 129 ARG   B C   
2677 O O   . ARG   B 36  ? 1.44997 1.83598 1.51368 0.37824  -0.17565 -0.38319 129 ARG   B O   
2678 C CB  . ARG   B 36  ? 1.37196 1.61069 1.34803 0.32157  -0.18553 -0.30765 129 ARG   B CB  
2679 C CG  . ARG   B 36  ? 1.36986 1.55994 1.32173 0.29302  -0.18713 -0.27372 129 ARG   B CG  
2680 C CD  . ARG   B 36  ? 1.39837 1.62908 1.37174 0.26019  -0.15749 -0.25437 129 ARG   B CD  
2681 N NE  . ARG   B 36  ? 1.31368 1.52027 1.28170 0.24063  -0.15926 -0.22971 129 ARG   B NE  
2682 C CZ  . ARG   B 36  ? 1.29538 1.51997 1.27379 0.21158  -0.13865 -0.20886 129 ARG   B CZ  
2683 N NH1 . ARG   B 36  ? 1.30570 1.56749 1.29678 0.19734  -0.11568 -0.20731 129 ARG   B NH1 
2684 N NH2 . ARG   B 36  ? 1.26252 1.46471 1.23563 0.19713  -0.14175 -0.18951 129 ARG   B NH2 
2685 N N   . ASP   B 37  ? 1.28597 1.55677 1.29608 0.40461  -0.23014 -0.37374 130 ASP   B N   
2686 C CA  . ASP   B 37  ? 1.39127 1.67932 1.41272 0.44632  -0.24743 -0.41121 130 ASP   B CA  
2687 C C   . ASP   B 37  ? 1.40349 1.60124 1.37119 0.46639  -0.28121 -0.41049 130 ASP   B C   
2688 O O   . ASP   B 37  ? 1.34508 1.48810 1.28853 0.47584  -0.30816 -0.40210 130 ASP   B O   
2689 C CB  . ASP   B 37  ? 1.25542 1.59119 1.31813 0.46832  -0.25728 -0.43186 130 ASP   B CB  
2690 C CG  . ASP   B 37  ? 1.38566 1.77505 1.48068 0.50640  -0.26256 -0.47542 130 ASP   B CG  
2691 O OD1 . ASP   B 37  ? 1.39235 1.75600 1.46420 0.52569  -0.27152 -0.49028 130 ASP   B OD1 
2692 O OD2 . ASP   B 37  ? 1.26018 1.71929 1.40508 0.51699  -0.25774 -0.49622 130 ASP   B OD2 
2693 N N   . GLN   B 38  ? 1.29029 1.46930 1.23603 0.47199  -0.28001 -0.41921 131 GLN   B N   
2694 C CA  . GLN   B 38  ? 1.38607 1.47525 1.27754 0.48768  -0.31099 -0.41805 131 GLN   B CA  
2695 C C   . GLN   B 38  ? 1.44117 1.50993 1.32841 0.53511  -0.34599 -0.44757 131 GLN   B C   
2696 O O   . GLN   B 38  ? 1.43612 1.42130 1.27372 0.55023  -0.37605 -0.44641 131 GLN   B O   
2697 C CB  . GLN   B 38  ? 1.42237 1.49963 1.29288 0.48285  -0.30143 -0.42269 131 GLN   B CB  
2698 C CG  . GLN   B 38  ? 1.44068 1.57524 1.33786 0.51341  -0.29525 -0.46155 131 GLN   B CG  
2699 C CD  . GLN   B 38  ? 1.42037 1.64257 1.35877 0.49185  -0.25454 -0.46396 131 GLN   B CD  
2700 O OE1 . GLN   B 38  ? 1.40934 1.66382 1.36953 0.46202  -0.23364 -0.44251 131 GLN   B OE1 
2701 N NE2 . GLN   B 38  ? 1.33685 1.59465 1.28254 0.50645  -0.24304 -0.49022 131 GLN   B NE2 
2702 N N   . HIS   B 39  ? 1.41412 1.55547 1.35127 0.55867  -0.34385 -0.47452 132 HIS   B N   
2703 C CA  . HIS   B 39  ? 1.47131 1.60289 1.41139 0.60735  -0.37822 -0.50632 132 HIS   B CA  
2704 C C   . HIS   B 39  ? 1.46028 1.61719 1.42846 0.61454  -0.38881 -0.50673 132 HIS   B C   
2705 O O   . HIS   B 39  ? 1.48226 1.68177 1.48359 0.65009  -0.40393 -0.53928 132 HIS   B O   
2706 C CB  . HIS   B 39  ? 1.50219 1.70274 1.47947 0.63803  -0.37027 -0.54858 132 HIS   B CB  
2707 C CG  . HIS   B 39  ? 1.45398 1.62507 1.39968 0.63759  -0.36485 -0.55290 132 HIS   B CG  
2708 N ND1 . HIS   B 39  ? 1.48403 1.72523 1.45993 0.64071  -0.33984 -0.57637 132 HIS   B ND1 
2709 C CD2 . HIS   B 39  ? 1.55683 1.63552 1.44175 0.63068  -0.38108 -0.53522 132 HIS   B CD2 
2710 C CE1 . HIS   B 39  ? 1.49464 1.68690 1.42946 0.64136  -0.34221 -0.57620 132 HIS   B CE1 
2711 N NE2 . HIS   B 39  ? 1.54042 1.63457 1.42096 0.63413  -0.36740 -0.55100 132 HIS   B NE2 
2712 N N   . PHE   B 40  ? 1.42767 1.56049 1.38323 0.57998  -0.38126 -0.47131 133 PHE   B N   
2713 C CA  . PHE   B 40  ? 1.37989 1.53187 1.35765 0.58543  -0.39215 -0.47045 133 PHE   B CA  
2714 C C   . PHE   B 40  ? 1.42831 1.50665 1.36737 0.62267  -0.43938 -0.47939 133 PHE   B C   
2715 O O   . PHE   B 40  ? 1.43897 1.53988 1.40059 0.64142  -0.45582 -0.49089 133 PHE   B O   
2716 C CB  . PHE   B 40  ? 1.26657 1.40905 1.23758 0.53916  -0.37156 -0.43075 133 PHE   B CB  
2717 C CG  . PHE   B 40  ? 1.27926 1.31841 1.18317 0.52088  -0.38645 -0.39786 133 PHE   B CG  
2718 C CD1 . PHE   B 40  ? 1.30904 1.28207 1.17614 0.53277  -0.41806 -0.38914 133 PHE   B CD1 
2719 C CD2 . PHE   B 40  ? 1.45005 1.45938 1.32737 0.49008  -0.36819 -0.37588 133 PHE   B CD2 
2720 C CE1 . PHE   B 40  ? 1.35710 1.23616 1.16116 0.51257  -0.42896 -0.35925 133 PHE   B CE1 
2721 C CE2 . PHE   B 40  ? 1.41892 1.33886 1.23846 0.47060  -0.37995 -0.34738 133 PHE   B CE2 
2722 C CZ  . PHE   B 40  ? 1.38033 1.23525 1.16286 0.48065  -0.40906 -0.33886 133 PHE   B CZ  
2723 N N   . LEU   B 41  ? 1.42329 1.41140 1.30232 0.63343  -0.46268 -0.47446 134 LEU   B N   
2724 C CA  . LEU   B 41  ? 1.60083 1.50803 1.43413 0.66932  -0.50950 -0.48239 134 LEU   B CA  
2725 C C   . LEU   B 41  ? 1.59995 1.54914 1.45477 0.69944  -0.52578 -0.51927 134 LEU   B C   
2726 O O   . LEU   B 41  ? 1.59150 1.48682 1.40991 0.71876  -0.56095 -0.52528 134 LEU   B O   
2727 C CB  . LEU   B 41  ? 1.56789 1.36399 1.32534 0.66139  -0.52605 -0.46324 134 LEU   B CB  
2728 C CG  . LEU   B 41  ? 1.59111 1.32650 1.30573 0.61366  -0.51527 -0.41797 134 LEU   B CG  
2729 C CD1 . LEU   B 41  ? 1.74575 1.37668 1.38915 0.60449  -0.53047 -0.40256 134 LEU   B CD1 
2730 C CD2 . LEU   B 41  ? 1.63282 1.34130 1.33370 0.61589  -0.53409 -0.40573 134 LEU   B CD2 
2731 N N   . GLU   B 42  ? 1.53359 1.57571 1.44342 0.70182  -0.50085 -0.54362 135 GLU   B N   
2732 C CA  . GLU   B 42  ? 1.50101 1.59751 1.44116 0.72650  -0.51296 -0.57871 135 GLU   B CA  
2733 C C   . GLU   B 42  ? 1.56067 1.70563 1.53715 0.72627  -0.51553 -0.58631 135 GLU   B C   
2734 O O   . GLU   B 42  ? 1.55869 1.72217 1.54525 0.75001  -0.53707 -0.61329 135 GLU   B O   
2735 C CB  . GLU   B 42  ? 1.52153 1.70556 1.51000 0.72409  -0.48220 -0.60055 135 GLU   B CB  
2736 C CG  . GLU   B 42  ? 1.60104 1.73992 1.55369 0.72687  -0.48080 -0.59778 135 GLU   B CG  
2737 C CD  . GLU   B 42  ? 1.57300 1.79771 1.57007 0.72242  -0.44847 -0.61836 135 GLU   B CD  
2738 O OE1 . GLU   B 42  ? 1.56872 1.88701 1.62379 0.71687  -0.42795 -0.63530 135 GLU   B OE1 
2739 O OE2 . GLU   B 42  ? 1.74433 1.94036 1.71565 0.72241  -0.44315 -0.61728 135 GLU   B OE2 
2740 N N   . GLN   B 43  ? 1.44302 1.60851 1.43911 0.70020  -0.49476 -0.56390 136 GLN   B N   
2741 C CA  . GLN   B 43  ? 1.44480 1.64237 1.46703 0.69797  -0.49958 -0.56727 136 GLN   B CA  
2742 C C   . GLN   B 43  ? 1.43366 1.53517 1.39607 0.71224  -0.53962 -0.55641 136 GLN   B C   
2743 O O   . GLN   B 43  ? 1.46527 1.58218 1.44052 0.71890  -0.55218 -0.56601 136 GLN   B O   
2744 C CB  . GLN   B 43  ? 1.37392 1.62140 1.43334 0.66421  -0.46521 -0.54511 136 GLN   B CB  
2745 C CG  . GLN   B 43  ? 1.35687 1.69311 1.46862 0.64493  -0.42274 -0.55241 136 GLN   B CG  
2746 C CD  . GLN   B 43  ? 1.32751 1.70109 1.46678 0.61056  -0.39086 -0.52734 136 GLN   B CD  
2747 O OE1 . GLN   B 43  ? 1.25734 1.70063 1.43594 0.58999  -0.35435 -0.53008 136 GLN   B OE1 
2748 N NE2 . GLN   B 43  ? 1.31538 1.64075 1.43077 0.60287  -0.40482 -0.50208 136 GLN   B NE2 
2749 N N   . HIS   B 44  ? 1.49887 1.49891 1.39344 0.71517  -0.55914 -0.53662 137 HIS   B N   
2750 C CA  . HIS   B 44  ? 1.54214 1.43823 1.36787 0.72510  -0.59634 -0.52399 137 HIS   B CA  
2751 C C   . HIS   B 44  ? 1.68242 1.51357 1.45842 0.75036  -0.62615 -0.53822 137 HIS   B C   
2752 O O   . HIS   B 44  ? 1.74415 1.49638 1.46654 0.74306  -0.63237 -0.51811 137 HIS   B O   
2753 C CB  . HIS   B 44  ? 1.61110 1.43706 1.39393 0.69777  -0.59142 -0.48188 137 HIS   B CB  
2754 C CG  . HIS   B 44  ? 1.53186 1.42823 1.36638 0.67019  -0.55781 -0.46541 137 HIS   B CG  
2755 N ND1 . HIS   B 44  ? 1.43375 1.34852 1.28278 0.66128  -0.55824 -0.45811 137 HIS   B ND1 
2756 C CD2 . HIS   B 44  ? 1.45538 1.40762 1.32880 0.64932  -0.52348 -0.45529 137 HIS   B CD2 
2757 C CE1 . HIS   B 44  ? 1.41731 1.39709 1.31209 0.63515  -0.52635 -0.44355 137 HIS   B CE1 
2758 N NE2 . HIS   B 44  ? 1.45519 1.45912 1.36546 0.62762  -0.50498 -0.44154 137 HIS   B NE2 
2759 N N   . PRO   B 45  ? 1.78718 1.64939 1.57924 0.77957  -0.64575 -0.57303 138 PRO   B N   
2760 C CA  . PRO   B 45  ? 1.78357 1.59602 1.53515 0.80486  -0.67308 -0.58902 138 PRO   B CA  
2761 C C   . PRO   B 45  ? 1.85873 1.53933 1.51897 0.80871  -0.70864 -0.56920 138 PRO   B C   
2762 O O   . PRO   B 45  ? 2.00325 1.62592 1.61950 0.81826  -0.72500 -0.56956 138 PRO   B O   
2763 C CB  . PRO   B 45  ? 1.78517 1.66415 1.57754 0.83464  -0.68773 -0.63040 138 PRO   B CB  
2764 C CG  . PRO   B 45  ? 1.70953 1.69598 1.57888 0.81892  -0.65505 -0.63748 138 PRO   B CG  
2765 C CD  . PRO   B 45  ? 1.69256 1.64373 1.54517 0.78990  -0.64204 -0.60081 138 PRO   B CD  
2766 N N   . LEU   B 46  ? 1.88000 1.50970 1.50803 0.79978  -0.72041 -0.55139 139 LEU   B N   
2767 C CA  . LEU   B 46  ? 2.00568 1.50734 1.54213 0.79966  -0.75260 -0.53202 139 LEU   B CA  
2768 C C   . LEU   B 46  ? 2.05981 1.49099 1.55058 0.76841  -0.73924 -0.49406 139 LEU   B C   
2769 O O   . LEU   B 46  ? 2.15454 1.47872 1.56673 0.76543  -0.76329 -0.47894 139 LEU   B O   
2770 C CB  . LEU   B 46  ? 2.10144 1.57195 1.61680 0.79956  -0.76826 -0.52646 139 LEU   B CB  
2771 C CG  . LEU   B 46  ? 2.25113 1.59411 1.67113 0.80530  -0.80648 -0.51526 139 LEU   B CG  
2772 C CD1 . LEU   B 46  ? 2.26669 1.58169 1.65872 0.83943  -0.84063 -0.54388 139 LEU   B CD1 
2773 C CD2 . LEU   B 46  ? 2.11250 1.43855 1.52101 0.80670  -0.81859 -0.51343 139 LEU   B CD2 
2774 N N   . LEU   B 47  ? 1.97592 1.46372 1.51270 0.74422  -0.70190 -0.47902 140 LEU   B N   
2775 C CA  . LEU   B 47  ? 1.95380 1.38109 1.45304 0.71370  -0.68768 -0.44428 140 LEU   B CA  
2776 C C   . LEU   B 47  ? 2.01357 1.43780 1.51034 0.71763  -0.68225 -0.45167 140 LEU   B C   
2777 O O   . LEU   B 47  ? 1.91348 1.41304 1.45930 0.73829  -0.67607 -0.48126 140 LEU   B O   
2778 C CB  . LEU   B 47  ? 1.82959 1.31639 1.37711 0.68626  -0.65204 -0.42382 140 LEU   B CB  
2779 C CG  . LEU   B 47  ? 1.85695 1.34907 1.40830 0.67709  -0.65352 -0.41175 140 LEU   B CG  
2780 C CD1 . LEU   B 47  ? 1.72237 1.27492 1.31978 0.64841  -0.61929 -0.38927 140 LEU   B CD1 
2781 C CD2 . LEU   B 47  ? 1.91738 1.28729 1.37974 0.66804  -0.68033 -0.38900 140 LEU   B CD2 
2782 N N   . GLN   B 48  ? 2.05547 1.39119 1.49355 0.69520  -0.68343 -0.42435 141 GLN   B N   
2783 C CA  . GLN   B 48  ? 2.02852 1.34772 1.45617 0.69319  -0.67735 -0.42708 141 GLN   B CA  
2784 C C   . GLN   B 48  ? 1.98879 1.30660 1.42495 0.65837  -0.64406 -0.40248 141 GLN   B C   
2785 O O   . GLN   B 48  ? 1.99736 1.29009 1.41984 0.63094  -0.63441 -0.37442 141 GLN   B O   
2786 C CB  . GLN   B 48  ? 2.11044 1.31631 1.45378 0.69677  -0.71157 -0.42008 141 GLN   B CB  
2787 C CG  . GLN   B 48  ? 2.23281 1.42906 1.55928 0.73298  -0.74812 -0.44601 141 GLN   B CG  
2788 C CD  . GLN   B 48  ? 2.17738 1.46966 1.56748 0.76555  -0.74519 -0.48434 141 GLN   B CD  
2789 O OE1 . GLN   B 48  ? 2.17906 1.51506 1.60185 0.76289  -0.72342 -0.49077 141 GLN   B OE1 
2790 N NE2 . GLN   B 48  ? 2.10873 1.43396 1.51558 0.79511  -0.76631 -0.51102 141 GLN   B NE2 
2791 N N   . PRO   B 49  ? 1.98201 1.32962 1.43977 0.65541  -0.62459 -0.41276 142 PRO   B N   
2792 C CA  . PRO   B 49  ? 1.88590 1.25639 1.35565 0.60453  -0.58534 -0.38595 142 PRO   B CA  
2793 C C   . PRO   B 49  ? 1.86897 1.13888 1.27000 0.56496  -0.58944 -0.34997 142 PRO   B C   
2794 O O   . PRO   B 49  ? 1.82823 1.12061 1.24083 0.51890  -0.55887 -0.32211 142 PRO   B O   
2795 C CB  . PRO   B 49  ? 1.82185 1.23288 1.31531 0.61239  -0.57121 -0.40729 142 PRO   B CB  
2796 C CG  . PRO   B 49  ? 1.78010 1.23714 1.30618 0.66607  -0.58967 -0.44819 142 PRO   B CG  
2797 C CD  . PRO   B 49  ? 1.92520 1.32089 1.40869 0.68282  -0.62837 -0.44410 142 PRO   B CD  
2798 N N   . LYS   B 50  ? 1.91992 1.07907 1.24911 0.58086  -0.62612 -0.35036 143 LYS   B N   
2799 C CA  . LYS   B 50  ? 1.93442 0.99602 1.19580 0.53989  -0.62861 -0.31685 143 LYS   B CA  
2800 C C   . LYS   B 50  ? 2.00043 1.04573 1.24729 0.51613  -0.62482 -0.28968 143 LYS   B C   
2801 O O   . LYS   B 50  ? 1.92894 0.94133 1.14961 0.46839  -0.60693 -0.25865 143 LYS   B O   
2802 C CB  . LYS   B 50  ? 2.10858 1.06051 1.29534 0.55845  -0.66741 -0.32187 143 LYS   B CB  
2803 C CG  . LYS   B 50  ? 2.19360 1.03714 1.30438 0.51563  -0.67169 -0.28865 143 LYS   B CG  
2804 C CD  . LYS   B 50  ? 2.21623 0.98553 1.26934 0.51927  -0.69668 -0.28920 143 LYS   B CD  
2805 C CE  . LYS   B 50  ? 2.32061 1.11991 1.39991 0.51649  -0.68173 -0.30273 143 LYS   B CE  
2806 N NZ  . LYS   B 50  ? 2.30675 1.02909 1.32843 0.51683  -0.70515 -0.30062 143 LYS   B NZ  
2807 N N   . MET   B 51  ? 1.94794 1.01837 1.21265 0.54858  -0.64116 -0.30217 144 MET   B N   
2808 C CA  . MET   B 51  ? 1.97841 1.03685 1.23003 0.52812  -0.63790 -0.27820 144 MET   B CA  
2809 C C   . MET   B 51  ? 1.77928 0.91918 1.08266 0.48209  -0.59153 -0.25710 144 MET   B C   
2810 O O   . MET   B 51  ? 1.77698 0.88639 1.05400 0.44538  -0.58004 -0.22788 144 MET   B O   
2811 C CB  . MET   B 51  ? 1.95704 1.04403 1.23015 0.57391  -0.66292 -0.29999 144 MET   B CB  
2812 C CG  . MET   B 51  ? 2.14316 1.18551 1.37693 0.60591  -0.69934 -0.32346 144 MET   B CG  
2813 S SD  . MET   B 51  ? 2.17462 1.27789 1.44447 0.64220  -0.71714 -0.35221 144 MET   B SD  
2814 C CE  . MET   B 51  ? 2.20316 1.25042 1.42322 0.67646  -0.75894 -0.37890 144 MET   B CE  
2815 N N   . ARG   B 52  ? 1.79425 1.03638 1.16916 0.48371  -0.56457 -0.27205 145 ARG   B N   
2816 C CA  . ARG   B 52  ? 1.67889 0.99499 1.10080 0.44177  -0.52201 -0.25300 145 ARG   B CA  
2817 C C   . ARG   B 52  ? 1.66496 0.93328 1.05212 0.39570  -0.50558 -0.22669 145 ARG   B C   
2818 O O   . ARG   B 52  ? 1.68966 0.97257 1.08340 0.35599  -0.48095 -0.20139 145 ARG   B O   
2819 C CB  . ARG   B 52  ? 1.61819 1.04461 1.11575 0.45459  -0.49898 -0.27562 145 ARG   B CB  
2820 C CG  . ARG   B 52  ? 1.55186 1.05227 1.09594 0.41381  -0.45651 -0.25754 145 ARG   B CG  
2821 C CD  . ARG   B 52  ? 1.44786 1.04878 1.05823 0.42698  -0.43528 -0.28030 145 ARG   B CD  
2822 N NE  . ARG   B 52  ? 1.39968 1.06191 1.04726 0.38863  -0.39685 -0.26270 145 ARG   B NE  
2823 C CZ  . ARG   B 52  ? 1.44498 1.10447 1.08732 0.36301  -0.37950 -0.25259 145 ARG   B CZ  
2824 N NH1 . ARG   B 52  ? 1.43280 1.03280 1.03535 0.36879  -0.39525 -0.25784 145 ARG   B NH1 
2825 N NH2 . ARG   B 52  ? 1.31417 1.03003 0.99084 0.33148  -0.34712 -0.23748 145 ARG   B NH2 
2826 N N   . ALA   B 53  ? 1.79121 1.00304 1.14209 0.40065  -0.51953 -0.23375 146 ALA   B N   
2827 C CA  . ALA   B 53  ? 1.71384 0.87841 1.03149 0.35696  -0.50652 -0.21124 146 ALA   B CA  
2828 C C   . ALA   B 53  ? 1.85571 0.93083 1.10927 0.33004  -0.51642 -0.18444 146 ALA   B C   
2829 O O   . ALA   B 53  ? 1.70939 0.78258 0.95884 0.28425  -0.49268 -0.15986 146 ALA   B O   
2830 C CB  . ALA   B 53  ? 1.77935 0.89961 1.07004 0.37079  -0.52253 -0.22734 146 ALA   B CB  
2831 N N   . ILE   B 54  ? 1.93128 0.93140 1.13305 0.35809  -0.55152 -0.18956 147 ILE   B N   
2832 C CA  . ILE   B 54  ? 1.89482 0.80407 1.02815 0.33323  -0.56176 -0.16412 147 ILE   B CA  
2833 C C   . ILE   B 54  ? 1.94775 0.90845 1.10981 0.31003  -0.53779 -0.14582 147 ILE   B C   
2834 O O   . ILE   B 54  ? 1.92802 0.84701 1.05459 0.26926  -0.52545 -0.11945 147 ILE   B O   
2835 C CB  . ILE   B 54  ? 2.06242 0.87808 1.13122 0.37340  -0.60793 -0.17538 147 ILE   B CB  
2836 C CG1 . ILE   B 54  ? 2.11538 0.88324 1.15879 0.39975  -0.63214 -0.19639 147 ILE   B CG1 
2837 C CG2 . ILE   B 54  ? 2.29392 1.00424 1.28088 0.34502  -0.61872 -0.14777 147 ILE   B CG2 
2838 C CD1 . ILE   B 54  ? 2.32997 1.01650 1.31542 0.44252  -0.67834 -0.21047 147 ILE   B CD1 
2839 N N   . LEU   B 55  ? 1.87546 0.92792 1.10200 0.33409  -0.52987 -0.16027 148 LEU   B N   
2840 C CA  . LEU   B 55  ? 1.80564 0.90862 1.06120 0.31396  -0.50798 -0.14478 148 LEU   B CA  
2841 C C   . LEU   B 55  ? 1.72689 0.88749 1.02145 0.26805  -0.46644 -0.12732 148 LEU   B C   
2842 O O   . LEU   B 55  ? 1.74550 0.89186 1.02392 0.23197  -0.44983 -0.10353 148 LEU   B O   
2843 C CB  . LEU   B 55  ? 1.75611 0.94127 1.07090 0.35164  -0.51183 -0.16694 148 LEU   B CB  
2844 C CG  . LEU   B 55  ? 1.74469 0.98836 1.09482 0.33423  -0.49024 -0.15425 148 LEU   B CG  
2845 C CD1 . LEU   B 55  ? 1.66828 0.83321 0.95504 0.32897  -0.50906 -0.13742 148 LEU   B CD1 
2846 C CD2 . LEU   B 55  ? 1.73669 1.07732 1.15810 0.36606  -0.48774 -0.17872 148 LEU   B CD2 
2847 N N   . LEU   B 56  ? 1.70067 0.92664 1.04571 0.26981  -0.44975 -0.13981 149 LEU   B N   
2848 C CA  . LEU   B 56  ? 1.58099 0.86375 0.96471 0.23030  -0.41306 -0.12532 149 LEU   B CA  
2849 C C   . LEU   B 56  ? 1.66817 0.88311 1.00389 0.18949  -0.40777 -0.10428 149 LEU   B C   
2850 O O   . LEU   B 56  ? 1.61529 0.85355 0.96445 0.15136  -0.38160 -0.08518 149 LEU   B O   
2851 C CB  . LEU   B 56  ? 1.48972 0.84628 0.92795 0.24308  -0.40010 -0.14400 149 LEU   B CB  
2852 C CG  . LEU   B 56  ? 1.43378 0.87407 0.92982 0.27582  -0.39683 -0.16501 149 LEU   B CG  
2853 C CD1 . LEU   B 56  ? 1.48821 0.98960 1.02652 0.28520  -0.38363 -0.18276 149 LEU   B CD1 
2854 C CD2 . LEU   B 56  ? 1.39915 0.89771 0.93251 0.25811  -0.37410 -0.15178 149 LEU   B CD2 
2855 N N   . ASP   B 57  ? 1.71946 0.85062 0.99956 0.19654  -0.43246 -0.10870 150 ASP   B N   
2856 C CA  . ASP   B 57  ? 1.74335 0.80477 0.97420 0.15569  -0.42868 -0.08970 150 ASP   B CA  
2857 C C   . ASP   B 57  ? 1.84142 0.85217 1.02849 0.13004  -0.42671 -0.06689 150 ASP   B C   
2858 O O   . ASP   B 57  ? 1.81525 0.81435 0.99113 0.08533  -0.40606 -0.04764 150 ASP   B O   
2859 C CB  . ASP   B 57  ? 1.88098 0.85661 1.05681 0.17066  -0.45831 -0.10040 150 ASP   B CB  
2860 C CG  . ASP   B 57  ? 2.01011 0.90986 1.13274 0.12618  -0.45519 -0.08184 150 ASP   B CG  
2861 O OD1 . ASP   B 57  ? 2.15083 1.08740 1.30234 0.09594  -0.43281 -0.07757 150 ASP   B OD1 
2862 O OD2 . ASP   B 57  ? 2.04153 0.84400 1.09229 0.12079  -0.47551 -0.07191 150 ASP   B OD2 
2863 N N   . TRP   B 58  ? 1.91349 0.89471 1.07510 0.15795  -0.44819 -0.06989 151 TRP   B N   
2864 C CA  . TRP   B 58  ? 1.88974 0.82685 1.00932 0.13571  -0.44575 -0.04889 151 TRP   B CA  
2865 C C   . TRP   B 58  ? 1.80768 0.82984 0.98268 0.10899  -0.40961 -0.03695 151 TRP   B C   
2866 O O   . TRP   B 58  ? 1.80632 0.80518 0.95665 0.07012  -0.39255 -0.01619 151 TRP   B O   
2867 C CB  . TRP   B 58  ? 2.04354 0.93772 1.12849 0.17625  -0.47890 -0.05734 151 TRP   B CB  
2868 C CG  . TRP   B 58  ? 2.06198 0.92235 1.10923 0.15847  -0.47623 -0.03787 151 TRP   B CG  
2869 C CD1 . TRP   B 58  ? 2.19903 0.97273 1.17414 0.12229  -0.47497 -0.01539 151 TRP   B CD1 
2870 C CD2 . TRP   B 58  ? 2.02013 0.93137 1.09736 0.17526  -0.47434 -0.03993 151 TRP   B CD2 
2871 N NE1 . TRP   B 58  ? 2.27154 1.03888 1.22823 0.11627  -0.47184 -0.00314 151 TRP   B NE1 
2872 C CE2 . TRP   B 58  ? 2.16498 1.01541 1.18386 0.14906  -0.47244 -0.01799 151 TRP   B CE2 
2873 C CE3 . TRP   B 58  ? 1.95187 0.95408 1.09880 0.20817  -0.47339 -0.05870 151 TRP   B CE3 
2874 C CZ2 . TRP   B 58  ? 2.15659 1.03323 1.18411 0.15667  -0.47117 -0.01454 151 TRP   B CZ2 
2875 C CZ3 . TRP   B 58  ? 1.96368 0.99255 1.12130 0.21432  -0.47225 -0.05532 151 TRP   B CZ3 
2876 C CH2 . TRP   B 58  ? 2.01750 0.98330 1.11547 0.18967  -0.47193 -0.03352 151 TRP   B CH2 
2877 N N   . LEU   B 59  ? 1.78465 0.90501 1.03356 0.12874  -0.39703 -0.05052 152 LEU   B N   
2878 C CA  . LEU   B 59  ? 1.61292 0.81354 0.91535 0.10527  -0.36380 -0.04046 152 LEU   B CA  
2879 C C   . LEU   B 59  ? 1.62696 0.84779 0.94598 0.06332  -0.33623 -0.02864 152 LEU   B C   
2880 O O   . LEU   B 59  ? 1.60008 0.85015 0.93492 0.03256  -0.31129 -0.01369 152 LEU   B O   
2881 C CB  . LEU   B 59  ? 1.49897 0.79420 0.87248 0.13518  -0.35774 -0.05838 152 LEU   B CB  
2882 C CG  . LEU   B 59  ? 1.54261 0.83626 0.91363 0.17672  -0.38277 -0.07300 152 LEU   B CG  
2883 C CD1 . LEU   B 59  ? 1.45870 0.85167 0.90419 0.20078  -0.37278 -0.09198 152 LEU   B CD1 
2884 C CD2 . LEU   B 59  ? 1.53684 0.80027 0.87664 0.16624  -0.38464 -0.05766 152 LEU   B CD2 
2885 N N   . MET   B 60  ? 1.58426 0.79134 0.90091 0.06253  -0.34115 -0.03656 153 MET   B N   
2886 C CA  . MET   B 60  ? 1.58805 0.80666 0.91553 0.02260  -0.31920 -0.02660 153 MET   B CA  
2887 C C   . MET   B 60  ? 1.59001 0.73962 0.86242 -0.01671 -0.31469 -0.00653 153 MET   B C   
2888 O O   . MET   B 60  ? 1.62733 0.80884 0.91988 -0.05289 -0.28813 0.00607  153 MET   B O   
2889 C CB  . MET   B 60  ? 1.65024 0.85418 0.97547 0.03078  -0.33035 -0.03997 153 MET   B CB  
2890 C CG  . MET   B 60  ? 1.60406 0.88133 0.98481 0.06300  -0.32919 -0.05984 153 MET   B CG  
2891 S SD  . MET   B 60  ? 1.62701 0.88831 1.00322 0.06293  -0.33683 -0.07279 153 MET   B SD  
2892 C CE  . MET   B 60  ? 1.52003 0.85934 0.95051 0.10757  -0.33805 -0.09776 153 MET   B CE  
2893 N N   . GLU   B 61  ? 1.73321 0.78640 0.93398 -0.01018 -0.34060 -0.00411 154 GLU   B N   
2894 C CA  . GLU   B 61  ? 1.89832 0.87697 1.03768 -0.04935 -0.33655 0.01521  154 GLU   B CA  
2895 C C   . GLU   B 61  ? 1.78632 0.78695 0.92882 -0.06390 -0.31894 0.02919  154 GLU   B C   
2896 O O   . GLU   B 61  ? 1.75811 0.75145 0.88836 -0.10650 -0.29667 0.04458  154 GLU   B O   
2897 C CB  . GLU   B 61  ? 2.03056 0.89497 1.08672 -0.03517 -0.37111 0.01455  154 GLU   B CB  
2898 C CG  . GLU   B 61  ? 2.14677 0.92167 1.12977 -0.07911 -0.36794 0.03419  154 GLU   B CG  
2899 C CD  . GLU   B 61  ? 2.29432 0.94986 1.19201 -0.06541 -0.40395 0.03284  154 GLU   B CD  
2900 O OE1 . GLU   B 61  ? 2.34404 0.99077 1.24405 -0.01990 -0.43174 0.01482  154 GLU   B OE1 
2901 O OE2 . GLU   B 61  ? 2.40716 0.97665 1.23416 -0.10031 -0.40437 0.04914  154 GLU   B OE2 
2902 N N   . VAL   B 62  ? 1.72981 0.75956 0.88979 -0.02925 -0.32833 0.02261  155 VAL   B N   
2903 C CA  . VAL   B 62  ? 1.62685 0.68310 0.79390 -0.04018 -0.31218 0.03393  155 VAL   B CA  
2904 C C   . VAL   B 62  ? 1.70093 0.84827 0.93529 -0.06679 -0.27574 0.03817  155 VAL   B C   
2905 O O   . VAL   B 62  ? 1.63115 0.78474 0.86007 -0.09750 -0.25432 0.05203  155 VAL   B O   
2906 C CB  . VAL   B 62  ? 1.77064 0.84726 0.95049 0.00440  -0.33129 0.02274  155 VAL   B CB  
2907 C CG1 . VAL   B 62  ? 1.63857 0.75621 0.83681 -0.00613 -0.31259 0.03228  155 VAL   B CG1 
2908 C CG2 . VAL   B 62  ? 1.90884 0.88766 1.01466 0.02970  -0.36912 0.01986  155 VAL   B CG2 
2909 N N   . CYS   B 63  ? 1.59942 0.81674 0.89577 -0.05491 -0.26863 0.02571  156 CYS   B N   
2910 C CA  . CYS   B 63  ? 1.52142 0.82272 0.88048 -0.07659 -0.23728 0.02870  156 CYS   B CA  
2911 C C   . CYS   B 63  ? 1.55119 0.83408 0.89630 -0.12261 -0.21898 0.04021  156 CYS   B C   
2912 O O   . CYS   B 63  ? 1.49195 0.81869 0.86457 -0.14857 -0.19313 0.04835  156 CYS   B O   
2913 C CB  . CYS   B 63  ? 1.43230 0.80214 0.85112 -0.05374 -0.23618 0.01307  156 CYS   B CB  
2914 S SG  . CYS   B 63  ? 1.38047 0.80774 0.84038 -0.00869 -0.24438 -0.00094 156 CYS   B SG  
2915 N N   . GLU   B 64  ? 1.57029 0.78919 0.87353 -0.13349 -0.23224 0.03973  157 GLU   B N   
2916 C CA  . GLU   B 64  ? 1.66941 0.87353 0.96235 -0.17928 -0.21504 0.04854  157 GLU   B CA  
2917 C C   . GLU   B 64  ? 1.69279 0.84773 0.93584 -0.21130 -0.20443 0.06495  157 GLU   B C   
2918 O O   . GLU   B 64  ? 1.72377 0.90468 0.98217 -0.24976 -0.17851 0.07229  157 GLU   B O   
2919 C CB  . GLU   B 64  ? 1.67369 0.81971 0.93355 -0.18294 -0.23322 0.04268  157 GLU   B CB  
2920 C CG  . GLU   B 64  ? 1.69364 0.83685 0.95462 -0.23008 -0.21559 0.04808  157 GLU   B CG  
2921 C CD  . GLU   B 64  ? 1.88960 0.96887 1.11328 -0.23489 -0.23518 0.04212  157 GLU   B CD  
2922 O OE1 . GLU   B 64  ? 1.89697 0.91677 1.07935 -0.20406 -0.26341 0.03630  157 GLU   B OE1 
2923 O OE2 . GLU   B 64  ? 1.95750 1.04640 1.19390 -0.26881 -0.22332 0.04197  157 GLU   B OE2 
2924 N N   . VAL   B 65  ? 1.75291 0.83682 0.93496 -0.19569 -0.22442 0.06990  158 VAL   B N   
2925 C CA  . VAL   B 65  ? 1.85932 0.88902 0.98480 -0.22537 -0.21531 0.08605  158 VAL   B CA  
2926 C C   . VAL   B 65  ? 1.75508 0.85825 0.92502 -0.23634 -0.18703 0.09095  158 VAL   B C   
2927 O O   . VAL   B 65  ? 1.77153 0.87317 0.92976 -0.27630 -0.16284 0.10139  158 VAL   B O   
2928 C CB  . VAL   B 65  ? 1.83550 0.77468 0.88616 -0.19997 -0.24646 0.08921  158 VAL   B CB  
2929 C CG1 . VAL   B 65  ? 1.99493 0.88116 0.98545 -0.22872 -0.23614 0.10638  158 VAL   B CG1 
2930 C CG2 . VAL   B 65  ? 1.87050 0.72613 0.86883 -0.19355 -0.27406 0.08517  158 VAL   B CG2 
2931 N N   . TYR   B 66  ? 1.70404 0.87299 0.92570 -0.20199 -0.18897 0.08248  159 TYR   B N   
2932 C CA  . TYR   B 66  ? 1.64735 0.88817 0.91489 -0.20839 -0.16415 0.08531  159 TYR   B CA  
2933 C C   . TYR   B 66  ? 1.49407 0.82715 0.84090 -0.21563 -0.14269 0.07820  159 TYR   B C   
2934 O O   . TYR   B 66  ? 1.43904 0.83745 0.83090 -0.21605 -0.12390 0.07833  159 TYR   B O   
2935 C CB  . TYR   B 66  ? 1.58252 0.83827 0.85708 -0.16949 -0.17858 0.08070  159 TYR   B CB  
2936 C CG  . TYR   B 66  ? 1.65793 0.82877 0.85500 -0.16468 -0.19699 0.08907  159 TYR   B CG  
2937 C CD1 . TYR   B 66  ? 1.82767 0.92117 0.97052 -0.14295 -0.22971 0.08588  159 TYR   B CD1 
2938 C CD2 . TYR   B 66  ? 1.62265 0.78768 0.79762 -0.18091 -0.18283 0.09959  159 TYR   B CD2 
2939 C CE1 . TYR   B 66  ? 1.86798 0.87847 0.93526 -0.13694 -0.24935 0.09366  159 TYR   B CE1 
2940 C CE2 . TYR   B 66  ? 1.80202 0.88525 0.90068 -0.17641 -0.20091 0.10768  159 TYR   B CE2 
2941 C CZ  . TYR   B 66  ? 1.85938 0.86435 0.90363 -0.15417 -0.23492 0.10505  159 TYR   B CZ  
2942 O OH  . TYR   B 66  ? 2.02541 0.94395 0.98937 -0.14791 -0.25572 0.11317  159 TYR   B OH  
2943 N N   . LYS   B 67  ? 1.60745 0.94366 0.96922 -0.22035 -0.14677 0.07165  160 LYS   B N   
2944 C CA  . LYS   B 67  ? 1.50554 0.91990 0.93464 -0.23041 -0.12852 0.06532  160 LYS   B CA  
2945 C C   . LYS   B 67  ? 1.34743 0.83855 0.83708 -0.19891 -0.12591 0.05714  160 LYS   B C   
2946 O O   . LYS   B 67  ? 1.26232 0.82131 0.80304 -0.20795 -0.10522 0.05662  160 LYS   B O   
2947 C CB  . LYS   B 67  ? 1.55045 0.98737 0.99029 -0.27314 -0.10006 0.07279  160 LYS   B CB  
2948 C CG  . LYS   B 67  ? 1.64670 1.00788 1.02506 -0.30940 -0.09966 0.08103  160 LYS   B CG  
2949 C CD  . LYS   B 67  ? 1.74699 1.13737 1.13994 -0.35314 -0.06916 0.08599  160 LYS   B CD  
2950 C CE  . LYS   B 67  ? 1.82996 1.14237 1.15847 -0.39252 -0.06751 0.09409  160 LYS   B CE  
2951 N NZ  . LYS   B 67  ? 1.83554 1.18073 1.18047 -0.43773 -0.03569 0.09672  160 LYS   B NZ  
2952 N N   . LEU   B 68  ? 1.41434 0.89386 0.89758 -0.16183 -0.14738 0.04982  161 LEU   B N   
2953 C CA  . LEU   B 68  ? 1.26566 0.81389 0.80287 -0.13284 -0.14574 0.04092  161 LEU   B CA  
2954 C C   . LEU   B 68  ? 1.20136 0.79190 0.77988 -0.12638 -0.14499 0.03083  161 LEU   B C   
2955 O O   . LEU   B 68  ? 1.24479 0.80004 0.80288 -0.13058 -0.15604 0.02705  161 LEU   B O   
2956 C CB  . LEU   B 68  ? 1.26671 0.79093 0.78396 -0.09651 -0.16842 0.03459  161 LEU   B CB  
2957 C CG  . LEU   B 68  ? 1.35918 0.88238 0.86558 -0.09004 -0.16700 0.04010  161 LEU   B CG  
2958 C CD1 . LEU   B 68  ? 1.21680 0.70835 0.68927 -0.12496 -0.15179 0.05494  161 LEU   B CD1 
2959 C CD2 . LEU   B 68  ? 1.24152 0.71611 0.71017 -0.05802 -0.19609 0.03370  161 LEU   B CD2 
2960 N N   . HIS   B 69  ? 1.12167 0.78499 0.75530 -0.11650 -0.13240 0.02653  162 HIS   B N   
2961 C CA  . HIS   B 69  ? 1.17269 0.87865 0.84432 -0.11154 -0.12994 0.01800  162 HIS   B CA  
2962 C C   . HIS   B 69  ? 1.10217 0.79240 0.76476 -0.08094 -0.15061 0.00545  162 HIS   B C   
2963 O O   . HIS   B 69  ? 1.11790 0.78503 0.76100 -0.05729 -0.16511 0.00119  162 HIS   B O   
2964 C CB  . HIS   B 69  ? 0.99642 0.77726 0.72239 -0.10793 -0.11233 0.01744  162 HIS   B CB  
2965 C CG  . HIS   B 69  ? 1.16967 0.97566 0.91364 -0.13669 -0.09185 0.02594  162 HIS   B CG  
2966 N ND1 . HIS   B 69  ? 1.18622 0.98185 0.91640 -0.14931 -0.08224 0.03467  162 HIS   B ND1 
2967 C CD2 . HIS   B 69  ? 1.18319 1.02566 0.95832 -0.15406 -0.07979 0.02540  162 HIS   B CD2 
2968 C CE1 . HIS   B 69  ? 1.16495 0.99177 0.91873 -0.17325 -0.06375 0.03843  162 HIS   B CE1 
2969 N NE2 . HIS   B 69  ? 1.15317 1.00948 0.93576 -0.17601 -0.06274 0.03264  162 HIS   B NE2 
2970 N N   . ARG   B 70  ? 1.20158 0.90590 0.87904 -0.08086 -0.15245 -0.00196 163 ARG   B N   
2971 C CA  . ARG   B 70  ? 1.16604 0.86263 0.83882 -0.05195 -0.16954 -0.01599 163 ARG   B CA  
2972 C C   . ARG   B 70  ? 0.99332 0.74086 0.69893 -0.02407 -0.16684 -0.02390 163 ARG   B C   
2973 O O   . ARG   B 70  ? 1.06268 0.79797 0.75821 0.00393  -0.18223 -0.03545 163 ARG   B O   
2974 C CB  . ARG   B 70  ? 1.03126 0.73969 0.71618 -0.05903 -0.16942 -0.02230 163 ARG   B CB  
2975 C CG  . ARG   B 70  ? 1.08474 0.74829 0.74230 -0.08926 -0.17156 -0.01648 163 ARG   B CG  
2976 C CD  . ARG   B 70  ? 1.17211 0.85000 0.84343 -0.09317 -0.17402 -0.02495 163 ARG   B CD  
2977 N NE  . ARG   B 70  ? 1.17230 0.80855 0.81940 -0.12356 -0.17685 -0.02116 163 ARG   B NE  
2978 C CZ  . ARG   B 70  ? 1.22673 0.79413 0.82729 -0.12466 -0.19488 -0.02434 163 ARG   B CZ  
2979 N NH1 . ARG   B 70  ? 1.23958 0.77132 0.81269 -0.09432 -0.21331 -0.03226 163 ARG   B NH1 
2980 N NH2 . ARG   B 70  ? 1.33929 0.87267 0.92062 -0.15704 -0.19490 -0.02052 163 ARG   B NH2 
2981 N N   . GLU   B 71  ? 0.98232 0.78754 0.72774 -0.03157 -0.14754 -0.01892 164 GLU   B N   
2982 C CA  . GLU   B 71  ? 0.98262 0.83588 0.75874 -0.01005 -0.14273 -0.02532 164 GLU   B CA  
2983 C C   . GLU   B 71  ? 1.01207 0.84349 0.77062 0.00582  -0.15328 -0.02662 164 GLU   B C   
2984 O O   . GLU   B 71  ? 0.96198 0.81448 0.73359 0.03140  -0.15985 -0.03852 164 GLU   B O   
2985 C CB  . GLU   B 71  ? 1.00679 0.91427 0.82108 -0.02440 -0.12117 -0.01746 164 GLU   B CB  
2986 C CG  . GLU   B 71  ? 1.06399 1.01668 0.90700 -0.00834 -0.11409 -0.02138 164 GLU   B CG  
2987 C CD  . GLU   B 71  ? 0.90582 0.89131 0.76812 0.01085  -0.11483 -0.03451 164 GLU   B CD  
2988 O OE1 . GLU   B 71  ? 0.95295 0.93090 0.80910 0.01093  -0.11904 -0.03954 164 GLU   B OE1 
2989 O OE2 . GLU   B 71  ? 0.92972 0.94909 0.81276 0.02467  -0.11056 -0.04044 164 GLU   B OE2 
2990 N N   . THR   B 72  ? 1.07888 0.86834 0.80695 -0.00933 -0.15530 -0.01545 165 THR   B N   
2991 C CA  . THR   B 72  ? 1.05790 0.82119 0.76386 0.00552  -0.16749 -0.01598 165 THR   B CA  
2992 C C   . THR   B 72  ? 1.05145 0.77182 0.72762 0.03239  -0.19344 -0.02867 165 THR   B C   
2993 O O   . THR   B 72  ? 1.00750 0.73566 0.68783 0.05859  -0.20529 -0.03870 165 THR   B O   
2994 C CB  . THR   B 72  ? 1.10188 0.82336 0.77411 -0.01885 -0.16345 -0.00062 165 THR   B CB  
2995 O OG1 . THR   B 72  ? 1.07187 0.83784 0.77535 -0.04094 -0.13942 0.00854  165 THR   B OG1 
2996 C CG2 . THR   B 72  ? 1.04766 0.73931 0.69298 -0.00277 -0.17766 -0.00086 165 THR   B CG2 
2997 N N   . PHE   B 73  ? 1.15819 0.83337 0.80495 0.02704  -0.20361 -0.02983 166 PHE   B N   
2998 C CA  . PHE   B 73  ? 1.18395 0.81418 0.80015 0.05421  -0.22982 -0.04314 166 PHE   B CA  
2999 C C   . PHE   B 73  ? 1.13876 0.82167 0.79313 0.08425  -0.23223 -0.06255 166 PHE   B C   
3000 O O   . PHE   B 73  ? 1.14392 0.82189 0.79442 0.11479  -0.24965 -0.07641 166 PHE   B O   
3001 C CB  . PHE   B 73  ? 1.18308 0.75440 0.76067 0.03981  -0.23898 -0.04066 166 PHE   B CB  
3002 C CG  . PHE   B 73  ? 1.19718 0.73380 0.75280 0.06966  -0.26384 -0.05770 166 PHE   B CG  
3003 C CD1 . PHE   B 73  ? 1.27588 0.75638 0.79084 0.09273  -0.28931 -0.06291 166 PHE   B CD1 
3004 C CD2 . PHE   B 73  ? 1.24386 0.80351 0.81831 0.07663  -0.26291 -0.06968 166 PHE   B CD2 
3005 C CE1 . PHE   B 73  ? 1.36644 0.81534 0.86208 0.12322  -0.31361 -0.08062 166 PHE   B CE1 
3006 C CE2 . PHE   B 73  ? 1.24221 0.77102 0.79661 0.10571  -0.28551 -0.08725 166 PHE   B CE2 
3007 C CZ  . PHE   B 73  ? 1.36362 0.83781 0.87990 0.12968  -0.31098 -0.09323 166 PHE   B CZ  
3008 N N   . TYR   B 74  ? 0.98822 0.72205 0.67875 0.07608  -0.21513 -0.06478 167 TYR   B N   
3009 C CA  . TYR   B 74  ? 1.07966 0.86199 0.80225 0.10112  -0.21469 -0.08312 167 TYR   B CA  
3010 C C   . TYR   B 74  ? 0.98605 0.82425 0.74538 0.11449  -0.20640 -0.08845 167 TYR   B C   
3011 O O   . TYR   B 74  ? 0.99802 0.86850 0.77781 0.14012  -0.21082 -0.10682 167 TYR   B O   
3012 C CB  . TYR   B 74  ? 0.92548 0.74187 0.67033 0.08712  -0.19895 -0.08269 167 TYR   B CB  
3013 C CG  . TYR   B 74  ? 1.02143 0.79266 0.73630 0.08678  -0.21220 -0.08813 167 TYR   B CG  
3014 C CD1 . TYR   B 74  ? 1.10176 0.87157 0.81301 0.11429  -0.22505 -0.10800 167 TYR   B CD1 
3015 C CD2 . TYR   B 74  ? 1.04141 0.77226 0.73205 0.05854  -0.21171 -0.07488 167 TYR   B CD2 
3016 C CE1 . TYR   B 74  ? 1.07157 0.79724 0.75344 0.11460  -0.23822 -0.11389 167 TYR   B CE1 
3017 C CE2 . TYR   B 74  ? 1.07400 0.76189 0.73673 0.05661  -0.22457 -0.08047 167 TYR   B CE2 
3018 C CZ  . TYR   B 74  ? 1.10918 0.79264 0.76632 0.08520  -0.23843 -0.09967 167 TYR   B CZ  
3019 O OH  . TYR   B 74  ? 1.17662 0.81468 0.80414 0.08387  -0.25219 -0.10610 167 TYR   B OH  
3020 N N   . LEU   B 75  ? 0.97539 0.82668 0.74395 0.09718  -0.19414 -0.07412 168 LEU   B N   
3021 C CA  . LEU   B 75  ? 0.93862 0.83121 0.73477 0.11000  -0.19072 -0.07945 168 LEU   B CA  
3022 C C   . LEU   B 75  ? 0.97590 0.83411 0.74866 0.13696  -0.21627 -0.09074 168 LEU   B C   
3023 O O   . LEU   B 75  ? 0.99129 0.88632 0.78955 0.16136  -0.22172 -0.10785 168 LEU   B O   
3024 C CB  . LEU   B 75  ? 0.96350 0.86941 0.76874 0.08577  -0.17408 -0.06183 168 LEU   B CB  
3025 C CG  . LEU   B 75  ? 0.89579 0.85154 0.73558 0.06531  -0.14881 -0.05373 168 LEU   B CG  
3026 C CD1 . LEU   B 75  ? 0.91986 0.87782 0.76159 0.04363  -0.13606 -0.03756 168 LEU   B CD1 
3027 C CD2 . LEU   B 75  ? 0.94566 0.96255 0.82569 0.07920  -0.13969 -0.06651 168 LEU   B CD2 
3028 N N   . ALA   B 76  ? 1.02281 0.80946 0.74585 0.13258  -0.23271 -0.08198 169 ALA   B N   
3029 C CA  . ALA   B 76  ? 1.12958 0.87277 0.82209 0.15957  -0.26087 -0.09190 169 ALA   B CA  
3030 C C   . ALA   B 76  ? 1.07940 0.82194 0.77397 0.19147  -0.27870 -0.11483 169 ALA   B C   
3031 O O   . ALA   B 76  ? 1.16569 0.91723 0.86744 0.22264  -0.29650 -0.13244 169 ALA   B O   
3032 C CB  . ALA   B 76  ? 1.14001 0.79830 0.77069 0.14477  -0.27381 -0.07596 169 ALA   B CB  
3033 N N   . GLN   B 77  ? 1.09726 0.83023 0.78615 0.18507  -0.27501 -0.11650 170 GLN   B N   
3034 C CA  . GLN   B 77  ? 1.10910 0.84483 0.80102 0.21510  -0.28970 -0.13965 170 GLN   B CA  
3035 C C   . GLN   B 77  ? 1.12144 0.94162 0.87007 0.23337  -0.27787 -0.15845 170 GLN   B C   
3036 O O   . GLN   B 77  ? 1.15558 0.98775 0.91332 0.26688  -0.29430 -0.18151 170 GLN   B O   
3037 C CB  . GLN   B 77  ? 1.18450 0.89749 0.86076 0.20097  -0.28535 -0.13686 170 GLN   B CB  
3038 C CG  . GLN   B 77  ? 1.18879 0.91890 0.87579 0.22883  -0.29367 -0.16139 170 GLN   B CG  
3039 C CD  . GLN   B 77  ? 1.09534 0.90581 0.83240 0.22365  -0.26752 -0.16774 170 GLN   B CD  
3040 O OE1 . GLN   B 77  ? 1.09766 0.92985 0.84789 0.19415  -0.24589 -0.15146 170 GLN   B OE1 
3041 N NE2 . GLN   B 77  ? 1.17310 1.02754 0.93700 0.25250  -0.26961 -0.19222 170 GLN   B NE2 
3042 N N   . ASP   B 78  ? 1.06179 0.94104 0.84856 0.21135  -0.24935 -0.14972 171 ASP   B N   
3043 C CA  . ASP   B 78  ? 1.00471 0.96252 0.84247 0.22321  -0.23500 -0.16589 171 ASP   B CA  
3044 C C   . ASP   B 78  ? 1.01621 0.99866 0.87345 0.23934  -0.24276 -0.17444 171 ASP   B C   
3045 O O   . ASP   B 78  ? 0.93713 0.96686 0.82616 0.26317  -0.24525 -0.19755 171 ASP   B O   
3046 C CB  . ASP   B 78  ? 0.97437 0.97924 0.84054 0.19424  -0.20434 -0.15232 171 ASP   B CB  
3047 C CG  . ASP   B 78  ? 0.95006 1.03097 0.86298 0.20228  -0.18738 -0.16783 171 ASP   B CG  
3048 O OD1 . ASP   B 78  ? 1.08822 1.18810 1.00854 0.21756  -0.18723 -0.18567 171 ASP   B OD1 
3049 O OD2 . ASP   B 78  ? 1.03003 1.15069 0.97068 0.19232  -0.17363 -0.16268 171 ASP   B OD2 
3050 N N   . PHE   B 79  ? 0.95092 0.90413 0.79028 0.22618  -0.24631 -0.15732 172 PHE   B N   
3051 C CA  . PHE   B 79  ? 1.02664 0.99626 0.87927 0.24215  -0.25736 -0.16547 172 PHE   B CA  
3052 C C   . PHE   B 79  ? 1.05436 0.99236 0.88772 0.27986  -0.29024 -0.18662 172 PHE   B C   
3053 O O   . PHE   B 79  ? 1.03305 1.01210 0.89669 0.30415  -0.29923 -0.20714 172 PHE   B O   
3054 C CB  . PHE   B 79  ? 0.95472 0.88978 0.78300 0.22057  -0.25606 -0.14248 172 PHE   B CB  
3055 C CG  . PHE   B 79  ? 0.97129 0.94298 0.82346 0.18769  -0.22560 -0.12461 172 PHE   B CG  
3056 C CD1 . PHE   B 79  ? 0.87189 0.90928 0.76853 0.18150  -0.20307 -0.13056 172 PHE   B CD1 
3057 C CD2 . PHE   B 79  ? 0.93348 0.87189 0.76112 0.16337  -0.21979 -0.10248 172 PHE   B CD2 
3058 C CE1 . PHE   B 79  ? 0.81919 0.88462 0.73412 0.15345  -0.17784 -0.11437 172 PHE   B CE1 
3059 C CE2 . PHE   B 79  ? 0.85613 0.82789 0.70630 0.13604  -0.19353 -0.08798 172 PHE   B CE2 
3060 C CZ  . PHE   B 79  ? 0.88248 0.91603 0.77579 0.13199  -0.17379 -0.09376 172 PHE   B CZ  
3061 N N   . PHE   B 80  ? 1.05818 0.92274 0.84128 0.28539  -0.30946 -0.18297 173 PHE   B N   
3062 C CA  . PHE   B 80  ? 1.22086 1.04518 0.97886 0.32307  -0.34384 -0.20276 173 PHE   B CA  
3063 C C   . PHE   B 80  ? 1.17078 1.04948 0.96745 0.35195  -0.34506 -0.23318 173 PHE   B C   
3064 O O   . PHE   B 80  ? 1.15473 1.05535 0.96942 0.38568  -0.36404 -0.25740 173 PHE   B O   
3065 C CB  . PHE   B 80  ? 1.26442 0.99220 0.95550 0.31821  -0.36233 -0.19021 173 PHE   B CB  
3066 C CG  . PHE   B 80  ? 1.33553 1.01204 0.99410 0.35780  -0.39950 -0.21035 173 PHE   B CG  
3067 C CD1 . PHE   B 80  ? 1.46276 1.10296 1.09656 0.37970  -0.42749 -0.21439 173 PHE   B CD1 
3068 C CD2 . PHE   B 80  ? 1.37902 1.04078 1.02930 0.37448  -0.40813 -0.22592 173 PHE   B CD2 
3069 C CE1 . PHE   B 80  ? 1.44024 1.02972 1.04199 0.41891  -0.46460 -0.23375 173 PHE   B CE1 
3070 C CE2 . PHE   B 80  ? 1.47314 1.08499 1.09228 0.41325  -0.44399 -0.24578 173 PHE   B CE2 
3071 C CZ  . PHE   B 80  ? 1.39804 0.97315 0.99292 0.43612  -0.47287 -0.24971 173 PHE   B CZ  
3072 N N   . ASP   B 81  ? 1.15097 1.05412 0.96130 0.33943  -0.32487 -0.23360 174 ASP   B N   
3073 C CA  . ASP   B 81  ? 1.16801 1.11820 1.00886 0.36555  -0.32454 -0.26272 174 ASP   B CA  
3074 C C   . ASP   B 81  ? 1.14088 1.18452 1.04441 0.37226  -0.30788 -0.27983 174 ASP   B C   
3075 O O   . ASP   B 81  ? 1.19649 1.27623 1.12583 0.40504  -0.31939 -0.30991 174 ASP   B O   
3076 C CB  . ASP   B 81  ? 1.12362 1.07443 0.95926 0.34794  -0.30628 -0.25739 174 ASP   B CB  
3077 C CG  . ASP   B 81  ? 1.24045 1.10249 1.01742 0.34773  -0.32648 -0.24917 174 ASP   B CG  
3078 O OD1 . ASP   B 81  ? 1.35375 1.16028 1.09736 0.37404  -0.35788 -0.25872 174 ASP   B OD1 
3079 O OD2 . ASP   B 81  ? 1.29220 1.13849 1.05541 0.32116  -0.31201 -0.23368 174 ASP   B OD2 
3080 N N   . ARG   B 82  ? 0.98672 1.07097 0.91588 0.34138  -0.28084 -0.26235 175 ARG   B N   
3081 C CA  . ARG   B 82  ? 0.99508 1.16561 0.98178 0.34302  -0.26324 -0.27735 175 ARG   B CA  
3082 C C   . ARG   B 82  ? 1.08917 1.26897 1.08916 0.36439  -0.28420 -0.28981 175 ARG   B C   
3083 O O   . ARG   B 82  ? 1.14220 1.39115 1.19015 0.37913  -0.28005 -0.31390 175 ARG   B O   
3084 C CB  . ARG   B 82  ? 0.93169 1.13589 0.93730 0.30399  -0.23002 -0.25469 175 ARG   B CB  
3085 C CG  . ARG   B 82  ? 0.89349 1.11404 0.90127 0.28672  -0.20649 -0.24988 175 ARG   B CG  
3086 C CD  . ARG   B 82  ? 0.81847 1.08255 0.85129 0.25371  -0.17486 -0.23310 175 ARG   B CD  
3087 N NE  . ARG   B 82  ? 0.91344 1.13876 0.92469 0.22904  -0.17299 -0.20439 175 ARG   B NE  
3088 C CZ  . ARG   B 82  ? 0.79246 1.03551 0.81978 0.21732  -0.16706 -0.19542 175 ARG   B CZ  
3089 N NH1 . ARG   B 82  ? 0.90742 1.20640 0.97366 0.22589  -0.16260 -0.21186 175 ARG   B NH1 
3090 N NH2 . ARG   B 82  ? 0.82621 1.03168 0.83090 0.19571  -0.16497 -0.17052 175 ARG   B NH2 
3091 N N   . TYR   B 83  ? 1.08887 1.20065 1.04649 0.36563  -0.30671 -0.27463 176 TYR   B N   
3092 C CA  . TYR   B 83  ? 1.02448 1.13809 0.98854 0.38810  -0.33057 -0.28659 176 TYR   B CA  
3093 C C   . TYR   B 83  ? 1.15476 1.26329 1.11924 0.43385  -0.36183 -0.31881 176 TYR   B C   
3094 O O   . TYR   B 83  ? 1.18654 1.34668 1.19045 0.45768  -0.37222 -0.34389 176 TYR   B O   
3095 C CB  . TYR   B 83  ? 1.09811 1.13544 1.00984 0.37525  -0.34512 -0.26027 176 TYR   B CB  
3096 C CG  . TYR   B 83  ? 1.13200 1.15347 1.03613 0.40200  -0.37633 -0.27194 176 TYR   B CG  
3097 C CD1 . TYR   B 83  ? 1.12649 1.20392 1.07079 0.39829  -0.36981 -0.27686 176 TYR   B CD1 
3098 C CD2 . TYR   B 83  ? 1.20735 1.15426 1.06123 0.43101  -0.41393 -0.27813 176 TYR   B CD2 
3099 C CE1 . TYR   B 83  ? 1.16196 1.22528 1.09904 0.42348  -0.40032 -0.28849 176 TYR   B CE1 
3100 C CE2 . TYR   B 83  ? 1.28906 1.21787 1.13229 0.45730  -0.44523 -0.28900 176 TYR   B CE2 
3101 C CZ  . TYR   B 83  ? 1.27915 1.26810 1.16521 0.45371  -0.43848 -0.29448 176 TYR   B CZ  
3102 O OH  . TYR   B 83  ? 1.23041 1.20199 1.10580 0.48060  -0.47148 -0.30629 176 TYR   B OH  
3103 N N   . MET   B 84  ? 1.18959 1.23655 1.11129 0.44722  -0.37818 -0.31998 177 MET   B N   
3104 C CA  . MET   B 84  ? 1.20294 1.24042 1.12218 0.49324  -0.40946 -0.35182 177 MET   B CA  
3105 C C   . MET   B 84  ? 1.23895 1.37052 1.22141 0.50920  -0.39337 -0.38425 177 MET   B C   
3106 O O   . MET   B 84  ? 1.29055 1.44809 1.29532 0.54891  -0.41559 -0.41731 177 MET   B O   
3107 C CB  . MET   B 84  ? 1.25473 1.20198 1.11150 0.50069  -0.42854 -0.34483 177 MET   B CB  
3108 C CG  . MET   B 84  ? 1.29405 1.14423 1.08354 0.48203  -0.44290 -0.31317 177 MET   B CG  
3109 S SD  . MET   B 84  ? 1.43325 1.23129 1.19039 0.51379  -0.48639 -0.31961 177 MET   B SD  
3110 C CE  . MET   B 84  ? 1.49007 1.22655 1.20933 0.56274  -0.52790 -0.34657 177 MET   B CE  
3111 N N   . ALA   B 85  ? 1.16332 1.34666 1.17414 0.47909  -0.35513 -0.37629 178 ALA   B N   
3112 C CA  . ALA   B 85  ? 1.04602 1.32188 1.11554 0.48808  -0.33466 -0.40511 178 ALA   B CA  
3113 C C   . ALA   B 85  ? 1.13990 1.49275 1.26614 0.49336  -0.33041 -0.42232 178 ALA   B C   
3114 O O   . ALA   B 85  ? 1.09978 1.52964 1.27658 0.50964  -0.32150 -0.45407 178 ALA   B O   
3115 C CB  . ALA   B 85  ? 1.06532 1.36966 1.14339 0.45162  -0.29526 -0.38895 178 ALA   B CB  
3116 N N   . THR   B 86  ? 1.06048 1.39560 1.17967 0.47908  -0.33598 -0.40326 179 THR   B N   
3117 C CA  . THR   B 86  ? 1.04577 1.44748 1.21545 0.48346  -0.33547 -0.41893 179 THR   B CA  
3118 C C   . THR   B 86  ? 1.07477 1.45385 1.23819 0.52493  -0.37871 -0.43999 179 THR   B C   
3119 O O   . THR   B 86  ? 1.09352 1.52836 1.29832 0.53015  -0.37923 -0.45952 179 THR   B O   
3120 C CB  . THR   B 86  ? 1.05271 1.45314 1.22089 0.44362  -0.31575 -0.38762 179 THR   B CB  
3121 O OG1 . THR   B 86  ? 1.06057 1.37254 1.17077 0.44186  -0.33900 -0.36286 179 THR   B OG1 
3122 C CG2 . THR   B 86  ? 0.97107 1.38647 1.14064 0.40448  -0.27647 -0.36578 179 THR   B CG2 
3123 N N   . GLN   B 87  ? 1.08434 1.37398 1.18849 0.54658  -0.41120 -0.43426 180 GLN   B N   
3124 C CA  . GLN   B 87  ? 1.16332 1.40750 1.24118 0.57698  -0.44984 -0.44788 180 GLN   B CA  
3125 C C   . GLN   B 87  ? 1.25449 1.48240 1.31966 0.60872  -0.46785 -0.47704 180 GLN   B C   
3126 O O   . GLN   B 87  ? 1.31754 1.55696 1.38697 0.61174  -0.45606 -0.48365 180 GLN   B O   
3127 C CB  . GLN   B 87  ? 1.18106 1.32292 1.18911 0.57309  -0.47480 -0.41606 180 GLN   B CB  
3128 C CG  . GLN   B 87  ? 1.16624 1.31423 1.17547 0.53337  -0.45343 -0.38560 180 GLN   B CG  
3129 C CD  . GLN   B 87  ? 1.13240 1.35208 1.19510 0.53734  -0.45299 -0.40201 180 GLN   B CD  
3130 O OE1 . GLN   B 87  ? 1.25860 1.46712 1.31687 0.55904  -0.47442 -0.42205 180 GLN   B OE1 
3131 N NE2 . GLN   B 87  ? 1.10674 1.38802 1.20992 0.50260  -0.41761 -0.39099 180 GLN   B NE2 
3132 N N   . GLU   B 88  ? 1.30588 1.50632 1.35391 0.63281  -0.49769 -0.49536 181 GLU   B N   
3133 C CA  . GLU   B 88  ? 1.43508 1.61912 1.46901 0.66488  -0.52045 -0.52516 181 GLU   B CA  
3134 C C   . GLU   B 88  ? 1.48221 1.56657 1.44932 0.68621  -0.56235 -0.52197 181 GLU   B C   
3135 O O   . GLU   B 88  ? 1.55576 1.61653 1.50965 0.68143  -0.57284 -0.51108 181 GLU   B O   
3136 C CB  . GLU   B 88  ? 1.44745 1.72839 1.54537 0.67481  -0.51161 -0.56318 181 GLU   B CB  
3137 C CG  . GLU   B 88  ? 1.42603 1.80703 1.58836 0.65024  -0.46805 -0.56795 181 GLU   B CG  
3138 C CD  . GLU   B 88  ? 1.42905 1.90164 1.65135 0.65477  -0.45901 -0.60292 181 GLU   B CD  
3139 O OE1 . GLU   B 88  ? 1.33270 1.79359 1.54918 0.68027  -0.48837 -0.62550 181 GLU   B OE1 
3140 O OE2 . GLU   B 88  ? 1.47942 2.03374 1.75266 0.63185  -0.42265 -0.60791 181 GLU   B OE2 
3141 N N   . ASN   B 89  ? 1.54198 1.56590 1.46429 0.70876  -0.58602 -0.53153 182 ASN   B N   
3142 C CA  . ASN   B 89  ? 1.61250 1.53969 1.46726 0.73108  -0.62738 -0.53331 182 ASN   B CA  
3143 C C   . ASN   B 89  ? 1.67155 1.50904 1.46644 0.71245  -0.63580 -0.49518 182 ASN   B C   
3144 O O   . ASN   B 89  ? 1.79222 1.62844 1.58804 0.70817  -0.64128 -0.48996 182 ASN   B O   
3145 C CB  . ASN   B 89  ? 1.65287 1.61840 1.53390 0.75515  -0.64654 -0.56666 182 ASN   B CB  
3146 C CG  . ASN   B 89  ? 1.69967 1.76253 1.64436 0.76980  -0.63571 -0.60466 182 ASN   B CG  
3147 O OD1 . ASN   B 89  ? 1.64994 1.69662 1.57816 0.79247  -0.65219 -0.62416 182 ASN   B OD1 
3148 N ND2 . ASN   B 89  ? 1.65771 1.82147 1.67386 0.75524  -0.60773 -0.61510 182 ASN   B ND2 
3149 N N   . VAL   B 90  ? 1.63352 1.39476 1.37456 0.70016  -0.63688 -0.46867 183 VAL   B N   
3150 C CA  . VAL   B 90  ? 1.65929 1.33022 1.33708 0.67831  -0.64327 -0.43067 183 VAL   B CA  
3151 C C   . VAL   B 90  ? 1.65298 1.20595 1.24478 0.68947  -0.67474 -0.42544 183 VAL   B C   
3152 O O   . VAL   B 90  ? 1.88261 1.42220 1.46393 0.70182  -0.68054 -0.43747 183 VAL   B O   
3153 C CB  . VAL   B 90  ? 1.70359 1.39328 1.39525 0.64406  -0.61175 -0.39867 183 VAL   B CB  
3154 C CG1 . VAL   B 90  ? 1.68833 1.27704 1.30551 0.61931  -0.61949 -0.35918 183 VAL   B CG1 
3155 C CG2 . VAL   B 90  ? 1.58182 1.37972 1.35028 0.62960  -0.58300 -0.40125 183 VAL   B CG2 
3156 N N   . VAL   B 91  ? 1.90274 1.36957 1.43105 0.68371  -0.69470 -0.40772 184 VAL   B N   
3157 C CA  . VAL   B 91  ? 2.07199 1.42046 1.51175 0.69088  -0.72556 -0.40201 184 VAL   B CA  
3158 C C   . VAL   B 91  ? 2.05569 1.33033 1.44199 0.65716  -0.71397 -0.36357 184 VAL   B C   
3159 O O   . VAL   B 91  ? 2.01206 1.32636 1.42867 0.63008  -0.68469 -0.34115 184 VAL   B O   
3160 C CB  . VAL   B 91  ? 2.04953 1.33999 1.44388 0.70086  -0.75278 -0.40402 184 VAL   B CB  
3161 C CG1 . VAL   B 91  ? 2.12740 1.36881 1.48414 0.66644  -0.74114 -0.36522 184 VAL   B CG1 
3162 C CG2 . VAL   B 91  ? 2.13136 1.32665 1.45141 0.72270  -0.79100 -0.41650 184 VAL   B CG2 
3163 N N   . LYS   B 92  ? 2.20933 1.37688 1.51462 0.65711  -0.73749 -0.35613 185 LYS   B N   
3164 C CA  . LYS   B 92  ? 2.25185 1.34417 1.50209 0.62269  -0.72739 -0.32121 185 LYS   B CA  
3165 C C   . LYS   B 92  ? 2.20054 1.24974 1.41485 0.58838  -0.71679 -0.28628 185 LYS   B C   
3166 O O   . LYS   B 92  ? 2.17657 1.22524 1.39004 0.55445  -0.69224 -0.25702 185 LYS   B O   
3167 C CB  . LYS   B 92  ? 2.35432 1.34496 1.52611 0.62989  -0.75607 -0.32427 185 LYS   B CB  
3168 C CG  . LYS   B 92  ? 2.35372 1.38133 1.55334 0.66300  -0.76858 -0.35753 185 LYS   B CG  
3169 C CD  . LYS   B 92  ? 2.48809 1.41876 1.60859 0.67829  -0.80636 -0.36590 185 LYS   B CD  
3170 C CE  . LYS   B 92  ? 2.59498 1.41467 1.63102 0.64194  -0.80720 -0.33092 185 LYS   B CE  
3171 N NZ  . LYS   B 92  ? 2.71338 1.43676 1.66824 0.65506  -0.84483 -0.33779 185 LYS   B NZ  
3172 N N   . THR   B 93  ? 2.23928 1.25233 1.42199 0.59629  -0.73535 -0.28928 186 THR   B N   
3173 C CA  . THR   B 93  ? 2.27687 1.24310 1.41809 0.56380  -0.72633 -0.25716 186 THR   B CA  
3174 C C   . THR   B 93  ? 2.20628 1.26449 1.41463 0.54685  -0.69590 -0.24503 186 THR   B C   
3175 O O   . THR   B 93  ? 2.13710 1.16712 1.31625 0.51339  -0.68156 -0.21457 186 THR   B O   
3176 C CB  . THR   B 93  ? 2.36377 1.27166 1.45621 0.57974  -0.75492 -0.26644 186 THR   B CB  
3177 O OG1 . THR   B 93  ? 2.33983 1.33031 1.49774 0.61455  -0.76343 -0.29880 186 THR   B OG1 
3178 C CG2 . THR   B 93  ? 2.38922 1.19662 1.40330 0.59175  -0.78656 -0.27487 186 THR   B CG2 
3179 N N   . LEU   B 94  ? 2.12546 1.29391 1.42085 0.56718  -0.68524 -0.26879 187 LEU   B N   
3180 C CA  . LEU   B 94  ? 2.02210 1.28330 1.38287 0.54964  -0.65625 -0.25891 187 LEU   B CA  
3181 C C   . LEU   B 94  ? 1.96923 1.25683 1.34704 0.52270  -0.63018 -0.23871 187 LEU   B C   
3182 O O   . LEU   B 94  ? 1.91968 1.27170 1.33866 0.49661  -0.60168 -0.22508 187 LEU   B O   
3183 C CB  . LEU   B 94  ? 1.97029 1.34035 1.41649 0.57927  -0.65454 -0.29432 187 LEU   B CB  
3184 C CG  . LEU   B 94  ? 1.90948 1.37668 1.42348 0.56478  -0.62968 -0.29045 187 LEU   B CG  
3185 C CD1 . LEU   B 94  ? 1.85891 1.28250 1.33308 0.54567  -0.63247 -0.26777 187 LEU   B CD1 
3186 C CD2 . LEU   B 94  ? 1.80749 1.37323 1.39955 0.59333  -0.62956 -0.32884 187 LEU   B CD2 
3187 N N   . LEU   B 95  ? 1.98161 1.22108 1.32855 0.52365  -0.63560 -0.23773 188 LEU   B N   
3188 C CA  . LEU   B 95  ? 1.82939 1.10191 1.20041 0.48883  -0.59970 -0.22363 188 LEU   B CA  
3189 C C   . LEU   B 95  ? 1.75753 0.99038 1.09083 0.43603  -0.57441 -0.18631 188 LEU   B C   
3190 O O   . LEU   B 95  ? 1.75302 1.05025 1.13118 0.40171  -0.53533 -0.17457 188 LEU   B O   
3191 C CB  . LEU   B 95  ? 1.96784 1.19390 1.31240 0.50197  -0.61223 -0.23381 188 LEU   B CB  
3192 C CG  . LEU   B 95  ? 1.87485 1.15350 1.26585 0.55062  -0.62911 -0.27287 188 LEU   B CG  
3193 C CD1 . LEU   B 95  ? 1.86599 1.08163 1.21735 0.56133  -0.64356 -0.28003 188 LEU   B CD1 
3194 C CD2 . LEU   B 95  ? 1.62318 1.03207 1.10792 0.54325  -0.59254 -0.28593 188 LEU   B CD2 
3195 N N   . GLN   B 96  ? 1.84299 0.96942 1.09258 0.42883  -0.59609 -0.16801 189 GLN   B N   
3196 C CA  . GLN   B 96  ? 1.89760 0.98377 1.10806 0.37745  -0.57121 -0.13407 189 GLN   B CA  
3197 C C   . GLN   B 96  ? 1.89428 1.05060 1.14800 0.35726  -0.54510 -0.12435 189 GLN   B C   
3198 O O   . GLN   B 96  ? 1.77104 0.95016 1.03669 0.31421  -0.50977 -0.10363 189 GLN   B O   
3199 C CB  . GLN   B 96  ? 1.90139 0.85690 1.00883 0.37476  -0.60061 -0.11789 189 GLN   B CB  
3200 C CG  . GLN   B 96  ? 1.99440 0.90114 1.05529 0.31919  -0.57413 -0.08429 189 GLN   B CG  
3201 C CD  . GLN   B 96  ? 2.22009 0.99507 1.17408 0.31412  -0.60188 -0.06777 189 GLN   B CD  
3202 O OE1 . GLN   B 96  ? 2.37367 1.11829 1.30632 0.34205  -0.62727 -0.08418 189 GLN   B OE1 
3203 N NE2 . GLN   B 96  ? 2.14760 0.86408 1.05219 0.26748  -0.58289 -0.04291 189 GLN   B NE2 
3204 N N   . LEU   B 97  ? 1.75357 0.94574 1.03241 0.38858  -0.56295 -0.14051 190 LEU   B N   
3205 C CA  . LEU   B 97  ? 1.79692 1.05473 1.11678 0.37126  -0.54034 -0.13328 190 LEU   B CA  
3206 C C   . LEU   B 97  ? 1.66556 1.03668 1.07450 0.35775  -0.50315 -0.14062 190 LEU   B C   
3207 O O   . LEU   B 97  ? 1.58492 0.99539 1.01749 0.32309  -0.47068 -0.12385 190 LEU   B O   
3208 C CB  . LEU   B 97  ? 1.71197 0.97656 1.03458 0.40918  -0.57219 -0.15063 190 LEU   B CB  
3209 C CG  . LEU   B 97  ? 1.57858 0.91179 0.94502 0.39602  -0.55340 -0.14714 190 LEU   B CG  
3210 C CD1 . LEU   B 97  ? 1.68584 0.97363 1.00509 0.35147  -0.53178 -0.11441 190 LEU   B CD1 
3211 C CD2 . LEU   B 97  ? 1.74142 1.08052 1.11222 0.43566  -0.58771 -0.16810 190 LEU   B CD2 
3212 N N   . ILE   B 98  ? 1.50302 0.92554 0.95951 0.38492  -0.50745 -0.16599 191 ILE   B N   
3213 C CA  . ILE   B 98  ? 1.59573 1.12083 1.13085 0.37226  -0.47275 -0.17324 191 ILE   B CA  
3214 C C   . ILE   B 98  ? 1.54611 1.06245 1.07381 0.33098  -0.44148 -0.15132 191 ILE   B C   
3215 O O   . ILE   B 98  ? 1.36364 0.94404 0.93636 0.30387  -0.40774 -0.14252 191 ILE   B O   
3216 C CB  . ILE   B 98  ? 1.60100 1.17829 1.18235 0.41098  -0.48479 -0.20669 191 ILE   B CB  
3217 C CG1 . ILE   B 98  ? 1.51389 1.11034 1.11102 0.45206  -0.51555 -0.23109 191 ILE   B CG1 
3218 C CG2 . ILE   B 98  ? 1.41043 1.08736 1.06536 0.39524  -0.44767 -0.21289 191 ILE   B CG2 
3219 C CD1 . ILE   B 98  ? 1.48650 1.13861 1.13162 0.49206  -0.52795 -0.26739 191 ILE   B CD1 
3220 N N   . GLY   B 99  ? 1.55856 0.99413 1.02866 0.32559  -0.45342 -0.14278 192 GLY   B N   
3221 C CA  . GLY   B 99  ? 1.50935 0.93731 0.97386 0.28719  -0.42620 -0.12445 192 GLY   B CA  
3222 C C   . GLY   B 99  ? 1.54796 0.96102 0.99347 0.24526  -0.40363 -0.09637 192 GLY   B C   
3223 O O   . GLY   B 99  ? 1.51629 0.97961 0.99799 0.21537  -0.37107 -0.08596 192 GLY   B O   
3224 N N   . ILE   B 100 ? 1.49346 0.83641 0.88023 0.24334  -0.42111 -0.08457 193 ILE   B N   
3225 C CA  . ILE   B 100 ? 1.60700 0.93166 0.97038 0.20321  -0.39932 -0.05891 193 ILE   B CA  
3226 C C   . ILE   B 100 ? 1.51031 0.91908 0.93203 0.19640  -0.37676 -0.05877 193 ILE   B C   
3227 O O   . ILE   B 100 ? 1.38223 0.81098 0.81352 0.16138  -0.34791 -0.04156 193 ILE   B O   
3228 C CB  . ILE   B 100 ? 1.76106 0.98317 1.03905 0.20261  -0.42407 -0.04647 193 ILE   B CB  
3229 C CG1 . ILE   B 100 ? 1.67390 0.86694 0.91894 0.15517  -0.39831 -0.01951 193 ILE   B CG1 
3230 C CG2 . ILE   B 100 ? 1.63980 0.86611 0.91624 0.23550  -0.44879 -0.05788 193 ILE   B CG2 
3231 C CD1 . ILE   B 100 ? 1.67493 0.85586 0.91542 0.12129  -0.37719 -0.00864 193 ILE   B CD1 
3232 N N   . SER   B 101 ? 1.50125 0.96131 0.96374 0.22919  -0.38946 -0.07900 194 SER   B N   
3233 C CA  . SER   B 101 ? 1.36575 0.90591 0.88498 0.22232  -0.36855 -0.08035 194 SER   B CA  
3234 C C   . SER   B 101 ? 1.24902 0.87027 0.83396 0.20863  -0.33760 -0.08389 194 SER   B C   
3235 O O   . SER   B 101 ? 1.13808 0.80808 0.75619 0.18575  -0.31099 -0.07454 194 SER   B O   
3236 C CB  . SER   B 101 ? 1.31866 0.88691 0.85977 0.25986  -0.39300 -0.10195 194 SER   B CB  
3237 O OG  . SER   B 101 ? 1.47459 0.96468 0.95113 0.27368  -0.42381 -0.09822 194 SER   B OG  
3238 N N   . SER   B 102 ? 1.26691 0.90042 0.86807 0.22296  -0.34147 -0.09754 195 SER   B N   
3239 C CA  . SER   B 102 ? 1.15854 0.85666 0.81037 0.20746  -0.31274 -0.09851 195 SER   B CA  
3240 C C   . SER   B 102 ? 1.14569 0.82372 0.78042 0.16721  -0.28907 -0.07466 195 SER   B C   
3241 O O   . SER   B 102 ? 1.05271 0.78661 0.72804 0.14662  -0.26143 -0.06834 195 SER   B O   
3242 C CB  . SER   B 102 ? 1.14688 0.85071 0.80863 0.23059  -0.32349 -0.11758 195 SER   B CB  
3243 O OG  . SER   B 102 ? 1.24874 0.97682 0.93057 0.26915  -0.34508 -0.14259 195 SER   B OG  
3244 N N   . LEU   B 103 ? 1.20255 0.80035 0.77669 0.15532  -0.30003 -0.06198 196 LEU   B N   
3245 C CA  . LEU   B 103 ? 1.19197 0.77110 0.74970 0.11560  -0.27793 -0.04080 196 LEU   B CA  
3246 C C   . LEU   B 103 ? 1.20108 0.79552 0.76228 0.09464  -0.26113 -0.02653 196 LEU   B C   
3247 O O   . LEU   B 103 ? 1.14857 0.76927 0.72791 0.06492  -0.23482 -0.01429 196 LEU   B O   
3248 C CB  . LEU   B 103 ? 1.25783 0.74486 0.74722 0.10638  -0.29398 -0.03198 196 LEU   B CB  
3249 C CG  . LEU   B 103 ? 1.30971 0.77414 0.78032 0.06400  -0.27254 -0.01278 196 LEU   B CG  
3250 C CD1 . LEU   B 103 ? 1.23385 0.75855 0.75553 0.05225  -0.25128 -0.01607 196 LEU   B CD1 
3251 C CD2 . LEU   B 103 ? 1.38409 0.75235 0.78309 0.05570  -0.29090 -0.00578 196 LEU   B CD2 
3252 N N   . PHE   B 104 ? 1.23765 0.81662 0.78193 0.11099  -0.27699 -0.02924 197 PHE   B N   
3253 C CA  . PHE   B 104 ? 1.21910 0.81332 0.76613 0.09364  -0.26224 -0.01768 197 PHE   B CA  
3254 C C   . PHE   B 104 ? 1.10955 0.79349 0.72641 0.08994  -0.23862 -0.02254 197 PHE   B C   
3255 O O   . PHE   B 104 ? 1.12440 0.83150 0.75488 0.06384  -0.21444 -0.01020 197 PHE   B O   
3256 C CB  . PHE   B 104 ? 1.31053 0.86684 0.82239 0.11522  -0.28815 -0.02165 197 PHE   B CB  
3257 C CG  . PHE   B 104 ? 1.36243 0.92548 0.86842 0.09837  -0.27557 -0.01026 197 PHE   B CG  
3258 C CD1 . PHE   B 104 ? 1.36960 0.90278 0.84448 0.06311  -0.25569 0.00941  197 PHE   B CD1 
3259 C CD2 . PHE   B 104 ? 1.33107 0.93093 0.86260 0.11763  -0.28379 -0.02072 197 PHE   B CD2 
3260 C CE1 . PHE   B 104 ? 1.42112 0.96047 0.88915 0.04859  -0.24359 0.01843  197 PHE   B CE1 
3261 C CE2 . PHE   B 104 ? 1.34452 0.94810 0.86828 0.10273  -0.27313 -0.01110 197 PHE   B CE2 
3262 C CZ  . PHE   B 104 ? 1.34203 0.91465 0.83303 0.06887  -0.25284 0.00850  197 PHE   B CZ  
3263 N N   . ILE   B 105 ? 1.10862 0.84291 0.76908 0.11568  -0.24518 -0.04125 198 ILE   B N   
3264 C CA  . ILE   B 105 ? 1.03628 0.85165 0.75950 0.11070  -0.22254 -0.04598 198 ILE   B CA  
3265 C C   . ILE   B 105 ? 0.99459 0.83003 0.73541 0.08645  -0.19851 -0.03676 198 ILE   B C   
3266 O O   . ILE   B 105 ? 0.92112 0.79755 0.69153 0.06752  -0.17537 -0.02905 198 ILE   B O   
3267 C CB  . ILE   B 105 ? 1.00642 0.86921 0.76930 0.14134  -0.23368 -0.06927 198 ILE   B CB  
3268 C CG1 . ILE   B 105 ? 0.97902 0.82437 0.72714 0.16741  -0.26043 -0.08068 198 ILE   B CG1 
3269 C CG2 . ILE   B 105 ? 0.84736 0.78915 0.66988 0.13292  -0.20910 -0.07316 198 ILE   B CG2 
3270 C CD1 . ILE   B 105 ? 0.98505 0.86926 0.76682 0.20061  -0.27599 -0.10687 198 ILE   B CD1 
3271 N N   . ALA   B 106 ? 1.00419 0.80919 0.72595 0.08762  -0.20534 -0.03823 199 ALA   B N   
3272 C CA  . ALA   B 106 ? 1.02415 0.84825 0.76276 0.06682  -0.18582 -0.03168 199 ALA   B CA  
3273 C C   . ALA   B 106 ? 0.95197 0.75512 0.67220 0.03393  -0.16963 -0.01254 199 ALA   B C   
3274 O O   . ALA   B 106 ? 0.91394 0.75655 0.66453 0.01555  -0.14801 -0.00660 199 ALA   B O   
3275 C CB  . ALA   B 106 ? 0.98913 0.78130 0.70827 0.07658  -0.19951 -0.03922 199 ALA   B CB  
3276 N N   . ALA   B 107 ? 0.97966 0.72059 0.64915 0.02627  -0.17986 -0.00348 200 ALA   B N   
3277 C CA  . ALA   B 107 ? 1.07723 0.79859 0.72760 -0.00665 -0.16290 0.01311  200 ALA   B CA  
3278 C C   . ALA   B 107 ? 1.02900 0.79636 0.70927 -0.01686 -0.14356 0.01834  200 ALA   B C   
3279 O O   . ALA   B 107 ? 1.04083 0.83092 0.73781 -0.04092 -0.12209 0.02664  200 ALA   B O   
3280 C CB  . ALA   B 107 ? 1.14353 0.78406 0.72694 -0.01326 -0.17778 0.02146  200 ALA   B CB  
3281 N N   . LYS   B 108 ? 1.10268 0.88460 0.79079 0.00182  -0.15189 0.01224  201 LYS   B N   
3282 C CA  . LYS   B 108 ? 1.07634 0.90035 0.79233 -0.00651 -0.13502 0.01586  201 LYS   B CA  
3283 C C   . LYS   B 108 ? 0.97879 0.87000 0.75163 -0.00904 -0.11701 0.01192  201 LYS   B C   
3284 O O   . LYS   B 108 ? 0.99083 0.91259 0.78522 -0.02374 -0.09840 0.01793  201 LYS   B O   
3285 C CB  . LYS   B 108 ? 1.05147 0.87539 0.76328 0.01456  -0.15044 0.00844  201 LYS   B CB  
3286 C CG  . LYS   B 108 ? 1.06805 0.82505 0.71954 0.01358  -0.16556 0.01530  201 LYS   B CG  
3287 C CD  . LYS   B 108 ? 1.11811 0.88215 0.76988 0.03201  -0.17890 0.00822  201 LYS   B CD  
3288 C CE  . LYS   B 108 ? 1.10369 0.88530 0.77584 0.06511  -0.20155 -0.01023 201 LYS   B CE  
3289 N NZ  . LYS   B 108 ? 1.12037 0.90718 0.79183 0.08333  -0.21759 -0.01876 201 LYS   B NZ  
3290 N N   . LEU   B 109 ? 0.99698 0.90914 0.79148 0.00545  -0.12257 0.00161  202 LEU   B N   
3291 C CA  . LEU   B 109 ? 0.97870 0.94912 0.82055 0.00318  -0.10648 -0.00177 202 LEU   B CA  
3292 C C   . LEU   B 109 ? 0.96153 0.93478 0.80790 -0.01843 -0.09182 0.00692  202 LEU   B C   
3293 O O   . LEU   B 109 ? 0.95770 0.97041 0.83469 -0.02868 -0.07490 0.01030  202 LEU   B O   
3294 C CB  . LEU   B 109 ? 0.88800 0.88087 0.74909 0.02606  -0.11648 -0.01712 202 LEU   B CB  
3295 C CG  . LEU   B 109 ? 0.96250 0.98256 0.84276 0.04698  -0.12495 -0.02997 202 LEU   B CG  
3296 C CD1 . LEU   B 109 ? 0.83875 0.87543 0.73272 0.06941  -0.13560 -0.04709 202 LEU   B CD1 
3297 C CD2 . LEU   B 109 ? 0.99047 1.06100 0.90775 0.03771  -0.10643 -0.02788 202 LEU   B CD2 
3298 N N   . GLU   B 110 ? 0.96734 0.89825 0.78325 -0.02540 -0.09926 0.00984  203 GLU   B N   
3299 C CA  . GLU   B 110 ? 0.99232 0.92908 0.81608 -0.04317 -0.08891 0.01423  203 GLU   B CA  
3300 C C   . GLU   B 110 ? 1.04137 0.95912 0.84917 -0.07048 -0.07717 0.02598  203 GLU   B C   
3301 O O   . GLU   B 110 ? 0.92403 0.87210 0.75691 -0.08582 -0.06197 0.02925  203 GLU   B O   
3302 C CB  . GLU   B 110 ? 0.94616 0.85226 0.75023 -0.03529 -0.10383 0.00788  203 GLU   B CB  
3303 C CG  . GLU   B 110 ? 0.99077 0.90696 0.80623 -0.05096 -0.09577 0.00963  203 GLU   B CG  
3304 C CD  . GLU   B 110 ? 1.08367 1.05785 0.94262 -0.04653 -0.08411 0.00570  203 GLU   B CD  
3305 O OE1 . GLU   B 110 ? 1.10667 1.10794 0.98326 -0.02777 -0.08564 -0.00175 203 GLU   B OE1 
3306 O OE2 . GLU   B 110 ? 1.16611 1.15824 1.04063 -0.06230 -0.07375 0.00959  203 GLU   B OE2 
3307 N N   . GLU   B 111 ? 0.99323 0.86168 0.75905 -0.07689 -0.08390 0.03156  204 GLU   B N   
3308 C CA  . GLU   B 111 ? 1.11057 0.95755 0.85646 -0.10555 -0.07154 0.04162  204 GLU   B CA  
3309 C C   . GLU   B 111 ? 1.13719 1.01638 0.90215 -0.11513 -0.05377 0.04629  204 GLU   B C   
3310 O O   . GLU   B 111 ? 1.12116 1.01571 0.89479 -0.10022 -0.05601 0.04408  204 GLU   B O   
3311 C CB  . GLU   B 111 ? 1.03089 0.80632 0.71696 -0.11088 -0.08480 0.04671  204 GLU   B CB  
3312 C CG  . GLU   B 111 ? 1.08907 0.82344 0.74978 -0.09908 -0.10541 0.04135  204 GLU   B CG  
3313 C CD  . GLU   B 111 ? 1.21021 0.94863 0.88102 -0.11639 -0.09950 0.04092  204 GLU   B CD  
3314 O OE1 . GLU   B 111 ? 1.20157 0.96184 0.88829 -0.14216 -0.08050 0.04630  204 GLU   B OE1 
3315 O OE2 . GLU   B 111 ? 1.15109 0.87201 0.81475 -0.10346 -0.11458 0.03377  204 GLU   B OE2 
3316 N N   . ILE   B 112 ? 1.06178 0.95255 0.83454 -0.14027 -0.03624 0.05131  205 ILE   B N   
3317 C CA  . ILE   B 112 ? 1.14544 1.06303 0.93274 -0.15043 -0.01878 0.05468  205 ILE   B CA  
3318 C C   . ILE   B 112 ? 1.16299 1.03552 0.90347 -0.15714 -0.02026 0.06083  205 ILE   B C   
3319 O O   . ILE   B 112 ? 1.12328 1.00558 0.86524 -0.14877 -0.01832 0.06096  205 ILE   B O   
3320 C CB  . ILE   B 112 ? 1.09610 1.04388 0.90901 -0.17356 -0.00015 0.05533  205 ILE   B CB  
3321 C CG1 . ILE   B 112 ? 0.98396 0.97449 0.84036 -0.16457 -0.00106 0.04925  205 ILE   B CG1 
3322 C CG2 . ILE   B 112 ? 1.00349 0.97730 0.82956 -0.18288 0.01781  0.05703  205 ILE   B CG2 
3323 C CD1 . ILE   B 112 ? 0.83369 0.85890 0.72026 -0.18329 0.01404  0.04761  205 ILE   B CD1 
3324 N N   . TYR   B 113 ? 1.11527 0.93449 0.81014 -0.17323 -0.02424 0.06609  206 TYR   B N   
3325 C CA  . TYR   B 113 ? 1.23460 0.99855 0.87312 -0.18060 -0.02803 0.07310  206 TYR   B CA  
3326 C C   . TYR   B 113 ? 1.24185 0.94527 0.83570 -0.16693 -0.05366 0.07328  206 TYR   B C   
3327 O O   . TYR   B 113 ? 1.30695 0.96213 0.86261 -0.18424 -0.05670 0.07799  206 TYR   B O   
3328 C CB  . TYR   B 113 ? 1.26152 1.01023 0.87820 -0.21592 -0.00767 0.07985  206 TYR   B CB  
3329 C CG  . TYR   B 113 ? 1.27526 1.08507 0.93749 -0.22799 0.01708  0.07724  206 TYR   B CG  
3330 C CD1 . TYR   B 113 ? 1.20239 1.02613 0.86480 -0.22448 0.02589  0.07789  206 TYR   B CD1 
3331 C CD2 . TYR   B 113 ? 1.33338 1.18592 1.03779 -0.24151 0.03000  0.07289  206 TYR   B CD2 
3332 C CE1 . TYR   B 113 ? 1.29019 1.16763 0.99320 -0.23327 0.04726  0.07408  206 TYR   B CE1 
3333 C CE2 . TYR   B 113 ? 1.24701 1.15482 0.99338 -0.24950 0.05030  0.06879  206 TYR   B CE2 
3334 C CZ  . TYR   B 113 ? 1.39488 1.31426 1.14011 -0.24496 0.05905  0.06933  206 TYR   B CZ  
3335 O OH  . TYR   B 113 ? 1.36036 1.33260 1.14630 -0.25076 0.07803  0.06392  206 TYR   B OH  
3336 N N   . PRO   B 114 ? 1.24877 0.95300 0.84643 -0.13606 -0.07294 0.06707  207 PRO   B N   
3337 C CA  . PRO   B 114 ? 1.25392 0.90445 0.81338 -0.11799 -0.09968 0.06426  207 PRO   B CA  
3338 C C   . PRO   B 114 ? 1.31432 0.88954 0.80256 -0.12573 -0.10988 0.07292  207 PRO   B C   
3339 O O   . PRO   B 114 ? 1.48058 1.05115 0.95185 -0.14020 -0.09720 0.07977  207 PRO   B O   
3340 C CB  . PRO   B 114 ? 1.21006 0.89617 0.80224 -0.08363 -0.11373 0.05299  207 PRO   B CB  
3341 C CG  . PRO   B 114 ? 1.16950 0.89924 0.78920 -0.08680 -0.09803 0.05425  207 PRO   B CG  
3342 C CD  . PRO   B 114 ? 1.20274 0.95859 0.84135 -0.11635 -0.07132 0.06088  207 PRO   B CD  
3343 N N   . PRO   B 115 ? 1.49468 1.00633 0.93623 -0.11639 -0.13312 0.07273  208 PRO   B N   
3344 C CA  . PRO   B 115 ? 1.39923 0.83038 0.76515 -0.12101 -0.14661 0.08138  208 PRO   B CA  
3345 C C   . PRO   B 115 ? 1.53682 0.96785 0.89519 -0.09432 -0.16205 0.07731  208 PRO   B C   
3346 O O   . PRO   B 115 ? 1.36301 0.84734 0.77067 -0.06762 -0.16873 0.06563  208 PRO   B O   
3347 C CB  . PRO   B 115 ? 1.47889 0.84663 0.80419 -0.11151 -0.17125 0.07941  208 PRO   B CB  
3348 C CG  . PRO   B 115 ? 1.48063 0.89463 0.85701 -0.11486 -0.16236 0.07265  208 PRO   B CG  
3349 C CD  . PRO   B 115 ? 1.42222 0.92683 0.87252 -0.10385 -0.14741 0.06513  208 PRO   B CD  
3350 N N   . LYS   B 116 ? 1.59372 0.96278 0.88739 -0.10328 -0.16761 0.08680  209 LYS   B N   
3351 C CA  . LYS   B 116 ? 1.60959 0.97139 0.88852 -0.07960 -0.18417 0.08324  209 LYS   B CA  
3352 C C   . LYS   B 116 ? 1.59127 0.91428 0.84785 -0.04230 -0.22235 0.07334  209 LYS   B C   
3353 O O   . LYS   B 116 ? 1.65461 0.94267 0.89418 -0.03688 -0.23619 0.07124  209 LYS   B O   
3354 C CB  . LYS   B 116 ? 1.73741 1.04398 0.95032 -0.10206 -0.17717 0.09666  209 LYS   B CB  
3355 C CG  . LYS   B 116 ? 1.64056 0.99562 0.88147 -0.13277 -0.14030 0.10246  209 LYS   B CG  
3356 C CD  . LYS   B 116 ? 1.63008 1.06665 0.93989 -0.11515 -0.13320 0.09231  209 LYS   B CD  
3357 C CE  . LYS   B 116 ? 1.61839 1.09953 0.95346 -0.14234 -0.09889 0.09668  209 LYS   B CE  
3358 N NZ  . LYS   B 116 ? 1.39837 0.90961 0.76524 -0.16802 -0.07495 0.09892  209 LYS   B NZ  
3359 N N   . LEU   B 117 ? 1.62747 0.95837 0.88559 -0.01541 -0.24034 0.06559  210 LEU   B N   
3360 C CA  . LEU   B 117 ? 1.63456 0.94068 0.88126 0.02420  -0.27765 0.05229  210 LEU   B CA  
3361 C C   . LEU   B 117 ? 1.77972 0.97923 0.93719 0.02555  -0.30299 0.06019  210 LEU   B C   
3362 O O   . LEU   B 117 ? 1.84088 1.01054 0.98690 0.04957  -0.32877 0.05112  210 LEU   B O   
3363 C CB  . LEU   B 117 ? 1.61872 0.95625 0.88492 0.04969  -0.29132 0.04187  210 LEU   B CB  
3364 C CG  . LEU   B 117 ? 1.63802 0.94261 0.88286 0.09147  -0.33339 0.02734  210 LEU   B CG  
3365 C CD1 . LEU   B 117 ? 1.59320 0.94345 0.89329 0.11653  -0.34261 0.00947  210 LEU   B CD1 
3366 C CD2 . LEU   B 117 ? 1.57917 0.90631 0.83313 0.11018  -0.34608 0.01916  210 LEU   B CD2 
3367 N N   . HIS   B 118 ? 1.85794 0.99637 0.94847 -0.00017 -0.29607 0.07672  211 HIS   B N   
3368 C CA  . HIS   B 118 ? 2.01938 1.04738 1.01543 -0.00036 -0.32105 0.08580  211 HIS   B CA  
3369 C C   . HIS   B 118 ? 1.94176 0.93173 0.91909 -0.01794 -0.31756 0.09095  211 HIS   B C   
3370 O O   . HIS   B 118 ? 2.00913 0.91676 0.92506 -0.00468 -0.34689 0.09153  211 HIS   B O   
3371 C CB  . HIS   B 118 ? 2.06734 1.04028 0.99397 -0.02846 -0.31005 0.10306  211 HIS   B CB  
3372 C CG  . HIS   B 118 ? 2.11532 1.09668 1.04012 -0.07788 -0.26939 0.11756  211 HIS   B CG  
3373 N ND1 . HIS   B 118 ? 2.11431 1.18693 1.11222 -0.09529 -0.23442 0.11558  211 HIS   B ND1 
3374 C CD2 . HIS   B 118 ? 2.15112 1.06171 1.01029 -0.11381 -0.25846 0.13302  211 HIS   B CD2 
3375 C CE1 . HIS   B 118 ? 2.07983 1.14187 1.06098 -0.13786 -0.20432 0.12777  211 HIS   B CE1 
3376 N NE2 . HIS   B 118 ? 2.17579 1.14178 1.07408 -0.15152 -0.21695 0.13851  211 HIS   B NE2 
3377 N N   . GLN   B 119 ? 1.87497 0.92153 0.90312 -0.04673 -0.28394 0.09389  212 GLN   B N   
3378 C CA  . GLN   B 119 ? 2.03875 1.05683 1.05654 -0.06319 -0.28099 0.09662  212 GLN   B CA  
3379 C C   . GLN   B 119 ? 1.85958 0.89091 0.90841 -0.02497 -0.30727 0.07933  212 GLN   B C   
3380 O O   . GLN   B 119 ? 1.85297 0.82148 0.86104 -0.02340 -0.32434 0.07957  212 GLN   B O   
3381 C CB  . GLN   B 119 ? 1.79881 0.88224 0.86989 -0.10017 -0.24059 0.10136  212 GLN   B CB  
3382 C CG  . GLN   B 119 ? 1.98817 1.05053 1.02249 -0.14325 -0.21262 0.11760  212 GLN   B CG  
3383 C CD  . GLN   B 119 ? 1.88333 1.01770 0.97754 -0.17582 -0.17474 0.11887  212 GLN   B CD  
3384 O OE1 . GLN   B 119 ? 1.79884 1.02026 0.96639 -0.16711 -0.15996 0.11099  212 GLN   B OE1 
3385 N NE2 . GLN   B 119 ? 1.89776 0.99492 0.96015 -0.21376 -0.15976 0.12816  212 GLN   B NE2 
3386 N N   . PHE   B 120 ? 1.75569 0.86779 0.87553 0.00518  -0.31016 0.06343  213 PHE   B N   
3387 C CA  . PHE   B 120 ? 1.76690 0.89508 0.91599 0.04379  -0.33501 0.04454  213 PHE   B CA  
3388 C C   . PHE   B 120 ? 1.81433 0.86359 0.90076 0.07754  -0.37745 0.03856  213 PHE   B C   
3389 O O   . PHE   B 120 ? 1.83240 0.85037 0.90692 0.10152  -0.40191 0.02757  213 PHE   B O   
3390 C CB  . PHE   B 120 ? 1.72659 0.96098 0.96463 0.06418  -0.32524 0.02904  213 PHE   B CB  
3391 C CG  . PHE   B 120 ? 1.55073 0.85893 0.85300 0.04173  -0.29216 0.02987  213 PHE   B CG  
3392 C CD1 . PHE   B 120 ? 1.53555 0.87869 0.85659 0.00835  -0.25981 0.04234  213 PHE   B CD1 
3393 C CD2 . PHE   B 120 ? 1.55344 0.89466 0.89535 0.05538  -0.29453 0.01721  213 PHE   B CD2 
3394 C CE1 . PHE   B 120 ? 1.55438 0.96284 0.93278 -0.00972 -0.23248 0.04227  213 PHE   B CE1 
3395 C CE2 . PHE   B 120 ? 1.42977 0.83470 0.82616 0.03586  -0.26643 0.01811  213 PHE   B CE2 
3396 C CZ  . PHE   B 120 ? 1.42016 0.85807 0.83487 0.00388  -0.23639 0.03074  213 PHE   B CZ  
3397 N N   . ALA   B 121 ? 1.92008 0.93502 0.96452 0.08145  -0.38815 0.04468  214 ALA   B N   
3398 C CA  . ALA   B 121 ? 2.02039 0.94802 0.99348 0.11130  -0.43038 0.04124  214 ALA   B CA  
3399 C C   . ALA   B 121 ? 2.04007 0.85270 0.91765 0.08758  -0.43851 0.05869  214 ALA   B C   
3400 O O   . ALA   B 121 ? 2.10824 0.83830 0.92399 0.11354  -0.47638 0.05479  214 ALA   B O   
3401 C CB  . ALA   B 121 ? 1.90849 0.83631 0.86583 0.12325  -0.44038 0.04178  214 ALA   B CB  
3402 N N   . TYR   B 122 ? 2.03653 0.84211 0.90108 0.03870  -0.40416 0.07684  215 TYR   B N   
3403 C CA  . TYR   B 122 ? 2.09854 0.79582 0.87118 0.00925  -0.40767 0.09436  215 TYR   B CA  
3404 C C   . TYR   B 122 ? 2.25788 0.92046 1.02299 0.01580  -0.42208 0.08792  215 TYR   B C   
3405 O O   . TYR   B 122 ? 2.26211 0.82607 0.95165 0.01978  -0.44748 0.09021  215 TYR   B O   
3406 C CB  . TYR   B 122 ? 2.08145 0.79236 0.85006 -0.04635 -0.36414 0.11294  215 TYR   B CB  
3407 C CG  . TYR   B 122 ? 2.22799 0.84189 0.91449 -0.08538 -0.35961 0.13009  215 TYR   B CG  
3408 C CD1 . TYR   B 122 ? 2.27764 0.81337 0.89192 -0.09187 -0.37102 0.13090  215 TYR   B CD1 
3409 C CD2 . TYR   B 122 ? 2.17488 0.80869 0.88783 -0.11763 -0.33581 0.13263  215 TYR   B CD2 
3410 C CE1 . TYR   B 122 ? 2.22064 0.69125 0.77877 -0.12965 -0.36137 0.13789  215 TYR   B CE1 
3411 C CE2 . TYR   B 122 ? 2.32776 0.88477 0.97611 -0.15610 -0.32884 0.14390  215 TYR   B CE2 
3412 C CZ  . TYR   B 122 ? 2.39727 0.88156 0.97431 -0.16180 -0.34005 0.14390  215 TYR   B CZ  
3413 O OH  . TYR   B 122 ? 2.46567 0.89177 0.98992 -0.20025 -0.33035 0.14917  215 TYR   B OH  
3414 N N   . VAL   B 123 ? 2.21338 0.96023 1.06036 0.01646  -0.40457 0.07671  216 VAL   B N   
3415 C CA  . VAL   B 123 ? 2.20244 0.92137 1.04533 0.02028  -0.41551 0.06995  216 VAL   B CA  
3416 C C   . VAL   B 123 ? 2.27368 0.95675 1.10083 0.07339  -0.45992 0.05135  216 VAL   B C   
3417 O O   . VAL   B 123 ? 2.40197 1.03515 1.20333 0.07997  -0.47663 0.04622  216 VAL   B O   
3418 C CB  . VAL   B 123 ? 2.18320 1.00451 1.11771 0.00856  -0.38555 0.06203  216 VAL   B CB  
3419 C CG1 . VAL   B 123 ? 2.13068 0.97686 1.07497 -0.04478 -0.34465 0.07905  216 VAL   B CG1 
3420 C CG2 . VAL   B 123 ? 2.06842 0.99307 1.08722 0.04208  -0.38345 0.04479  216 VAL   B CG2 
3421 N N   . THR   B 124 ? 2.21105 0.91870 1.05370 0.11199  -0.48028 0.03960  217 THR   B N   
3422 C CA  . THR   B 124 ? 2.25706 0.93688 1.08907 0.16559  -0.52383 0.01890  217 THR   B CA  
3423 C C   . THR   B 124 ? 2.40893 0.97783 1.15288 0.16928  -0.55056 0.01881  217 THR   B C   
3424 O O   . THR   B 124 ? 2.29640 0.84992 1.03805 0.21125  -0.58248 -0.00436 217 THR   B O   
3425 C CB  . THR   B 124 ? 2.23264 0.99471 1.12703 0.20262  -0.53193 0.00107  217 THR   B CB  
3426 O OG1 . THR   B 124 ? 2.27162 1.00924 1.12862 0.19290  -0.53189 0.01389  217 THR   B OG1 
3427 C CG2 . THR   B 124 ? 2.07332 0.96283 1.07211 0.19340  -0.49605 -0.00710 217 THR   B CG2 
3428 N N   . ASP   B 125 ? 2.64340 1.14699 1.32352 0.12368  -0.53391 0.03958  218 ASP   B N   
3429 C CA  . ASP   B 125 ? 2.77618 1.18184 1.37290 0.11874  -0.55311 0.03831  218 ASP   B CA  
3430 C C   . ASP   B 125 ? 2.75488 1.15506 1.34278 0.15295  -0.57680 0.02458  218 ASP   B C   
3431 O O   . ASP   B 125 ? 2.80439 1.13821 1.34183 0.17461  -0.60771 0.01120  218 ASP   B O   
3432 C CB  . ASP   B 125 ? 2.86590 1.21395 1.43016 0.13239  -0.57784 0.02593  218 ASP   B CB  
3433 C CG  . ASP   B 125 ? 3.00059 1.24340 1.46867 0.10858  -0.58826 0.03255  218 ASP   B CG  
3434 O OD1 . ASP   B 125 ? 3.08432 1.29865 1.51773 0.05752  -0.56141 0.05322  218 ASP   B OD1 
3435 O OD2 . ASP   B 125 ? 3.05020 1.24125 1.47781 0.14047  -0.62303 0.01605  218 ASP   B OD2 
3436 N N   . GLY   B 126 ? 2.58874 1.05877 1.22489 0.15792  -0.56335 0.02702  219 GLY   B N   
3437 C CA  . GLY   B 126 ? 2.65951 1.13078 1.29290 0.18748  -0.58327 0.01451  219 GLY   B CA  
3438 C C   . GLY   B 126 ? 2.59642 1.11295 1.28247 0.24407  -0.61352 -0.01540 219 GLY   B C   
3439 O O   . GLY   B 126 ? 2.63083 1.13515 1.30699 0.27170  -0.63610 -0.02971 219 GLY   B O   
3440 N N   . ALA   B 127 ? 2.45165 1.02215 1.19440 0.26186  -0.61406 -0.02672 220 ALA   B N   
3441 C CA  . ALA   B 127 ? 2.40403 1.02815 1.20390 0.31412  -0.63893 -0.05805 220 ALA   B CA  
3442 C C   . ALA   B 127 ? 2.35333 1.09280 1.24241 0.32822  -0.62526 -0.06531 220 ALA   B C   
3443 O O   . ALA   B 127 ? 2.29887 1.09354 1.24144 0.36946  -0.64280 -0.09303 220 ALA   B O   
3444 C CB  . ALA   B 127 ? 2.47410 1.09391 1.28537 0.32854  -0.64859 -0.07055 220 ALA   B CB  
3445 N N   . CYS   B 128 ? 2.28083 1.06002 1.18694 0.29388  -0.59412 -0.04291 221 CYS   B N   
3446 C CA  . CYS   B 128 ? 2.22482 1.11284 1.21090 0.30230  -0.58014 -0.04896 221 CYS   B CA  
3447 C C   . CYS   B 128 ? 2.19633 1.08438 1.16267 0.27188  -0.56048 -0.02850 221 CYS   B C   
3448 O O   . CYS   B 128 ? 2.22750 1.08173 1.15450 0.22964  -0.53670 -0.00290 221 CYS   B O   
3449 C CB  . CYS   B 128 ? 2.09879 1.05875 1.14358 0.29142  -0.55749 -0.04746 221 CYS   B CB  
3450 S SG  . CYS   B 128 ? 2.15428 1.12248 1.22645 0.32786  -0.57844 -0.07279 221 CYS   B SG  
3451 N N   . SER   B 129 ? 2.13673 1.06381 1.13106 0.29254  -0.56955 -0.04108 222 SER   B N   
3452 C CA  . SER   B 129 ? 2.05963 0.99202 1.03898 0.26732  -0.55222 -0.02463 222 SER   B CA  
3453 C C   . SER   B 129 ? 2.05096 1.07058 1.08706 0.24466  -0.52085 -0.01534 222 SER   B C   
3454 O O   . SER   B 129 ? 1.88824 0.98732 1.00152 0.25200  -0.50751 -0.02956 222 SER   B O   
3455 C CB  . SER   B 129 ? 2.03340 0.98202 1.02739 0.29737  -0.57316 -0.04272 222 SER   B CB  
3456 O OG  . SER   B 129 ? 2.42459 1.29740 1.37031 0.32186  -0.60423 -0.05545 222 SER   B OG  
3457 N N   . GLY   B 130 ? 2.00161 1.01846 1.01842 0.21014  -0.49523 0.00340  223 GLY   B N   
3458 C CA  . GLY   B 130 ? 1.78309 0.89691 0.87617 0.18509  -0.45395 0.00525  223 GLY   B CA  
3459 C C   . GLY   B 130 ? 1.85380 1.05956 1.02568 0.21336  -0.45974 -0.01696 223 GLY   B C   
3460 O O   . GLY   B 130 ? 1.63431 0.92914 0.88478 0.20478  -0.43266 -0.02335 223 GLY   B O   
3461 N N   . ASP   B 131 ? 1.87129 1.05570 1.02216 0.24690  -0.49580 -0.02953 224 ASP   B N   
3462 C CA  . ASP   B 131 ? 1.82113 1.09240 1.04709 0.27474  -0.50446 -0.05348 224 ASP   B CA  
3463 C C   . ASP   B 131 ? 1.72070 1.03234 0.99724 0.30906  -0.52193 -0.07824 224 ASP   B C   
3464 O O   . ASP   B 131 ? 1.65482 1.05988 1.01289 0.32131  -0.51422 -0.09748 224 ASP   B O   
3465 C CB  . ASP   B 131 ? 2.00397 1.24386 1.19612 0.29514  -0.53300 -0.05976 224 ASP   B CB  
3466 C CG  . ASP   B 131 ? 2.14051 1.33989 1.27868 0.26263  -0.51650 -0.03658 224 ASP   B CG  
3467 O OD1 . ASP   B 131 ? 2.27255 1.38964 1.33825 0.23923  -0.50961 -0.01621 224 ASP   B OD1 
3468 O OD2 . ASP   B 131 ? 2.17111 1.42203 1.34055 0.25899  -0.50866 -0.03988 224 ASP   B OD2 
3469 N N   . GLU   B 132 ? 1.78878 1.03076 1.01699 0.32411  -0.54483 -0.07880 225 GLU   B N   
3470 C CA  . GLU   B 132 ? 1.79747 1.07773 1.07300 0.35392  -0.55701 -0.10205 225 GLU   B CA  
3471 C C   . GLU   B 132 ? 1.60165 0.95743 0.94436 0.32878  -0.51580 -0.10022 225 GLU   B C   
3472 O O   . GLU   B 132 ? 1.55781 0.99213 0.97218 0.34748  -0.51258 -0.12222 225 GLU   B O   
3473 C CB  . GLU   B 132 ? 1.82604 1.01358 1.04080 0.36645  -0.57828 -0.10322 225 GLU   B CB  
3474 C CG  . GLU   B 132 ? 1.94496 1.08568 1.13225 0.39705  -0.60902 -0.12094 225 GLU   B CG  
3475 C CD  . GLU   B 132 ? 2.02656 1.08361 1.16074 0.41252  -0.63149 -0.12745 225 GLU   B CD  
3476 O OE1 . GLU   B 132 ? 2.05894 1.06308 1.14969 0.38830  -0.62174 -0.10828 225 GLU   B OE1 
3477 O OE2 . GLU   B 132 ? 2.07516 1.11955 1.21054 0.44823  -0.65925 -0.15301 225 GLU   B OE2 
3478 N N   . ILE   B 133 ? 1.61093 0.94436 0.93065 0.28623  -0.48411 -0.07494 226 ILE   B N   
3479 C CA  . ILE   B 133 ? 1.54542 0.94689 0.92490 0.26154  -0.44609 -0.07194 226 ILE   B CA  
3480 C C   . ILE   B 133 ? 1.52136 1.02148 0.97636 0.25506  -0.42255 -0.07893 226 ILE   B C   
3481 O O   . ILE   B 133 ? 1.41342 0.98961 0.93585 0.25623  -0.40483 -0.09053 226 ILE   B O   
3482 C CB  . ILE   B 133 ? 1.52527 0.87756 0.86066 0.21837  -0.42058 -0.04471 226 ILE   B CB  
3483 C CG1 . ILE   B 133 ? 1.63956 0.89479 0.90249 0.22285  -0.44314 -0.03905 226 ILE   B CG1 
3484 C CG2 . ILE   B 133 ? 1.33573 0.76068 0.73369 0.19311  -0.38239 -0.04157 226 ILE   B CG2 
3485 C CD1 . ILE   B 133 ? 1.75551 0.95904 0.97209 0.17860  -0.41943 -0.01366 226 ILE   B CD1 
3486 N N   . LEU   B 134 ? 1.49688 0.99404 0.93840 0.24759  -0.42227 -0.07209 227 LEU   B N   
3487 C CA  . LEU   B 134 ? 1.42050 1.00453 0.92876 0.24049  -0.40155 -0.07850 227 LEU   B CA  
3488 C C   . LEU   B 134 ? 1.38898 1.03933 0.95781 0.27552  -0.41900 -0.10792 227 LEU   B C   
3489 O O   . LEU   B 134 ? 1.34822 1.08274 0.98711 0.26941  -0.39692 -0.11708 227 LEU   B O   
3490 C CB  . LEU   B 134 ? 1.40637 0.96501 0.88028 0.22725  -0.40117 -0.06630 227 LEU   B CB  
3491 C CG  . LEU   B 134 ? 1.53208 1.10108 1.00609 0.18516  -0.36259 -0.04453 227 LEU   B CG  
3492 C CD1 . LEU   B 134 ? 1.43142 0.97879 0.89267 0.16117  -0.34176 -0.03032 227 LEU   B CD1 
3493 C CD2 . LEU   B 134 ? 1.56521 1.07527 0.97542 0.17333  -0.36800 -0.03015 227 LEU   B CD2 
3494 N N   . THR   B 135 ? 1.40755 1.02103 0.94984 0.31218  -0.45874 -0.12382 228 THR   B N   
3495 C CA  . THR   B 135 ? 1.39776 1.07741 1.00036 0.34723  -0.47618 -0.15519 228 THR   B CA  
3496 C C   . THR   B 135 ? 1.40731 1.13031 1.05422 0.35204  -0.46291 -0.16678 228 THR   B C   
3497 O O   . THR   B 135 ? 1.34499 1.15463 1.06408 0.36013  -0.45209 -0.18675 228 THR   B O   
3498 C CB  . THR   B 135 ? 1.50979 1.13548 1.07030 0.38804  -0.52490 -0.17056 228 THR   B CB  
3499 O OG1 . THR   B 135 ? 1.56536 1.15069 1.08220 0.38314  -0.53730 -0.15983 228 THR   B OG1 
3500 C CG2 . THR   B 135 ? 1.30803 1.00959 0.93674 0.42549  -0.54323 -0.20648 228 THR   B CG2 
3501 N N   . MET   B 136 ? 1.43219 1.09525 1.03508 0.34522  -0.46254 -0.15456 229 MET   B N   
3502 C CA  . MET   B 136 ? 1.30408 1.00019 0.94154 0.35182  -0.45304 -0.16623 229 MET   B CA  
3503 C C   . MET   B 136 ? 1.27502 1.04039 0.96565 0.31868  -0.40922 -0.15738 229 MET   B C   
3504 O O   . MET   B 136 ? 1.19257 1.02498 0.93954 0.32654  -0.39751 -0.17439 229 MET   B O   
3505 C CB  . MET   B 136 ? 1.41524 1.02182 0.98644 0.35307  -0.46716 -0.15572 229 MET   B CB  
3506 C CG  . MET   B 136 ? 1.38160 1.01059 0.97926 0.36704  -0.46541 -0.17122 229 MET   B CG  
3507 S SD  . MET   B 136 ? 1.63209 1.29506 1.26358 0.42401  -0.50170 -0.21185 229 MET   B SD  
3508 C CE  . MET   B 136 ? 1.25437 1.05221 0.98948 0.41793  -0.46756 -0.23037 229 MET   B CE  
3509 N N   . GLU   B 137 ? 1.25426 1.00398 0.92644 0.28206  -0.38486 -0.13168 230 GLU   B N   
3510 C CA  . GLU   B 137 ? 1.14835 0.95820 0.86700 0.25212  -0.34581 -0.12290 230 GLU   B CA  
3511 C C   . GLU   B 137 ? 1.14858 1.04798 0.93660 0.25628  -0.33382 -0.13866 230 GLU   B C   
3512 O O   . GLU   B 137 ? 1.06851 1.02803 0.90480 0.24513  -0.30884 -0.14228 230 GLU   B O   
3513 C CB  . GLU   B 137 ? 1.19611 0.97150 0.88141 0.21476  -0.32439 -0.09460 230 GLU   B CB  
3514 C CG  . GLU   B 137 ? 1.24492 1.02106 0.92267 0.20747  -0.32453 -0.08827 230 GLU   B CG  
3515 C CD  . GLU   B 137 ? 1.22594 1.01710 0.91014 0.16996  -0.29086 -0.06782 230 GLU   B CD  
3516 O OE1 . GLU   B 137 ? 1.22293 1.02297 0.91709 0.15001  -0.26882 -0.05840 230 GLU   B OE1 
3517 O OE2 . GLU   B 137 ? 1.28206 1.07673 0.96177 0.16163  -0.28745 -0.06244 230 GLU   B OE2 
3518 N N   . LEU   B 138 ? 1.14625 1.05383 0.93808 0.27135  -0.35178 -0.14840 231 LEU   B N   
3519 C CA  . LEU   B 138 ? 1.11477 1.10700 0.97292 0.27503  -0.34239 -0.16570 231 LEU   B CA  
3520 C C   . LEU   B 138 ? 1.10259 1.14711 1.00682 0.30312  -0.35162 -0.19477 231 LEU   B C   
3521 O O   . LEU   B 138 ? 1.00915 1.12881 0.97188 0.29532  -0.32919 -0.20526 231 LEU   B O   
3522 C CB  . LEU   B 138 ? 1.09598 1.08122 0.94454 0.28362  -0.36129 -0.16959 231 LEU   B CB  
3523 C CG  . LEU   B 138 ? 1.18051 1.15489 1.01357 0.25189  -0.34125 -0.14712 231 LEU   B CG  
3524 C CD1 . LEU   B 138 ? 1.15584 1.11045 0.96785 0.26427  -0.36554 -0.15187 231 LEU   B CD1 
3525 C CD2 . LEU   B 138 ? 1.08463 1.13433 0.97788 0.22847  -0.30669 -0.14664 231 LEU   B CD2 
3526 N N   . MET   B 139 ? 1.11124 1.11551 0.98789 0.33582  -0.38426 -0.20864 232 MET   B N   
3527 C CA  . MET   B 139 ? 1.13568 1.18918 1.05519 0.36528  -0.39394 -0.23882 232 MET   B CA  
3528 C C   . MET   B 139 ? 1.09491 1.17167 1.03283 0.35152  -0.36727 -0.23602 232 MET   B C   
3529 O O   . MET   B 139 ? 0.99177 1.14119 0.98536 0.35838  -0.35473 -0.25671 232 MET   B O   
3530 C CB  . MET   B 139 ? 1.23614 1.23208 1.11549 0.40520  -0.43729 -0.25367 232 MET   B CB  
3531 C CG  . MET   B 139 ? 1.17294 1.15985 1.04448 0.42761  -0.46876 -0.26507 232 MET   B CG  
3532 S SD  . MET   B 139 ? 1.65875 1.57778 1.48354 0.47912  -0.52298 -0.28534 232 MET   B SD  
3533 C CE  . MET   B 139 ? 1.37366 1.16629 1.09781 0.46033  -0.52803 -0.24937 232 MET   B CE  
3534 N N   . ILE   B 140 ? 1.14757 1.16444 1.03893 0.33094  -0.35787 -0.21128 233 ILE   B N   
3535 C CA  . ILE   B 140 ? 0.97145 1.00569 0.87613 0.31740  -0.33445 -0.20781 233 ILE   B CA  
3536 C C   . ILE   B 140 ? 0.96987 1.07719 0.92616 0.28959  -0.29757 -0.20292 233 ILE   B C   
3537 O O   . ILE   B 140 ? 0.93151 1.09680 0.93009 0.29200  -0.28219 -0.21760 233 ILE   B O   
3538 C CB  . ILE   B 140 ? 1.12955 1.08359 0.97357 0.29918  -0.33358 -0.18260 233 ILE   B CB  
3539 C CG1 . ILE   B 140 ? 1.17124 1.05091 0.96292 0.32781  -0.36983 -0.18990 233 ILE   B CG1 
3540 C CG2 . ILE   B 140 ? 1.05162 1.02921 0.91274 0.27899  -0.30591 -0.17603 233 ILE   B CG2 
3541 C CD1 . ILE   B 140 ? 1.24310 1.03979 0.97200 0.30779  -0.36997 -0.16594 233 ILE   B CD1 
3542 N N   . MET   B 141 ? 0.97160 1.07456 0.92209 0.26289  -0.28302 -0.18253 234 MET   B N   
3543 C CA  . MET   B 141 ? 0.92110 1.08290 0.91322 0.23557  -0.24940 -0.17550 234 MET   B CA  
3544 C C   . MET   B 141 ? 0.89828 1.13858 0.94928 0.24565  -0.24504 -0.19928 234 MET   B C   
3545 O O   . MET   B 141 ? 0.88333 1.17849 0.97266 0.23055  -0.21888 -0.20188 234 MET   B O   
3546 C CB  . MET   B 141 ? 0.92659 1.06312 0.89758 0.20818  -0.23782 -0.15072 234 MET   B CB  
3547 C CG  . MET   B 141 ? 0.98489 1.05514 0.90496 0.19091  -0.23455 -0.12696 234 MET   B CG  
3548 S SD  . MET   B 141 ? 1.07617 1.12643 0.97712 0.15818  -0.21683 -0.10074 234 MET   B SD  
3549 C CE  . MET   B 141 ? 0.91282 0.93757 0.79157 0.17594  -0.24421 -0.10729 234 MET   B CE  
3550 N N   . LYS   B 142 ? 0.81789 1.06421 0.87584 0.27018  -0.27052 -0.21725 235 LYS   B N   
3551 C CA  . LYS   B 142 ? 0.80916 1.13443 0.92685 0.27926  -0.26715 -0.24276 235 LYS   B CA  
3552 C C   . LYS   B 142 ? 0.83601 1.20337 0.98476 0.30016  -0.26748 -0.26851 235 LYS   B C   
3553 O O   . LYS   B 142 ? 0.83288 1.27328 1.03322 0.29320  -0.24706 -0.28356 235 LYS   B O   
3554 C CB  . LYS   B 142 ? 0.89263 1.21351 1.00994 0.29988  -0.29634 -0.25575 235 LYS   B CB  
3555 C CG  . LYS   B 142 ? 0.93870 1.23932 1.03908 0.27729  -0.29111 -0.23552 235 LYS   B CG  
3556 C CD  . LYS   B 142 ? 0.88387 1.15896 0.96600 0.30054  -0.32578 -0.24546 235 LYS   B CD  
3557 C CE  . LYS   B 142 ? 0.94126 1.28773 1.08095 0.32377  -0.33908 -0.28007 235 LYS   B CE  
3558 N NZ  . LYS   B 142 ? 0.97172 1.29291 1.09318 0.34831  -0.37598 -0.29082 235 LYS   B NZ  
3559 N N   . ALA   B 143 ? 0.82870 1.14942 0.94467 0.32512  -0.28994 -0.27442 236 ALA   B N   
3560 C CA  . ALA   B 143 ? 0.90340 1.26054 1.04547 0.34696  -0.29088 -0.30001 236 ALA   B CA  
3561 C C   . ALA   B 143 ? 0.83897 1.21672 0.98969 0.32261  -0.25740 -0.28980 236 ALA   B C   
3562 O O   . ALA   B 143 ? 0.92987 1.36605 1.11902 0.32931  -0.24455 -0.31102 236 ALA   B O   
3563 C CB  . ALA   B 143 ? 0.92406 1.21761 1.02333 0.38084  -0.32587 -0.30850 236 ALA   B CB  
3564 N N   . LEU   B 144 ? 0.89906 1.23093 1.01439 0.29470  -0.24319 -0.25879 237 LEU   B N   
3565 C CA  . LEU   B 144 ? 0.79433 1.14195 0.91481 0.27066  -0.21325 -0.24715 237 LEU   B CA  
3566 C C   . LEU   B 144 ? 0.81079 1.21683 0.96964 0.24239  -0.18246 -0.24134 237 LEU   B C   
3567 O O   . LEU   B 144 ? 0.84041 1.25474 0.99926 0.21977  -0.15768 -0.22822 237 LEU   B O   
3568 C CB  . LEU   B 144 ? 0.88445 1.16000 0.95296 0.25359  -0.21278 -0.21845 237 LEU   B CB  
3569 C CG  . LEU   B 144 ? 0.94651 1.15539 0.96967 0.27527  -0.23967 -0.22076 237 LEU   B CG  
3570 C CD1 . LEU   B 144 ? 0.78643 0.93085 0.76282 0.25158  -0.23494 -0.19191 237 LEU   B CD1 
3571 C CD2 . LEU   B 144 ? 0.85655 1.08995 0.89470 0.29645  -0.24139 -0.24408 237 LEU   B CD2 
3572 N N   . LYS   B 145 ? 0.76337 1.20678 0.95245 0.24341  -0.18504 -0.25109 238 LYS   B N   
3573 C CA  . LYS   B 145 ? 0.73860 1.23192 0.96120 0.21576  -0.15802 -0.24571 238 LYS   B CA  
3574 C C   . LYS   B 145 ? 0.77327 1.22930 0.96794 0.18500  -0.14123 -0.21298 238 LYS   B C   
3575 O O   . LYS   B 145 ? 0.75861 1.24385 0.96998 0.16023  -0.11470 -0.20429 238 LYS   B O   
3576 C CB  . LYS   B 145 ? 0.84280 1.40251 1.10522 0.21088  -0.13456 -0.26319 238 LYS   B CB  
3577 C CG  . LYS   B 145 ? 0.77173 1.38134 1.07067 0.24028  -0.14780 -0.29939 238 LYS   B CG  
3578 C CD  . LYS   B 145 ? 0.98502 1.62332 1.31253 0.24802  -0.16233 -0.31325 238 LYS   B CD  
3579 C CE  . LYS   B 145 ? 1.00173 1.68835 1.36198 0.21594  -0.13531 -0.30831 238 LYS   B CE  
3580 N NZ  . LYS   B 145 ? 1.05168 1.80662 1.45135 0.20552  -0.10806 -0.32582 238 LYS   B NZ  
3581 N N   . TRP   B 146 ? 0.72458 1.11477 0.87516 0.18664  -0.15699 -0.19549 239 TRP   B N   
3582 C CA  . TRP   B 146 ? 0.80830 1.16101 0.93144 0.16024  -0.14403 -0.16651 239 TRP   B CA  
3583 C C   . TRP   B 146 ? 0.81346 1.16884 0.93353 0.14311  -0.12205 -0.15522 239 TRP   B C   
3584 O O   . TRP   B 146 ? 0.76271 1.10888 0.87549 0.11910  -0.10545 -0.13511 239 TRP   B O   
3585 C CB  . TRP   B 146 ? 0.76847 1.14267 0.90890 0.14183  -0.13304 -0.15899 239 TRP   B CB  
3586 C CG  . TRP   B 146 ? 0.77360 1.13866 0.91129 0.15670  -0.15581 -0.16756 239 TRP   B CG  
3587 C CD1 . TRP   B 146 ? 0.65959 1.06976 0.83230 0.17216  -0.16594 -0.19139 239 TRP   B CD1 
3588 C CD2 . TRP   B 146 ? 0.81562 1.12285 0.91200 0.15733  -0.17180 -0.15327 239 TRP   B CD2 
3589 N NE1 . TRP   B 146 ? 0.76570 1.14808 0.92080 0.18401  -0.18946 -0.19266 239 TRP   B NE1 
3590 C CE2 . TRP   B 146 ? 0.78571 1.10278 0.89132 0.17481  -0.19288 -0.16878 239 TRP   B CE2 
3591 C CE3 . TRP   B 146 ? 0.80171 1.05114 0.85405 0.14386  -0.16978 -0.12975 239 TRP   B CE3 
3592 C CZ2 . TRP   B 146 ? 0.82116 1.08750 0.88835 0.17971  -0.21239 -0.16019 239 TRP   B CZ2 
3593 C CZ3 . TRP   B 146 ? 0.78633 0.98797 0.80210 0.14682  -0.18662 -0.12156 239 TRP   B CZ3 
3594 C CH2 . TRP   B 146 ? 0.93290 1.14080 0.95371 0.16487  -0.20795 -0.13606 239 TRP   B CH2 
3595 N N   . ARG   B 147 ? 0.77274 1.14017 0.89747 0.15642  -0.12280 -0.16892 240 ARG   B N   
3596 C CA  . ARG   B 147 ? 0.78329 1.14836 0.90003 0.14305  -0.10558 -0.15963 240 ARG   B CA  
3597 C C   . ARG   B 147 ? 0.73576 1.03644 0.80906 0.14577  -0.11964 -0.14687 240 ARG   B C   
3598 O O   . ARG   B 147 ? 0.82061 1.10143 0.87926 0.16494  -0.13441 -0.15815 240 ARG   B O   
3599 C CB  . ARG   B 147 ? 0.80230 1.21281 0.94365 0.15464  -0.09799 -0.18157 240 ARG   B CB  
3600 C CG  . ARG   B 147 ? 0.78619 1.26248 0.97172 0.15187  -0.08496 -0.19776 240 ARG   B CG  
3601 C CD  . ARG   B 147 ? 0.88259 1.37273 1.07681 0.12163  -0.06275 -0.17961 240 ARG   B CD  
3602 N NE  . ARG   B 147 ? 0.90329 1.40430 1.09447 0.10376  -0.03977 -0.17112 240 ARG   B NE  
3603 C CZ  . ARG   B 147 ? 1.05931 1.60906 1.27543 0.09220  -0.01853 -0.17986 240 ARG   B CZ  
3604 N NH1 . ARG   B 147 ? 0.93681 1.53451 1.18791 0.09467  -0.01548 -0.19829 240 ARG   B NH1 
3605 N NH2 . ARG   B 147 ? 1.03391 1.58355 1.23824 0.07678  -0.00008 -0.17019 240 ARG   B NH2 
3606 N N   . LEU   B 148 ? 0.78496 1.05267 0.83741 0.12564  -0.11473 -0.12399 241 LEU   B N   
3607 C CA  . LEU   B 148 ? 0.73814 0.94397 0.74908 0.12337  -0.12703 -0.11078 241 LEU   B CA  
3608 C C   . LEU   B 148 ? 0.88617 1.08139 0.88774 0.10049  -0.11069 -0.09337 241 LEU   B C   
3609 O O   . LEU   B 148 ? 0.86675 1.01915 0.84044 0.08858  -0.11395 -0.07820 241 LEU   B O   
3610 C CB  . LEU   B 148 ? 0.87106 1.04227 0.86103 0.12093  -0.13862 -0.10104 241 LEU   B CB  
3611 C CG  . LEU   B 148 ? 0.86870 1.05086 0.86827 0.14281  -0.15650 -0.11736 241 LEU   B CG  
3612 C CD1 . LEU   B 148 ? 0.83747 0.98890 0.81585 0.13549  -0.16351 -0.10513 241 LEU   B CD1 
3613 C CD2 . LEU   B 148 ? 0.78998 0.94672 0.77235 0.17129  -0.18129 -0.13390 241 LEU   B CD2 
3614 N N   . SER   B 149 ? 0.75485 0.98843 0.77835 0.09379  -0.09339 -0.09606 242 SER   B N   
3615 C CA  . SER   B 149 ? 0.73458 0.96168 0.75113 0.07457  -0.07982 -0.08157 242 SER   B CA  
3616 C C   . SER   B 149 ? 0.87938 1.11522 0.89480 0.08179  -0.07802 -0.09140 242 SER   B C   
3617 O O   . SER   B 149 ? 0.85641 1.12465 0.88704 0.07375  -0.06165 -0.09154 242 SER   B O   
3618 C CB  . SER   B 149 ? 0.76188 1.02079 0.79977 0.05612  -0.05987 -0.07148 242 SER   B CB  
3619 O OG  . SER   B 149 ? 0.91168 1.16122 0.94900 0.04959  -0.06147 -0.06309 242 SER   B OG  
3620 N N   . PRO   B 150 ? 0.88519 1.08896 0.87896 0.09673  -0.09503 -0.09967 243 PRO   B N   
3621 C CA  . PRO   B 150 ? 0.75832 0.96722 0.74800 0.10445  -0.09434 -0.11008 243 PRO   B CA  
3622 C C   . PRO   B 150 ? 0.88584 1.06742 0.85591 0.08774  -0.09135 -0.09604 243 PRO   B C   
3623 O O   . PRO   B 150 ? 0.92265 1.07530 0.87948 0.07257  -0.09314 -0.08032 243 PRO   B O   
3624 C CB  . PRO   B 150 ? 0.85859 1.04018 0.83209 0.12993  -0.11713 -0.12631 243 PRO   B CB  
3625 C CG  . PRO   B 150 ? 0.88385 1.01810 0.83353 0.12561  -0.13104 -0.11391 243 PRO   B CG  
3626 C CD  . PRO   B 150 ? 0.87980 1.03680 0.84762 0.10813  -0.11694 -0.10057 243 PRO   B CD  
3627 N N   . LEU   B 151 ? 0.79602 0.98949 0.76499 0.09054  -0.08651 -0.10337 244 LEU   B N   
3628 C CA  . LEU   B 151 ? 0.91504 1.08312 0.86513 0.07837  -0.08742 -0.09444 244 LEU   B CA  
3629 C C   . LEU   B 151 ? 0.96132 1.08528 0.88404 0.09171  -0.10772 -0.10338 244 LEU   B C   
3630 O O   . LEU   B 151 ? 1.03193 1.16060 0.95062 0.10911  -0.11286 -0.12016 244 LEU   B O   
3631 C CB  . LEU   B 151 ? 0.78329 0.98275 0.74144 0.07405  -0.07291 -0.09708 244 LEU   B CB  
3632 C CG  . LEU   B 151 ? 0.91485 1.15054 0.89409 0.05961  -0.05361 -0.08713 244 LEU   B CG  
3633 C CD1 . LEU   B 151 ? 0.78179 1.03733 0.75886 0.05448  -0.04148 -0.08812 244 LEU   B CD1 
3634 C CD2 . LEU   B 151 ? 0.89350 1.11367 0.87344 0.04165  -0.05234 -0.06813 244 LEU   B CD2 
3635 N N   . THR   B 152 ? 0.88104 0.96021 0.78280 0.08290  -0.11888 -0.09263 245 THR   B N   
3636 C CA  . THR   B 152 ? 0.93571 0.96365 0.80608 0.09414  -0.13989 -0.09953 245 THR   B CA  
3637 C C   . THR   B 152 ? 0.94011 0.95293 0.79548 0.09244  -0.14354 -0.10436 245 THR   B C   
3638 O O   . THR   B 152 ? 0.90095 0.93985 0.76815 0.08067  -0.13060 -0.10025 245 THR   B O   
3639 C CB  . THR   B 152 ? 0.92746 0.90875 0.77490 0.07954  -0.14799 -0.08472 245 THR   B CB  
3640 O OG1 . THR   B 152 ? 0.97028 0.95253 0.82058 0.05236  -0.13630 -0.06907 245 THR   B OG1 
3641 C CG2 . THR   B 152 ? 0.90662 0.89837 0.76407 0.08333  -0.14681 -0.08126 245 THR   B CG2 
3642 N N   . ILE   B 153 ? 0.92543 0.89186 0.75149 0.10527  -0.16325 -0.11366 246 ILE   B N   
3643 C CA  . ILE   B 153 ? 0.93888 0.88314 0.74626 0.10373  -0.16976 -0.11919 246 ILE   B CA  
3644 C C   . ILE   B 153 ? 0.98081 0.90860 0.78187 0.07365  -0.16486 -0.10195 246 ILE   B C   
3645 O O   . ILE   B 153 ? 0.96057 0.89897 0.76382 0.06536  -0.16046 -0.10260 246 ILE   B O   
3646 C CB  . ILE   B 153 ? 0.99195 0.88248 0.76580 0.12364  -0.19393 -0.13249 246 ILE   B CB  
3647 C CG1 . ILE   B 153 ? 0.99403 0.90769 0.77949 0.15628  -0.19964 -0.15283 246 ILE   B CG1 
3648 C CG2 . ILE   B 153 ? 1.00259 0.86741 0.75546 0.12154  -0.20157 -0.13908 246 ILE   B CG2 
3649 C CD1 . ILE   B 153 ? 1.03013 0.88978 0.78253 0.18046  -0.22606 -0.16763 246 ILE   B CD1 
3650 N N   . VAL   B 154 ? 0.94422 0.84769 0.73768 0.05692  -0.16553 -0.08740 247 VAL   B N   
3651 C CA  . VAL   B 154 ? 0.86959 0.76045 0.65986 0.02759  -0.16040 -0.07321 247 VAL   B CA  
3652 C C   . VAL   B 154 ? 0.84510 0.78882 0.66968 0.01370  -0.14046 -0.06385 247 VAL   B C   
3653 O O   . VAL   B 154 ? 0.91692 0.86438 0.74656 -0.00585 -0.13611 -0.05723 247 VAL   B O   
3654 C CB  . VAL   B 154 ? 0.93837 0.78267 0.70471 0.01310  -0.16674 -0.06204 247 VAL   B CB  
3655 C CG1 . VAL   B 154 ? 0.98826 0.85717 0.77224 0.01062  -0.15536 -0.05272 247 VAL   B CG1 
3656 C CG2 . VAL   B 154 ? 0.94429 0.76678 0.70120 -0.01686 -0.16491 -0.05251 247 VAL   B CG2 
3657 N N   . SER   B 155 ? 0.83057 0.81462 0.67877 0.02353  -0.12932 -0.06411 248 SER   B N   
3658 C CA  . SER   B 155 ? 0.86334 0.89225 0.74000 0.01186  -0.11184 -0.05557 248 SER   B CA  
3659 C C   . SER   B 155 ? 0.87055 0.92230 0.75301 0.01473  -0.10820 -0.06171 248 SER   B C   
3660 O O   . SER   B 155 ? 0.95007 1.02172 0.84557 0.00096  -0.09990 -0.05382 248 SER   B O   
3661 C CB  . SER   B 155 ? 0.78041 0.84193 0.67754 0.02031  -0.10160 -0.05477 248 SER   B CB  
3662 O OG  . SER   B 155 ? 0.89076 0.96986 0.79154 0.04220  -0.10315 -0.06963 248 SER   B OG  
3663 N N   . TRP   B 156 ? 0.88500 0.93361 0.75647 0.03354  -0.11497 -0.07656 249 TRP   B N   
3664 C CA  . TRP   B 156 ? 0.85532 0.91998 0.72530 0.03624  -0.11234 -0.08315 249 TRP   B CA  
3665 C C   . TRP   B 156 ? 0.85973 0.89728 0.71533 0.02204  -0.12203 -0.08024 249 TRP   B C   
3666 O O   . TRP   B 156 ? 0.85601 0.91085 0.71699 0.01420  -0.11776 -0.07765 249 TRP   B O   
3667 C CB  . TRP   B 156 ? 0.89643 0.96350 0.75672 0.06006  -0.11692 -0.10188 249 TRP   B CB  
3668 C CG  . TRP   B 156 ? 0.90006 1.00952 0.78053 0.07159  -0.10319 -0.10762 249 TRP   B CG  
3669 C CD1 . TRP   B 156 ? 0.86828 0.98416 0.75608 0.08779  -0.10559 -0.11702 249 TRP   B CD1 
3670 C CD2 . TRP   B 156 ? 0.84900 0.99964 0.74411 0.06665  -0.08538 -0.10501 249 TRP   B CD2 
3671 N NE1 . TRP   B 156 ? 0.83592 0.99883 0.74587 0.09170  -0.08913 -0.12136 249 TRP   B NE1 
3672 C CE2 . TRP   B 156 ? 0.89082 1.07318 0.80325 0.07790  -0.07585 -0.11328 249 TRP   B CE2 
3673 C CE3 . TRP   B 156 ? 0.93877 1.10046 0.83214 0.05375  -0.07766 -0.09677 249 TRP   B CE3 
3674 C CZ2 . TRP   B 156 ? 0.84244 1.06539 0.76895 0.07368  -0.05697 -0.11278 249 TRP   B CZ2 
3675 C CZ3 . TRP   B 156 ? 0.95944 1.15693 0.86286 0.05172  -0.06054 -0.09540 249 TRP   B CZ3 
3676 C CH2 . TRP   B 156 ? 0.99602 1.22297 0.91514 0.06018  -0.04937 -0.10296 249 TRP   B CH2 
3677 N N   . LEU   B 157 ? 0.94000 0.93330 0.77566 0.01807  -0.13601 -0.08104 250 LEU   B N   
3678 C CA  . LEU   B 157 ? 0.90523 0.87253 0.72868 0.00108  -0.14506 -0.07893 250 LEU   B CA  
3679 C C   . LEU   B 157 ? 0.93793 0.92679 0.78312 -0.02213 -0.13546 -0.06530 250 LEU   B C   
3680 O O   . LEU   B 157 ? 0.85281 0.84489 0.70042 -0.03373 -0.13878 -0.06553 250 LEU   B O   
3681 C CB  . LEU   B 157 ? 0.96590 0.87767 0.76129 -0.00205 -0.16034 -0.08072 250 LEU   B CB  
3682 C CG  . LEU   B 157 ? 0.99275 0.87263 0.77372 -0.02339 -0.16998 -0.07918 250 LEU   B CG  
3683 C CD1 . LEU   B 157 ? 0.98647 0.86901 0.76017 -0.01626 -0.17747 -0.09113 250 LEU   B CD1 
3684 C CD2 . LEU   B 157 ? 1.18215 1.00134 0.93032 -0.02833 -0.18376 -0.07909 250 LEU   B CD2 
3685 N N   . ASN   B 158 ? 1.01696 1.02172 0.87874 -0.02804 -0.12455 -0.05488 251 ASN   B N   
3686 C CA  . ASN   B 158 ? 1.00071 1.03061 0.88582 -0.04687 -0.11462 -0.04393 251 ASN   B CA  
3687 C C   . ASN   B 158 ? 0.98180 1.04976 0.88340 -0.04224 -0.10809 -0.04441 251 ASN   B C   
3688 O O   . ASN   B 158 ? 1.00422 1.08547 0.91814 -0.05474 -0.10817 -0.04119 251 ASN   B O   
3689 C CB  . ASN   B 158 ? 0.96668 1.00497 0.86349 -0.05121 -0.10419 -0.03423 251 ASN   B CB  
3690 C CG  . ASN   B 158 ? 1.07970 1.09935 0.97506 -0.07417 -0.10346 -0.02642 251 ASN   B CG  
3691 O OD1 . ASN   B 158 ? 1.16653 1.14735 1.03877 -0.07804 -0.10989 -0.02570 251 ASN   B OD1 
3692 N ND2 . ASN   B 158 ? 1.02087 1.06751 0.93958 -0.08950 -0.09566 -0.02122 251 ASN   B ND2 
3693 N N   . VAL   B 159 ? 1.03110 1.11646 0.93204 -0.02460 -0.10273 -0.04908 252 VAL   B N   
3694 C CA  . VAL   B 159 ? 0.86669 0.98110 0.77476 -0.02074 -0.09644 -0.04903 252 VAL   B CA  
3695 C C   . VAL   B 159 ? 0.99920 1.10194 0.89165 -0.02025 -0.10785 -0.05696 252 VAL   B C   
3696 O O   . VAL   B 159 ? 0.97587 1.09225 0.87412 -0.02650 -0.10888 -0.05401 252 VAL   B O   
3697 C CB  . VAL   B 159 ? 0.99310 1.12754 0.90144 -0.00495 -0.08620 -0.05328 252 VAL   B CB  
3698 C CG1 . VAL   B 159 ? 1.07563 1.23423 0.98463 -0.00372 -0.07857 -0.05162 252 VAL   B CG1 
3699 C CG2 . VAL   B 159 ? 0.87196 1.01741 0.79618 -0.00565 -0.07683 -0.04668 252 VAL   B CG2 
3700 N N   . TYR   B 160 ? 0.98992 1.06539 0.86101 -0.01160 -0.11829 -0.06803 253 TYR   B N   
3701 C CA  . TYR   B 160 ? 1.02451 1.08637 0.87771 -0.00983 -0.12997 -0.07732 253 TYR   B CA  
3702 C C   . TYR   B 160 ? 1.08916 1.13984 0.94765 -0.02939 -0.13969 -0.07373 253 TYR   B C   
3703 O O   . TYR   B 160 ? 1.05642 1.11047 0.91037 -0.03172 -0.14722 -0.07786 253 TYR   B O   
3704 C CB  . TYR   B 160 ? 1.05464 1.08655 0.88320 0.00477  -0.13990 -0.09119 253 TYR   B CB  
3705 C CG  . TYR   B 160 ? 1.02657 1.07447 0.85308 0.02549  -0.13106 -0.09908 253 TYR   B CG  
3706 C CD1 . TYR   B 160 ? 0.98957 1.07562 0.82941 0.02873  -0.11504 -0.09516 253 TYR   B CD1 
3707 C CD2 . TYR   B 160 ? 0.94275 0.96738 0.75392 0.04162  -0.13921 -0.11160 253 TYR   B CD2 
3708 C CE1 . TYR   B 160 ? 0.98073 1.08582 0.82175 0.04487  -0.10539 -0.10395 253 TYR   B CE1 
3709 C CE2 . TYR   B 160 ? 0.88151 0.92706 0.69588 0.06110  -0.13122 -0.12169 253 TYR   B CE2 
3710 C CZ  . TYR   B 160 ? 0.92909 1.01715 0.75992 0.06138  -0.11332 -0.11806 253 TYR   B CZ  
3711 O OH  . TYR   B 160 ? 0.98390 1.09715 0.82085 0.07804  -0.10377 -0.12955 253 TYR   B OH  
3712 N N   . MET   B 161 ? 1.01505 1.05351 0.88276 -0.04425 -0.13951 -0.06693 254 MET   B N   
3713 C CA  . MET   B 161 ? 1.10102 1.13381 0.97759 -0.06577 -0.14635 -0.06496 254 MET   B CA  
3714 C C   . MET   B 161 ? 1.13052 1.20211 1.03594 -0.07396 -0.13949 -0.05794 254 MET   B C   
3715 O O   . MET   B 161 ? 1.16383 1.24200 1.07914 -0.08621 -0.14743 -0.06074 254 MET   B O   
3716 C CB  . MET   B 161 ? 0.98826 0.99377 0.86149 -0.08117 -0.14633 -0.06024 254 MET   B CB  
3717 C CG  . MET   B 161 ? 0.94353 0.89978 0.78366 -0.07692 -0.15903 -0.06807 254 MET   B CG  
3718 S SD  . MET   B 161 ? 1.20468 1.13909 1.02816 -0.08280 -0.17688 -0.08047 254 MET   B SD  
3719 C CE  . MET   B 161 ? 1.17532 1.12867 1.02690 -0.11513 -0.17477 -0.07477 254 MET   B CE  
3720 N N   . GLN   B 162 ? 1.09138 1.18844 1.01082 -0.06693 -0.12616 -0.05001 255 GLN   B N   
3721 C CA  . GLN   B 162 ? 1.11913 1.24918 1.06347 -0.07200 -0.12105 -0.04381 255 GLN   B CA  
3722 C C   . GLN   B 162 ? 1.21526 1.35671 1.15213 -0.06202 -0.12780 -0.04800 255 GLN   B C   
3723 O O   . GLN   B 162 ? 1.16448 1.32054 1.11489 -0.06828 -0.13504 -0.04886 255 GLN   B O   
3724 C CB  . GLN   B 162 ? 1.10835 1.25651 1.06586 -0.06769 -0.10572 -0.03432 255 GLN   B CB  
3725 C CG  . GLN   B 162 ? 1.16325 1.34147 1.14530 -0.07161 -0.10094 -0.02808 255 GLN   B CG  
3726 C CD  . GLN   B 162 ? 1.18354 1.37001 1.18818 -0.08958 -0.10371 -0.02846 255 GLN   B CD  
3727 O OE1 . GLN   B 162 ? 1.21159 1.38208 1.21516 -0.10240 -0.10248 -0.02880 255 GLN   B OE1 
3728 N NE2 . GLN   B 162 ? 1.25719 1.46831 1.28136 -0.09077 -0.10765 -0.02914 255 GLN   B NE2 
3729 N N   . VAL   B 163 ? 1.11103 1.24644 1.02554 -0.04623 -0.12577 -0.05159 256 VAL   B N   
3730 C CA  . VAL   B 163 ? 1.19795 1.33963 1.09769 -0.03716 -0.13096 -0.05507 256 VAL   B CA  
3731 C C   . VAL   B 163 ? 1.18085 1.30703 1.06942 -0.04121 -0.14883 -0.06504 256 VAL   B C   
3732 O O   . VAL   B 163 ? 1.11982 1.25392 1.00497 -0.03964 -0.15784 -0.06682 256 VAL   B O   
3733 C CB  . VAL   B 163 ? 1.04492 1.18510 0.92250 -0.02162 -0.12164 -0.05803 256 VAL   B CB  
3734 C CG1 . VAL   B 163 ? 1.09030 1.23464 0.94705 -0.01409 -0.12464 -0.06012 256 VAL   B CG1 
3735 C CG2 . VAL   B 163 ? 1.05967 1.21612 0.95110 -0.01981 -0.10470 -0.04943 256 VAL   B CG2 
3736 N N   . ALA   B 164 ? 1.08754 1.18873 0.96818 -0.04644 -0.15571 -0.07192 257 ALA   B N   
3737 C CA  . ALA   B 164 ? 1.24330 1.32709 1.11309 -0.05246 -0.17328 -0.08219 257 ALA   B CA  
3738 C C   . ALA   B 164 ? 1.29902 1.40070 1.19596 -0.06896 -0.18083 -0.08076 257 ALA   B C   
3739 O O   . ALA   B 164 ? 1.23911 1.34203 1.13244 -0.07036 -0.19552 -0.08830 257 ALA   B O   
3740 C CB  . ALA   B 164 ? 1.17669 1.22494 1.03096 -0.05642 -0.17900 -0.08886 257 ALA   B CB  
3741 N N   . TYR   B 165 ? 1.23717 1.35481 1.16221 -0.08102 -0.17128 -0.07261 258 TYR   B N   
3742 C CA  . TYR   B 165 ? 1.18085 1.32263 1.13719 -0.09610 -0.17636 -0.07322 258 TYR   B CA  
3743 C C   . TYR   B 165 ? 1.23273 1.40736 1.21015 -0.08903 -0.16832 -0.06504 258 TYR   B C   
3744 O O   . TYR   B 165 ? 1.39251 1.58654 1.39807 -0.09903 -0.15950 -0.06006 258 TYR   B O   
3745 C CB  . TYR   B 165 ? 1.18254 1.31710 1.15448 -0.11839 -0.17195 -0.07255 258 TYR   B CB  
3746 C CG  . TYR   B 165 ? 1.25064 1.35213 1.20421 -0.13020 -0.18441 -0.08201 258 TYR   B CG  
3747 C CD1 . TYR   B 165 ? 1.20958 1.27105 1.13000 -0.12354 -0.18511 -0.08316 258 TYR   B CD1 
3748 C CD2 . TYR   B 165 ? 1.22255 1.33251 1.19217 -0.14754 -0.19667 -0.09111 258 TYR   B CD2 
3749 C CE1 . TYR   B 165 ? 1.26647 1.29192 1.16636 -0.13369 -0.19793 -0.09205 258 TYR   B CE1 
3750 C CE2 . TYR   B 165 ? 1.16323 1.23975 1.11424 -0.16028 -0.20848 -0.09999 258 TYR   B CE2 
3751 C CZ  . TYR   B 165 ? 1.21376 1.24540 1.12796 -0.15320 -0.20921 -0.09988 258 TYR   B CZ  
3752 O OH  . TYR   B 165 ? 1.29462 1.28747 1.18685 -0.16534 -0.22228 -0.10889 258 TYR   B OH  
3753 N N   . LEU   B 166 ? 1.22650 1.40469 1.18731 -0.07209 -0.17114 -0.06388 259 LEU   B N   
3754 C CA  . LEU   B 166 ? 1.36156 1.56339 1.33504 -0.06413 -0.16687 -0.05645 259 LEU   B CA  
3755 C C   . LEU   B 166 ? 1.54594 1.76061 1.52559 -0.06130 -0.18533 -0.06292 259 LEU   B C   
3756 O O   . LEU   B 166 ? 1.46050 1.66133 1.41957 -0.05815 -0.19980 -0.07137 259 LEU   B O   
3757 C CB  . LEU   B 166 ? 1.36773 1.56155 1.31444 -0.04866 -0.15616 -0.04940 259 LEU   B CB  
3758 C CG  . LEU   B 166 ? 1.32890 1.52536 1.28210 -0.04869 -0.13674 -0.04049 259 LEU   B CG  
3759 C CD1 . LEU   B 166 ? 1.30506 1.49738 1.23328 -0.03557 -0.12678 -0.03585 259 LEU   B CD1 
3760 C CD2 . LEU   B 166 ? 1.30280 1.52170 1.28890 -0.05565 -0.13083 -0.03391 259 LEU   B CD2 
3761 N N   . ASN   B 167 ? 1.72221 1.96290 1.72973 -0.06105 -0.18607 -0.06006 260 ASN   B N   
3762 C CA  . ASN   B 167 ? 1.89119 2.14708 1.90791 -0.05507 -0.20526 -0.06657 260 ASN   B CA  
3763 C C   . ASN   B 167 ? 2.13494 2.38764 2.13181 -0.03717 -0.20517 -0.05769 260 ASN   B C   
3764 O O   . ASN   B 167 ? 2.09904 2.33620 2.07104 -0.03118 -0.19048 -0.04799 260 ASN   B O   
3765 C CB  . ASN   B 167 ? 1.87042 2.15966 1.93570 -0.06748 -0.20842 -0.07307 260 ASN   B CB  
3766 C CG  . ASN   B 167 ? 1.78309 2.07146 1.86456 -0.08959 -0.20206 -0.07845 260 ASN   B CG  
3767 O OD1 . ASN   B 167 ? 1.71521 2.01564 1.81963 -0.10121 -0.18680 -0.07465 260 ASN   B OD1 
3768 N ND2 . ASN   B 167 ? 1.75702 2.02744 1.82279 -0.09608 -0.21397 -0.08727 260 ASN   B ND2 
3769 N N   . ASP   B 168 ? 2.26951 2.53617 2.27673 -0.02888 -0.22243 -0.06172 261 ASP   B N   
3770 C CA  . ASP   B 168 ? 2.35089 2.60932 2.33667 -0.01255 -0.22424 -0.05263 261 ASP   B CA  
3771 C C   . ASP   B 168 ? 2.29121 2.56303 2.29910 -0.01245 -0.20832 -0.04337 261 ASP   B C   
3772 O O   . ASP   B 168 ? 2.32741 2.58733 2.31467 -0.00081 -0.20680 -0.03413 261 ASP   B O   
3773 C CB  . ASP   B 168 ? 2.47706 2.74170 2.46345 -0.00094 -0.25130 -0.06057 261 ASP   B CB  
3774 C CG  . ASP   B 168 ? 2.58708 2.82779 2.53345 0.00443  -0.26728 -0.06616 261 ASP   B CG  
3775 O OD1 . ASP   B 168 ? 2.64765 2.86217 2.55478 0.00483  -0.25554 -0.06031 261 ASP   B OD1 
3776 O OD2 . ASP   B 168 ? 2.63890 2.88859 2.59368 0.00866  -0.29179 -0.07772 261 ASP   B OD2 
3777 N N   . LEU   B 169 ? 2.04799 2.34113 2.09375 -0.02591 -0.19653 -0.04561 262 LEU   B N   
3778 C CA  . LEU   B 169 ? 1.96172 2.26566 2.02566 -0.02626 -0.18016 -0.03733 262 LEU   B CA  
3779 C C   . LEU   B 169 ? 1.94366 2.22478 1.97787 -0.02520 -0.16106 -0.02494 262 LEU   B C   
3780 O O   . LEU   B 169 ? 1.90713 2.18773 1.94094 -0.02030 -0.15112 -0.01617 262 LEU   B O   
3781 C CB  . LEU   B 169 ? 1.83798 2.16834 1.94500 -0.04254 -0.17122 -0.04328 262 LEU   B CB  
3782 C CG  . LEU   B 169 ? 1.65722 2.02253 1.80682 -0.04591 -0.18454 -0.05674 262 LEU   B CG  
3783 C CD1 . LEU   B 169 ? 1.64276 2.01012 1.79390 -0.05282 -0.20177 -0.06916 262 LEU   B CD1 
3784 C CD2 . LEU   B 169 ? 1.43890 1.82970 1.62661 -0.06118 -0.16801 -0.05890 262 LEU   B CD2 
3785 N N   . HIS   B 170 ? 1.97656 2.23985 1.98713 -0.02944 -0.15633 -0.02556 263 HIS   B N   
3786 C CA  . HIS   B 170 ? 1.91366 2.15984 1.89858 -0.02798 -0.13917 -0.01733 263 HIS   B CA  
3787 C C   . HIS   B 170 ? 1.83699 2.09274 1.84310 -0.03455 -0.12108 -0.01110 263 HIS   B C   
3788 O O   . HIS   B 170 ? 1.79365 2.04133 1.78485 -0.03173 -0.10734 -0.00360 263 HIS   B O   
3789 C CB  . HIS   B 170 ? 1.90780 2.13778 1.85740 -0.01628 -0.13949 -0.01010 263 HIS   B CB  
3790 C CG  . HIS   B 170 ? 1.98674 2.19931 1.90182 -0.01024 -0.15214 -0.01515 263 HIS   B CG  
3791 N ND1 . HIS   B 170 ? 2.03327 2.24444 1.94961 -0.01413 -0.16254 -0.02595 263 HIS   B ND1 
3792 C CD2 . HIS   B 170 ? 1.97159 2.16468 1.84645 -0.00139 -0.15592 -0.01100 263 HIS   B CD2 
3793 C CE1 . HIS   B 170 ? 2.08063 2.27404 1.96051 -0.00662 -0.17265 -0.02900 263 HIS   B CE1 
3794 N NE2 . HIS   B 170 ? 2.00930 2.19141 1.86242 0.00096  -0.16839 -0.01979 263 HIS   B NE2 
3795 N N   . GLU   B 171 ? 1.81457 2.08808 1.85466 -0.04432 -0.12039 -0.01483 264 GLU   B N   
3796 C CA  . GLU   B 171 ? 1.71325 1.99404 1.77088 -0.05127 -0.10395 -0.00963 264 GLU   B CA  
3797 C C   . GLU   B 171 ? 1.59966 1.86556 1.64627 -0.05868 -0.09611 -0.01044 264 GLU   B C   
3798 O O   . GLU   B 171 ? 1.50784 1.77287 1.56443 -0.07004 -0.09891 -0.01611 264 GLU   B O   
3799 C CB  . GLU   B 171 ? 1.67362 1.97930 1.76888 -0.05930 -0.10508 -0.01416 264 GLU   B CB  
3800 C CG  . GLU   B 171 ? 1.58991 1.90356 1.70036 -0.06343 -0.08877 -0.00823 264 GLU   B CG  
3801 C CD  . GLU   B 171 ? 1.64275 1.95302 1.74375 -0.05108 -0.08440 -0.00002 264 GLU   B CD  
3802 O OE1 . GLU   B 171 ? 1.56526 1.87854 1.66474 -0.04053 -0.09586 -0.00085 264 GLU   B OE1 
3803 O OE2 . GLU   B 171 ? 1.63524 1.93764 1.72858 -0.05204 -0.07066 0.00694  264 GLU   B OE2 
3804 N N   . VAL   B 172 ? 1.44360 1.69679 1.46861 -0.05230 -0.08657 -0.00542 265 VAL   B N   
3805 C CA  . VAL   B 172 ? 1.36483 1.60231 1.37592 -0.05422 -0.08227 -0.00817 265 VAL   B CA  
3806 C C   . VAL   B 172 ? 1.19869 1.43600 1.22303 -0.06215 -0.07190 -0.00515 265 VAL   B C   
3807 O O   . VAL   B 172 ? 1.16742 1.38848 1.18067 -0.06371 -0.07126 -0.00807 265 VAL   B O   
3808 C CB  . VAL   B 172 ? 1.35277 1.58180 1.33786 -0.04335 -0.07642 -0.00703 265 VAL   B CB  
3809 C CG1 . VAL   B 172 ? 1.21491 1.45079 1.20524 -0.04198 -0.06129 0.00005  265 VAL   B CG1 
3810 C CG2 . VAL   B 172 ? 1.27977 1.49228 1.24644 -0.04062 -0.07991 -0.01523 265 VAL   B CG2 
3811 N N   . LEU   B 173 ? 1.18056 1.43300 1.22574 -0.06623 -0.06487 -0.00001 266 LEU   B N   
3812 C CA  . LEU   B 173 ? 1.08713 1.33798 1.14101 -0.07356 -0.05461 0.00325  266 LEU   B CA  
3813 C C   . LEU   B 173 ? 1.04724 1.30002 1.11635 -0.08892 -0.05597 0.00012  266 LEU   B C   
3814 O O   . LEU   B 173 ? 0.99740 1.23905 1.06361 -0.09676 -0.04939 0.00211  266 LEU   B O   
3815 C CB  . LEU   B 173 ? 1.01182 1.27599 1.07677 -0.06999 -0.04436 0.01004  266 LEU   B CB  
3816 C CG  . LEU   B 173 ? 1.00087 1.26163 1.05033 -0.05949 -0.03873 0.01390  266 LEU   B CG  
3817 C CD1 . LEU   B 173 ? 0.95349 1.22340 1.01344 -0.05886 -0.02868 0.02025  266 LEU   B CD1 
3818 C CD2 . LEU   B 173 ? 1.02453 1.27164 1.05808 -0.05674 -0.03672 0.01079  266 LEU   B CD2 
3819 N N   . LEU   B 174 ? 1.04179 1.30828 1.12604 -0.09415 -0.06432 -0.00525 267 LEU   B N   
3820 C CA  . LEU   B 174 ? 0.98781 1.25950 1.08812 -0.11201 -0.06422 -0.00998 267 LEU   B CA  
3821 C C   . LEU   B 174 ? 1.12558 1.37330 1.20774 -0.11947 -0.07348 -0.01530 267 LEU   B C   
3822 O O   . LEU   B 174 ? 1.18427 1.42980 1.25905 -0.11301 -0.08571 -0.02047 267 LEU   B O   
3823 C CB  . LEU   B 174 ? 0.99316 1.29629 1.12370 -0.11446 -0.06920 -0.01594 267 LEU   B CB  
3824 C CG  . LEU   B 174 ? 0.92694 1.24842 1.08367 -0.13368 -0.06199 -0.02077 267 LEU   B CG  
3825 C CD1 . LEU   B 174 ? 0.86702 1.20092 1.03567 -0.13293 -0.04713 -0.01553 267 LEU   B CD1 
3826 C CD2 . LEU   B 174 ? 0.95933 1.31111 1.14547 -0.13750 -0.07251 -0.03205 267 LEU   B CD2 
3827 N N   . PRO   B 175 ? 1.06096 1.28659 1.13182 -0.13261 -0.06913 -0.01431 268 PRO   B N   
3828 C CA  . PRO   B 175 ? 1.09948 1.29439 1.14731 -0.13815 -0.07927 -0.01917 268 PRO   B CA  
3829 C C   . PRO   B 175 ? 1.14163 1.34650 1.20389 -0.15275 -0.08861 -0.02797 268 PRO   B C   
3830 O O   . PRO   B 175 ? 1.10572 1.33564 1.19535 -0.16754 -0.08351 -0.03049 268 PRO   B O   
3831 C CB  . PRO   B 175 ? 1.13287 1.29906 1.16351 -0.14934 -0.07204 -0.01452 268 PRO   B CB  
3832 C CG  . PRO   B 175 ? 1.11158 1.30153 1.16488 -0.15906 -0.05805 -0.01005 268 PRO   B CG  
3833 C CD  . PRO   B 175 ? 1.01991 1.24277 1.09365 -0.14254 -0.05564 -0.00859 268 PRO   B CD  
3834 N N   . GLN   B 176 ? 1.11561 1.30235 1.16013 -0.14848 -0.10247 -0.03423 269 GLN   B N   
3835 C CA  . GLN   B 176 ? 1.13764 1.33115 1.19361 -0.16227 -0.11396 -0.04412 269 GLN   B CA  
3836 C C   . GLN   B 176 ? 1.17249 1.33021 1.19641 -0.15760 -0.12771 -0.04968 269 GLN   B C   
3837 O O   . GLN   B 176 ? 1.23964 1.39826 1.25257 -0.13953 -0.13634 -0.05258 269 GLN   B O   
3838 C CB  . GLN   B 176 ? 1.11801 1.35119 1.20207 -0.15433 -0.12012 -0.04876 269 GLN   B CB  
3839 C CG  . GLN   B 176 ? 1.25676 1.50701 1.36240 -0.16996 -0.13180 -0.06081 269 GLN   B CG  
3840 C CD  . GLN   B 176 ? 1.32702 1.55716 1.41082 -0.16395 -0.15011 -0.06850 269 GLN   B CD  
3841 O OE1 . GLN   B 176 ? 1.32132 1.54275 1.38438 -0.14275 -0.15601 -0.06653 269 GLN   B OE1 
3842 N NE2 . GLN   B 176 ? 1.19818 1.42006 1.28493 -0.18397 -0.15850 -0.07782 269 GLN   B NE2 
3843 N N   . TYR   B 177 ? 1.13150 1.25550 1.13770 -0.17407 -0.12950 -0.05130 270 TYR   B N   
3844 C CA  . TYR   B 177 ? 1.15563 1.24143 1.13098 -0.17202 -0.14388 -0.05827 270 TYR   B CA  
3845 C C   . TYR   B 177 ? 1.03781 1.08887 0.99931 -0.19790 -0.14433 -0.05909 270 TYR   B C   
3846 O O   . TYR   B 177 ? 1.19839 1.24715 1.16390 -0.21197 -0.13141 -0.05179 270 TYR   B O   
3847 C CB  . TYR   B 177 ? 1.10295 1.16492 1.04822 -0.14677 -0.14495 -0.05609 270 TYR   B CB  
3848 C CG  . TYR   B 177 ? 1.21067 1.25870 1.14646 -0.14296 -0.13303 -0.04692 270 TYR   B CG  
3849 C CD1 . TYR   B 177 ? 1.07920 1.08202 0.98744 -0.15097 -0.13578 -0.04598 270 TYR   B CD1 
3850 C CD2 . TYR   B 177 ? 1.10661 1.18332 1.05813 -0.13090 -0.12069 -0.03954 270 TYR   B CD2 
3851 C CE1 . TYR   B 177 ? 1.04414 1.03254 0.94147 -0.14587 -0.12744 -0.03822 270 TYR   B CE1 
3852 C CE2 . TYR   B 177 ? 1.04233 1.10719 0.98560 -0.12711 -0.11138 -0.03232 270 TYR   B CE2 
3853 C CZ  . TYR   B 177 ? 1.11170 1.13325 1.02813 -0.13392 -0.11527 -0.03186 270 TYR   B CZ  
3854 O OH  . TYR   B 177 ? 1.07563 1.08383 0.98176 -0.12865 -0.10842 -0.02525 270 TYR   B OH  
3855 N N   . PRO   B 178 ? 1.14046 1.16166 1.08265 -0.20559 -0.15896 -0.06787 271 PRO   B N   
3856 C CA  . PRO   B 178 ? 1.08138 1.06269 1.00510 -0.23285 -0.16014 -0.06840 271 PRO   B CA  
3857 C C   . PRO   B 178 ? 1.10315 1.03785 0.99095 -0.22761 -0.15555 -0.05961 271 PRO   B C   
3858 O O   . PRO   B 178 ? 1.01464 0.92681 0.87775 -0.20200 -0.16204 -0.05999 271 PRO   B O   
3859 C CB  . PRO   B 178 ? 0.98542 0.94088 0.89115 -0.23511 -0.17954 -0.08044 271 PRO   B CB  
3860 C CG  . PRO   B 178 ? 1.19009 1.18888 1.11968 -0.21804 -0.18644 -0.08713 271 PRO   B CG  
3861 C CD  . PRO   B 178 ? 1.06818 1.09201 1.00532 -0.19294 -0.17522 -0.07832 271 PRO   B CD  
3862 N N   . GLN   B 179 ? 1.01870 0.93984 0.90336 -0.25213 -0.14441 -0.05264 272 GLN   B N   
3863 C CA  . GLN   B 179 ? 1.11375 0.98387 0.95925 -0.24950 -0.14255 -0.04426 272 GLN   B CA  
3864 C C   . GLN   B 179 ? 1.14398 0.94768 0.94383 -0.25269 -0.15967 -0.04917 272 GLN   B C   
3865 O O   . GLN   B 179 ? 1.16084 0.91809 0.92344 -0.23772 -0.16563 -0.04567 272 GLN   B O   
3866 C CB  . GLN   B 179 ? 1.12439 0.99546 0.97421 -0.27681 -0.12552 -0.03530 272 GLN   B CB  
3867 C CG  . GLN   B 179 ? 1.14390 1.07986 1.03978 -0.27613 -0.10868 -0.03222 272 GLN   B CG  
3868 C CD  . GLN   B 179 ? 1.29231 1.23464 1.19617 -0.30831 -0.09126 -0.02731 272 GLN   B CD  
3869 O OE1 . GLN   B 179 ? 1.32280 1.24752 1.21973 -0.33940 -0.09063 -0.03079 272 GLN   B OE1 
3870 N NE2 . GLN   B 179 ? 1.25656 1.22390 1.17400 -0.30227 -0.07623 -0.01987 272 GLN   B NE2 
3871 N N   . GLN   B 180 ? 1.17273 0.97035 0.97473 -0.27113 -0.16918 -0.05834 273 GLN   B N   
3872 C CA  . GLN   B 180 ? 1.22669 0.95672 0.98349 -0.27765 -0.18603 -0.06356 273 GLN   B CA  
3873 C C   . GLN   B 180 ? 1.26029 0.96707 0.99237 -0.24010 -0.20149 -0.06998 273 GLN   B C   
3874 O O   . GLN   B 180 ? 1.29372 0.94205 0.98273 -0.22957 -0.21095 -0.06896 273 GLN   B O   
3875 C CB  . GLN   B 180 ? 1.37933 1.11497 1.14902 -0.30557 -0.19305 -0.07370 273 GLN   B CB  
3876 C CG  . GLN   B 180 ? 1.48348 1.14602 1.20560 -0.31670 -0.21095 -0.07972 273 GLN   B CG  
3877 C CD  . GLN   B 180 ? 1.59075 1.19808 1.27882 -0.34961 -0.20507 -0.07086 273 GLN   B CD  
3878 O OE1 . GLN   B 180 ? 1.45344 1.04713 1.12721 -0.34689 -0.19418 -0.05887 273 GLN   B OE1 
3879 N NE2 . GLN   B 180 ? 1.51219 1.08556 1.18471 -0.38230 -0.21241 -0.07685 273 GLN   B NE2 
3880 N N   . ILE   B 181 ? 1.21169 0.96302 0.96900 -0.21901 -0.20449 -0.07749 274 ILE   B N   
3881 C CA  . ILE   B 181 ? 1.18337 0.91775 0.91854 -0.18487 -0.21687 -0.08564 274 ILE   B CA  
3882 C C   . ILE   B 181 ? 1.14023 0.88401 0.87368 -0.15730 -0.20867 -0.07955 274 ILE   B C   
3883 O O   . ILE   B 181 ? 1.17138 0.89165 0.88088 -0.13019 -0.21816 -0.08655 274 ILE   B O   
3884 C CB  . ILE   B 181 ? 1.18294 0.95740 0.93918 -0.17326 -0.22259 -0.09592 274 ILE   B CB  
3885 C CG1 . ILE   B 181 ? 1.05510 0.88515 0.83949 -0.15062 -0.21007 -0.09164 274 ILE   B CG1 
3886 C CG2 . ILE   B 181 ? 1.29318 1.08939 1.07435 -0.20338 -0.22430 -0.09936 274 ILE   B CG2 
3887 C CD1 . ILE   B 181 ? 1.21722 1.05754 0.99323 -0.12254 -0.21773 -0.10189 274 ILE   B CD1 
3888 N N   . PHE   B 182 ? 1.11293 0.89187 0.87222 -0.16321 -0.19156 -0.06826 275 PHE   B N   
3889 C CA  . PHE   B 182 ? 1.13403 0.92135 0.89231 -0.13936 -0.18435 -0.06299 275 PHE   B CA  
3890 C C   . PHE   B 182 ? 1.09168 0.81675 0.80798 -0.13458 -0.19321 -0.06123 275 PHE   B C   
3891 O O   . PHE   B 182 ? 1.09904 0.81206 0.80042 -0.10574 -0.19970 -0.06630 275 PHE   B O   
3892 C CB  . PHE   B 182 ? 1.01070 0.84482 0.80343 -0.14887 -0.16518 -0.05172 275 PHE   B CB  
3893 C CG  . PHE   B 182 ? 1.01074 0.85313 0.80337 -0.12798 -0.15772 -0.04616 275 PHE   B CG  
3894 C CD1 . PHE   B 182 ? 1.00996 0.89160 0.82089 -0.10330 -0.15336 -0.04936 275 PHE   B CD1 
3895 C CD2 . PHE   B 182 ? 1.05652 0.86641 0.82901 -0.13431 -0.15522 -0.03805 275 PHE   B CD2 
3896 C CE1 . PHE   B 182 ? 1.03310 0.92514 0.84676 -0.08601 -0.14656 -0.04569 275 PHE   B CE1 
3897 C CE2 . PHE   B 182 ? 1.11064 0.92950 0.88431 -0.11477 -0.15022 -0.03432 275 PHE   B CE2 
3898 C CZ  . PHE   B 182 ? 1.02402 0.88596 0.82063 -0.09096 -0.14582 -0.03870 275 PHE   B CZ  
3899 N N   . ILE   B 183 ? 1.16350 0.84790 0.85924 -0.16286 -0.19389 -0.05476 276 ILE   B N   
3900 C CA  . ILE   B 183 ? 1.23533 0.85165 0.88391 -0.15970 -0.20432 -0.05185 276 ILE   B CA  
3901 C C   . ILE   B 183 ? 1.25646 0.81970 0.86797 -0.14512 -0.22658 -0.06430 276 ILE   B C   
3902 O O   . ILE   B 183 ? 1.35496 0.86395 0.92727 -0.12918 -0.23969 -0.06569 276 ILE   B O   
3903 C CB  . ILE   B 183 ? 1.27145 0.85481 0.90266 -0.19742 -0.19725 -0.04053 276 ILE   B CB  
3904 C CG1 . ILE   B 183 ? 1.29369 0.85472 0.91690 -0.22735 -0.20335 -0.04558 276 ILE   B CG1 
3905 C CG2 . ILE   B 183 ? 1.11820 0.75820 0.78854 -0.21170 -0.17446 -0.03049 276 ILE   B CG2 
3906 C CD1 . ILE   B 183 ? 1.38351 0.87139 0.95890 -0.25638 -0.20770 -0.03889 276 ILE   B CD1 
3907 N N   . GLN   B 184 ? 1.24664 0.82256 0.86817 -0.14880 -0.23271 -0.07440 277 GLN   B N   
3908 C CA  . GLN   B 184 ? 1.31934 0.84753 0.90641 -0.13237 -0.25390 -0.08815 277 GLN   B CA  
3909 C C   . GLN   B 184 ? 1.22238 0.77086 0.81305 -0.08976 -0.25815 -0.09856 277 GLN   B C   
3910 O O   . GLN   B 184 ? 1.32775 0.82870 0.88363 -0.06712 -0.27452 -0.10769 277 GLN   B O   
3911 C CB  . GLN   B 184 ? 1.35538 0.89197 0.95164 -0.15001 -0.25950 -0.09663 277 GLN   B CB  
3912 C CG  . GLN   B 184 ? 1.44414 0.95838 1.03608 -0.19399 -0.25692 -0.09007 277 GLN   B CG  
3913 C CD  . GLN   B 184 ? 1.58193 1.11260 1.18928 -0.21071 -0.26336 -0.10032 277 GLN   B CD  
3914 O OE1 . GLN   B 184 ? 1.63104 1.18430 1.24702 -0.18848 -0.27098 -0.11179 277 GLN   B OE1 
3915 N NE2 . GLN   B 184 ? 1.54147 1.06149 1.15172 -0.25089 -0.26017 -0.09705 277 GLN   B NE2 
3916 N N   . ILE   B 185 ? 1.21330 0.83168 0.84514 -0.07859 -0.24358 -0.09822 278 ILE   B N   
3917 C CA  . ILE   B 185 ? 1.20285 0.84695 0.84107 -0.04184 -0.24364 -0.10808 278 ILE   B CA  
3918 C C   . ILE   B 185 ? 1.17746 0.81284 0.80974 -0.02585 -0.24148 -0.10324 278 ILE   B C   
3919 O O   . ILE   B 185 ? 1.20374 0.82758 0.82264 0.00478  -0.25072 -0.11478 278 ILE   B O   
3920 C CB  . ILE   B 185 ? 1.15476 0.87090 0.83377 -0.03832 -0.22827 -0.10791 278 ILE   B CB  
3921 C CG1 . ILE   B 185 ? 1.18771 0.90989 0.87058 -0.05391 -0.23338 -0.11304 278 ILE   B CG1 
3922 C CG2 . ILE   B 185 ? 1.10884 0.85203 0.79264 -0.00404 -0.22608 -0.11908 278 ILE   B CG2 
3923 C CD1 . ILE   B 185 ? 1.10916 0.89505 0.82739 -0.05353 -0.22045 -0.11090 278 ILE   B CD1 
3924 N N   . ALA   B 186 ? 1.13025 0.77251 0.77294 -0.04554 -0.22979 -0.08761 279 ALA   B N   
3925 C CA  . ALA   B 186 ? 1.16515 0.79304 0.79777 -0.03243 -0.22992 -0.08257 279 ALA   B CA  
3926 C C   . ALA   B 186 ? 1.20536 0.75423 0.78670 -0.02417 -0.25186 -0.08719 279 ALA   B C   
3927 O O   . ALA   B 186 ? 1.25143 0.78450 0.81931 0.00241  -0.26086 -0.09225 279 ALA   B O   
3928 C CB  . ALA   B 186 ? 1.06120 0.70684 0.71009 -0.05800 -0.21334 -0.06516 279 ALA   B CB  
3929 N N   . GLU   B 187 ? 1.29371 0.79090 0.84527 -0.04667 -0.26186 -0.08626 280 GLU   B N   
3930 C CA  . GLU   B 187 ? 1.33217 0.74548 0.82879 -0.03954 -0.28487 -0.09093 280 GLU   B CA  
3931 C C   . GLU   B 187 ? 1.43342 0.83847 0.91972 0.00104  -0.30183 -0.11111 280 GLU   B C   
3932 O O   . GLU   B 187 ? 1.36757 0.72390 0.82040 0.02459  -0.31963 -0.11718 280 GLU   B O   
3933 C CB  . GLU   B 187 ? 1.54216 0.90635 1.01190 -0.07431 -0.29089 -0.08748 280 GLU   B CB  
3934 C CG  . GLU   B 187 ? 1.60571 0.87455 1.01290 -0.07001 -0.31603 -0.09215 280 GLU   B CG  
3935 C CD  . GLU   B 187 ? 1.90390 1.12628 1.28616 -0.10876 -0.32027 -0.08886 280 GLU   B CD  
3936 O OE1 . GLU   B 187 ? 1.86416 1.13270 1.28117 -0.13927 -0.30314 -0.08311 280 GLU   B OE1 
3937 O OE2 . GLU   B 187 ? 2.08741 1.22685 1.41553 -0.10865 -0.34150 -0.09296 280 GLU   B OE2 
3938 N N   . LEU   B 188 ? 1.35647 0.80840 0.86991 0.01056  -0.29705 -0.12267 281 LEU   B N   
3939 C CA  . LEU   B 188 ? 1.36268 0.81652 0.87038 0.04914  -0.30935 -0.14360 281 LEU   B CA  
3940 C C   . LEU   B 188 ? 1.35959 0.85580 0.89059 0.07931  -0.30309 -0.14815 281 LEU   B C   
3941 O O   . LEU   B 188 ? 1.34655 0.82279 0.86151 0.11275  -0.31841 -0.16402 281 LEU   B O   
3942 C CB  . LEU   B 188 ? 1.22888 0.72418 0.75766 0.04918  -0.30335 -0.15379 281 LEU   B CB  
3943 C CG  . LEU   B 188 ? 1.39524 0.90315 0.92167 0.08723  -0.31136 -0.17679 281 LEU   B CG  
3944 C CD1 . LEU   B 188 ? 1.45214 0.88289 0.93031 0.10636  -0.33833 -0.19019 281 LEU   B CD1 
3945 C CD2 . LEU   B 188 ? 1.32878 0.87280 0.87006 0.08252  -0.30474 -0.18446 281 LEU   B CD2 
3946 N N   . LEU   B 189 ? 1.25005 0.80536 0.81983 0.06827  -0.28142 -0.13573 282 LEU   B N   
3947 C CA  . LEU   B 189 ? 1.24849 0.84765 0.84341 0.09337  -0.27430 -0.14005 282 LEU   B CA  
3948 C C   . LEU   B 189 ? 1.29372 0.84639 0.86238 0.10306  -0.28794 -0.13619 282 LEU   B C   
3949 O O   . LEU   B 189 ? 1.28587 0.84989 0.85961 0.13472  -0.29519 -0.14869 282 LEU   B O   
3950 C CB  . LEU   B 189 ? 1.14357 0.81304 0.78365 0.07717  -0.24840 -0.12750 282 LEU   B CB  
3951 C CG  . LEU   B 189 ? 1.10852 0.83220 0.77621 0.07678  -0.23520 -0.13360 282 LEU   B CG  
3952 C CD1 . LEU   B 189 ? 1.12044 0.89795 0.82442 0.05567  -0.21285 -0.11805 282 LEU   B CD1 
3953 C CD2 . LEU   B 189 ? 1.12823 0.88368 0.80637 0.11077  -0.23542 -0.15346 282 LEU   B CD2 
3954 N N   . ASP   B 190 ? 1.30817 0.80881 0.84792 0.07584  -0.29170 -0.11974 283 ASP   B N   
3955 C CA  . ASP   B 190 ? 1.33727 0.78355 0.84247 0.08371  -0.30650 -0.11484 283 ASP   B CA  
3956 C C   . ASP   B 190 ? 1.50065 0.88688 0.96557 0.11564  -0.33547 -0.13246 283 ASP   B C   
3957 O O   . ASP   B 190 ? 1.50529 0.86840 0.95425 0.14066  -0.35029 -0.13739 283 ASP   B O   
3958 C CB  . ASP   B 190 ? 1.36085 0.75813 0.83659 0.04456  -0.30339 -0.09407 283 ASP   B CB  
3959 C CG  . ASP   B 190 ? 1.41812 0.87258 0.93233 0.01784  -0.27650 -0.07775 283 ASP   B CG  
3960 O OD1 . ASP   B 190 ? 1.30361 0.82113 0.85772 0.03288  -0.26425 -0.07985 283 ASP   B OD1 
3961 O OD2 . ASP   B 190 ? 1.44345 0.87971 0.94801 -0.01853 -0.26758 -0.06384 283 ASP   B OD2 
3962 N N   . LEU   B 191 ? 1.46654 0.82646 0.91432 0.11683  -0.34540 -0.14331 284 LEU   B N   
3963 C CA  . LEU   B 191 ? 1.49925 0.80229 0.90906 0.14965  -0.37369 -0.16243 284 LEU   B CA  
3964 C C   . LEU   B 191 ? 1.58110 0.94187 1.02449 0.19223  -0.37435 -0.18551 284 LEU   B C   
3965 O O   . LEU   B 191 ? 1.59197 0.92692 1.01866 0.22667  -0.39475 -0.19956 284 LEU   B O   
3966 C CB  . LEU   B 191 ? 1.65822 0.91510 1.03895 0.13645  -0.38375 -0.16773 284 LEU   B CB  
3967 C CG  . LEU   B 191 ? 1.71155 0.90352 1.04930 0.16952  -0.41416 -0.18872 284 LEU   B CG  
3968 C CD1 . LEU   B 191 ? 1.85008 0.95591 1.13386 0.17635  -0.43799 -0.18258 284 LEU   B CD1 
3969 C CD2 . LEU   B 191 ? 1.69948 0.85556 1.01452 0.15360  -0.42103 -0.19424 284 LEU   B CD2 
3970 N N   . CYS   B 192 ? 1.48476 0.92427 0.97509 0.19018  -0.35223 -0.19040 285 CYS   B N   
3971 C CA  . CYS   B 192 ? 1.45044 0.94827 0.97262 0.22633  -0.34920 -0.21339 285 CYS   B CA  
3972 C C   . CYS   B 192 ? 1.43965 0.97554 0.98805 0.24435  -0.34554 -0.21457 285 CYS   B C   
3973 O O   . CYS   B 192 ? 1.45717 1.01671 1.01857 0.28087  -0.35376 -0.23710 285 CYS   B O   
3974 C CB  . CYS   B 192 ? 1.46611 1.03453 1.02646 0.21492  -0.32464 -0.21520 285 CYS   B CB  
3975 S SG  . CYS   B 192 ? 1.55403 1.08727 1.08791 0.19909  -0.33060 -0.21906 285 CYS   B SG  
3976 N N   . VAL   B 193 ? 1.41095 0.95540 0.96870 0.21965  -0.33347 -0.19232 286 VAL   B N   
3977 C CA  . VAL   B 193 ? 1.42384 1.00565 1.00716 0.23458  -0.32987 -0.19308 286 VAL   B CA  
3978 C C   . VAL   B 193 ? 1.32532 0.84698 0.87258 0.26290  -0.36004 -0.20214 286 VAL   B C   
3979 O O   . VAL   B 193 ? 1.38452 0.93782 0.95324 0.28700  -0.36385 -0.21198 286 VAL   B O   
3980 C CB  . VAL   B 193 ? 1.33874 0.94295 0.93891 0.20048  -0.30923 -0.16732 286 VAL   B CB  
3981 C CG1 . VAL   B 193 ? 1.38028 0.90673 0.93305 0.18152  -0.32250 -0.14927 286 VAL   B CG1 
3982 C CG2 . VAL   B 193 ? 1.14598 0.81594 0.78872 0.21336  -0.29726 -0.17074 286 VAL   B CG2 
3983 N N   . LEU   B 194 ? 1.41980 0.85333 0.91125 0.26081  -0.38299 -0.19973 287 LEU   B N   
3984 C CA  . LEU   B 194 ? 1.54052 0.90785 0.99061 0.29052  -0.41528 -0.20915 287 LEU   B CA  
3985 C C   . LEU   B 194 ? 1.54252 0.93234 1.00695 0.33835  -0.43112 -0.24210 287 LEU   B C   
3986 O O   . LEU   B 194 ? 1.67728 1.04862 1.13173 0.37178  -0.45386 -0.25529 287 LEU   B O   
3987 C CB  . LEU   B 194 ? 1.59043 0.85207 0.97234 0.27311  -0.43516 -0.19741 287 LEU   B CB  
3988 C CG  . LEU   B 194 ? 1.59381 0.82863 0.95772 0.22381  -0.41965 -0.16667 287 LEU   B CG  
3989 C CD1 . LEU   B 194 ? 1.77103 0.89806 1.06438 0.20712  -0.44030 -0.15782 287 LEU   B CD1 
3990 C CD2 . LEU   B 194 ? 1.53971 0.79183 0.91322 0.21905  -0.41286 -0.15281 287 LEU   B CD2 
3991 N N   . ASP   B 195 ? 1.51315 0.94340 1.00047 0.34303  -0.41997 -0.25686 288 ASP   B N   
3992 C CA  . ASP   B 195 ? 1.63596 1.09894 1.14232 0.38677  -0.42997 -0.29014 288 ASP   B CA  
3993 C C   . ASP   B 195 ? 1.57426 1.13956 1.14499 0.39737  -0.40780 -0.29981 288 ASP   B C   
3994 O O   . ASP   B 195 ? 1.53033 1.15502 1.13618 0.36903  -0.37740 -0.28592 288 ASP   B O   
3995 C CB  . ASP   B 195 ? 1.60684 1.06879 1.10684 0.38588  -0.42609 -0.30221 288 ASP   B CB  
3996 C CG  . ASP   B 195 ? 1.58961 1.05794 1.09106 0.43343  -0.44390 -0.33832 288 ASP   B CG  
3997 O OD1 . ASP   B 195 ? 1.62605 1.15403 1.16600 0.46270  -0.44197 -0.35753 288 ASP   B OD1 
3998 O OD2 . ASP   B 195 ? 1.84822 1.26289 1.31311 0.44144  -0.45994 -0.34887 288 ASP   B OD2 
3999 N N   . VAL   B 196 ? 1.56273 1.14774 1.14859 0.43831  -0.42397 -0.32462 289 VAL   B N   
4000 C CA  . VAL   B 196 ? 1.58127 1.26075 1.22777 0.44744  -0.40491 -0.33475 289 VAL   B CA  
4001 C C   . VAL   B 196 ? 1.53098 1.29070 1.22011 0.44827  -0.37809 -0.35124 289 VAL   B C   
4002 O O   . VAL   B 196 ? 1.47170 1.31086 1.20900 0.43653  -0.35093 -0.34948 289 VAL   B O   
4003 C CB  . VAL   B 196 ? 1.59106 1.26905 1.24268 0.49156  -0.43231 -0.35870 289 VAL   B CB  
4004 C CG1 . VAL   B 196 ? 1.46994 1.23764 1.18126 0.49339  -0.41389 -0.36377 289 VAL   B CG1 
4005 C CG2 . VAL   B 196 ? 1.63237 1.21021 1.22474 0.49450  -0.46472 -0.34419 289 VAL   B CG2 
4006 N N   . ASP   B 197 ? 1.59686 1.33460 1.26585 0.46083  -0.38489 -0.36716 290 ASP   B N   
4007 C CA  . ASP   B 197 ? 1.53239 1.34074 1.23459 0.46347  -0.36059 -0.38462 290 ASP   B CA  
4008 C C   . ASP   B 197 ? 1.49083 1.33417 1.20788 0.42020  -0.32776 -0.35992 290 ASP   B C   
4009 O O   . ASP   B 197 ? 1.44721 1.34766 1.18799 0.41839  -0.30556 -0.37112 290 ASP   B O   
4010 C CB  . ASP   B 197 ? 1.60770 1.37478 1.27766 0.48692  -0.37799 -0.40689 290 ASP   B CB  
4011 C CG  . ASP   B 197 ? 1.66567 1.42015 1.33268 0.53729  -0.40686 -0.44007 290 ASP   B CG  
4012 O OD1 . ASP   B 197 ? 1.67480 1.48959 1.38389 0.55725  -0.40358 -0.45542 290 ASP   B OD1 
4013 O OD2 . ASP   B 197 ? 1.72422 1.40843 1.34728 0.55741  -0.43384 -0.45191 290 ASP   B OD2 
4014 N N   . CYS   B 198 ? 1.50982 1.32042 1.21226 0.38621  -0.32431 -0.32778 291 CYS   B N   
4015 C CA  . CYS   B 198 ? 1.39453 1.23988 1.11336 0.34785  -0.29521 -0.30564 291 CYS   B CA  
4016 C C   . CYS   B 198 ? 1.34791 1.27940 1.11847 0.34258  -0.26832 -0.30590 291 CYS   B C   
4017 O O   . CYS   B 198 ? 1.24950 1.22402 1.03825 0.32011  -0.24260 -0.29693 291 CYS   B O   
4018 C CB  . CYS   B 198 ? 1.41326 1.20368 1.10539 0.31442  -0.29892 -0.27395 291 CYS   B CB  
4019 S SG  . CYS   B 198 ? 1.37648 1.16228 1.07702 0.31012  -0.30329 -0.25810 291 CYS   B SG  
4020 N N   . LEU   B 199 ? 1.27891 1.23420 1.07181 0.36272  -0.27497 -0.31635 292 LEU   B N   
4021 C CA  . LEU   B 199 ? 1.27365 1.30850 1.11564 0.35597  -0.25047 -0.31706 292 LEU   B CA  
4022 C C   . LEU   B 199 ? 1.32859 1.43280 1.20046 0.36537  -0.22930 -0.33982 292 LEU   B C   
4023 O O   . LEU   B 199 ? 1.28536 1.45493 1.19402 0.35163  -0.20355 -0.33757 292 LEU   B O   
4024 C CB  . LEU   B 199 ? 1.31338 1.35645 1.17189 0.37759  -0.26587 -0.32639 292 LEU   B CB  
4025 C CG  . LEU   B 199 ? 1.25242 1.23270 1.08185 0.36609  -0.28345 -0.30266 292 LEU   B CG  
4026 C CD1 . LEU   B 199 ? 1.27845 1.27266 1.12541 0.39015  -0.29914 -0.31470 292 LEU   B CD1 
4027 C CD2 . LEU   B 199 ? 1.13328 1.12010 0.96663 0.32389  -0.26062 -0.27067 292 LEU   B CD2 
4028 N N   . GLU   B 200 ? 1.31781 1.40726 1.17222 0.38763  -0.23913 -0.36196 293 GLU   B N   
4029 C CA  . GLU   B 200 ? 1.28718 1.43795 1.16287 0.39293  -0.21662 -0.38232 293 GLU   B CA  
4030 C C   . GLU   B 200 ? 1.23143 1.40194 1.10690 0.35574  -0.18866 -0.35972 293 GLU   B C   
4031 O O   . GLU   B 200 ? 1.22724 1.46241 1.12980 0.34802  -0.16152 -0.36640 293 GLU   B O   
4032 C CB  . GLU   B 200 ? 1.27772 1.39731 1.12637 0.42156  -0.23400 -0.40774 293 GLU   B CB  
4033 C CG  . GLU   B 200 ? 1.32802 1.50020 1.18756 0.42364  -0.21028 -0.42671 293 GLU   B CG  
4034 C CD  . GLU   B 200 ? 1.35999 1.49129 1.18549 0.44798  -0.22797 -0.44829 293 GLU   B CD  
4035 O OE1 . GLU   B 200 ? 1.42836 1.49485 1.22616 0.46833  -0.26013 -0.45294 293 GLU   B OE1 
4036 O OE2 . GLU   B 200 ? 1.33610 1.49656 1.15906 0.44644  -0.21014 -0.46051 293 GLU   B OE2 
4037 N N   . PHE   B 201 ? 1.13142 1.24644 0.97580 0.33202  -0.19521 -0.33342 294 PHE   B N   
4038 C CA  . PHE   B 201 ? 1.15366 1.27897 0.99439 0.29873  -0.17415 -0.31160 294 PHE   B CA  
4039 C C   . PHE   B 201 ? 1.08154 1.22030 0.94103 0.27201  -0.16252 -0.28478 294 PHE   B C   
4040 O O   . PHE   B 201 ? 1.06458 1.17093 0.91992 0.27169  -0.17768 -0.27422 294 PHE   B O   
4041 C CB  . PHE   B 201 ? 1.15953 1.22054 0.95876 0.28847  -0.18882 -0.30129 294 PHE   B CB  
4042 C CG  . PHE   B 201 ? 1.22811 1.25681 1.00147 0.31664  -0.20799 -0.32651 294 PHE   B CG  
4043 C CD1 . PHE   B 201 ? 1.14647 1.20901 0.92089 0.32876  -0.19611 -0.34790 294 PHE   B CD1 
4044 C CD2 . PHE   B 201 ? 1.20599 1.16729 0.95051 0.33082  -0.23795 -0.32909 294 PHE   B CD2 
4045 C CE1 . PHE   B 201 ? 1.24086 1.27341 0.99096 0.35618  -0.21402 -0.37277 294 PHE   B CE1 
4046 C CE2 . PHE   B 201 ? 1.34504 1.27212 1.06341 0.35800  -0.25723 -0.35302 294 PHE   B CE2 
4047 C CZ  . PHE   B 201 ? 1.30897 1.27309 1.03159 0.37153  -0.24538 -0.37555 294 PHE   B CZ  
4048 N N   . PRO   B 202 ? 1.00698 1.19032 0.88402 0.24997  -0.13622 -0.27386 295 PRO   B N   
4049 C CA  . PRO   B 202 ? 0.93118 1.12479 0.82419 0.22462  -0.12541 -0.24857 295 PRO   B CA  
4050 C C   . PRO   B 202 ? 1.07536 1.21155 0.94324 0.20578  -0.13841 -0.22484 295 PRO   B C   
4051 O O   . PRO   B 202 ? 0.97713 1.07347 0.81652 0.20400  -0.14939 -0.22434 295 PRO   B O   
4052 C CB  . PRO   B 202 ? 0.95420 1.19562 0.86012 0.20625  -0.09723 -0.24333 295 PRO   B CB  
4053 C CG  . PRO   B 202 ? 0.89401 1.16770 0.80226 0.22598  -0.08979 -0.27095 295 PRO   B CG  
4054 C CD  . PRO   B 202 ? 0.91459 1.14094 0.79602 0.24861  -0.11498 -0.28560 295 PRO   B CD  
4055 N N   . TYR   B 203 ? 0.95452 1.08839 0.83389 0.19072  -0.13646 -0.20616 296 TYR   B N   
4056 C CA  . TYR   B 203 ? 0.91681 1.00111 0.77558 0.17124  -0.14650 -0.18460 296 TYR   B CA  
4057 C C   . TYR   B 203 ? 0.88823 0.96921 0.73739 0.14940  -0.13761 -0.17221 296 TYR   B C   
4058 O O   . TYR   B 203 ? 0.97781 1.01379 0.80301 0.13966  -0.15011 -0.16485 296 TYR   B O   
4059 C CB  . TYR   B 203 ? 0.94967 1.04097 0.82483 0.15821  -0.14166 -0.16795 296 TYR   B CB  
4060 C CG  . TYR   B 203 ? 0.97861 1.05514 0.85379 0.17770  -0.15746 -0.17653 296 TYR   B CG  
4061 C CD1 . TYR   B 203 ? 1.02860 1.08050 0.88769 0.20555  -0.17734 -0.19705 296 TYR   B CD1 
4062 C CD2 . TYR   B 203 ? 0.97150 1.05633 0.86073 0.16964  -0.15424 -0.16486 296 TYR   B CD2 
4063 C CE1 . TYR   B 203 ? 1.04428 1.07992 0.90121 0.22576  -0.19485 -0.20553 296 TYR   B CE1 
4064 C CE2 . TYR   B 203 ? 1.01832 1.08758 0.90480 0.18832  -0.17082 -0.17286 296 TYR   B CE2 
4065 C CZ  . TYR   B 203 ? 1.10690 1.15128 0.97710 0.21677  -0.19176 -0.19307 296 TYR   B CZ  
4066 O OH  . TYR   B 203 ? 1.07757 1.10389 0.94301 0.23771  -0.21119 -0.20168 296 TYR   B OH  
4067 N N   . GLY   B 204 ? 0.86818 0.99504 0.73442 0.14090  -0.11686 -0.17014 297 GLY   B N   
4068 C CA  . GLY   B 204 ? 0.93728 1.06114 0.79259 0.12345  -0.11075 -0.16011 297 GLY   B CA  
4069 C C   . GLY   B 204 ? 0.99680 1.09744 0.82596 0.13396  -0.12141 -0.17433 297 GLY   B C   
4070 O O   . GLY   B 204 ? 0.98372 1.06066 0.79641 0.12057  -0.12708 -0.16639 297 GLY   B O   
4071 N N   . ILE   B 205 ? 0.97975 1.08831 0.80586 0.15856  -0.12489 -0.19703 298 ILE   B N   
4072 C CA  . ILE   B 205 ? 0.93384 1.01761 0.73307 0.17133  -0.13630 -0.21304 298 ILE   B CA  
4073 C C   . ILE   B 205 ? 0.99890 1.01970 0.77317 0.17239  -0.16150 -0.21107 298 ILE   B C   
4074 O O   . ILE   B 205 ? 1.12891 1.11731 0.87861 0.16685  -0.17170 -0.21188 298 ILE   B O   
4075 C CB  . ILE   B 205 ? 0.99077 1.10447 0.79613 0.19884  -0.13197 -0.24021 298 ILE   B CB  
4076 C CG1 . ILE   B 205 ? 0.99473 1.16639 0.81649 0.19254  -0.10483 -0.24252 298 ILE   B CG1 
4077 C CG2 . ILE   B 205 ? 0.99361 1.07340 0.76911 0.21663  -0.14818 -0.25927 298 ILE   B CG2 
4078 C CD1 . ILE   B 205 ? 1.16662 1.33455 0.96458 0.18253  -0.09857 -0.24075 298 ILE   B CD1 
4079 N N   . LEU   B 206 ? 1.00986 1.00995 0.78745 0.17820  -0.17229 -0.20831 299 LEU   B N   
4080 C CA  . LEU   B 206 ? 1.08445 1.01867 0.83280 0.17787  -0.19598 -0.20578 299 LEU   B CA  
4081 C C   . LEU   B 206 ? 0.99831 0.90648 0.73689 0.14651  -0.19662 -0.18461 299 LEU   B C   
4082 O O   . LEU   B 206 ? 1.13634 0.99752 0.84715 0.14112  -0.21195 -0.18613 299 LEU   B O   
4083 C CB  . LEU   B 206 ? 1.00850 0.92572 0.75954 0.18870  -0.20626 -0.20479 299 LEU   B CB  
4084 C CG  . LEU   B 206 ? 1.11438 1.03798 0.86724 0.22457  -0.21673 -0.22996 299 LEU   B CG  
4085 C CD1 . LEU   B 206 ? 1.19353 1.11188 0.95533 0.23260  -0.22415 -0.22627 299 LEU   B CD1 
4086 C CD2 . LEU   B 206 ? 1.14164 1.00925 0.85752 0.24216  -0.24027 -0.24573 299 LEU   B CD2 
4087 N N   . ALA   B 207 ? 0.87572 0.81456 0.63784 0.12554  -0.18051 -0.16609 300 ALA   B N   
4088 C CA  . ALA   B 207 ? 1.01369 0.93542 0.77242 0.09660  -0.18031 -0.14805 300 ALA   B CA  
4089 C C   . ALA   B 207 ? 0.95207 0.87896 0.70292 0.08966  -0.17970 -0.15166 300 ALA   B C   
4090 O O   . ALA   B 207 ? 0.97392 0.86783 0.70947 0.07373  -0.19035 -0.14719 300 ALA   B O   
4091 C CB  . ALA   B 207 ? 0.84851 0.80501 0.63566 0.07950  -0.16342 -0.13001 300 ALA   B CB  
4092 N N   . ALA   B 208 ? 0.99190 0.95930 0.75151 0.10037  -0.16741 -0.16022 301 ALA   B N   
4093 C CA  . ALA   B 208 ? 1.04953 1.02030 0.79711 0.09542  -0.16763 -0.16406 301 ALA   B CA  
4094 C C   . ALA   B 208 ? 0.98418 0.91174 0.70051 0.10702  -0.18681 -0.18050 301 ALA   B C   
4095 O O   . ALA   B 208 ? 1.04038 0.94893 0.74160 0.09587  -0.19544 -0.18034 301 ALA   B O   
4096 C CB  . ALA   B 208 ? 0.99511 1.01433 0.75248 0.10403  -0.14915 -0.16960 301 ALA   B CB  
4097 N N   . SER   B 209 ? 1.04395 0.95481 0.75024 0.13037  -0.19518 -0.19599 302 SER   B N   
4098 C CA  . SER   B 209 ? 1.11576 0.98050 0.78986 0.14386  -0.21510 -0.21291 302 SER   B CA  
4099 C C   . SER   B 209 ? 1.19265 0.99886 0.84700 0.12577  -0.23349 -0.20338 302 SER   B C   
4100 O O   . SER   B 209 ? 1.20776 0.97670 0.83606 0.12327  -0.24827 -0.21121 302 SER   B O   
4101 C CB  . SER   B 209 ? 1.18395 1.04630 0.85396 0.17601  -0.22078 -0.23320 302 SER   B CB  
4102 O OG  . SER   B 209 ? 1.20628 1.12748 0.89757 0.18988  -0.20130 -0.24318 302 SER   B OG  
4103 N N   . ALA   B 210 ? 1.11298 0.90943 0.77752 0.11169  -0.23234 -0.18709 303 ALA   B N   
4104 C CA  . ALA   B 210 ? 1.09884 0.84136 0.74388 0.08973  -0.24636 -0.17685 303 ALA   B CA  
4105 C C   . ALA   B 210 ? 1.07525 0.82899 0.72934 0.06050  -0.24177 -0.16584 303 ALA   B C   
4106 O O   . ALA   B 210 ? 1.20540 0.91721 0.83913 0.04445  -0.25547 -0.16600 303 ALA   B O   
4107 C CB  . ALA   B 210 ? 1.07928 0.80946 0.72997 0.08252  -0.24459 -0.16293 303 ALA   B CB  
4108 N N   . LEU   B 211 ? 1.10098 0.91020 0.78538 0.05324  -0.22363 -0.15700 304 LEU   B N   
4109 C CA  . LEU   B 211 ? 1.21639 1.04081 0.91141 0.02994  -0.22120 -0.14906 304 LEU   B CA  
4110 C C   . LEU   B 211 ? 1.12101 0.93574 0.79605 0.03659  -0.23171 -0.16366 304 LEU   B C   
4111 O O   . LEU   B 211 ? 1.20490 1.00515 0.87529 0.01776  -0.24099 -0.16244 304 LEU   B O   
4112 C CB  . LEU   B 211 ? 1.19430 1.07582 0.92220 0.02478  -0.20141 -0.13721 304 LEU   B CB  
4113 C CG  . LEU   B 211 ? 1.15955 1.06601 0.90033 0.00833  -0.19898 -0.13153 304 LEU   B CG  
4114 C CD1 . LEU   B 211 ? 1.14318 1.02693 0.88667 -0.01833 -0.20862 -0.12524 304 LEU   B CD1 
4115 C CD2 . LEU   B 211 ? 1.17067 1.12584 0.93967 0.00642  -0.18059 -0.11965 304 LEU   B CD2 
4116 N N   . TYR   B 212 ? 1.20424 1.02825 0.86768 0.06296  -0.23031 -0.17891 305 TYR   B N   
4117 C CA  . TYR   B 212 ? 1.16813 0.98072 0.80813 0.07128  -0.24009 -0.19440 305 TYR   B CA  
4118 C C   . TYR   B 212 ? 1.20855 0.95981 0.81901 0.06636  -0.26289 -0.20282 305 TYR   B C   
4119 O O   . TYR   B 212 ? 1.28448 1.02107 0.88152 0.05639  -0.27377 -0.20802 305 TYR   B O   
4120 C CB  . TYR   B 212 ? 1.13844 0.97208 0.77069 0.10096  -0.23251 -0.21107 305 TYR   B CB  
4121 C CG  . TYR   B 212 ? 1.20189 1.01119 0.80217 0.11429  -0.24545 -0.23106 305 TYR   B CG  
4122 C CD1 . TYR   B 212 ? 1.25421 1.07759 0.84626 0.10743  -0.24470 -0.23271 305 TYR   B CD1 
4123 C CD2 . TYR   B 212 ? 1.21825 0.98788 0.79422 0.13495  -0.25998 -0.24899 305 TYR   B CD2 
4124 C CE1 . TYR   B 212 ? 1.23569 1.03567 0.79607 0.11953  -0.25684 -0.25156 305 TYR   B CE1 
4125 C CE2 . TYR   B 212 ? 1.38526 1.13121 0.93073 0.14797  -0.27213 -0.26853 305 TYR   B CE2 
4126 C CZ  . TYR   B 212 ? 1.36533 1.12727 0.90310 0.13954  -0.26988 -0.26968 305 TYR   B CZ  
4127 O OH  . TYR   B 212 ? 1.40416 1.14163 0.90923 0.15249  -0.28218 -0.28973 305 TYR   B OH  
4128 N N   . HIS   B 213 ? 1.24902 0.96089 0.84661 0.07305  -0.27167 -0.20451 306 HIS   B N   
4129 C CA  . HIS   B 213 ? 1.31910 0.96440 0.88284 0.06825  -0.29410 -0.21217 306 HIS   B CA  
4130 C C   . HIS   B 213 ? 1.23444 0.86029 0.80124 0.03151  -0.29933 -0.19886 306 HIS   B C   
4131 O O   . HIS   B 213 ? 1.34799 0.92474 0.88789 0.02151  -0.31713 -0.20606 306 HIS   B O   
4132 C CB  . HIS   B 213 ? 1.29417 0.89805 0.84007 0.08453  -0.30324 -0.21561 306 HIS   B CB  
4133 C CG  . HIS   B 213 ? 1.41915 1.02557 0.95310 0.12291  -0.30701 -0.23695 306 HIS   B CG  
4134 N ND1 . HIS   B 213 ? 1.34683 0.99992 0.90439 0.14397  -0.29222 -0.23957 306 HIS   B ND1 
4135 C CD2 . HIS   B 213 ? 1.35347 0.92386 0.85593 0.14404  -0.32362 -0.25848 306 HIS   B CD2 
4136 C CE1 . HIS   B 213 ? 1.37742 1.02680 0.92105 0.17630  -0.29877 -0.26251 306 HIS   B CE1 
4137 N NE2 . HIS   B 213 ? 1.42875 1.02746 0.93809 0.17808  -0.31793 -0.27442 306 HIS   B NE2 
4138 N N   . PHE   B 214 ? 1.21004 0.87404 0.80957 0.01091  -0.28419 -0.18110 307 PHE   B N   
4139 C CA  . PHE   B 214 ? 1.31167 0.96954 0.92167 -0.02432 -0.28624 -0.17032 307 PHE   B CA  
4140 C C   . PHE   B 214 ? 1.27203 0.97700 0.90605 -0.03430 -0.28131 -0.16961 307 PHE   B C   
4141 O O   . PHE   B 214 ? 1.33693 1.05170 0.98954 -0.06226 -0.28092 -0.16168 307 PHE   B O   
4142 C CB  . PHE   B 214 ? 1.16412 0.82861 0.79283 -0.04168 -0.27416 -0.15233 307 PHE   B CB  
4143 C CG  . PHE   B 214 ? 1.20840 0.81218 0.80639 -0.04179 -0.28373 -0.15082 307 PHE   B CG  
4144 C CD1 . PHE   B 214 ? 1.24121 0.79337 0.81778 -0.06969 -0.29459 -0.14768 307 PHE   B CD1 
4145 C CD2 . PHE   B 214 ? 1.17155 0.76841 0.76054 -0.01452 -0.28264 -0.15309 307 PHE   B CD2 
4146 C CE1 . PHE   B 214 ? 1.38702 0.87546 0.92797 -0.07036 -0.30450 -0.14512 307 PHE   B CE1 
4147 C CE2 . PHE   B 214 ? 1.34189 0.87826 0.89850 -0.01237 -0.29441 -0.15182 307 PHE   B CE2 
4148 C CZ  . PHE   B 214 ? 1.35676 0.83568 0.88641 -0.04029 -0.30552 -0.14700 307 PHE   B CZ  
4149 N N   . SER   B 215 ? 1.28356 1.01762 0.91650 -0.01208 -0.27780 -0.17849 308 SER   B N   
4150 C CA  . SER   B 215 ? 1.22446 0.99756 0.87314 -0.01855 -0.27550 -0.17799 308 SER   B CA  
4151 C C   . SER   B 215 ? 1.19678 0.97160 0.82143 0.00482  -0.28040 -0.19394 308 SER   B C   
4152 O O   . SER   B 215 ? 1.22051 0.95688 0.81644 0.00820  -0.29736 -0.20830 308 SER   B O   
4153 C CB  . SER   B 215 ? 1.11700 0.94379 0.80084 -0.02170 -0.25593 -0.16267 308 SER   B CB  
4154 O OG  . SER   B 215 ? 1.17293 1.01703 0.85701 0.00084  -0.24210 -0.16220 308 SER   B OG  
4155 N N   . SER   B 216 ? 1.17547 0.99260 0.80908 0.01996  -0.26519 -0.19190 309 SER   B N   
4156 C CA  . SER   B 216 ? 1.24929 1.07219 0.85860 0.04020  -0.26618 -0.20629 309 SER   B CA  
4157 C C   . SER   B 216 ? 1.23559 1.09898 0.85418 0.05713  -0.24432 -0.20305 309 SER   B C   
4158 O O   . SER   B 216 ? 1.19976 1.08844 0.84541 0.05158  -0.23024 -0.18883 309 SER   B O   
4159 C CB  . SER   B 216 ? 1.33903 1.17059 0.94378 0.02950  -0.27597 -0.20780 309 SER   B CB  
4160 O OG  . SER   B 216 ? 1.26360 1.13547 0.89731 0.01767  -0.26556 -0.19194 309 SER   B OG  
4161 N N   . SER   B 217 ? 1.33727 1.20644 0.93195 0.07678  -0.24103 -0.21737 310 SER   B N   
4162 C CA  . SER   B 217 ? 1.25263 1.16150 0.85329 0.09042  -0.21881 -0.21640 310 SER   B CA  
4163 C C   . SER   B 217 ? 1.23690 1.18005 0.84945 0.07833  -0.20779 -0.20113 310 SER   B C   
4164 O O   . SER   B 217 ? 1.20571 1.18177 0.83179 0.08153  -0.18796 -0.19358 310 SER   B O   
4165 C CB  . SER   B 217 ? 1.35302 1.25861 0.92276 0.11336  -0.21696 -0.23791 310 SER   B CB  
4166 O OG  . SER   B 217 ? 1.52358 1.41424 1.06522 0.11093  -0.22909 -0.24522 310 SER   B OG  
4167 N N   . GLU   B 218 ? 1.27615 1.21118 0.88353 0.06485  -0.22146 -0.19725 311 GLU   B N   
4168 C CA  . GLU   B 218 ? 1.24382 1.20684 0.86101 0.05522  -0.21493 -0.18313 311 GLU   B CA  
4169 C C   . GLU   B 218 ? 1.14607 1.12849 0.80236 0.04115  -0.20691 -0.16501 311 GLU   B C   
4170 O O   . GLU   B 218 ? 1.23069 1.24151 0.89871 0.04089  -0.19089 -0.15357 311 GLU   B O   
4171 C CB  . GLU   B 218 ? 1.33569 1.28522 0.93857 0.04684  -0.23520 -0.18635 311 GLU   B CB  
4172 C CG  . GLU   B 218 ? 1.29136 1.22402 0.85111 0.06065  -0.24236 -0.20318 311 GLU   B CG  
4173 C CD  . GLU   B 218 ? 1.42953 1.32725 0.97208 0.06866  -0.25454 -0.22114 311 GLU   B CD  
4174 O OE1 . GLU   B 218 ? 1.44403 1.32484 1.00556 0.06033  -0.26135 -0.21938 311 GLU   B OE1 
4175 O OE2 . GLU   B 218 ? 1.59537 1.47985 1.10245 0.08332  -0.25742 -0.23725 311 GLU   B OE2 
4176 N N   . LEU   B 219 ? 1.24458 1.20998 0.91895 0.02827  -0.21741 -0.16248 312 LEU   B N   
4177 C CA  . LEU   B 219 ? 1.10446 1.08685 0.81391 0.01499  -0.20876 -0.14675 312 LEU   B CA  
4178 C C   . LEU   B 219 ? 1.09139 1.08585 0.80929 0.02556  -0.19078 -0.14333 312 LEU   B C   
4179 O O   . LEU   B 219 ? 1.01229 1.03257 0.75374 0.02041  -0.17729 -0.13006 312 LEU   B O   
4180 C CB  . LEU   B 219 ? 1.18441 1.14282 0.90593 -0.00274 -0.22221 -0.14618 312 LEU   B CB  
4181 C CG  . LEU   B 219 ? 1.14672 1.12038 0.90212 -0.01832 -0.21307 -0.13117 312 LEU   B CG  
4182 C CD1 . LEU   B 219 ? 1.24771 1.25714 1.02663 -0.02635 -0.20868 -0.12082 312 LEU   B CD1 
4183 C CD2 . LEU   B 219 ? 1.22079 1.16534 0.98072 -0.03718 -0.22417 -0.13206 312 LEU   B CD2 
4184 N N   . MET   B 220 ? 1.07087 1.04736 0.77047 0.04135  -0.19155 -0.15661 313 MET   B N   
4185 C CA  . MET   B 220 ? 1.14855 1.13953 0.85763 0.05375  -0.17648 -0.15678 313 MET   B CA  
4186 C C   . MET   B 220 ? 1.16925 1.19939 0.88330 0.05883  -0.15671 -0.15200 313 MET   B C   
4187 O O   . MET   B 220 ? 1.06181 1.11552 0.79904 0.05500  -0.14283 -0.14081 313 MET   B O   
4188 C CB  . MET   B 220 ? 1.20383 1.17037 0.89104 0.07338  -0.18339 -0.17579 313 MET   B CB  
4189 C CG  . MET   B 220 ? 1.16262 1.14527 0.86106 0.08940  -0.17103 -0.18029 313 MET   B CG  
4190 S SD  . MET   B 220 ? 1.17055 1.19928 0.86768 0.10440  -0.14829 -0.18870 313 MET   B SD  
4191 C CE  . MET   B 220 ? 1.30956 1.32012 0.96784 0.11311  -0.15799 -0.20581 313 MET   B CE  
4192 N N   . GLN   B 221 ? 1.20296 1.23776 0.89225 0.06625  -0.15513 -0.16037 314 GLN   B N   
4193 C CA  . GLN   B 221 ? 1.25393 1.32045 0.94038 0.06902  -0.13548 -0.15611 314 GLN   B CA  
4194 C C   . GLN   B 221 ? 1.20167 1.28314 0.90330 0.05335  -0.13178 -0.13667 314 GLN   B C   
4195 O O   . GLN   B 221 ? 1.23406 1.34018 0.94347 0.05168  -0.11418 -0.12808 314 GLN   B O   
4196 C CB  . GLN   B 221 ? 1.15861 1.22097 0.80827 0.07906  -0.13530 -0.16962 314 GLN   B CB  
4197 C CG  . GLN   B 221 ? 1.25906 1.35059 0.89851 0.08225  -0.11218 -0.16865 314 GLN   B CG  
4198 C CD  . GLN   B 221 ? 1.22893 1.31523 0.82895 0.09343  -0.10981 -0.18517 314 GLN   B CD  
4199 O OE1 . GLN   B 221 ? 1.36087 1.42040 0.94013 0.09907  -0.12758 -0.19654 314 GLN   B OE1 
4200 N NE2 . GLN   B 221 ? 1.36489 1.47620 0.95298 0.09545  -0.08710 -0.18719 314 GLN   B NE2 
4201 N N   . LYS   B 222 ? 1.25019 1.31756 0.95697 0.04182  -0.14850 -0.13076 315 LYS   B N   
4202 C CA  . LYS   B 222 ? 1.21957 1.30182 0.94271 0.02956  -0.14749 -0.11471 315 LYS   B CA  
4203 C C   . LYS   B 222 ? 1.22786 1.32656 0.98498 0.02256  -0.13606 -0.10254 315 LYS   B C   
4204 O O   . LYS   B 222 ? 1.26812 1.38557 1.03593 0.01791  -0.12613 -0.09031 315 LYS   B O   
4205 C CB  . LYS   B 222 ? 1.28203 1.35017 1.00789 0.01964  -0.16902 -0.11498 315 LYS   B CB  
4206 C CG  . LYS   B 222 ? 1.34774 1.43280 1.09870 0.00798  -0.17104 -0.10103 315 LYS   B CG  
4207 C CD  . LYS   B 222 ? 1.43181 1.50819 1.19192 -0.00233 -0.19255 -0.10496 315 LYS   B CD  
4208 C CE  . LYS   B 222 ? 1.51019 1.60818 1.30182 -0.01257 -0.19449 -0.09386 315 LYS   B CE  
4209 N NZ  . LYS   B 222 ? 1.43314 1.52962 1.23994 -0.02385 -0.21467 -0.10009 315 LYS   B NZ  
4210 N N   . VAL   B 223 ? 1.17131 1.25973 0.94209 0.02221  -0.13807 -0.10585 316 VAL   B N   
4211 C CA  . VAL   B 223 ? 1.17869 1.27788 0.97904 0.01448  -0.13000 -0.09478 316 VAL   B CA  
4212 C C   . VAL   B 223 ? 1.13123 1.24064 0.93614 0.02509  -0.11589 -0.09784 316 VAL   B C   
4213 O O   . VAL   B 223 ? 0.99972 1.12198 0.82707 0.02001  -0.10695 -0.08825 316 VAL   B O   
4214 C CB  . VAL   B 223 ? 1.19197 1.27029 1.00439 0.00255  -0.14301 -0.09382 316 VAL   B CB  
4215 C CG1 . VAL   B 223 ? 1.15822 1.22844 0.96711 -0.00742 -0.15865 -0.09558 316 VAL   B CG1 
4216 C CG2 . VAL   B 223 ? 1.02286 1.07364 0.82098 0.01116  -0.14935 -0.10520 316 VAL   B CG2 
4217 N N   . SER   B 224 ? 1.16628 1.27230 0.95205 0.04019  -0.11404 -0.11233 317 SER   B N   
4218 C CA  . SER   B 224 ? 1.12350 1.24461 0.91720 0.05194  -0.10171 -0.11864 317 SER   B CA  
4219 C C   . SER   B 224 ? 1.14198 1.29213 0.92867 0.05791  -0.08349 -0.12233 317 SER   B C   
4220 O O   . SER   B 224 ? 1.15077 1.32404 0.95287 0.06241  -0.06961 -0.12404 317 SER   B O   
4221 C CB  . SER   B 224 ? 1.05738 1.15487 0.83863 0.06688  -0.11310 -0.13563 317 SER   B CB  
4222 O OG  . SER   B 224 ? 1.18660 1.27428 0.94049 0.07618  -0.11857 -0.14962 317 SER   B OG  
4223 N N   . GLY   B 225 ? 1.14930 1.29819 0.91179 0.05693  -0.08316 -0.12392 318 GLY   B N   
4224 C CA  . GLY   B 225 ? 1.19204 1.36364 0.94038 0.06011  -0.06483 -0.12758 318 GLY   B CA  
4225 C C   . GLY   B 225 ? 1.33177 1.51120 1.06769 0.07654  -0.05859 -0.14893 318 GLY   B C   
4226 O O   . GLY   B 225 ? 1.39517 1.59341 1.11500 0.07794  -0.04211 -0.15441 318 GLY   B O   
4227 N N   . TYR   B 226 ? 1.23728 1.40171 0.97823 0.08902  -0.07111 -0.16186 319 TYR   B N   
4228 C CA  . TYR   B 226 ? 1.26139 1.43382 0.99358 0.10826  -0.06737 -0.18497 319 TYR   B CA  
4229 C C   . TYR   B 226 ? 1.38193 1.52966 1.07901 0.11550  -0.07901 -0.19739 319 TYR   B C   
4230 O O   . TYR   B 226 ? 1.33181 1.44577 1.01883 0.11095  -0.09909 -0.19329 319 TYR   B O   
4231 C CB  . TYR   B 226 ? 1.24282 1.40672 0.99460 0.12114  -0.07770 -0.19377 319 TYR   B CB  
4232 C CG  . TYR   B 226 ? 1.22297 1.40925 1.00792 0.11557  -0.06841 -0.18323 319 TYR   B CG  
4233 C CD1 . TYR   B 226 ? 1.24199 1.46383 1.03975 0.10474  -0.04695 -0.17425 319 TYR   B CD1 
4234 C CD2 . TYR   B 226 ? 1.16955 1.33761 0.96925 0.12048  -0.08176 -0.18221 319 TYR   B CD2 
4235 C CE1 . TYR   B 226 ? 1.23851 1.47967 1.06587 0.09943  -0.03940 -0.16556 319 TYR   B CE1 
4236 C CE2 . TYR   B 226 ? 1.16472 1.35172 0.99214 0.11591  -0.07436 -0.17322 319 TYR   B CE2 
4237 C CZ  . TYR   B 226 ? 1.09051 1.31536 0.93318 0.10563  -0.05333 -0.16543 319 TYR   B CZ  
4238 O OH  . TYR   B 226 ? 1.16009 1.40287 1.02974 0.10084  -0.04678 -0.15739 319 TYR   B OH  
4239 N N   . GLN   B 227 ? 1.46689 1.63256 1.14538 0.12571  -0.06577 -0.21354 320 GLN   B N   
4240 C CA  . GLN   B 227 ? 1.42682 1.57012 1.06918 0.13451  -0.07563 -0.22788 320 GLN   B CA  
4241 C C   . GLN   B 227 ? 1.40068 1.51680 1.04186 0.15258  -0.09529 -0.24564 320 GLN   B C   
4242 O O   . GLN   B 227 ? 1.43468 1.55284 1.10061 0.16081  -0.09885 -0.24898 320 GLN   B O   
4243 C CB  . GLN   B 227 ? 1.46432 1.63578 1.08567 0.14004  -0.05339 -0.24139 320 GLN   B CB  
4244 C CG  . GLN   B 227 ? 1.68299 1.83203 1.25920 0.14211  -0.06001 -0.24907 320 GLN   B CG  
4245 C CD  . GLN   B 227 ? 1.74172 1.91840 1.29395 0.14647  -0.03547 -0.26321 320 GLN   B CD  
4246 O OE1 . GLN   B 227 ? 1.80049 1.96195 1.31379 0.15231  -0.03845 -0.27495 320 GLN   B OE1 
4247 N NE2 . GLN   B 227 ? 1.76132 1.97912 1.33579 0.14232  -0.01039 -0.26281 320 GLN   B NE2 
4248 N N   . TRP   B 228 ? 1.30822 1.39472 0.91691 0.15910  -0.10974 -0.25726 321 TRP   B N   
4249 C CA  . TRP   B 228 ? 1.38577 1.43792 0.98660 0.17565  -0.13072 -0.27419 321 TRP   B CA  
4250 C C   . TRP   B 228 ? 1.46910 1.54268 1.07947 0.20030  -0.12230 -0.29757 321 TRP   B C   
4251 O O   . TRP   B 228 ? 1.47310 1.52525 1.09207 0.21416  -0.13750 -0.30642 321 TRP   B O   
4252 C CB  . TRP   B 228 ? 1.41279 1.43122 0.97475 0.17789  -0.14646 -0.28408 321 TRP   B CB  
4253 C CG  . TRP   B 228 ? 1.37680 1.36135 0.92362 0.19861  -0.16493 -0.30659 321 TRP   B CG  
4254 C CD1 . TRP   B 228 ? 1.45344 1.43902 0.97676 0.22067  -0.16302 -0.33292 321 TRP   B CD1 
4255 C CD2 . TRP   B 228 ? 1.42744 1.36920 0.97890 0.19943  -0.18814 -0.30532 321 TRP   B CD2 
4256 N NE1 . TRP   B 228 ? 1.53661 1.48104 1.05003 0.23702  -0.18549 -0.34852 321 TRP   B NE1 
4257 C CE2 . TRP   B 228 ? 1.41704 1.33166 0.94548 0.22345  -0.20133 -0.33116 321 TRP   B CE2 
4258 C CE3 . TRP   B 228 ? 1.24859 1.17061 0.81885 0.18150  -0.19851 -0.28519 321 TRP   B CE3 
4259 C CZ2 . TRP   B 228 ? 1.46988 1.33359 0.99068 0.22972  -0.22582 -0.33617 321 TRP   B CZ2 
4260 C CZ3 . TRP   B 228 ? 1.26743 1.14116 0.82984 0.18572  -0.22070 -0.28991 321 TRP   B CZ3 
4261 C CH2 . TRP   B 228 ? 1.37134 1.21398 0.90786 0.20949  -0.23484 -0.31458 321 TRP   B CH2 
4262 N N   . CYS   B 229 ? 1.49789 1.61337 1.10597 0.20602  -0.09846 -0.30868 322 CYS   B N   
4263 C CA  . CYS   B 229 ? 1.46676 1.61150 1.08844 0.22994  -0.08888 -0.33428 322 CYS   B CA  
4264 C C   . CYS   B 229 ? 1.38984 1.55813 1.05380 0.23212  -0.08485 -0.32926 322 CYS   B C   
4265 O O   . CYS   B 229 ? 1.40480 1.58530 1.08378 0.25554  -0.08776 -0.35080 322 CYS   B O   
4266 C CB  . CYS   B 229 ? 1.44897 1.63741 1.05906 0.23077  -0.06079 -0.34685 322 CYS   B CB  
4267 S SG  . CYS   B 229 ? 1.52574 1.75188 1.14691 0.20104  -0.03253 -0.32065 322 CYS   B SG  
4268 N N   . ASP   B 230 ? 1.39013 1.56460 1.07304 0.20974  -0.07961 -0.30262 323 ASP   B N   
4269 C CA  . ASP   B 230 ? 1.42363 1.61817 1.14438 0.21085  -0.07674 -0.29718 323 ASP   B CA  
4270 C C   . ASP   B 230 ? 1.33251 1.48330 1.05595 0.22165  -0.10407 -0.29770 323 ASP   B C   
4271 O O   . ASP   B 230 ? 1.28277 1.44479 1.02961 0.23575  -0.10724 -0.30582 323 ASP   B O   
4272 C CB  . ASP   B 230 ? 1.28162 1.49185 1.01849 0.18402  -0.06379 -0.26907 323 ASP   B CB  
4273 C CG  . ASP   B 230 ? 1.36952 1.61650 1.09896 0.17150  -0.03713 -0.26639 323 ASP   B CG  
4274 O OD1 . ASP   B 230 ? 1.45692 1.73110 1.17911 0.18351  -0.02303 -0.28799 323 ASP   B OD1 
4275 O OD2 . ASP   B 230 ? 1.36022 1.60762 1.08939 0.14958  -0.03016 -0.24320 323 ASP   B OD2 
4276 N N   . ILE   B 231 ? 1.28930 1.38891 0.98752 0.21459  -0.12448 -0.28958 324 ILE   B N   
4277 C CA  . ILE   B 231 ? 1.34140 1.39192 1.03587 0.21870  -0.14969 -0.28645 324 ILE   B CA  
4278 C C   . ILE   B 231 ? 1.33777 1.34703 1.00278 0.24031  -0.17048 -0.30877 324 ILE   B C   
4279 O O   . ILE   B 231 ? 1.30262 1.26349 0.95762 0.24500  -0.19297 -0.30814 324 ILE   B O   
4280 C CB  . ILE   B 231 ? 1.27167 1.29274 0.96305 0.19063  -0.15785 -0.25953 324 ILE   B CB  
4281 C CG1 . ILE   B 231 ? 1.32637 1.31896 0.98712 0.18219  -0.16779 -0.26021 324 ILE   B CG1 
4282 C CG2 . ILE   B 231 ? 1.18063 1.24154 0.89776 0.17037  -0.13742 -0.23865 324 ILE   B CG2 
4283 C CD1 . ILE   B 231 ? 1.27052 1.23255 0.92978 0.15674  -0.17961 -0.23895 324 ILE   B CD1 
4284 N N   . GLU   B 232 ? 1.26287 1.28635 0.91034 0.25324  -0.16381 -0.32867 325 GLU   B N   
4285 C CA  . GLU   B 232 ? 1.34150 1.32270 0.95798 0.27402  -0.18445 -0.35081 325 GLU   B CA  
4286 C C   . GLU   B 232 ? 1.32949 1.29680 0.95357 0.30261  -0.19898 -0.36927 325 GLU   B C   
4287 O O   . GLU   B 232 ? 1.42002 1.32855 1.02017 0.31240  -0.22519 -0.37529 325 GLU   B O   
4288 C CB  . GLU   B 232 ? 1.38545 1.39128 0.98289 0.28436  -0.17140 -0.37081 325 GLU   B CB  
4289 C CG  . GLU   B 232 ? 1.31313 1.27853 0.87857 0.30919  -0.19171 -0.39736 325 GLU   B CG  
4290 C CD  . GLU   B 232 ? 1.53808 1.52802 1.08190 0.31872  -0.17751 -0.41758 325 GLU   B CD  
4291 O OE1 . GLU   B 232 ? 1.51725 1.55005 1.06628 0.30293  -0.15265 -0.40832 325 GLU   B OE1 
4292 O OE2 . GLU   B 232 ? 1.66789 1.63134 1.18633 0.34193  -0.19140 -0.44290 325 GLU   B OE2 
4293 N N   . ASN   B 233 ? 1.26304 1.28222 0.91926 0.31627  -0.18349 -0.37905 326 ASN   B N   
4294 C CA  . ASN   B 233 ? 1.28284 1.29233 0.94905 0.34588  -0.19919 -0.39769 326 ASN   B CA  
4295 C C   . ASN   B 233 ? 1.36523 1.32507 1.02957 0.33657  -0.21985 -0.37728 326 ASN   B C   
4296 O O   . ASN   B 233 ? 1.36629 1.27745 1.01352 0.35705  -0.24546 -0.38827 326 ASN   B O   
4297 C CB  . ASN   B 233 ? 1.37068 1.45339 1.07717 0.35912  -0.17726 -0.41201 326 ASN   B CB  
4298 C CG  . ASN   B 233 ? 1.46028 1.54475 1.17487 0.39891  -0.19240 -0.44387 326 ASN   B CG  
4299 O OD1 . ASN   B 233 ? 1.41648 1.46430 1.10331 0.42167  -0.21056 -0.46475 326 ASN   B OD1 
4300 N ND2 . ASN   B 233 ? 1.42924 1.55593 1.18202 0.40861  -0.18647 -0.44895 326 ASN   B ND2 
4301 N N   . CYS   B 234 ? 1.24920 1.21786 0.92790 0.30573  -0.20926 -0.34776 327 CYS   B N   
4302 C CA  . CYS   B 234 ? 1.27612 1.19961 0.95137 0.29345  -0.22567 -0.32748 327 CYS   B CA  
4303 C C   . CYS   B 234 ? 1.34776 1.20079 0.98481 0.28024  -0.24679 -0.31900 327 CYS   B C   
4304 O O   . CYS   B 234 ? 1.32141 1.11714 0.93895 0.28401  -0.26928 -0.31637 327 CYS   B O   
4305 C CB  . CYS   B 234 ? 1.21163 1.16984 0.91530 0.26541  -0.20653 -0.30078 327 CYS   B CB  
4306 S SG  . CYS   B 234 ? 1.22738 1.13665 0.92745 0.24758  -0.22199 -0.27546 327 CYS   B SG  
4307 N N   . VAL   B 235 ? 1.36933 1.22395 0.99352 0.26370  -0.24046 -0.31480 328 VAL   B N   
4308 C CA  . VAL   B 235 ? 1.23678 1.02899 0.82712 0.24973  -0.26034 -0.30926 328 VAL   B CA  
4309 C C   . VAL   B 235 ? 1.44792 1.18770 1.00586 0.27740  -0.28490 -0.33321 328 VAL   B C   
4310 O O   . VAL   B 235 ? 1.49311 1.16647 1.02415 0.27144  -0.30747 -0.32823 328 VAL   B O   
4311 C CB  . VAL   B 235 ? 1.40494 1.21461 0.98886 0.23108  -0.25012 -0.30428 328 VAL   B CB  
4312 C CG1 . VAL   B 235 ? 1.38112 1.12947 0.92878 0.22319  -0.27266 -0.30755 328 VAL   B CG1 
4313 C CG2 . VAL   B 235 ? 1.28345 1.12581 0.89312 0.20093  -0.23329 -0.27734 328 VAL   B CG2 
4314 N N   . LYS   B 236 ? 1.47339 1.24106 1.03220 0.30782  -0.28064 -0.36029 329 LYS   B N   
4315 C CA  . LYS   B 236 ? 1.54917 1.26913 1.07818 0.33864  -0.30463 -0.38618 329 LYS   B CA  
4316 C C   . LYS   B 236 ? 1.56465 1.24835 1.09206 0.35527  -0.32376 -0.38728 329 LYS   B C   
4317 O O   . LYS   B 236 ? 1.59838 1.21168 1.08999 0.36792  -0.35128 -0.39609 329 LYS   B O   
4318 C CB  . LYS   B 236 ? 1.61430 1.38151 1.14973 0.36864  -0.29292 -0.41687 329 LYS   B CB  
4319 C CG  . LYS   B 236 ? 1.79369 1.51380 1.29733 0.40305  -0.31758 -0.44706 329 LYS   B CG  
4320 C CD  . LYS   B 236 ? 1.80605 1.57719 1.31529 0.42936  -0.30273 -0.47815 329 LYS   B CD  
4321 C CE  . LYS   B 236 ? 1.77732 1.62436 1.33171 0.44597  -0.28168 -0.48910 329 LYS   B CE  
4322 N NZ  . LYS   B 236 ? 1.71977 1.61873 1.27987 0.47073  -0.26539 -0.52180 329 LYS   B NZ  
4323 N N   . TRP   B 237 ? 1.46934 1.19606 1.03183 0.35537  -0.31100 -0.37842 330 TRP   B N   
4324 C CA  . TRP   B 237 ? 1.53590 1.22644 1.09454 0.36993  -0.33034 -0.37745 330 TRP   B CA  
4325 C C   . TRP   B 237 ? 1.50939 1.13605 1.04421 0.33907  -0.34308 -0.34894 330 TRP   B C   
4326 O O   . TRP   B 237 ? 1.57163 1.13019 1.07549 0.34886  -0.36881 -0.34984 330 TRP   B O   
4327 C CB  . TRP   B 237 ? 1.41034 1.16841 1.01424 0.37900  -0.31326 -0.37802 330 TRP   B CB  
4328 C CG  . TRP   B 237 ? 1.55482 1.27686 1.15487 0.38778  -0.33202 -0.37125 330 TRP   B CG  
4329 C CD1 . TRP   B 237 ? 1.55296 1.24573 1.14120 0.42509  -0.35655 -0.39298 330 TRP   B CD1 
4330 C CD2 . TRP   B 237 ? 1.45381 1.16275 1.05871 0.35972  -0.32897 -0.34132 330 TRP   B CD2 
4331 N NE1 . TRP   B 237 ? 1.50501 1.16450 1.08759 0.42155  -0.36976 -0.37729 330 TRP   B NE1 
4332 C CE2 . TRP   B 237 ? 1.56617 1.23556 1.15857 0.38090  -0.35206 -0.34556 330 TRP   B CE2 
4333 C CE3 . TRP   B 237 ? 1.41760 1.14413 1.03527 0.32005  -0.30959 -0.31247 330 TRP   B CE3 
4334 C CZ2 . TRP   B 237 ? 1.52673 1.17301 1.11647 0.36200  -0.35487 -0.32121 330 TRP   B CZ2 
4335 C CZ3 . TRP   B 237 ? 1.40896 1.11583 1.02756 0.30209  -0.31168 -0.28967 330 TRP   B CZ3 
4336 C CH2 . TRP   B 237 ? 1.44811 1.11478 1.05156 0.32216  -0.33343 -0.29376 330 TRP   B CH2 
4337 N N   . MET   B 238 ? 1.44522 1.09212 0.99274 0.30167  -0.32540 -0.32413 331 MET   B N   
4338 C CA  . MET   B 238 ? 1.45028 1.04551 0.97928 0.26847  -0.33339 -0.29824 331 MET   B CA  
4339 C C   . MET   B 238 ? 1.58803 1.11283 1.07338 0.25914  -0.35379 -0.30144 331 MET   B C   
4340 O O   . MET   B 238 ? 1.62136 1.09829 1.08793 0.23013  -0.36150 -0.28240 331 MET   B O   
4341 C CB  . MET   B 238 ? 1.31592 0.96224 0.87661 0.23441  -0.30791 -0.27454 331 MET   B CB  
4342 C CG  . MET   B 238 ? 1.30751 0.92113 0.86309 0.20127  -0.30973 -0.24763 331 MET   B CG  
4343 S SD  . MET   B 238 ? 1.32300 1.00519 0.92189 0.16933  -0.27990 -0.22379 331 MET   B SD  
4344 C CE  . MET   B 238 ? 1.19410 0.93772 0.82940 0.19238  -0.26451 -0.22876 331 MET   B CE  
4345 N N   . VAL   B 239 ? 1.57714 1.09492 1.04571 0.28210  -0.36213 -0.32597 332 VAL   B N   
4346 C CA  . VAL   B 239 ? 1.73677 1.18905 1.16380 0.27281  -0.38160 -0.33071 332 VAL   B CA  
4347 C C   . VAL   B 239 ? 1.73078 1.09295 1.11713 0.26797  -0.40823 -0.32417 332 VAL   B C   
4348 O O   . VAL   B 239 ? 1.66242 0.98144 1.02919 0.23373  -0.41382 -0.30794 332 VAL   B O   
4349 C CB  . VAL   B 239 ? 1.63369 1.09303 1.04784 0.30375  -0.38687 -0.36120 332 VAL   B CB  
4350 C CG1 . VAL   B 239 ? 1.69756 1.07068 1.06063 0.30688  -0.41595 -0.37226 332 VAL   B CG1 
4351 C CG2 . VAL   B 239 ? 1.64185 1.16555 1.07811 0.29156  -0.36333 -0.36095 332 VAL   B CG2 
4352 N N   . PRO   B 240 ? 1.78614 1.11496 1.15674 0.29907  -0.42571 -0.33587 333 PRO   B N   
4353 C CA  . PRO   B 240 ? 1.83192 1.06384 1.15397 0.29284  -0.45283 -0.32856 333 PRO   B CA  
4354 C C   . PRO   B 240 ? 1.82407 1.04086 1.14794 0.25359  -0.44512 -0.29684 333 PRO   B C   
4355 O O   . PRO   B 240 ? 1.82414 0.96639 1.10830 0.22820  -0.45945 -0.28492 333 PRO   B O   
4356 C CB  . PRO   B 240 ? 1.98078 1.19441 1.29262 0.33963  -0.47155 -0.34906 333 PRO   B CB  
4357 C CG  . PRO   B 240 ? 1.87965 1.17181 1.22791 0.37161  -0.45762 -0.37452 333 PRO   B CG  
4358 C CD  . PRO   B 240 ? 1.78324 1.15635 1.17607 0.34207  -0.42393 -0.35824 333 PRO   B CD  
4359 N N   . PHE   B 241 ? 1.73868 1.02367 1.10651 0.24668  -0.42211 -0.28351 334 PHE   B N   
4360 C CA  . PHE   B 241 ? 1.79107 1.06633 1.16214 0.21058  -0.41303 -0.25475 334 PHE   B CA  
4361 C C   . PHE   B 241 ? 1.69461 0.97560 1.07123 0.16653  -0.40062 -0.23869 334 PHE   B C   
4362 O O   . PHE   B 241 ? 1.66668 0.90833 1.02678 0.13297  -0.40138 -0.21895 334 PHE   B O   
4363 C CB  . PHE   B 241 ? 1.59533 0.94468 1.01319 0.21630  -0.39182 -0.24688 334 PHE   B CB  
4364 C CG  . PHE   B 241 ? 1.59936 0.96348 1.02431 0.26104  -0.40121 -0.26667 334 PHE   B CG  
4365 C CD1 . PHE   B 241 ? 1.74226 1.05397 1.14064 0.27518  -0.42080 -0.26448 334 PHE   B CD1 
4366 C CD2 . PHE   B 241 ? 1.65425 1.08575 1.11214 0.28861  -0.39045 -0.28831 334 PHE   B CD2 
4367 C CE1 . PHE   B 241 ? 1.72972 1.05866 1.13813 0.31815  -0.43158 -0.28490 334 PHE   B CE1 
4368 C CE2 . PHE   B 241 ? 1.64799 1.09999 1.11775 0.32925  -0.39836 -0.30915 334 PHE   B CE2 
4369 C CZ  . PHE   B 241 ? 1.64071 1.04291 1.08778 0.34510  -0.41995 -0.30810 334 PHE   B CZ  
4370 N N   . ALA   B 242 ? 1.58394 0.91413 0.98311 0.16588  -0.38928 -0.24767 335 ALA   B N   
4371 C CA  . ALA   B 242 ? 1.68139 1.02430 1.09062 0.12682  -0.37891 -0.23445 335 ALA   B CA  
4372 C C   . ALA   B 242 ? 1.73377 0.99573 1.09752 0.10740  -0.40019 -0.23584 335 ALA   B C   
4373 O O   . ALA   B 242 ? 1.75493 1.00019 1.11684 0.06801  -0.39651 -0.21899 335 ALA   B O   
4374 C CB  . ALA   B 242 ? 1.65129 1.06317 1.09091 0.13394  -0.36388 -0.24443 335 ALA   B CB  
4375 N N   . MET   B 243 ? 1.66720 0.87856 0.99430 0.13397  -0.42238 -0.25692 336 MET   B N   
4376 C CA  . MET   B 243 ? 1.84362 0.97376 1.12441 0.11573  -0.44391 -0.25980 336 MET   B CA  
4377 C C   . MET   B 243 ? 1.89111 0.94247 1.13314 0.09806  -0.45714 -0.24504 336 MET   B C   
4378 O O   . MET   B 243 ? 1.89686 0.89425 1.11157 0.06286  -0.46492 -0.23653 336 MET   B O   
4379 C CB  . MET   B 243 ? 1.89697 0.99300 1.14730 0.15142  -0.46462 -0.28787 336 MET   B CB  
4380 C CG  . MET   B 243 ? 1.92316 1.06718 1.19171 0.15308  -0.45683 -0.30114 336 MET   B CG  
4381 S SD  . MET   B 243 ? 2.10204 1.22875 1.36601 0.10183  -0.45773 -0.28973 336 MET   B SD  
4382 C CE  . MET   B 243 ? 1.83080 1.06454 1.15892 0.08275  -0.42492 -0.27315 336 MET   B CE  
4383 N N   . VAL   B 244 ? 1.90251 0.94466 1.13957 0.12093  -0.46026 -0.24237 337 VAL   B N   
4384 C CA  . VAL   B 244 ? 1.89832 0.86415 1.09428 0.10379  -0.47206 -0.22646 337 VAL   B CA  
4385 C C   . VAL   B 244 ? 1.96072 0.94521 1.17477 0.05275  -0.45144 -0.20058 337 VAL   B C   
4386 O O   . VAL   B 244 ? 2.01289 0.92841 1.18829 0.01961  -0.45910 -0.18820 337 VAL   B O   
4387 C CB  . VAL   B 244 ? 2.13461 1.09843 1.32767 0.13988  -0.47849 -0.22883 337 VAL   B CB  
4388 C CG1 . VAL   B 244 ? 2.12655 1.02011 1.27947 0.11814  -0.48635 -0.20832 337 VAL   B CG1 
4389 C CG2 . VAL   B 244 ? 2.13397 1.06354 1.30097 0.18935  -0.50393 -0.25660 337 VAL   B CG2 
4390 N N   . ILE   B 245 ? 1.88314 0.96058 1.15528 0.04504  -0.42468 -0.19296 338 ILE   B N   
4391 C CA  . ILE   B 245 ? 1.83980 0.94457 1.13550 -0.00110 -0.40444 -0.17178 338 ILE   B CA  
4392 C C   . ILE   B 245 ? 1.90542 0.99958 1.19820 -0.03279 -0.40661 -0.17448 338 ILE   B C   
4393 O O   . ILE   B 245 ? 1.97847 1.04938 1.26368 -0.07533 -0.40171 -0.16070 338 ILE   B O   
4394 C CB  . ILE   B 245 ? 1.75224 0.95652 1.10919 0.00306  -0.37765 -0.16470 338 ILE   B CB  
4395 C CG1 . ILE   B 245 ? 1.72172 0.93561 1.08187 0.03295  -0.37675 -0.16319 338 ILE   B CG1 
4396 C CG2 . ILE   B 245 ? 1.84876 1.08377 1.23216 -0.04177 -0.35746 -0.14502 338 ILE   B CG2 
4397 C CD1 . ILE   B 245 ? 1.80314 0.95382 1.12659 0.01742  -0.38324 -0.14739 338 ILE   B CD1 
4398 N N   . ARG   B 246 ? 1.82674 0.93860 1.12522 -0.01327 -0.41390 -0.19340 339 ARG   B N   
4399 C CA  . ARG   B 246 ? 1.83894 0.94070 1.13404 -0.04085 -0.41882 -0.19831 339 ARG   B CA  
4400 C C   . ARG   B 246 ? 1.94616 0.94532 1.18156 -0.05805 -0.44229 -0.20076 339 ARG   B C   
4401 O O   . ARG   B 246 ? 1.96412 0.94518 1.19514 -0.09788 -0.44291 -0.19650 339 ARG   B O   
4402 C CB  . ARG   B 246 ? 1.81556 0.95887 1.12647 -0.01359 -0.42145 -0.21849 339 ARG   B CB  
4403 C CG  . ARG   B 246 ? 1.68756 0.93023 1.05508 -0.00720 -0.39750 -0.21496 339 ARG   B CG  
4404 C CD  . ARG   B 246 ? 1.64140 0.92446 1.04280 -0.04884 -0.38272 -0.20028 339 ARG   B CD  
4405 N NE  . ARG   B 246 ? 1.45629 0.82346 0.90276 -0.04070 -0.36608 -0.20120 339 ARG   B NE  
4406 C CZ  . ARG   B 246 ? 1.49493 0.91619 0.98137 -0.06604 -0.34965 -0.18826 339 ARG   B CZ  
4407 N NH1 . ARG   B 246 ? 1.54789 0.95629 1.04023 -0.10198 -0.34482 -0.17412 339 ARG   B NH1 
4408 N NH2 . ARG   B 246 ? 1.41432 0.90319 0.93397 -0.05489 -0.33766 -0.19015 339 ARG   B NH2 
4409 N N   . GLU   B 247 ? 2.06029 0.99085 1.24914 -0.02891 -0.46254 -0.20844 340 GLU   B N   
4410 C CA  . GLU   B 247 ? 2.06221 0.88565 1.18719 -0.04366 -0.48700 -0.21073 340 GLU   B CA  
4411 C C   . GLU   B 247 ? 2.12245 0.90272 1.22695 -0.08869 -0.48040 -0.18746 340 GLU   B C   
4412 O O   . GLU   B 247 ? 2.12559 0.84271 1.19530 -0.12506 -0.48959 -0.18443 340 GLU   B O   
4413 C CB  . GLU   B 247 ? 2.12556 0.88598 1.20513 0.00343  -0.51233 -0.22612 340 GLU   B CB  
4414 C CG  . GLU   B 247 ? 2.19831 0.98016 1.28373 0.04370  -0.52302 -0.25323 340 GLU   B CG  
4415 C CD  . GLU   B 247 ? 2.33244 1.05482 1.37694 0.08961  -0.54743 -0.26775 340 GLU   B CD  
4416 O OE1 . GLU   B 247 ? 2.55024 1.20592 1.55659 0.08667  -0.55865 -0.25393 340 GLU   B OE1 
4417 O OE2 . GLU   B 247 ? 2.30839 1.06115 1.36472 0.12909  -0.55208 -0.28956 340 GLU   B OE2 
4418 N N   . THR   B 248 ? 2.04434 0.85729 1.16858 -0.08845 -0.46384 -0.17143 341 THR   B N   
4419 C CA  . THR   B 248 ? 2.16113 0.93718 1.26523 -0.13063 -0.45474 -0.14933 341 THR   B CA  
4420 C C   . THR   B 248 ? 2.15894 1.00647 1.31473 -0.17496 -0.42727 -0.13733 341 THR   B C   
4421 O O   . THR   B 248 ? 2.19328 1.00738 1.33127 -0.21985 -0.41976 -0.12292 341 THR   B O   
4422 C CB  . THR   B 248 ? 2.18952 0.95916 1.28401 -0.10911 -0.45202 -0.13830 341 THR   B CB  
4423 O OG1 . THR   B 248 ? 2.39655 1.12175 1.46268 -0.15115 -0.44366 -0.11700 341 THR   B OG1 
4424 C CG2 . THR   B 248 ? 2.11825 0.99750 1.28100 -0.08843 -0.42923 -0.13726 341 THR   B CG2 
4425 N N   . GLY   B 249 ? 2.24956 1.19279 1.46688 -0.16362 -0.41243 -0.14362 342 GLY   B N   
4426 C CA  . GLY   B 249 ? 2.15017 1.16589 1.41998 -0.19960 -0.38878 -0.13477 342 GLY   B CA  
4427 C C   . GLY   B 249 ? 2.13073 1.22018 1.44568 -0.19205 -0.36500 -0.12217 342 GLY   B C   
4428 O O   . GLY   B 249 ? 2.06390 1.14345 1.36682 -0.16525 -0.36572 -0.11769 342 GLY   B O   
4429 N N   . SER   B 250 ? 2.17709 1.34155 1.54529 -0.21587 -0.34495 -0.11751 343 SER   B N   
4430 C CA  . SER   B 250 ? 2.06666 1.30527 1.48150 -0.21203 -0.32165 -0.10630 343 SER   B CA  
4431 C C   . SER   B 250 ? 2.10266 1.32428 1.51002 -0.25018 -0.30704 -0.08869 343 SER   B C   
4432 O O   . SER   B 250 ? 2.09665 1.29767 1.49719 -0.29182 -0.30450 -0.08617 343 SER   B O   
4433 C CB  . SER   B 250 ? 2.04092 1.36771 1.51519 -0.21444 -0.30928 -0.11150 343 SER   B CB  
4434 O OG  . SER   B 250 ? 1.94682 1.27887 1.41930 -0.18774 -0.32373 -0.12848 343 SER   B OG  
4435 N N   . SER   B 251 ? 2.12991 1.36133 1.53841 -0.23694 -0.29694 -0.07753 344 SER   B N   
4436 C CA  . SER   B 251 ? 2.10247 1.31437 1.49793 -0.27039 -0.28260 -0.06086 344 SER   B CA  
4437 C C   . SER   B 251 ? 2.04901 1.33886 1.50153 -0.30152 -0.25767 -0.05575 344 SER   B C   
4438 O O   . SER   B 251 ? 1.98112 1.34458 1.48525 -0.29019 -0.25140 -0.06297 344 SER   B O   
4439 C CB  . SER   B 251 ? 2.03754 1.23835 1.41725 -0.24461 -0.28077 -0.05176 344 SER   B CB  
4440 O OG  . SER   B 251 ? 2.13043 1.25454 1.45506 -0.21673 -0.30571 -0.05725 344 SER   B OG  
4441 N N   . LYS   B 252 ? 1.84537 1.11653 1.28581 -0.34091 -0.24373 -0.04376 345 LYS   B N   
4442 C CA  . LYS   B 252 ? 1.73569 1.07631 1.22740 -0.37311 -0.21949 -0.03997 345 LYS   B CA  
4443 C C   . LYS   B 252 ? 1.66367 1.04986 1.17959 -0.36219 -0.20034 -0.02893 345 LYS   B C   
4444 O O   . LYS   B 252 ? 1.60600 0.95448 1.08806 -0.34226 -0.20436 -0.02111 345 LYS   B O   
4445 C CB  . LYS   B 252 ? 1.75404 1.05297 1.22101 -0.42643 -0.21245 -0.03539 345 LYS   B CB  
4446 C CG  . LYS   B 252 ? 1.83785 1.09431 1.28422 -0.44417 -0.23004 -0.04682 345 LYS   B CG  
4447 C CD  . LYS   B 252 ? 1.69624 1.03103 1.20514 -0.44682 -0.22827 -0.06072 345 LYS   B CD  
4448 C CE  . LYS   B 252 ? 1.80964 1.10244 1.29843 -0.46942 -0.24532 -0.07263 345 LYS   B CE  
4449 N NZ  . LYS   B 252 ? 1.76832 1.13717 1.31739 -0.47506 -0.24468 -0.08665 345 LYS   B NZ  
4450 N N   . LEU   B 253 ? 1.60723 1.07485 1.18235 -0.37461 -0.18085 -0.02947 346 LEU   B N   
4451 C CA  . LEU   B 253 ? 1.51123 1.02608 1.11296 -0.36667 -0.16172 -0.02016 346 LEU   B CA  
4452 C C   . LEU   B 253 ? 1.54935 1.02680 1.11954 -0.40048 -0.14716 -0.00753 346 LEU   B C   
4453 O O   . LEU   B 253 ? 1.59605 1.06326 1.16268 -0.44265 -0.13839 -0.00771 346 LEU   B O   
4454 C CB  . LEU   B 253 ? 1.42248 1.03136 1.09442 -0.36880 -0.14724 -0.02583 346 LEU   B CB  
4455 C CG  . LEU   B 253 ? 1.39727 1.05887 1.10094 -0.36495 -0.12609 -0.01752 346 LEU   B CG  
4456 C CD1 . LEU   B 253 ? 1.34926 1.00529 1.04109 -0.32416 -0.13138 -0.01263 346 LEU   B CD1 
4457 C CD2 . LEU   B 253 ? 1.23761 0.98530 1.00746 -0.36818 -0.11504 -0.02486 346 LEU   B CD2 
4458 N N   . LYS   B 254 ? 1.61523 1.07290 1.16182 -0.38298 -0.14426 0.00277  347 LYS   B N   
4459 C CA  . LYS   B 254 ? 1.63134 1.04884 1.14065 -0.41144 -0.13100 0.01570  347 LYS   B CA  
4460 C C   . LYS   B 254 ? 1.64381 1.13428 1.20049 -0.42365 -0.10382 0.01978  347 LYS   B C   
4461 O O   . LYS   B 254 ? 1.58722 1.14531 1.19317 -0.39715 -0.09907 0.01621  347 LYS   B O   
4462 C CB  . LYS   B 254 ? 1.62017 0.96901 1.07149 -0.38536 -0.14552 0.02412  347 LYS   B CB  
4463 C CG  . LYS   B 254 ? 1.59673 0.85355 0.98531 -0.37972 -0.17196 0.02192  347 LYS   B CG  
4464 C CD  . LYS   B 254 ? 1.77378 0.96332 1.10467 -0.35540 -0.18615 0.03024  347 LYS   B CD  
4465 C CE  . LYS   B 254 ? 1.91019 0.99901 1.17197 -0.35093 -0.21371 0.02830  347 LYS   B CE  
4466 N NZ  . LYS   B 254 ? 1.81528 0.83508 1.01808 -0.32702 -0.22979 0.03594  347 LYS   B NZ  
4467 N N   . HIS   B 255 ? 1.80199 1.27603 1.34091 -0.46493 -0.08559 0.02683  348 HIS   B N   
4468 C CA  . HIS   B 255 ? 1.76717 1.29561 1.33715 -0.47744 -0.05933 0.03153  348 HIS   B CA  
4469 C C   . HIS   B 255 ? 1.81360 1.28568 1.32750 -0.47392 -0.05699 0.04567  348 HIS   B C   
4470 O O   . HIS   B 255 ? 1.88317 1.26936 1.32920 -0.48948 -0.06585 0.05332  348 HIS   B O   
4471 C CB  . HIS   B 255 ? 1.86070 1.41903 1.45387 -0.52713 -0.03734 0.02746  348 HIS   B CB  
4472 C CG  . HIS   B 255 ? 1.89772 1.49147 1.50443 -0.54585 -0.00940 0.03302  348 HIS   B CG  
4473 N ND1 . HIS   B 255 ? 1.87304 1.54270 1.53373 -0.52294 0.00175  0.03026  348 HIS   B ND1 
4474 C CD2 . HIS   B 255 ? 1.88576 1.44686 1.45584 -0.58552 0.00995  0.04082  348 HIS   B CD2 
4475 C CE1 . HIS   B 255 ? 1.78863 1.47280 1.44751 -0.54612 0.02627  0.03508  348 HIS   B CE1 
4476 N NE2 . HIS   B 255 ? 1.80120 1.42167 1.40547 -0.58469 0.03257  0.04155  348 HIS   B NE2 
4477 N N   . PHE   B 256 ? 1.77692 1.29406 1.31646 -0.45304 -0.04656 0.04896  349 PHE   B N   
4478 C CA  . PHE   B 256 ? 1.84609 1.31759 1.33745 -0.44465 -0.04589 0.06108  349 PHE   B CA  
4479 C C   . PHE   B 256 ? 1.76087 1.27284 1.26985 -0.46992 -0.01629 0.06547  349 PHE   B C   
4480 O O   . PHE   B 256 ? 1.63616 1.23148 1.21027 -0.46617 -0.00139 0.05831  349 PHE   B O   
4481 C CB  . PHE   B 256 ? 1.69897 1.18160 1.19940 -0.39376 -0.06264 0.06005  349 PHE   B CB  
4482 C CG  . PHE   B 256 ? 1.65022 1.09033 1.12866 -0.36640 -0.09134 0.05450  349 PHE   B CG  
4483 C CD1 . PHE   B 256 ? 1.72223 1.07087 1.12929 -0.36062 -0.11113 0.06033  349 PHE   B CD1 
4484 C CD2 . PHE   B 256 ? 1.68188 1.17135 1.20832 -0.34567 -0.09916 0.04273  349 PHE   B CD2 
4485 C CE1 . PHE   B 256 ? 1.71307 1.02349 1.10075 -0.33334 -0.13802 0.05304  349 PHE   B CE1 
4486 C CE2 . PHE   B 256 ? 1.61494 1.06701 1.12070 -0.32022 -0.12424 0.03599  349 PHE   B CE2 
4487 C CZ  . PHE   B 256 ? 1.73707 1.10114 1.17523 -0.31343 -0.14359 0.04041  349 PHE   B CZ  
4488 N N   . ARG   B 257 ? 1.79406 1.24426 1.24199 -0.49500 -0.00840 0.07677  350 ARG   B N   
4489 C CA  . ARG   B 257 ? 1.76154 1.24295 1.21742 -0.52135 0.02104  0.08067  350 ARG   B CA  
4490 C C   . ARG   B 257 ? 1.65866 1.19334 1.14948 -0.48718 0.02522  0.08051  350 ARG   B C   
4491 O O   . ARG   B 257 ? 1.62464 1.12697 1.08853 -0.45335 0.00713  0.08561  350 ARG   B O   
4492 C CB  . ARG   B 257 ? 1.93591 1.32840 1.30703 -0.55113 0.02568  0.09426  350 ARG   B CB  
4493 C CG  . ARG   B 257 ? 1.88996 1.30914 1.26257 -0.58858 0.05972  0.09711  350 ARG   B CG  
4494 C CD  . ARG   B 257 ? 2.01897 1.35530 1.30602 -0.59940 0.06034  0.11013  350 ARG   B CD  
4495 N NE  . ARG   B 257 ? 2.16674 1.41429 1.38825 -0.60743 0.04029  0.11483  350 ARG   B NE  
4496 C CZ  . ARG   B 257 ? 2.20779 1.36851 1.36491 -0.58439 0.01099  0.12456  350 ARG   B CZ  
4497 N NH1 . ARG   B 257 ? 2.13608 1.29275 1.28934 -0.54762 -0.00267 0.12920  350 ARG   B NH1 
4498 N NH2 . ARG   B 257 ? 2.21787 1.30196 1.31832 -0.59194 -0.00665 0.12675  350 ARG   B NH2 
4499 N N   . GLY   B 258 ? 1.53789 1.15484 1.08971 -0.49590 0.04834  0.07337  351 GLY   B N   
4500 C CA  . GLY   B 258 ? 1.48345 1.15462 1.07275 -0.46620 0.05349  0.07196  351 GLY   B CA  
4501 C C   . GLY   B 258 ? 1.50945 1.23559 1.15624 -0.42886 0.03949  0.06313  351 GLY   B C   
4502 O O   . GLY   B 258 ? 1.50247 1.28365 1.18988 -0.40853 0.04644  0.06024  351 GLY   B O   
4503 N N   . VAL   B 259 ? 1.54567 1.25597 1.19400 -0.41992 0.02024  0.05871  352 VAL   B N   
4504 C CA  . VAL   B 259 ? 1.46188 1.21964 1.15879 -0.38673 0.00718  0.05029  352 VAL   B CA  
4505 C C   . VAL   B 259 ? 1.39951 1.21506 1.15005 -0.40429 0.01569  0.03920  352 VAL   B C   
4506 O O   . VAL   B 259 ? 1.52064 1.31336 1.25864 -0.43178 0.01464  0.03628  352 VAL   B O   
4507 C CB  . VAL   B 259 ? 1.45812 1.16339 1.12206 -0.36203 -0.02037 0.05058  352 VAL   B CB  
4508 C CG1 . VAL   B 259 ? 1.39828 1.15413 1.10991 -0.32902 -0.03103 0.04180  352 VAL   B CG1 
4509 C CG2 . VAL   B 259 ? 1.49806 1.14400 1.10763 -0.34504 -0.03104 0.05984  352 VAL   B CG2 
4510 N N   . ALA   B 260 ? 1.32880 1.21721 1.13780 -0.38847 0.02282  0.03247  353 ALA   B N   
4511 C CA  . ALA   B 260 ? 1.45641 1.40332 1.31930 -0.39956 0.02749  0.02046  353 ALA   B CA  
4512 C C   . ALA   B 260 ? 1.46939 1.40050 1.33143 -0.39008 0.00595  0.01491  353 ALA   B C   
4513 O O   . ALA   B 260 ? 1.40425 1.30534 1.24472 -0.36184 -0.01189 0.01786  353 ALA   B O   
4514 C CB  . ALA   B 260 ? 1.40209 1.42128 1.32094 -0.37809 0.03479  0.01501  353 ALA   B CB  
4515 N N   . ASP   B 261 ? 1.54018 1.49391 1.42707 -0.41425 0.00783  0.00524  354 ASP   B N   
4516 C CA  . ASP   B 261 ? 1.56103 1.49637 1.44379 -0.40934 -0.01251 -0.00106 354 ASP   B CA  
4517 C C   . ASP   B 261 ? 1.45029 1.42342 1.36541 -0.37147 -0.02612 -0.00626 354 ASP   B C   
4518 O O   . ASP   B 261 ? 1.43027 1.37609 1.32848 -0.35558 -0.04514 -0.00870 354 ASP   B O   
4519 C CB  . ASP   B 261 ? 1.63630 1.59247 1.54219 -0.44550 -0.00719 -0.01167 354 ASP   B CB  
4520 C CG  . ASP   B 261 ? 1.70075 1.60145 1.56101 -0.48586 0.00218  -0.00629 354 ASP   B CG  
4521 O OD1 . ASP   B 261 ? 1.67424 1.50252 1.47453 -0.48149 -0.00557 0.00497  354 ASP   B OD1 
4522 O OD2 . ASP   B 261 ? 1.77947 1.70834 1.66290 -0.52219 0.01695  -0.01392 354 ASP   B OD2 
4523 N N   . GLU   B 262 ? 1.41797 1.45072 1.37626 -0.35691 -0.01664 -0.00827 355 GLU   B N   
4524 C CA  . GLU   B 262 ? 1.34601 1.40936 1.32847 -0.32200 -0.02802 -0.01125 355 GLU   B CA  
4525 C C   . GLU   B 262 ? 1.29837 1.32830 1.24930 -0.29277 -0.03571 -0.00265 355 GLU   B C   
4526 O O   . GLU   B 262 ? 1.31422 1.36710 1.28108 -0.26490 -0.04279 -0.00424 355 GLU   B O   
4527 C CB  . GLU   B 262 ? 1.37013 1.50136 1.40415 -0.31608 -0.01645 -0.01583 355 GLU   B CB  
4528 C CG  . GLU   B 262 ? 1.40028 1.54334 1.43782 -0.33098 0.00483  -0.01141 355 GLU   B CG  
4529 C CD  . GLU   B 262 ? 1.38642 1.59633 1.47800 -0.33921 0.01678  -0.02172 355 GLU   B CD  
4530 O OE1 . GLU   B 262 ? 1.37312 1.62269 1.49961 -0.31988 0.00748  -0.02881 355 GLU   B OE1 
4531 O OE2 . GLU   B 262 ? 1.44046 1.66246 1.53815 -0.36474 0.03516  -0.02351 355 GLU   B OE2 
4532 N N   . ASP   B 263 ? 1.34320 1.31963 1.24922 -0.29893 -0.03480 0.00569  356 ASP   B N   
4533 C CA  . ASP   B 263 ? 1.18026 1.12274 1.05557 -0.27158 -0.04463 0.01152  356 ASP   B CA  
4534 C C   . ASP   B 263 ? 1.14488 1.01430 0.96533 -0.27755 -0.05746 0.01448  356 ASP   B C   
4535 O O   . ASP   B 263 ? 1.11621 0.95130 0.90655 -0.25667 -0.06652 0.01851  356 ASP   B O   
4536 C CB  . ASP   B 263 ? 1.18873 1.14347 1.06577 -0.26470 -0.03161 0.01906  356 ASP   B CB  
4537 C CG  . ASP   B 263 ? 1.29211 1.23404 1.15522 -0.23206 -0.04149 0.02175  356 ASP   B CG  
4538 O OD1 . ASP   B 263 ? 1.35929 1.33506 1.24874 -0.20990 -0.04595 0.01729  356 ASP   B OD1 
4539 O OD2 . ASP   B 263 ? 1.28809 1.18596 1.11304 -0.22907 -0.04503 0.02773  356 ASP   B OD2 
4540 N N   . ALA   B 264 ? 1.19071 1.03478 0.99737 -0.30515 -0.05967 0.01159  357 ALA   B N   
4541 C CA  . ALA   B 264 ? 1.21238 0.97909 0.96124 -0.31397 -0.07193 0.01519  357 ALA   B CA  
4542 C C   . ALA   B 264 ? 1.21733 0.95448 0.94671 -0.28331 -0.09470 0.00995  357 ALA   B C   
4543 O O   . ALA   B 264 ? 1.23784 0.91071 0.91771 -0.27609 -0.10786 0.01315  357 ALA   B O   
4544 C CB  . ALA   B 264 ? 1.31375 1.06235 1.05456 -0.35377 -0.06804 0.01243  357 ALA   B CB  
4545 N N   . HIS   B 265 ? 1.23391 1.01534 0.99918 -0.26444 -0.10008 0.00118  358 HIS   B N   
4546 C CA  . HIS   B 265 ? 1.18716 0.94599 0.93584 -0.23558 -0.11951 -0.00577 358 HIS   B CA  
4547 C C   . HIS   B 265 ? 1.14960 0.90572 0.88941 -0.20275 -0.12311 -0.00341 358 HIS   B C   
4548 O O   . HIS   B 265 ? 1.08330 0.80618 0.79767 -0.17989 -0.13960 -0.00902 358 HIS   B O   
4549 C CB  . HIS   B 265 ? 1.08278 0.88959 0.86906 -0.22659 -0.12286 -0.01571 358 HIS   B CB  
4550 C CG  . HIS   B 265 ? 1.08712 0.96060 0.91847 -0.21316 -0.11058 -0.01467 358 HIS   B CG  
4551 N ND1 . HIS   B 265 ? 1.14058 1.05579 1.00445 -0.23145 -0.09393 -0.01084 358 HIS   B ND1 
4552 C CD2 . HIS   B 265 ? 0.93752 0.84101 0.78485 -0.18384 -0.11247 -0.01748 358 HIS   B CD2 
4553 C CE1 . HIS   B 265 ? 1.01859 0.98261 0.91459 -0.21265 -0.08790 -0.01079 358 HIS   B CE1 
4554 N NE2 . HIS   B 265 ? 1.00707 0.96423 0.89276 -0.18520 -0.09830 -0.01411 358 HIS   B NE2 
4555 N N   . ASN   B 266 ? 1.14820 0.93966 0.90949 -0.19968 -0.10855 0.00317  359 ASN   B N   
4556 C CA  . ASN   B 266 ? 1.11623 0.91163 0.87439 -0.17053 -0.11117 0.00435  359 ASN   B CA  
4557 C C   . ASN   B 266 ? 1.14475 0.87973 0.85532 -0.16860 -0.11922 0.01005  359 ASN   B C   
4558 O O   . ASN   B 266 ? 1.11237 0.84704 0.81830 -0.14350 -0.12440 0.00935  359 ASN   B O   
4559 C CB  . ASN   B 266 ? 1.01150 0.86598 0.80992 -0.16839 -0.09361 0.00865  359 ASN   B CB  
4560 C CG  . ASN   B 266 ? 1.01016 0.92051 0.85066 -0.15989 -0.08986 0.00262  359 ASN   B CG  
4561 O OD1 . ASN   B 266 ? 1.11288 1.02470 0.95308 -0.14170 -0.10055 -0.00513 359 ASN   B OD1 
4562 N ND2 . ASN   B 266 ? 0.94785 0.90275 0.82242 -0.17230 -0.07514 0.00556  359 ASN   B ND2 
4563 N N   . ILE   B 267 ? 1.19415 0.87722 0.86810 -0.19465 -0.12107 0.01520  360 ILE   B N   
4564 C CA  . ILE   B 267 ? 1.22889 0.84598 0.84958 -0.19491 -0.12986 0.02201  360 ILE   B CA  
4565 C C   . ILE   B 267 ? 1.29192 0.85287 0.87451 -0.17367 -0.15517 0.01454  360 ILE   B C   
4566 O O   . ILE   B 267 ? 1.31087 0.85521 0.88760 -0.18048 -0.16344 0.00820  360 ILE   B O   
4567 C CB  . ILE   B 267 ? 1.26430 0.84703 0.85753 -0.23550 -0.11862 0.03166  360 ILE   B CB  
4568 C CG1 . ILE   B 267 ? 1.26340 0.90735 0.89827 -0.25421 -0.09300 0.03623  360 ILE   B CG1 
4569 C CG2 . ILE   B 267 ? 1.41351 0.92015 0.94329 -0.23584 -0.12896 0.03995  360 ILE   B CG2 
4570 C CD1 . ILE   B 267 ? 1.19997 0.87097 0.84743 -0.23365 -0.08700 0.04003  360 ILE   B CD1 
4571 N N   . GLN   B 268 ? 1.25458 0.78692 0.81192 -0.14675 -0.16863 0.01382  361 GLN   B N   
4572 C CA  . GLN   B 268 ? 1.32490 0.80414 0.84621 -0.12181 -0.19442 0.00468  361 GLN   B CA  
4573 C C   . GLN   B 268 ? 1.50405 0.89789 0.96482 -0.14485 -0.20580 0.01034  361 GLN   B C   
4574 O O   . GLN   B 268 ? 1.52217 0.87747 0.94898 -0.16733 -0.20018 0.02276  361 GLN   B O   
4575 C CB  . GLN   B 268 ? 1.24462 0.71725 0.75623 -0.08738 -0.20672 0.00125  361 GLN   B CB  
4576 C CG  . GLN   B 268 ? 1.32015 0.74259 0.79814 -0.05634 -0.23487 -0.01110 361 GLN   B CG  
4577 C CD  . GLN   B 268 ? 1.36341 0.82426 0.87386 -0.03759 -0.23837 -0.02665 361 GLN   B CD  
4578 O OE1 . GLN   B 268 ? 1.22191 0.75602 0.78372 -0.02876 -0.22438 -0.03128 361 GLN   B OE1 
4579 N NE2 . GLN   B 268 ? 1.38435 0.79243 0.86132 -0.03208 -0.25717 -0.03477 361 GLN   B NE2 
4580 N N   . THR   B 269 ? 1.43855 0.80054 0.88303 -0.14041 -0.22139 0.00111  362 THR   B N   
4581 C CA  . THR   B 269 ? 1.59377 0.86905 0.97810 -0.16103 -0.23496 0.00477  362 THR   B CA  
4582 C C   . THR   B 269 ? 1.67835 0.88685 1.01512 -0.12618 -0.26533 -0.00346 362 THR   B C   
4583 O O   . THR   B 269 ? 1.56317 0.79953 0.91872 -0.08702 -0.27444 -0.01331 362 THR   B O   
4584 C CB  . THR   B 269 ? 1.58099 0.86496 0.97984 -0.18494 -0.23141 -0.00047 362 THR   B CB  
4585 O OG1 . THR   B 269 ? 1.59428 0.91759 1.02561 -0.15477 -0.24005 -0.01597 362 THR   B OG1 
4586 C CG2 . THR   B 269 ? 1.59398 0.93835 1.03629 -0.22073 -0.20347 0.00679  362 THR   B CG2 
4587 N N   . HIS   B 270 ? 1.84388 0.96290 1.11828 -0.14098 -0.28145 -0.00038 363 HIS   B N   
4588 C CA  . HIS   B 270 ? 1.93039 0.97540 1.15281 -0.10807 -0.31328 -0.00862 363 HIS   B CA  
4589 C C   . HIS   B 270 ? 2.03665 0.99472 1.20227 -0.12978 -0.32842 -0.00810 363 HIS   B C   
4590 O O   . HIS   B 270 ? 2.12459 1.04009 1.25693 -0.17251 -0.31857 0.00611  363 HIS   B O   
4591 C CB  . HIS   B 270 ? 1.88577 0.88877 1.06871 -0.09477 -0.32265 0.00006  363 HIS   B CB  
4592 C CG  . HIS   B 270 ? 1.98450 0.89522 1.10222 -0.06590 -0.35796 -0.00654 363 HIS   B CG  
4593 N ND1 . HIS   B 270 ? 2.18974 0.99431 1.22838 -0.08788 -0.37189 0.00442  363 HIS   B ND1 
4594 C CD2 . HIS   B 270 ? 1.97802 0.88584 1.09703 -0.01631 -0.38275 -0.02399 363 HIS   B CD2 
4595 C CE1 . HIS   B 270 ? 2.24422 0.98055 1.23607 -0.05114 -0.40582 -0.00548 363 HIS   B CE1 
4596 N NE2 . HIS   B 270 ? 2.13327 0.93338 1.17510 -0.00649 -0.41300 -0.02378 363 HIS   B NE2 
4597 N N   . ARG   B 271 ? 2.05145 0.98396 1.20590 -0.10136 -0.35143 -0.02442 364 ARG   B N   
4598 C CA  . ARG   B 271 ? 2.18707 1.02361 1.27863 -0.11211 -0.37315 -0.02667 364 ARG   B CA  
4599 C C   . ARG   B 271 ? 2.36200 1.12799 1.40296 -0.06734 -0.40743 -0.03626 364 ARG   B C   
4600 O O   . ARG   B 271 ? 2.35236 1.14543 1.40775 -0.03283 -0.41260 -0.04002 364 ARG   B O   
4601 C CB  . ARG   B 271 ? 2.33326 1.19800 1.45408 -0.11823 -0.37211 -0.03977 364 ARG   B CB  
4602 C CG  . ARG   B 271 ? 2.30932 1.22523 1.46862 -0.06968 -0.38253 -0.06101 364 ARG   B CG  
4603 C CD  . ARG   B 271 ? 2.36245 1.24735 1.50728 -0.06572 -0.39867 -0.07635 364 ARG   B CD  
4604 N NE  . ARG   B 271 ? 2.24814 1.17915 1.42938 -0.10185 -0.37955 -0.07460 364 ARG   B NE  
4605 C CZ  . ARG   B 271 ? 2.24522 1.16603 1.42492 -0.10372 -0.38905 -0.08765 364 ARG   B CZ  
4606 N NH1 . ARG   B 271 ? 2.35834 1.22390 1.50149 -0.07201 -0.41623 -0.10369 364 ARG   B NH1 
4607 N NH2 . ARG   B 271 ? 2.16621 1.13380 1.38208 -0.13690 -0.37198 -0.08588 364 ARG   B NH2 
4608 N N   . ASP   B 272 ? 2.54022 1.21512 1.52209 -0.06725 -0.43223 -0.04157 365 ASP   B N   
4609 C CA  . ASP   B 272 ? 2.66983 1.27711 1.60528 -0.02025 -0.46839 -0.05487 365 ASP   B CA  
4610 C C   . ASP   B 272 ? 2.67521 1.33605 1.65528 0.02144  -0.47765 -0.08062 365 ASP   B C   
4611 O O   . ASP   B 272 ? 2.74798 1.35427 1.69603 0.03650  -0.50062 -0.09467 365 ASP   B O   
4612 C CB  . ASP   B 272 ? 2.86851 1.34436 1.71289 -0.03852 -0.49238 -0.04840 365 ASP   B CB  
4613 C CG  . ASP   B 272 ? 3.01558 1.40914 1.80128 0.00880  -0.53150 -0.05819 365 ASP   B CG  
4614 O OD1 . ASP   B 272 ? 3.05652 1.43325 1.82149 0.02208  -0.53728 -0.04970 365 ASP   B OD1 
4615 O OD2 . ASP   B 272 ? 3.08223 1.44391 1.84937 0.03429  -0.55449 -0.07312 365 ASP   B OD2 
4616 N N   . SER   B 273 ? 2.46957 1.23874 1.52333 0.03910  -0.45829 -0.08690 366 SER   B N   
4617 C CA  . SER   B 273 ? 2.39922 1.23474 1.50257 0.07239  -0.45912 -0.10982 366 SER   B CA  
4618 C C   . SER   B 273 ? 2.39934 1.21188 1.48716 0.12912  -0.48859 -0.13156 366 SER   B C   
4619 O O   . SER   B 273 ? 2.41057 1.27069 1.53277 0.15886  -0.49100 -0.15324 366 SER   B O   
4620 C CB  . SER   B 273 ? 2.24886 1.20389 1.43189 0.06908  -0.42745 -0.10796 366 SER   B CB  
4621 O OG  . SER   B 273 ? 2.28702 1.26970 1.48412 0.08597  -0.42409 -0.10305 366 SER   B OG  
4622 N N   . LEU   B 274 ? 2.39918 1.14155 1.43611 0.14552  -0.51118 -0.12746 367 LEU   B N   
4623 C CA  . LEU   B 274 ? 2.36373 1.08153 1.38522 0.20183  -0.54267 -0.15050 367 LEU   B CA  
4624 C C   . LEU   B 274 ? 2.48998 1.13657 1.46842 0.21695  -0.56892 -0.16718 367 LEU   B C   
4625 O O   . LEU   B 274 ? 2.40188 1.06459 1.39381 0.26398  -0.58645 -0.19375 367 LEU   B O   
4626 C CB  . LEU   B 274 ? 2.33793 0.99090 1.31004 0.21528  -0.56357 -0.14148 367 LEU   B CB  
4627 C CG  . LEU   B 274 ? 2.19087 0.91382 1.20474 0.21064  -0.54280 -0.12972 367 LEU   B CG  
4628 C CD1 . LEU   B 274 ? 2.16408 0.81037 1.11871 0.22348  -0.56719 -0.12092 367 LEU   B CD1 
4629 C CD2 . LEU   B 274 ? 1.99281 0.82835 1.08607 0.24652  -0.53244 -0.15094 367 LEU   B CD2 
4630 N N   . ASP   B 275 ? 2.61593 1.18479 1.54313 0.17726  -0.57154 -0.15331 368 ASP   B N   
4631 C CA  . ASP   B 275 ? 2.69973 1.20482 1.58873 0.18665  -0.59401 -0.16804 368 ASP   B CA  
4632 C C   . ASP   B 275 ? 2.65919 1.24556 1.60690 0.19118  -0.57807 -0.18584 368 ASP   B C   
4633 O O   . ASP   B 275 ? 2.63385 1.20973 1.57648 0.22503  -0.59642 -0.20880 368 ASP   B O   
4634 C CB  . ASP   B 275 ? 2.80397 1.23090 1.63601 0.13669  -0.59323 -0.14277 368 ASP   B CB  
4635 C CG  . ASP   B 275 ? 2.96046 1.34012 1.75989 0.14414  -0.61241 -0.15014 368 ASP   B CG  
4636 O OD1 . ASP   B 275 ? 2.97059 1.35827 1.77550 0.19389  -0.63331 -0.17157 368 ASP   B OD1 
4637 O OD2 . ASP   B 275 ? 3.08469 1.42206 1.85476 0.09967  -0.60598 -0.13534 368 ASP   B OD2 
4638 N N   . LEU   B 276 ? 2.53055 1.20451 1.53616 0.15797  -0.54275 -0.17391 369 LEU   B N   
4639 C CA  . LEU   B 276 ? 2.46637 1.21931 1.52590 0.15985  -0.52639 -0.18798 369 LEU   B CA  
4640 C C   . LEU   B 276 ? 2.35650 1.18933 1.46617 0.20959  -0.52496 -0.21104 369 LEU   B C   
4641 O O   . LEU   B 276 ? 2.26490 1.13948 1.40083 0.22443  -0.52157 -0.22977 369 LEU   B O   
4642 C CB  . LEU   B 276 ? 2.37558 1.19748 1.48113 0.11239  -0.49116 -0.16872 369 LEU   B CB  
4643 C CG  . LEU   B 276 ? 2.45389 1.22016 1.52589 0.05748  -0.48608 -0.14998 369 LEU   B CG  
4644 C CD1 . LEU   B 276 ? 2.53492 1.21193 1.55128 0.05757  -0.51244 -0.16167 369 LEU   B CD1 
4645 C CD2 . LEU   B 276 ? 2.54263 1.26105 1.58008 0.03085  -0.48291 -0.12623 369 LEU   B CD2 
4646 N N   . LEU   B 277 ? 2.29690 1.15226 1.41961 0.23452  -0.52715 -0.21090 370 LEU   B N   
4647 C CA  . LEU   B 277 ? 2.17991 1.11523 1.35318 0.27947  -0.52445 -0.23403 370 LEU   B CA  
4648 C C   . LEU   B 277 ? 2.27217 1.16468 1.41788 0.32714  -0.55563 -0.26391 370 LEU   B C   
4649 O O   . LEU   B 277 ? 2.19140 1.15064 1.37812 0.35748  -0.55016 -0.28798 370 LEU   B O   
4650 C CB  . LEU   B 277 ? 2.01308 0.98182 1.20732 0.29196  -0.52036 -0.22688 370 LEU   B CB  
4651 C CG  . LEU   B 277 ? 1.94655 1.00184 1.19624 0.33556  -0.51645 -0.25044 370 LEU   B CG  
4652 C CD1 . LEU   B 277 ? 1.80067 0.96147 1.11626 0.32198  -0.48180 -0.25247 370 LEU   B CD1 
4653 C CD2 . LEU   B 277 ? 1.85204 0.91871 1.10942 0.34822  -0.52034 -0.24389 370 LEU   B CD2 
4654 N N   . ASP   B 278 ? 2.31114 1.09156 1.38581 0.33422  -0.58818 -0.26346 371 ASP   B N   
4655 C CA  . ASP   B 278 ? 2.37455 1.11940 1.42606 0.38067  -0.61798 -0.28823 371 ASP   B CA  
4656 C C   . ASP   B 278 ? 2.45052 1.19921 1.50377 0.37618  -0.61527 -0.29963 371 ASP   B C   
4657 O O   . ASP   B 278 ? 2.45183 1.22857 1.52116 0.41589  -0.62498 -0.32336 371 ASP   B O   
4658 C CB  . ASP   B 278 ? 2.47465 1.12284 1.45998 0.38350  -0.64758 -0.27181 371 ASP   B CB  
4659 C CG  . ASP   B 278 ? 2.47278 1.11030 1.44908 0.38447  -0.65110 -0.25812 371 ASP   B CG  
4660 O OD1 . ASP   B 278 ? 2.32112 1.03256 1.34908 0.39773  -0.63588 -0.26784 371 ASP   B OD1 
4661 O OD2 . ASP   B 278 ? 2.50716 1.06273 1.42266 0.37130  -0.66889 -0.23796 371 ASP   B OD2 
4662 N N   . LYS   B 279 ? 2.48315 1.20684 1.52140 0.32800  -0.60229 -0.28388 372 LYS   B N   
4663 C CA  . LYS   B 279 ? 2.44038 1.16680 1.47944 0.32113  -0.60023 -0.29398 372 LYS   B CA  
4664 C C   . LYS   B 279 ? 2.37964 1.20452 1.47701 0.33840  -0.58014 -0.31748 372 LYS   B C   
4665 O O   . LYS   B 279 ? 2.45683 1.29315 1.55816 0.34892  -0.58165 -0.33260 372 LYS   B O   
4666 C CB  . LYS   B 279 ? 2.36362 1.04655 1.37739 0.26282  -0.59084 -0.27154 372 LYS   B CB  
4667 C CG  . LYS   B 279 ? 2.46655 1.05176 1.41842 0.23963  -0.60722 -0.24710 372 LYS   B CG  
4668 C CD  . LYS   B 279 ? 2.43880 0.99906 1.37748 0.17715  -0.59112 -0.22464 372 LYS   B CD  
4669 C CE  . LYS   B 279 ? 2.67599 1.14478 1.55243 0.15112  -0.60307 -0.19931 372 LYS   B CE  
4670 N NZ  . LYS   B 279 ? 2.68832 1.14395 1.55876 0.08787  -0.58306 -0.17753 372 LYS   B NZ  
4671 N N   . ALA   B 280 ? 2.37637 1.29020 1.52905 0.33788  -0.55516 -0.31175 373 ALA   B N   
4672 C CA  . ALA   B 280 ? 2.34666 1.36837 1.56142 0.34991  -0.52975 -0.32575 373 ALA   B CA  
4673 C C   . ALA   B 280 ? 2.41879 1.47721 1.65314 0.40594  -0.53961 -0.35769 373 ALA   B C   
4674 O O   . ALA   B 280 ? 2.35458 1.50562 1.64060 0.41752  -0.51701 -0.37042 373 ALA   B O   
4675 C CB  . ALA   B 280 ? 2.14898 1.25169 1.41572 0.32062  -0.49650 -0.30297 373 ALA   B CB  
4676 N N   . ARG   B 281 ? 2.47765 1.46749 1.67261 0.44023  -0.57227 -0.37071 374 ARG   B N   
4677 C CA  . ARG   B 281 ? 2.39404 1.43381 1.61914 0.49208  -0.57980 -0.39683 374 ARG   B CA  
4678 C C   . ARG   B 281 ? 2.49565 1.54932 1.72336 0.51280  -0.58311 -0.41796 374 ARG   B C   
4679 O O   . ARG   B 281 ? 2.52434 1.65600 1.79533 0.54337  -0.57243 -0.44271 374 ARG   B O   
4680 C CB  . ARG   B 281 ? 2.51498 1.49919 1.71064 0.51686  -0.61013 -0.39207 374 ARG   B CB  
4681 C CG  . ARG   B 281 ? 2.60710 1.64398 1.83447 0.57003  -0.62212 -0.41976 374 ARG   B CG  
4682 C CD  . ARG   B 281 ? 2.64525 1.63426 1.84468 0.59125  -0.65251 -0.41375 374 ARG   B CD  
4683 N NE  . ARG   B 281 ? 2.70324 1.73953 1.92950 0.64104  -0.66876 -0.44212 374 ARG   B NE  
4684 C CZ  . ARG   B 281 ? 2.69100 1.81811 1.97581 0.66396  -0.65722 -0.46001 374 ARG   B CZ  
4685 N NH1 . ARG   B 281 ? 2.64901 1.82892 1.97131 0.64427  -0.62940 -0.45256 374 ARG   B NH1 
4686 N NH2 . ARG   B 281 ? 2.68825 1.85586 1.99489 0.70629  -0.67399 -0.48697 374 ARG   B NH2 
4687 N N   . ALA   B 282 ? 2.47831 1.45911 1.66057 0.49511  -0.59662 -0.40886 375 ALA   B N   
4688 C CA  . ALA   B 282 ? 2.39684 1.38276 1.57611 0.51282  -0.60121 -0.42798 375 ALA   B CA  
4689 C C   . ALA   B 282 ? 2.35680 1.40998 1.56859 0.49464  -0.57132 -0.43576 375 ALA   B C   
4690 O O   . ALA   B 282 ? 2.29039 1.31727 1.48477 0.45492  -0.56381 -0.42074 375 ALA   B O   
4691 C CB  . ALA   B 282 ? 2.43993 1.32428 1.55852 0.49782  -0.62576 -0.41514 375 ALA   B CB  
4692 C C11 . A1CAG C .   ? 0.52472 0.92324 0.71404 -0.07809 0.00453  -0.05629 301 A1CAG A C11 
4693 C C12 . A1CAG C .   ? 0.55699 0.93983 0.73194 -0.07667 0.01300  -0.04293 301 A1CAG A C12 
4694 C C13 . A1CAG C .   ? 0.58302 0.98223 0.77845 -0.09672 0.01503  -0.05461 301 A1CAG A C13 
4695 C C14 . A1CAG C .   ? 0.49110 0.86299 0.67061 -0.10376 0.01756  -0.04656 301 A1CAG A C14 
4696 C C15 . A1CAG C .   ? 0.54404 0.92373 0.73462 -0.12186 0.02676  -0.04892 301 A1CAG A C15 
4697 C C17 . A1CAG C .   ? 0.62837 0.95073 0.78399 -0.12571 0.02668  -0.03654 301 A1CAG A C17 
4698 C C18 . A1CAG C .   ? 0.65665 0.95237 0.79986 -0.13584 0.03039  -0.03342 301 A1CAG A C18 
4699 C C19 . A1CAG C .   ? 0.72199 1.00179 0.85277 -0.12987 0.01988  -0.03932 301 A1CAG A C19 
4700 C C20 . A1CAG C .   ? 0.79229 1.08725 0.93654 -0.13642 0.01002  -0.05430 301 A1CAG A C20 
4701 C C21 . A1CAG C .   ? 0.82733 1.15472 0.99875 -0.14797 0.01127  -0.06386 301 A1CAG A C21 
4702 C C23 . A1CAG C .   ? 0.79308 1.12436 0.96964 -0.14951 -0.00994 -0.08523 301 A1CAG A C23 
4703 C C24 . A1CAG C .   ? 0.81245 1.10855 0.95811 -0.13800 -0.01161 -0.07602 301 A1CAG A C24 
4704 C C25 . A1CAG C .   ? 0.73619 1.01665 0.86791 -0.13218 -0.00082 -0.06113 301 A1CAG A C25 
4705 C C01 . A1CAG C .   ? 0.62101 0.90056 0.72056 -0.07877 0.00571  -0.02240 301 A1CAG A C01 
4706 C C02 . A1CAG C .   ? 0.75687 1.03444 0.85603 -0.07981 0.01634  -0.01179 301 A1CAG A C02 
4707 C C03 . A1CAG C .   ? 0.55582 0.84178 0.66815 -0.08964 0.02773  -0.00796 301 A1CAG A C03 
4708 C C04 . A1CAG C .   ? 0.80883 1.07179 0.90144 -0.08581 0.02736  -0.00356 301 A1CAG A C04 
4709 C C06 . A1CAG C .   ? 0.61683 0.91357 0.72447 -0.06705 0.00815  -0.01512 301 A1CAG A C06 
4710 C C08 . A1CAG C .   ? 0.55366 0.90216 0.70096 -0.06616 0.00503  -0.03369 301 A1CAG A C08 
4711 C C09 . A1CAG C .   ? 0.60045 0.94817 0.74519 -0.05557 -0.01171 -0.04428 301 A1CAG A C09 
4712 C C10 . A1CAG C .   ? 0.57207 0.94489 0.73978 -0.06396 -0.01176 -0.05595 301 A1CAG A C10 
4713 N N05 . A1CAG C .   ? 0.69825 0.97388 0.79071 -0.07155 0.01246  -0.00900 301 A1CAG A N05 
4714 N N16 . A1CAG C .   ? 0.60408 0.95918 0.78280 -0.13292 0.03076  -0.04370 301 A1CAG A N16 
4715 N N22 . A1CAG C .   ? 0.82873 1.17580 1.01759 -0.15485 0.00248  -0.07918 301 A1CAG A N22 
4716 N N27 . A1CAG C .   ? 0.59286 1.00787 0.80713 -0.12775 0.03161  -0.05849 301 A1CAG A N27 
4717 N N28 . A1CAG C .   ? 0.50875 0.93591 0.72641 -0.11128 0.02434  -0.06228 301 A1CAG A N28 
4718 O O07 . A1CAG C .   ? 0.63156 0.95545 0.76314 -0.07321 0.01114  -0.02326 301 A1CAG A O07 
4719 O O26 . A1CAG C .   ? 0.66642 0.98026 0.81062 -0.11242 0.02089  -0.03360 301 A1CAG A O26 
4720 O O29 . A1CAG C .   ? 0.70841 1.00159 0.80958 -0.05911 0.00281  -0.01467 301 A1CAG A O29 
4721 O O   . HOH   D .   ? 0.83621 1.14116 0.85573 -0.00018 0.00232  -0.03832 401 HOH   A O   
4722 O O   . HOH   D .   ? 0.57174 0.83903 0.62948 -0.04177 -0.01164 0.04710  402 HOH   A O   
4723 O O   . HOH   D .   ? 0.73448 0.96449 0.78706 -0.07728 0.03880  0.02192  403 HOH   A O   
4724 O O   . HOH   D .   ? 0.60565 0.85642 0.62962 -0.05149 0.01060  0.05548  404 HOH   A O   
4725 O O   . HOH   D .   ? 0.60623 1.10982 0.81394 -0.15827 0.11575  -0.04855 405 HOH   A O   
4726 O O   . HOH   D .   ? 0.68049 0.99218 0.68176 -0.01590 0.01799  -0.02530 406 HOH   A O   
4727 O O   . HOH   D .   ? 0.76705 0.97355 0.85726 -0.05523 0.06864  0.00714  407 HOH   A O   
4728 O O   . HOH   D .   ? 0.63230 1.01931 0.80855 -0.16561 0.12601  -0.00868 408 HOH   A O   
4729 O O   . HOH   D .   ? 0.53467 0.92265 0.69521 -0.07307 0.03995  -0.02192 409 HOH   A O   
4730 O O   . HOH   D .   ? 0.63411 0.85182 0.76361 -0.00648 0.03800  0.00885  410 HOH   A O   
4731 O O   . HOH   D .   ? 0.89620 1.13261 0.97383 -0.13068 0.00538  0.02271  411 HOH   A O   
4732 O O   . HOH   D .   ? 0.49524 0.81928 0.65834 -0.06757 0.04749  0.02592  412 HOH   A O   
4733 O O   . HOH   D .   ? 0.51427 0.77199 0.58863 -0.06672 0.02830  0.02583  413 HOH   A O   
4734 O O   . HOH   D .   ? 0.57238 0.80870 0.66114 -0.10055 0.04009  -0.00171 414 HOH   A O   
4735 O O   . HOH   D .   ? 0.58358 0.90591 0.72567 -0.07008 -0.00666 0.02393  415 HOH   A O   
4736 O O   . HOH   D .   ? 0.76531 0.91425 0.74387 -0.06086 -0.01004 0.02635  416 HOH   A O   
4737 O O   . HOH   D .   ? 0.56342 0.84571 0.73518 -0.00696 0.05110  -0.00678 417 HOH   A O   
4738 O O   . HOH   D .   ? 0.53411 0.81671 0.64977 -0.07155 0.04654  0.04015  418 HOH   A O   
4739 O O   . HOH   D .   ? 0.55382 0.91061 0.69950 -0.05849 0.01579  -0.02455 419 HOH   A O   
4740 O O   . HOH   D .   ? 0.76057 1.22792 0.98439 0.22144  -0.22271 -0.24467 420 HOH   A O   
4741 O O   . HOH   D .   ? 0.48954 0.85540 0.71242 -0.02817 0.05567  -0.01067 421 HOH   A O   
4742 O O   . HOH   D .   ? 1.09011 0.99806 0.82693 0.05848  -0.14790 0.10721  422 HOH   A O   
4743 O O   . HOH   D .   ? 0.51900 0.87137 0.69891 -0.07797 0.00407  0.01597  423 HOH   A O   
4744 O O   . HOH   D .   ? 0.70566 1.14001 0.92031 -0.32231 0.14546  -0.05657 424 HOH   A O   
4745 O O   . HOH   D .   ? 0.56247 0.83532 0.64601 -0.03125 -0.02023 0.04557  425 HOH   A O   
4746 O O   . HOH   D .   ? 1.17721 0.91440 0.80774 0.08501  -0.18294 0.12634  426 HOH   A O   
4747 O O   . HOH   D .   ? 0.74339 0.92281 0.69400 -0.00434 -0.06663 0.06313  427 HOH   A O   
4748 O O   . HOH   D .   ? 0.52028 0.89915 0.72783 -0.10039 0.00278  0.00218  428 HOH   A O   
4749 O O   . HOH   D .   ? 0.79975 1.32047 1.07176 -0.20566 0.17466  -0.05768 429 HOH   A O   
4750 O O   . HOH   D .   ? 1.05032 0.89230 0.74967 -0.08152 -0.06874 0.04999  430 HOH   A O   
4751 O O   . HOH   D .   ? 0.78254 1.31082 1.04674 -0.32844 0.16237  -0.08189 431 HOH   A O   
4752 O O   . HOH   D .   ? 0.64035 1.05839 0.93308 0.09454  -0.12103 -0.05087 432 HOH   A O   
4753 O O   . HOH   D .   ? 0.65901 1.26872 1.00448 -0.20195 0.18994  -0.09088 433 HOH   A O   
4754 O O   . HOH   D .   ? 0.92837 1.07789 0.86217 0.02177  -0.10065 0.06330  434 HOH   A O   
4755 O O   . HOH   E .   ? 0.69821 0.93511 0.67481 -0.05949 0.02334  0.05877  401 HOH   B O   
4756 O O   . HOH   E .   ? 0.81348 1.13846 0.78231 -0.09519 0.09586  0.02192  402 HOH   B O   
4757 O O   . HOH   E .   ? 1.28105 0.85048 0.88869 -0.23845 -0.15075 0.00349  403 HOH   B O   
# 
