data_9OB2
# 
_entry.id   9OB2 
# 
_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   9OB2         pdb_00009ob2 10.2210/pdb9ob2/pdb 
WWPDB D_1000295146 ?            ?                   
# 
_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                        9OB2 
_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-{2-[4-(methanesulfonyl)phenyl]acetamido}-1H-pyrazol-5-yl)cyclopentyl (1-methylcyclopropyl)carbamate' 460.547   1  ? 
? ? ? 
4 water       nat water 18.015    51 ?         ? ? ? 
# 
_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-{2-[4-(methanesulfonyl)phenyl]acetamido}-1H-pyrazol-5-yl)cyclopentyl (1-methylcyclopropyl)carbamate' A1CAE 
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 
A1CAE non-polymer         . 
'(1R,3R)-3-(3-{2-[4-(methanesulfonyl)phenyl]acetamido}-1H-pyrazol-5-yl)cyclopentyl (1-methylcyclopropyl)carbamate' ? 
'C22 H28 N4 O5 S' 460.547 
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        A1CAE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1CAE 
_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 A1CAE 1  301 1  A1CAE LI1 A . 
D 4 HOH   1  401 2  HOH   HOH A . 
D 4 HOH   2  402 42 HOH   HOH A . 
D 4 HOH   3  403 40 HOH   HOH A . 
D 4 HOH   4  404 31 HOH   HOH A . 
D 4 HOH   5  405 28 HOH   HOH A . 
D 4 HOH   6  406 30 HOH   HOH A . 
D 4 HOH   7  407 13 HOH   HOH A . 
D 4 HOH   8  408 20 HOH   HOH A . 
D 4 HOH   9  409 1  HOH   HOH A . 
D 4 HOH   10 410 8  HOH   HOH A . 
D 4 HOH   11 411 19 HOH   HOH A . 
D 4 HOH   12 412 37 HOH   HOH A . 
D 4 HOH   13 413 48 HOH   HOH A . 
D 4 HOH   14 414 36 HOH   HOH A . 
D 4 HOH   15 415 5  HOH   HOH A . 
D 4 HOH   16 416 9  HOH   HOH A . 
D 4 HOH   17 417 25 HOH   HOH A . 
D 4 HOH   18 418 41 HOH   HOH A . 
D 4 HOH   19 419 43 HOH   HOH A . 
D 4 HOH   20 420 29 HOH   HOH A . 
D 4 HOH   21 421 14 HOH   HOH A . 
D 4 HOH   22 422 34 HOH   HOH A . 
D 4 HOH   23 423 38 HOH   HOH A . 
D 4 HOH   24 424 47 HOH   HOH A . 
D 4 HOH   25 425 35 HOH   HOH A . 
D 4 HOH   26 426 15 HOH   HOH A . 
D 4 HOH   27 427 6  HOH   HOH A . 
D 4 HOH   28 428 18 HOH   HOH A . 
D 4 HOH   29 429 7  HOH   HOH A . 
D 4 HOH   30 430 44 HOH   HOH A . 
D 4 HOH   31 431 4  HOH   HOH A . 
D 4 HOH   32 432 16 HOH   HOH A . 
D 4 HOH   33 433 50 HOH   HOH A . 
D 4 HOH   34 434 26 HOH   HOH A . 
D 4 HOH   35 435 11 HOH   HOH A . 
D 4 HOH   36 436 51 HOH   HOH A . 
D 4 HOH   37 437 21 HOH   HOH A . 
D 4 HOH   38 438 46 HOH   HOH A . 
D 4 HOH   39 439 27 HOH   HOH A . 
D 4 HOH   40 440 3  HOH   HOH A . 
D 4 HOH   41 441 33 HOH   HOH A . 
D 4 HOH   42 442 39 HOH   HOH A . 
D 4 HOH   43 443 22 HOH   HOH A . 
E 4 HOH   1  401 32 HOH   HOH B . 
E 4 HOH   2  402 24 HOH   HOH B . 
E 4 HOH   3  403 23 HOH   HOH B . 
E 4 HOH   4  404 17 HOH   HOH B . 
E 4 HOH   5  405 10 HOH   HOH B . 
E 4 HOH   6  406 49 HOH   HOH B . 
E 4 HOH   7  407 45 HOH   HOH B . 
E 4 HOH   8  408 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                     9OB2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.140 
_cell.length_a_esd                 ? 
_cell.length_b                     101.140 
_cell.length_b_esd                 ? 
_cell.length_c                     150.910 
_cell.length_c_esd                 ? 
_cell.volume                       1543703.603 
_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                         9OB2 
_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                   9OB2 
_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             2.86 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.00 
_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                          56.34 
_reflns.entry_id                                       9OB2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.12 
_reflns.d_resolution_low                               150.91 
_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                                     45192 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                25.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.105 
_reflns.pdbx_Rpim_I_all                                0.028 
_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                              0.101 
_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                                    2.12 
_reflns_shell.d_res_low                                     2.18 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.358 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3642 
_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                               27.2 
_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                                  0.358 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_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                               78.89 
_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                                 9OB2 
_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                            2.12 
_refine.ls_d_res_low                             84.02 
_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                     45103 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  43104 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 4.43 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2215 
_refine.ls_R_factor_R_free                       0.2543 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2200 
_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                          1.34 
_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                 31.4850 
_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                            0.3810 
_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                       2.12 
_refine_hist.d_res_low                        84.02 
_refine_hist.number_atoms_solvent             51 
_refine_hist.number_atoms_total               4727 
_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         32 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0017  ? 4846 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.4277  ? 6585 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 0.0372  ? 735  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.0035  ? 826  ? f_plane_restr      ? ? ? 
'X-RAY DIFFRACTION' ? 12.4825 ? 1787 ? 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' 2.12 2.17  . . 140 3025 100.00 . . . . 0.3957 . . . . . . . . . . . . . . . 0.4785 
'X-RAY DIFFRACTION' 2.17 2.23  . . 141 3025 99.97  . . . . 0.3594 . . . . . . . . . . . . . . . 0.3959 
'X-RAY DIFFRACTION' 2.23 2.30  . . 140 3033 100.00 . . . . 0.3587 . . . . . . . . . . . . . . . 0.3957 
'X-RAY DIFFRACTION' 2.30 2.37  . . 139 3005 99.97  . . . . 0.3320 . . . . . . . . . . . . . . . 0.3782 
'X-RAY DIFFRACTION' 2.37 2.46  . . 143 3063 99.97  . . . . 0.3090 . . . . . . . . . . . . . . . 0.3443 
'X-RAY DIFFRACTION' 2.46 2.55  . . 141 3023 100.00 . . . . 0.2779 . . . . . . . . . . . . . . . 0.3506 
'X-RAY DIFFRACTION' 2.55 2.67  . . 141 3051 99.97  . . . . 0.2588 . . . . . . . . . . . . . . . 0.3176 
'X-RAY DIFFRACTION' 2.67 2.81  . . 140 3062 99.97  . . . . 0.2666 . . . . . . . . . . . . . . . 0.3190 
'X-RAY DIFFRACTION' 2.81 2.99  . . 143 3057 100.00 . . . . 0.2757 . . . . . . . . . . . . . . . 0.2896 
'X-RAY DIFFRACTION' 2.99 3.22  . . 142 3068 100.00 . . . . 0.2574 . . . . . . . . . . . . . . . 0.3270 
'X-RAY DIFFRACTION' 3.22 3.54  . . 144 3090 99.97  . . . . 0.2270 . . . . . . . . . . . . . . . 0.2580 
'X-RAY DIFFRACTION' 3.54 4.06  . . 144 3124 100.00 . . . . 0.2032 . . . . . . . . . . . . . . . 0.2360 
'X-RAY DIFFRACTION' 4.06 5.11  . . 147 3155 100.00 . . . . 0.1699 . . . . . . . . . . . . . . . 0.2156 
'X-RAY DIFFRACTION' 5.11 84.02 . . 154 3323 99.83  . . . . 0.1862 . . . . . . . . . . . . . . . 0.1932 
# 
_struct.entry_id                     9OB2 
_struct.title                        'CDK2/CyclinE bound to compound 11 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        9OB2 
_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 9OB2 A 4 ? 301 ? P24941 1  ? 298 ? 1  298 
2 2 9OB2 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 9OB2 SER A 1 ? UNP P24941 ? ? 'expression tag' -2 1 
1 9OB2 HIS A 2 ? UNP P24941 ? ? 'expression tag' -1 2 
1 9OB2 MET A 3 ? UNP P24941 ? ? 'expression tag' 0  3 
2 9OB2 GLY B 1 ? UNP P24864 ? ? 'expression tag' 94 4 
2 9OB2 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)' 4450  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  24980 ? 
# 
_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 PRO A 48  ? LYS A 59  ? PRO A 45  LYS A 56  1 ? 12 
HELX_P HELX_P2  AA2 LEU A 90  ? SER A 97  ? LEU A 87  SER A 94  1 ? 8  
HELX_P HELX_P3  AA3 PRO A 103 ? HIS A 124 ? PRO A 100 HIS A 121 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 132 ? GLN A 134 ? LYS A 129 GLN A 131 5 ? 3  
HELX_P HELX_P5  AA5 THR A 168 ? ARG A 172 ? THR A 165 ARG A 169 5 ? 5  
HELX_P HELX_P6  AA6 ALA A 173 ? LEU A 178 ? ALA A 170 LEU A 175 1 ? 6  
HELX_P HELX_P7  AA7 THR A 185 ? ARG A 202 ? THR A 182 ARG A 199 1 ? 18 
HELX_P HELX_P8  AA8 SER A 210 ? GLY A 223 ? SER A 207 GLY A 220 1 ? 14 
HELX_P HELX_P9  AA9 GLY A 232 ? MET A 236 ? GLY A 229 MET A 233 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 250 ? VAL A 255 ? ASP A 247 VAL A 252 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 259 ? LEU A 270 ? ASP A 256 LEU A 267 1 ? 12 
HELX_P HELX_P12 AB3 SER A 279 ? ALA A 285 ? SER A 276 ALA A 282 1 ? 7  
HELX_P HELX_P13 AB4 HIS A 286 ? GLN A 290 ? HIS A 283 GLN A 287 5 ? 5  
HELX_P HELX_P14 AB5 ASN B 19  ? LYS B 32  ? ASN B 112 LYS B 125 1 ? 14 
HELX_P HELX_P15 AB6 HIS B 39  ? HIS B 44  ? HIS B 132 HIS B 137 5 ? 6  
HELX_P HELX_P16 AB7 GLN B 48  ? TYR B 66  ? GLN B 141 TYR B 159 1 ? 19 
HELX_P HELX_P17 AB8 HIS B 69  ? ALA B 85  ? HIS B 162 ALA B 178 1 ? 17 
HELX_P HELX_P18 AB9 VAL B 91  ? THR B 93  ? VAL B 184 THR B 186 5 ? 3  
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 ? SER B 215 ? PRO B 295 SER B 308 1 ? 14 
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 ? GLY B 249 ? GLN B 320 GLY B 342 1 ? 23 
HELX_P HELX_P28 AD1 ALA B 260 ? ILE B 267 ? ALA B 353 ILE B 360 5 ? 8  
HELX_P HELX_P29 AD2 LEU B 274 ? ALA B 282 ? LEU B 367 ALA B 375 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       2.93 
# 
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  ? HIS A 74  ? LEU A 66  HIS A 71  
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 GLU A 11  ? N GLU A 8   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                   9OB2 
_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 LEU A 58  ? ? -118.43 62.50   
2  1 ASP A 127 ? ? -155.88 46.78   
3  1 ASP A 145 ? ? 58.52   79.46   
4  1 VAL A 164 ? ? 68.76   138.40  
5  1 SER A 181 ? ? -146.69 -126.25 
6  1 TRP A 227 ? ? -154.22 89.57   
7  1 ASN B 182 ? ? 61.92   100.48  
8  1 GLN B 269 ? ? -165.29 98.78   
9  1 SER B 308 ? ? -137.09 -110.34 
10 1 SER B 366 ? ? 55.84   -131.36 
11 1 LEU B 367 ? ? 56.09   -65.89  
# 
_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         26.3781612606 
_pdbx_refine_tls.origin_y         6.75286325408 
_pdbx_refine_tls.origin_z         -18.335555446 
_pdbx_refine_tls.T[1][1]          0.380812012758 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0133777404629 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0249142714788 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.504855330366 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.00169710041195 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.470183367926 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.16962487482 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.21620778899 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.781733046813 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.6907826946 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.03700299492 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.54884024149 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.214751173604 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.170447055255 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.144815490679 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0846970970862 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.058370739912 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0830530133593 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.463929422455 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.222188883377 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.22812615577 
_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     51 
_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 
A1CAE C11  C Y N 1   
A1CAE C14  C Y N 2   
A1CAE C15  C N S 3   
A1CAE C16  C N N 4   
A1CAE C17  C N R 5   
A1CAE C19  C N N 6   
A1CAE C21  C N N 7   
A1CAE C22  C N N 8   
A1CAE C23  C N N 9   
A1CAE C24  C N N 10  
A1CAE C26  C N N 11  
A1CAE C27  C N N 12  
A1CAE C28  C Y N 13  
A1CAE C30  C Y N 14  
A1CAE C03  C N N 15  
A1CAE C04  C Y N 16  
A1CAE C05  C Y N 17  
A1CAE C06  C Y N 18  
A1CAE C07  C Y N 19  
A1CAE C08  C N N 20  
A1CAE C09  C N N 21  
A1CAE C31  C Y N 22  
A1CAE N10  N N N 23  
A1CAE N12  N Y N 24  
A1CAE N13  N Y N 25  
A1CAE N20  N N N 26  
A1CAE O01  O N N 27  
A1CAE O18  O N N 28  
A1CAE O25  O N N 29  
A1CAE O29  O N N 30  
A1CAE O32  O N N 31  
A1CAE S02  S N N 32  
A1CAE H151 H N N 33  
A1CAE H162 H N N 34  
A1CAE H161 H N N 35  
A1CAE H171 H N N 36  
A1CAE H221 H N N 37  
A1CAE H222 H N N 38  
A1CAE H223 H N N 39  
A1CAE H232 H N N 40  
A1CAE H231 H N N 41  
A1CAE H242 H N N 42  
A1CAE H241 H N N 43  
A1CAE H262 H N N 44  
A1CAE H261 H N N 45  
A1CAE H272 H N N 46  
A1CAE H271 H N N 47  
A1CAE H281 H N N 48  
A1CAE H301 H N N 49  
A1CAE H031 H N N 50  
A1CAE H032 H N N 51  
A1CAE H033 H N N 52  
A1CAE H051 H N N 53  
A1CAE H061 H N N 54  
A1CAE H081 H N N 55  
A1CAE H082 H N N 56  
A1CAE H311 H N N 57  
A1CAE H101 H N N 58  
A1CAE H131 H N N 59  
A1CAE H201 H N N 60  
ALA   N    N N N 61  
ALA   CA   C N S 62  
ALA   C    C N N 63  
ALA   O    O N N 64  
ALA   CB   C N N 65  
ALA   OXT  O N N 66  
ALA   H    H N N 67  
ALA   H2   H N N 68  
ALA   HA   H N N 69  
ALA   HB1  H N N 70  
ALA   HB2  H N N 71  
ALA   HB3  H N N 72  
ALA   HXT  H N N 73  
ARG   N    N N N 74  
ARG   CA   C N S 75  
ARG   C    C N N 76  
ARG   O    O N N 77  
ARG   CB   C N N 78  
ARG   CG   C N N 79  
ARG   CD   C N N 80  
ARG   NE   N N N 81  
ARG   CZ   C N N 82  
ARG   NH1  N N N 83  
ARG   NH2  N N N 84  
ARG   OXT  O N N 85  
ARG   H    H N N 86  
ARG   H2   H N N 87  
ARG   HA   H N N 88  
ARG   HB2  H N N 89  
ARG   HB3  H N N 90  
ARG   HG2  H N N 91  
ARG   HG3  H N N 92  
ARG   HD2  H N N 93  
ARG   HD3  H N N 94  
ARG   HE   H N N 95  
ARG   HH11 H N N 96  
ARG   HH12 H N N 97  
ARG   HH21 H N N 98  
ARG   HH22 H N N 99  
ARG   HXT  H N N 100 
ASN   N    N N N 101 
ASN   CA   C N S 102 
ASN   C    C N N 103 
ASN   O    O N N 104 
ASN   CB   C N N 105 
ASN   CG   C N N 106 
ASN   OD1  O N N 107 
ASN   ND2  N N N 108 
ASN   OXT  O N N 109 
ASN   H    H N N 110 
ASN   H2   H N N 111 
ASN   HA   H N N 112 
ASN   HB2  H N N 113 
ASN   HB3  H N N 114 
ASN   HD21 H N N 115 
ASN   HD22 H N N 116 
ASN   HXT  H N N 117 
ASP   N    N N N 118 
ASP   CA   C N S 119 
ASP   C    C N N 120 
ASP   O    O N N 121 
ASP   CB   C N N 122 
ASP   CG   C N N 123 
ASP   OD1  O N N 124 
ASP   OD2  O N N 125 
ASP   OXT  O N N 126 
ASP   H    H N N 127 
ASP   H2   H N N 128 
ASP   HA   H N N 129 
ASP   HB2  H N N 130 
ASP   HB3  H N N 131 
ASP   HD2  H N N 132 
ASP   HXT  H N N 133 
CYS   N    N N N 134 
CYS   CA   C N R 135 
CYS   C    C N N 136 
CYS   O    O N N 137 
CYS   CB   C N N 138 
CYS   SG   S N N 139 
CYS   OXT  O N N 140 
CYS   H    H N N 141 
CYS   H2   H N N 142 
CYS   HA   H N N 143 
CYS   HB2  H N N 144 
CYS   HB3  H N N 145 
CYS   HG   H N N 146 
CYS   HXT  H N N 147 
GLN   N    N N N 148 
GLN   CA   C N S 149 
GLN   C    C N N 150 
GLN   O    O N N 151 
GLN   CB   C N N 152 
GLN   CG   C N N 153 
GLN   CD   C N N 154 
GLN   OE1  O N N 155 
GLN   NE2  N N N 156 
GLN   OXT  O N N 157 
GLN   H    H N N 158 
GLN   H2   H N N 159 
GLN   HA   H N N 160 
GLN   HB2  H N N 161 
GLN   HB3  H N N 162 
GLN   HG2  H N N 163 
GLN   HG3  H N N 164 
GLN   HE21 H N N 165 
GLN   HE22 H N N 166 
GLN   HXT  H N N 167 
GLU   N    N N N 168 
GLU   CA   C N S 169 
GLU   C    C N N 170 
GLU   O    O N N 171 
GLU   CB   C N N 172 
GLU   CG   C N N 173 
GLU   CD   C N N 174 
GLU   OE1  O N N 175 
GLU   OE2  O N N 176 
GLU   OXT  O N N 177 
GLU   H    H N N 178 
GLU   H2   H N N 179 
GLU   HA   H N N 180 
GLU   HB2  H N N 181 
GLU   HB3  H N N 182 
GLU   HG2  H N N 183 
GLU   HG3  H N N 184 
GLU   HE2  H N N 185 
GLU   HXT  H N N 186 
GLY   N    N N N 187 
GLY   CA   C N N 188 
GLY   C    C N N 189 
GLY   O    O N N 190 
GLY   OXT  O N N 191 
GLY   H    H N N 192 
GLY   H2   H N N 193 
GLY   HA2  H N N 194 
GLY   HA3  H N N 195 
GLY   HXT  H N N 196 
HIS   N    N N N 197 
HIS   CA   C N S 198 
HIS   C    C N N 199 
HIS   O    O N N 200 
HIS   CB   C N N 201 
HIS   CG   C Y N 202 
HIS   ND1  N Y N 203 
HIS   CD2  C Y N 204 
HIS   CE1  C Y N 205 
HIS   NE2  N Y N 206 
HIS   OXT  O N N 207 
HIS   H    H N N 208 
HIS   H2   H N N 209 
HIS   HA   H N N 210 
HIS   HB2  H N N 211 
HIS   HB3  H N N 212 
HIS   HD1  H N N 213 
HIS   HD2  H N N 214 
HIS   HE1  H N N 215 
HIS   HE2  H N N 216 
HIS   HXT  H N N 217 
HOH   O    O N N 218 
HOH   H1   H N N 219 
HOH   H2   H N N 220 
ILE   N    N N N 221 
ILE   CA   C N S 222 
ILE   C    C N N 223 
ILE   O    O N N 224 
ILE   CB   C N S 225 
ILE   CG1  C N N 226 
ILE   CG2  C N N 227 
ILE   CD1  C N N 228 
ILE   OXT  O N N 229 
ILE   H    H N N 230 
ILE   H2   H N N 231 
ILE   HA   H N N 232 
ILE   HB   H N N 233 
ILE   HG12 H N N 234 
ILE   HG13 H N N 235 
ILE   HG21 H N N 236 
ILE   HG22 H N N 237 
ILE   HG23 H N N 238 
ILE   HD11 H N N 239 
ILE   HD12 H N N 240 
ILE   HD13 H N N 241 
ILE   HXT  H N N 242 
LEU   N    N N N 243 
LEU   CA   C N S 244 
LEU   C    C N N 245 
LEU   O    O N N 246 
LEU   CB   C N N 247 
LEU   CG   C N N 248 
LEU   CD1  C N N 249 
LEU   CD2  C N N 250 
LEU   OXT  O N N 251 
LEU   H    H N N 252 
LEU   H2   H N N 253 
LEU   HA   H N N 254 
LEU   HB2  H N N 255 
LEU   HB3  H N N 256 
LEU   HG   H N N 257 
LEU   HD11 H N N 258 
LEU   HD12 H N N 259 
LEU   HD13 H N N 260 
LEU   HD21 H N N 261 
LEU   HD22 H N N 262 
LEU   HD23 H N N 263 
LEU   HXT  H N N 264 
LYS   N    N N N 265 
LYS   CA   C N S 266 
LYS   C    C N N 267 
LYS   O    O N N 268 
LYS   CB   C N N 269 
LYS   CG   C N N 270 
LYS   CD   C N N 271 
LYS   CE   C N N 272 
LYS   NZ   N N N 273 
LYS   OXT  O N N 274 
LYS   H    H N N 275 
LYS   H2   H N N 276 
LYS   HA   H N N 277 
LYS   HB2  H N N 278 
LYS   HB3  H N N 279 
LYS   HG2  H N N 280 
LYS   HG3  H N N 281 
LYS   HD2  H N N 282 
LYS   HD3  H N N 283 
LYS   HE2  H N N 284 
LYS   HE3  H N N 285 
LYS   HZ1  H N N 286 
LYS   HZ2  H N N 287 
LYS   HZ3  H N N 288 
LYS   HXT  H N N 289 
MET   N    N N N 290 
MET   CA   C N S 291 
MET   C    C N N 292 
MET   O    O N N 293 
MET   CB   C N N 294 
MET   CG   C N N 295 
MET   SD   S N N 296 
MET   CE   C N N 297 
MET   OXT  O N N 298 
MET   H    H N N 299 
MET   H2   H N N 300 
MET   HA   H N N 301 
MET   HB2  H N N 302 
MET   HB3  H N N 303 
MET   HG2  H N N 304 
MET   HG3  H N N 305 
MET   HE1  H N N 306 
MET   HE2  H N N 307 
MET   HE3  H N N 308 
MET   HXT  H N N 309 
PHE   N    N N N 310 
PHE   CA   C N S 311 
PHE   C    C N N 312 
PHE   O    O N N 313 
PHE   CB   C N N 314 
PHE   CG   C Y N 315 
PHE   CD1  C Y N 316 
PHE   CD2  C Y N 317 
PHE   CE1  C Y N 318 
PHE   CE2  C Y N 319 
PHE   CZ   C Y N 320 
PHE   OXT  O N N 321 
PHE   H    H N N 322 
PHE   H2   H N N 323 
PHE   HA   H N N 324 
PHE   HB2  H N N 325 
PHE   HB3  H N N 326 
PHE   HD1  H N N 327 
PHE   HD2  H N N 328 
PHE   HE1  H N N 329 
PHE   HE2  H N N 330 
PHE   HZ   H N N 331 
PHE   HXT  H N N 332 
PRO   N    N N N 333 
PRO   CA   C N S 334 
PRO   C    C N N 335 
PRO   O    O N N 336 
PRO   CB   C N N 337 
PRO   CG   C N N 338 
PRO   CD   C N N 339 
PRO   OXT  O N N 340 
PRO   H    H N N 341 
PRO   HA   H N N 342 
PRO   HB2  H N N 343 
PRO   HB3  H N N 344 
PRO   HG2  H N N 345 
PRO   HG3  H N N 346 
PRO   HD2  H N N 347 
PRO   HD3  H N N 348 
PRO   HXT  H N N 349 
SER   N    N N N 350 
SER   CA   C N S 351 
SER   C    C N N 352 
SER   O    O N N 353 
SER   CB   C N N 354 
SER   OG   O N N 355 
SER   OXT  O N N 356 
SER   H    H N N 357 
SER   H2   H N N 358 
SER   HA   H N N 359 
SER   HB2  H N N 360 
SER   HB3  H N N 361 
SER   HG   H N N 362 
SER   HXT  H N N 363 
THR   N    N N N 364 
THR   CA   C N S 365 
THR   C    C N N 366 
THR   O    O N N 367 
THR   CB   C N R 368 
THR   OG1  O N N 369 
THR   CG2  C N N 370 
THR   OXT  O N N 371 
THR   H    H N N 372 
THR   H2   H N N 373 
THR   HA   H N N 374 
THR   HB   H N N 375 
THR   HG1  H N N 376 
THR   HG21 H N N 377 
THR   HG22 H N N 378 
THR   HG23 H N N 379 
THR   HXT  H N N 380 
TPO   N    N N N 381 
TPO   CA   C N S 382 
TPO   CB   C N R 383 
TPO   CG2  C N N 384 
TPO   OG1  O N N 385 
TPO   P    P N N 386 
TPO   O1P  O N N 387 
TPO   O2P  O N N 388 
TPO   O3P  O N N 389 
TPO   C    C N N 390 
TPO   O    O N N 391 
TPO   OXT  O N N 392 
TPO   H    H N N 393 
TPO   H2   H N N 394 
TPO   HA   H N N 395 
TPO   HB   H N N 396 
TPO   HG21 H N N 397 
TPO   HG22 H N N 398 
TPO   HG23 H N N 399 
TPO   HOP2 H N N 400 
TPO   HOP3 H N N 401 
TPO   HXT  H N N 402 
TRP   N    N N N 403 
TRP   CA   C N S 404 
TRP   C    C N N 405 
TRP   O    O N N 406 
TRP   CB   C N N 407 
TRP   CG   C Y N 408 
TRP   CD1  C Y N 409 
TRP   CD2  C Y N 410 
TRP   NE1  N Y N 411 
TRP   CE2  C Y N 412 
TRP   CE3  C Y N 413 
TRP   CZ2  C Y N 414 
TRP   CZ3  C Y N 415 
TRP   CH2  C Y N 416 
TRP   OXT  O N N 417 
TRP   H    H N N 418 
TRP   H2   H N N 419 
TRP   HA   H N N 420 
TRP   HB2  H N N 421 
TRP   HB3  H N N 422 
TRP   HD1  H N N 423 
TRP   HE1  H N N 424 
TRP   HE3  H N N 425 
TRP   HZ2  H N N 426 
TRP   HZ3  H N N 427 
TRP   HH2  H N N 428 
TRP   HXT  H N N 429 
TYR   N    N N N 430 
TYR   CA   C N S 431 
TYR   C    C N N 432 
TYR   O    O N N 433 
TYR   CB   C N N 434 
TYR   CG   C Y N 435 
TYR   CD1  C Y N 436 
TYR   CD2  C Y N 437 
TYR   CE1  C Y N 438 
TYR   CE2  C Y N 439 
TYR   CZ   C Y N 440 
TYR   OH   O N N 441 
TYR   OXT  O N N 442 
TYR   H    H N N 443 
TYR   H2   H N N 444 
TYR   HA   H N N 445 
TYR   HB2  H N N 446 
TYR   HB3  H N N 447 
TYR   HD1  H N N 448 
TYR   HD2  H N N 449 
TYR   HE1  H N N 450 
TYR   HE2  H N N 451 
TYR   HH   H N N 452 
TYR   HXT  H N N 453 
VAL   N    N N N 454 
VAL   CA   C N S 455 
VAL   C    C N N 456 
VAL   O    O N N 457 
VAL   CB   C N N 458 
VAL   CG1  C N N 459 
VAL   CG2  C N N 460 
VAL   OXT  O N N 461 
VAL   H    H N N 462 
VAL   H2   H N N 463 
VAL   HA   H N N 464 
VAL   HB   H N N 465 
VAL   HG11 H N N 466 
VAL   HG12 H N N 467 
VAL   HG13 H N N 468 
VAL   HG21 H N N 469 
VAL   HG22 H N N 470 
VAL   HG23 H N N 471 
VAL   HXT  H N N 472 
# 
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 
A1CAE S02 O01  doub N N 1   
A1CAE C03 S02  sing N N 2   
A1CAE C05 C04  doub Y N 3   
A1CAE C06 C05  sing Y N 4   
A1CAE C07 C06  doub Y N 5   
A1CAE C09 C08  sing N N 6   
A1CAE C11 N10  sing N N 7   
A1CAE N12 C11  doub Y N 8   
A1CAE N13 N12  sing Y N 9   
A1CAE C14 N13  sing Y N 10  
A1CAE C16 C15  sing N N 11  
A1CAE C17 C16  sing N N 12  
A1CAE C19 O18  sing N N 13  
A1CAE C21 N20  sing N N 14  
A1CAE C22 C21  sing N N 15  
A1CAE C23 C21  sing N N 16  
A1CAE C24 C23  sing N N 17  
A1CAE N20 C19  sing N N 18  
A1CAE O25 C19  doub N N 19  
A1CAE O18 C17  sing N N 20  
A1CAE C26 C17  sing N N 21  
A1CAE C27 C26  sing N N 22  
A1CAE C15 C14  sing N N 23  
A1CAE C28 C14  doub Y N 24  
A1CAE N10 C09  sing N N 25  
A1CAE O29 C09  doub N N 26  
A1CAE C08 C07  sing N N 27  
A1CAE C30 C07  sing Y N 28  
A1CAE C31 C30  doub Y N 29  
A1CAE C04 S02  sing N N 30  
A1CAE O32 S02  doub N N 31  
A1CAE C04 C31  sing Y N 32  
A1CAE C11 C28  sing Y N 33  
A1CAE C15 C27  sing N N 34  
A1CAE C21 C24  sing N N 35  
A1CAE C15 H151 sing N N 36  
A1CAE C16 H162 sing N N 37  
A1CAE C16 H161 sing N N 38  
A1CAE C17 H171 sing N N 39  
A1CAE C22 H221 sing N N 40  
A1CAE C22 H222 sing N N 41  
A1CAE C22 H223 sing N N 42  
A1CAE C23 H232 sing N N 43  
A1CAE C23 H231 sing N N 44  
A1CAE C24 H242 sing N N 45  
A1CAE C24 H241 sing N N 46  
A1CAE C26 H262 sing N N 47  
A1CAE C26 H261 sing N N 48  
A1CAE C27 H272 sing N N 49  
A1CAE C27 H271 sing N N 50  
A1CAE C28 H281 sing N N 51  
A1CAE C30 H301 sing N N 52  
A1CAE C03 H031 sing N N 53  
A1CAE C03 H032 sing N N 54  
A1CAE C03 H033 sing N N 55  
A1CAE C05 H051 sing N N 56  
A1CAE C06 H061 sing N N 57  
A1CAE C08 H081 sing N N 58  
A1CAE C08 H082 sing N N 59  
A1CAE C31 H311 sing N N 60  
A1CAE N10 H101 sing N N 61  
A1CAE N13 H131 sing N N 62  
A1CAE N20 H201 sing N N 63  
ALA   N   CA   sing N N 64  
ALA   N   H    sing N N 65  
ALA   N   H2   sing N N 66  
ALA   CA  C    sing N N 67  
ALA   CA  CB   sing N N 68  
ALA   CA  HA   sing N N 69  
ALA   C   O    doub N N 70  
ALA   C   OXT  sing N N 71  
ALA   CB  HB1  sing N N 72  
ALA   CB  HB2  sing N N 73  
ALA   CB  HB3  sing N N 74  
ALA   OXT HXT  sing N N 75  
ARG   N   CA   sing N N 76  
ARG   N   H    sing N N 77  
ARG   N   H2   sing N N 78  
ARG   CA  C    sing N N 79  
ARG   CA  CB   sing N N 80  
ARG   CA  HA   sing N N 81  
ARG   C   O    doub N N 82  
ARG   C   OXT  sing N N 83  
ARG   CB  CG   sing N N 84  
ARG   CB  HB2  sing N N 85  
ARG   CB  HB3  sing N N 86  
ARG   CG  CD   sing N N 87  
ARG   CG  HG2  sing N N 88  
ARG   CG  HG3  sing N N 89  
ARG   CD  NE   sing N N 90  
ARG   CD  HD2  sing N N 91  
ARG   CD  HD3  sing N N 92  
ARG   NE  CZ   sing N N 93  
ARG   NE  HE   sing N N 94  
ARG   CZ  NH1  sing N N 95  
ARG   CZ  NH2  doub N N 96  
ARG   NH1 HH11 sing N N 97  
ARG   NH1 HH12 sing N N 98  
ARG   NH2 HH21 sing N N 99  
ARG   NH2 HH22 sing N N 100 
ARG   OXT HXT  sing N N 101 
ASN   N   CA   sing N N 102 
ASN   N   H    sing N N 103 
ASN   N   H2   sing N N 104 
ASN   CA  C    sing N N 105 
ASN   CA  CB   sing N N 106 
ASN   CA  HA   sing N N 107 
ASN   C   O    doub N N 108 
ASN   C   OXT  sing N N 109 
ASN   CB  CG   sing N N 110 
ASN   CB  HB2  sing N N 111 
ASN   CB  HB3  sing N N 112 
ASN   CG  OD1  doub N N 113 
ASN   CG  ND2  sing N N 114 
ASN   ND2 HD21 sing N N 115 
ASN   ND2 HD22 sing N N 116 
ASN   OXT HXT  sing N N 117 
ASP   N   CA   sing N N 118 
ASP   N   H    sing N N 119 
ASP   N   H2   sing N N 120 
ASP   CA  C    sing N N 121 
ASP   CA  CB   sing N N 122 
ASP   CA  HA   sing N N 123 
ASP   C   O    doub N N 124 
ASP   C   OXT  sing N N 125 
ASP   CB  CG   sing N N 126 
ASP   CB  HB2  sing N N 127 
ASP   CB  HB3  sing N N 128 
ASP   CG  OD1  doub N N 129 
ASP   CG  OD2  sing N N 130 
ASP   OD2 HD2  sing N N 131 
ASP   OXT HXT  sing N N 132 
CYS   N   CA   sing N N 133 
CYS   N   H    sing N N 134 
CYS   N   H2   sing N N 135 
CYS   CA  C    sing N N 136 
CYS   CA  CB   sing N N 137 
CYS   CA  HA   sing N N 138 
CYS   C   O    doub N N 139 
CYS   C   OXT  sing N N 140 
CYS   CB  SG   sing N N 141 
CYS   CB  HB2  sing N N 142 
CYS   CB  HB3  sing N N 143 
CYS   SG  HG   sing N N 144 
CYS   OXT HXT  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TPO   N   CA   sing N N 369 
TPO   N   H    sing N N 370 
TPO   N   H2   sing N N 371 
TPO   CA  CB   sing N N 372 
TPO   CA  C    sing N N 373 
TPO   CA  HA   sing N N 374 
TPO   CB  CG2  sing N N 375 
TPO   CB  OG1  sing N N 376 
TPO   CB  HB   sing N N 377 
TPO   CG2 HG21 sing N N 378 
TPO   CG2 HG22 sing N N 379 
TPO   CG2 HG23 sing N N 380 
TPO   OG1 P    sing N N 381 
TPO   P   O1P  doub N N 382 
TPO   P   O2P  sing N N 383 
TPO   P   O3P  sing N N 384 
TPO   O2P HOP2 sing N N 385 
TPO   O3P HOP3 sing N N 386 
TPO   C   O    doub N N 387 
TPO   C   OXT  sing N N 388 
TPO   OXT HXT  sing N N 389 
TRP   N   CA   sing N N 390 
TRP   N   H    sing N N 391 
TRP   N   H2   sing N N 392 
TRP   CA  C    sing N N 393 
TRP   CA  CB   sing N N 394 
TRP   CA  HA   sing N N 395 
TRP   C   O    doub N N 396 
TRP   C   OXT  sing N N 397 
TRP   CB  CG   sing N N 398 
TRP   CB  HB2  sing N N 399 
TRP   CB  HB3  sing N N 400 
TRP   CG  CD1  doub Y N 401 
TRP   CG  CD2  sing Y N 402 
TRP   CD1 NE1  sing Y N 403 
TRP   CD1 HD1  sing N N 404 
TRP   CD2 CE2  doub Y N 405 
TRP   CD2 CE3  sing Y N 406 
TRP   NE1 CE2  sing Y N 407 
TRP   NE1 HE1  sing N N 408 
TRP   CE2 CZ2  sing Y N 409 
TRP   CE3 CZ3  doub Y N 410 
TRP   CE3 HE3  sing N N 411 
TRP   CZ2 CH2  doub Y N 412 
TRP   CZ2 HZ2  sing N N 413 
TRP   CZ3 CH2  sing Y N 414 
TRP   CZ3 HZ3  sing N N 415 
TRP   CH2 HH2  sing N N 416 
TRP   OXT HXT  sing N N 417 
TYR   N   CA   sing N N 418 
TYR   N   H    sing N N 419 
TYR   N   H2   sing N N 420 
TYR   CA  C    sing N N 421 
TYR   CA  CB   sing N N 422 
TYR   CA  HA   sing N N 423 
TYR   C   O    doub N N 424 
TYR   C   OXT  sing N N 425 
TYR   CB  CG   sing N N 426 
TYR   CB  HB2  sing N N 427 
TYR   CB  HB3  sing N N 428 
TYR   CG  CD1  doub Y N 429 
TYR   CG  CD2  sing Y N 430 
TYR   CD1 CE1  sing Y N 431 
TYR   CD1 HD1  sing N N 432 
TYR   CD2 CE2  doub Y N 433 
TYR   CD2 HD2  sing N N 434 
TYR   CE1 CZ   doub Y N 435 
TYR   CE1 HE1  sing N N 436 
TYR   CE2 CZ   sing Y N 437 
TYR   CE2 HE2  sing N N 438 
TYR   CZ  OH   sing N N 439 
TYR   OH  HH   sing N N 440 
TYR   OXT HXT  sing N N 441 
VAL   N   CA   sing N N 442 
VAL   N   H    sing N N 443 
VAL   N   H2   sing N N 444 
VAL   CA  C    sing N N 445 
VAL   CA  CB   sing N N 446 
VAL   CA  HA   sing N N 447 
VAL   C   O    doub N N 448 
VAL   C   OXT  sing N N 449 
VAL   CB  CG1  sing N N 450 
VAL   CB  CG2  sing N N 451 
VAL   CB  HB   sing N N 452 
VAL   CG1 HG11 sing N N 453 
VAL   CG1 HG12 sing N N 454 
VAL   CG1 HG13 sing N N 455 
VAL   CG2 HG21 sing N N 456 
VAL   CG2 HG22 sing N N 457 
VAL   CG2 HG23 sing N N 458 
VAL   OXT HXT  sing N N 459 
# 
_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 Model' 
# 
_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                    9OB2 
_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]   0.009887 
_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]   0.009887 
_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]   0.006626 
_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   ? 52.29449 11.83505  -3.87127  1.000 102.37122 ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 4   ? 51.60800 12.98026  -3.28294  1.000 124.96966 ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 4   ? 52.56222 13.86475  -2.48728  1.000 128.39050 ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 4   ? 52.19315 14.40882  -1.44669  1.000 125.00681 ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 4   ? 50.46140 12.51323  -2.38303  1.000 124.37620 ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 4   ? 49.21520 12.08115  -3.13620  1.000 109.28327 ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 4   ? 48.53164 13.41876  -4.13344  1.000 116.30083 ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 4   ? 48.38210 14.71037  -2.90240  1.000 105.84539 ? 1   MET   A CE  1 
ATOM   9    N N   . GLU   A 1 5   ? 53.78914 14.01165  -2.98645  1.000 134.30077 ? 2   GLU   A N   1 
ATOM   10   C CA  . GLU   A 1 5   ? 54.80242 14.80242  -2.29803  1.000 137.17050 ? 2   GLU   A CA  1 
ATOM   11   C C   . GLU   A 1 5   ? 54.84590 16.24862  -2.77899  1.000 136.48418 ? 2   GLU   A C   1 
ATOM   12   O O   . GLU   A 1 5   ? 54.93937 17.16912  -1.95929  1.000 126.93380 ? 2   GLU   A O   1 
ATOM   13   C CB  . GLU   A 1 5   ? 56.18093 14.15884  -2.47376  1.000 138.42761 ? 2   GLU   A CB  1 
ATOM   14   C CG  . GLU   A 1 5   ? 57.31264 14.92961  -1.81169  1.000 140.06502 ? 2   GLU   A CG  1 
ATOM   15   C CD  . GLU   A 1 5   ? 58.67185 14.31127  -2.07211  1.000 145.41925 ? 2   GLU   A CD  1 
ATOM   16   O OE1 . GLU   A 1 5   ? 58.73233 13.27521  -2.76735  1.000 153.65162 ? 2   GLU   A OE1 1 
ATOM   17   O OE2 . GLU   A 1 5   ? 59.68003 14.86235  -1.58217  1.000 137.24400 ? 2   GLU   A OE2 1 
ATOM   18   N N   . ASN   A 1 6   ? 54.77529 16.46976  -4.09313  1.000 135.63627 ? 3   ASN   A N   1 
ATOM   19   C CA  . ASN   A 1 6   ? 54.91072 17.80974  -4.65557  1.000 123.14852 ? 3   ASN   A CA  1 
ATOM   20   C C   . ASN   A 1 6   ? 53.69787 18.69802  -4.40848  1.000 110.23326 ? 3   ASN   A C   1 
ATOM   21   O O   . ASN   A 1 6   ? 53.74216 19.87689  -4.77776  1.000 111.07924 ? 3   ASN   A O   1 
ATOM   22   C CB  . ASN   A 1 6   ? 55.18025 17.72299  -6.15998  1.000 119.89341 ? 3   ASN   A CB  1 
ATOM   23   C CG  . ASN   A 1 6   ? 56.59077 17.26414  -6.47546  1.000 131.57969 ? 3   ASN   A CG  1 
ATOM   24   O OD1 . ASN   A 1 6   ? 57.51808 18.07143  -6.53753  1.000 132.46590 ? 3   ASN   A OD1 1 
ATOM   25   N ND2 . ASN   A 1 6   ? 56.75907 15.96310  -6.68178  1.000 136.32403 ? 3   ASN   A ND2 1 
ATOM   26   N N   . PHE   A 1 7   ? 52.63138 18.18462  -3.80295  1.000 101.89636 ? 4   PHE   A N   1 
ATOM   27   C CA  . PHE   A 1 7   ? 51.42172 18.96032  -3.56989  1.000 97.51672  ? 4   PHE   A CA  1 
ATOM   28   C C   . PHE   A 1 7   ? 51.35279 19.42703  -2.12261  1.000 88.07009  ? 4   PHE   A C   1 
ATOM   29   O O   . PHE   A 1 7   ? 51.62326 18.65986  -1.19398  1.000 94.58018  ? 4   PHE   A O   1 
ATOM   30   C CB  . PHE   A 1 7   ? 50.17492 18.14593  -3.91729  1.000 94.67568  ? 4   PHE   A CB  1 
ATOM   31   C CG  . PHE   A 1 7   ? 49.97108 17.95895  -5.39147  1.000 97.63746  ? 4   PHE   A CG  1 
ATOM   32   C CD1 . PHE   A 1 7   ? 50.49171 18.87224  -6.29430  1.000 93.18084  ? 4   PHE   A CD1 1 
ATOM   33   C CD2 . PHE   A 1 7   ? 49.26461 16.87117  -5.87623  1.000 89.87604  ? 4   PHE   A CD2 1 
ATOM   34   C CE1 . PHE   A 1 7   ? 50.31033 18.70565  -7.65247  1.000 98.79743  ? 4   PHE   A CE1 1 
ATOM   35   C CE2 . PHE   A 1 7   ? 49.07937 16.69864  -7.23352  1.000 81.07546  ? 4   PHE   A CE2 1 
ATOM   36   C CZ  . PHE   A 1 7   ? 49.60304 17.61711  -8.12320  1.000 98.42726  ? 4   PHE   A CZ  1 
ATOM   37   N N   . GLN   A 1 8   ? 50.98489 20.69297  -1.94202  1.000 76.30093  ? 5   GLN   A N   1 
ATOM   38   C CA  . GLN   A 1 8   ? 50.86443 21.30839  -0.62678  1.000 80.66366  ? 5   GLN   A CA  1 
ATOM   39   C C   . GLN   A 1 8   ? 49.49407 21.95932  -0.53098  1.000 83.28228  ? 5   GLN   A C   1 
ATOM   40   O O   . GLN   A 1 8   ? 49.17184 22.84771  -1.32664  1.000 82.99226  ? 5   GLN   A O   1 
ATOM   41   C CB  . GLN   A 1 8   ? 51.97514 22.33842  -0.39783  1.000 78.80373  ? 5   GLN   A CB  1 
ATOM   42   C CG  . GLN   A 1 8   ? 51.86574 23.10067  0.91114   1.000 92.71456  ? 5   GLN   A CG  1 
ATOM   43   C CD  . GLN   A 1 8   ? 52.97912 24.11631  1.08832   1.000 109.76448 ? 5   GLN   A CD  1 
ATOM   44   O OE1 . GLN   A 1 8   ? 52.92581 24.96337  1.97989   1.000 109.30474 ? 5   GLN   A OE1 1 
ATOM   45   N NE2 . GLN   A 1 8   ? 53.99693 24.03455  0.23819   1.000 111.53690 ? 5   GLN   A NE2 1 
ATOM   46   N N   . LYS   A 1 9   ? 48.68961 21.51313  0.43053   1.000 78.21012  ? 6   LYS   A N   1 
ATOM   47   C CA  . LYS   A 1 9   ? 47.34460 22.04835  0.58885   1.000 76.32267  ? 6   LYS   A CA  1 
ATOM   48   C C   . LYS   A 1 9   ? 47.39578 23.51446  0.99982   1.000 64.09206  ? 6   LYS   A C   1 
ATOM   49   O O   . LYS   A 1 9   ? 48.18113 23.90756  1.86545   1.000 71.23769  ? 6   LYS   A O   1 
ATOM   50   C CB  . LYS   A 1 9   ? 46.56753 21.23407  1.62348   1.000 79.14901  ? 6   LYS   A CB  1 
ATOM   51   C CG  . LYS   A 1 9   ? 46.28808 19.80079  1.19514   1.000 73.90482  ? 6   LYS   A CG  1 
ATOM   52   C CD  . LYS   A 1 9   ? 45.54370 19.02948  2.27338   1.000 76.30135  ? 6   LYS   A CD  1 
ATOM   53   C CE  . LYS   A 1 9   ? 45.23992 17.60907  1.82053   1.000 79.05395  ? 6   LYS   A CE  1 
ATOM   54   N NZ  . LYS   A 1 9   ? 44.55143 16.81945  2.87923   1.000 90.49860  ? 6   LYS   A NZ  1 
ATOM   55   N N   . VAL   A 1 10  ? 46.55545 24.32592  0.36536   1.000 63.30118  ? 7   VAL   A N   1 
ATOM   56   C CA  . VAL   A 1 10  ? 46.49594 25.76102  0.61327   1.000 75.58263  ? 7   VAL   A CA  1 
ATOM   57   C C   . VAL   A 1 10  ? 45.23669 26.13958  1.38467   1.000 67.07206  ? 7   VAL   A C   1 
ATOM   58   O O   . VAL   A 1 10  ? 45.29633 26.89490  2.35517   1.000 74.79216  ? 7   VAL   A O   1 
ATOM   59   C CB  . VAL   A 1 10  ? 46.59426 26.55512  -0.70918  1.000 69.62411  ? 7   VAL   A CB  1 
ATOM   60   C CG1 . VAL   A 1 10  ? 46.56796 28.05246  -0.43583  1.000 66.32528  ? 7   VAL   A CG1 1 
ATOM   61   C CG2 . VAL   A 1 10  ? 47.85197 26.16820  -1.46509  1.000 71.46901  ? 7   VAL   A CG2 1 
ATOM   62   N N   . GLU   A 1 11  ? 44.08595 25.61978  0.96623   1.000 67.29802  ? 8   GLU   A N   1 
ATOM   63   C CA  . GLU   A 1 11  ? 42.82763 25.93964  1.62286   1.000 66.41352  ? 8   GLU   A CA  1 
ATOM   64   C C   . GLU   A 1 11  ? 41.80577 24.86988  1.27025   1.000 62.47959  ? 8   GLU   A C   1 
ATOM   65   O O   . GLU   A 1 11  ? 41.84974 24.28785  0.18365   1.000 62.55571  ? 8   GLU   A O   1 
ATOM   66   C CB  . GLU   A 1 11  ? 42.32295 27.32718  1.20844   1.000 66.18154  ? 8   GLU   A CB  1 
ATOM   67   C CG  . GLU   A 1 11  ? 41.13159 27.82692  2.00826   1.000 85.07127  ? 8   GLU   A CG  1 
ATOM   68   C CD  . GLU   A 1 11  ? 40.73417 29.24057  1.63548   1.000 93.94372  ? 8   GLU   A CD  1 
ATOM   69   O OE1 . GLU   A 1 11  ? 41.42606 29.84880  0.79093   1.000 85.20106  ? 8   GLU   A OE1 1 
ATOM   70   O OE2 . GLU   A 1 11  ? 39.72961 29.74202  2.18498   1.000 92.89616  ? 8   GLU   A OE2 1 
ATOM   71   N N   . LYS   A 1 12  ? 40.89212 24.61199  2.20249   1.000 57.21922  ? 9   LYS   A N   1 
ATOM   72   C CA  . LYS   A 1 12  ? 39.79026 23.69122  1.95346   1.000 60.93456  ? 9   LYS   A CA  1 
ATOM   73   C C   . LYS   A 1 12  ? 38.71522 24.39799  1.13594   1.000 58.30240  ? 9   LYS   A C   1 
ATOM   74   O O   . LYS   A 1 12  ? 38.19051 25.43621  1.55320   1.000 64.85172  ? 9   LYS   A O   1 
ATOM   75   C CB  . LYS   A 1 12  ? 39.21637 23.17248  3.26966   1.000 62.51087  ? 9   LYS   A CB  1 
ATOM   76   C CG  . LYS   A 1 12  ? 38.00628 22.26340  3.10557   1.000 63.83562  ? 9   LYS   A CG  1 
ATOM   77   C CD  . LYS   A 1 12  ? 37.55260 21.70961  4.44662   1.000 60.37564  ? 9   LYS   A CD  1 
ATOM   78   C CE  . LYS   A 1 12  ? 36.30898 20.85220  4.30757   1.000 64.80604  ? 9   LYS   A CE  1 
ATOM   79   N NZ  . LYS   A 1 12  ? 35.93649 20.21815  5.60228   1.000 71.26472  ? 9   LYS   A NZ  1 
ATOM   80   N N   . ILE   A 1 13  ? 38.39207 23.83894  -0.03027  1.000 58.99502  ? 10  ILE   A N   1 
ATOM   81   C CA  . ILE   A 1 13  ? 37.36496 24.43195  -0.88038  1.000 61.54840  ? 10  ILE   A CA  1 
ATOM   82   C C   . ILE   A 1 13  ? 35.97348 24.11064  -0.34971  1.000 59.76765  ? 10  ILE   A C   1 
ATOM   83   O O   . ILE   A 1 13  ? 35.08297 24.96780  -0.35060  1.000 75.59175  ? 10  ILE   A O   1 
ATOM   84   C CB  . ILE   A 1 13  ? 37.54917 23.95907  -2.33446  1.000 57.37032  ? 10  ILE   A CB  1 
ATOM   85   C CG1 . ILE   A 1 13  ? 38.82838 24.55543  -2.92534  1.000 56.83353  ? 10  ILE   A CG1 1 
ATOM   86   C CG2 . ILE   A 1 13  ? 36.33582 24.31888  -3.18250  1.000 55.04052  ? 10  ILE   A CG2 1 
ATOM   87   C CD1 . ILE   A 1 13  ? 39.12984 24.08315  -4.32947  1.000 54.19048  ? 10  ILE   A CD1 1 
ATOM   88   N N   A GLY   A 1 14  ? 35.75628 22.87767  0.08766   0.443 67.59021  ? 11  GLY   A N   1 
ATOM   89   N N   B GLY   A 1 14  ? 35.77292 22.89007  0.13991   0.557 68.22923  ? 11  GLY   A N   1 
ATOM   90   C CA  A GLY   A 1 14  ? 34.44797 22.46198  0.55126   0.443 66.91131  ? 11  GLY   A CA  1 
ATOM   91   C CA  B GLY   A 1 14  ? 34.51203 22.52804  0.75538   0.557 66.63169  ? 11  GLY   A CA  1 
ATOM   92   C C   A GLY   A 1 14  ? 34.44354 20.97678  0.83878   0.443 68.43065  ? 11  GLY   A C   1 
ATOM   93   C C   B GLY   A 1 14  ? 34.32698 21.03725  0.94678   0.557 68.47420  ? 11  GLY   A C   1 
ATOM   94   O O   A GLY   A 1 14  ? 35.43710 20.27453  0.62645   0.443 62.07761  ? 11  GLY   A O   1 
ATOM   95   O O   B GLY   A 1 14  ? 35.04573 20.23268  0.34514   0.557 62.61292  ? 11  GLY   A O   1 
ATOM   96   N N   A GLU   A 1 15  ? 33.29565 20.50614  1.32415   0.443 73.79048  ? 12  GLU   A N   1 
ATOM   97   N N   B GLU   A 1 15  ? 33.37050 20.65654  1.79143   0.557 70.15896  ? 12  GLU   A N   1 
ATOM   98   C CA  A GLU   A 1 15  ? 33.13238 19.11704  1.72399   0.443 73.28727  ? 12  GLU   A CA  1 
ATOM   99   C CA  B GLU   A 1 15  ? 33.01137 19.25989  2.00201   0.557 72.47420  ? 12  GLU   A CA  1 
ATOM   100  C C   A GLU   A 1 15  ? 31.86665 18.53767  1.11091   0.443 79.81628  ? 12  GLU   A C   1 
ATOM   101  C C   B GLU   A 1 15  ? 31.51105 19.11346  1.79642   0.557 75.73259  ? 12  GLU   A C   1 
ATOM   102  O O   A GLU   A 1 15  ? 30.82062 19.19278  1.08602   0.443 78.77915  ? 12  GLU   A O   1 
ATOM   103  O O   B GLU   A 1 15  ? 30.72096 19.81048  2.44187   0.557 73.56059  ? 12  GLU   A O   1 
ATOM   104  C CB  A GLU   A 1 15  ? 33.07718 18.98475  3.25182   0.443 68.79325  ? 12  GLU   A CB  1 
ATOM   105  C CB  B GLU   A 1 15  ? 33.40599 18.77669  3.39838   0.557 69.30615  ? 12  GLU   A CB  1 
ATOM   106  C CG  A GLU   A 1 15  ? 32.86948 17.56347  3.73881   0.443 71.58713  ? 12  GLU   A CG  1 
ATOM   107  C CG  B GLU   A 1 15  ? 33.20284 17.27855  3.59012   0.557 72.94789  ? 12  GLU   A CG  1 
ATOM   108  C CD  A GLU   A 1 15  ? 33.00593 17.43504  5.24002   0.443 74.34296  ? 12  GLU   A CD  1 
ATOM   109  C CD  B GLU   A 1 15  ? 33.12760 16.86999  5.04568   0.557 76.06588  ? 12  GLU   A CD  1 
ATOM   110  O OE1 A GLU   A 1 15  ? 33.19847 18.47071  5.91173   0.443 74.40003  ? 12  GLU   A OE1 1 
ATOM   111  O OE1 B GLU   A 1 15  ? 33.23554 17.75436  5.92056   0.557 76.51603  ? 12  GLU   A OE1 1 
ATOM   112  O OE2 A GLU   A 1 15  ? 32.92372 16.29670  5.74734   0.443 80.31589  ? 12  GLU   A OE2 1 
ATOM   113  O OE2 B GLU   A 1 15  ? 32.95415 15.66055  5.31138   0.557 76.48862  ? 12  GLU   A OE2 1 
ATOM   114  N N   A GLY   A 1 16  ? 31.97183 17.30633  0.61457   0.443 74.70869  ? 13  GLY   A N   1 
ATOM   115  N N   B GLY   A 1 16  ? 31.12413 18.21776  0.90594   0.557 78.05928  ? 13  GLY   A N   1 
ATOM   116  C CA  A GLY   A 1 16  ? 30.82399 16.58385  0.10231   0.443 73.98799  ? 13  GLY   A CA  1 
ATOM   117  C CA  B GLY   A 1 16  ? 29.72605 18.00027  0.57476   0.557 67.59908  ? 13  GLY   A CA  1 
ATOM   118  C C   A GLY   A 1 16  ? 30.54901 15.32216  0.89394   0.443 73.13937  ? 13  GLY   A C   1 
ATOM   119  C C   B GLY   A 1 16  ? 29.51668 16.58076  0.10483   0.557 68.55612  ? 13  GLY   A C   1 
ATOM   120  O O   A GLY   A 1 16  ? 31.02136 15.17774  2.02548   0.443 72.55033  ? 13  GLY   A O   1 
ATOM   121  O O   B GLY   A 1 16  ? 30.27697 15.67945  0.46931   0.557 74.74564  ? 13  GLY   A O   1 
ATOM   122  N N   A THR   A 1 17  ? 29.79065 14.39746  0.30761   0.443 71.19842  ? 14  THR   A N   1 
ATOM   123  N N   B THR   A 1 17  ? 28.47659 16.38042  -0.70893  0.557 61.34571  ? 14  THR   A N   1 
ATOM   124  C CA  A THR   A 1 17  ? 29.46085 13.14550  0.97750   0.443 67.20698  ? 14  THR   A CA  1 
ATOM   125  C CA  B THR   A 1 17  ? 28.22972 15.06997  -1.30064  0.557 64.60153  ? 14  THR   A CA  1 
ATOM   126  C C   A THR   A 1 17  ? 30.70176 12.28139  1.17012   0.443 69.20050  ? 14  THR   A C   1 
ATOM   127  C C   B THR   A 1 17  ? 29.37622 14.63740  -2.20467  0.557 67.96648  ? 14  THR   A C   1 
ATOM   128  O O   A THR   A 1 17  ? 31.12116 12.03132  2.30476   0.443 65.90438  ? 14  THR   A O   1 
ATOM   129  O O   B THR   A 1 17  ? 29.61824 13.43631  -2.37248  0.557 70.91607  ? 14  THR   A O   1 
ATOM   130  C CB  A THR   A 1 17  ? 28.39671 12.37701  0.18623   0.443 73.51772  ? 14  THR   A CB  1 
ATOM   131  C CB  B THR   A 1 17  ? 26.92460 15.09852  -2.09258  0.557 68.30002  ? 14  THR   A CB  1 
ATOM   132  O OG1 A THR   A 1 17  ? 27.20334 13.16502  0.09795   0.443 74.28822  ? 14  THR   A OG1 1 
ATOM   133  O OG1 B THR   A 1 17  ? 27.04197 16.04147  -3.16724  0.557 69.36000  ? 14  THR   A OG1 1 
ATOM   134  C CG2 A THR   A 1 17  ? 28.07337 11.05105  0.86558   0.443 69.15244  ? 14  THR   A CG2 1 
ATOM   135  C CG2 B THR   A 1 17  ? 25.76626 15.51084  -1.20001  0.557 67.31667  ? 14  THR   A CG2 1 
ATOM   136  N N   A TYR   A 1 18  ? 31.28820 11.80940  0.07021   0.443 79.00305  ? 15  TYR   A N   1 
ATOM   137  N N   B TYR   A 1 18  ? 30.08498 15.59926  -2.79816  0.557 68.80159  ? 15  TYR   A N   1 
ATOM   138  C CA  A TYR   A 1 18  ? 32.47725 10.97088  0.14190   0.443 73.28223  ? 15  TYR   A CA  1 
ATOM   139  C CA  B TYR   A 1 18  ? 31.23120 15.27709  -3.63900  0.557 70.22097  ? 15  TYR   A CA  1 
ATOM   140  C C   A TYR   A 1 18  ? 33.77208 11.75455  -0.00423  0.443 73.64152  ? 15  TYR   A C   1 
ATOM   141  C C   B TYR   A 1 18  ? 32.37869 14.68024  -2.83365  0.557 71.59623  ? 15  TYR   A C   1 
ATOM   142  O O   A TYR   A 1 18  ? 34.81776 11.28889  0.46177   0.443 72.82502  ? 15  TYR   A O   1 
ATOM   143  O O   B TYR   A 1 18  ? 33.12773 13.84640  -3.35313  0.557 73.55259  ? 15  TYR   A O   1 
ATOM   144  C CB  A TYR   A 1 18  ? 32.43606 9.89042   -0.94401  0.443 67.62808  ? 15  TYR   A CB  1 
ATOM   145  C CB  B TYR   A 1 18  ? 31.69599 16.53125  -4.37955  0.557 69.95741  ? 15  TYR   A CB  1 
ATOM   146  C CG  A TYR   A 1 18  ? 31.26032 8.94526   -0.84891  0.443 71.96429  ? 15  TYR   A CG  1 
ATOM   147  C CG  B TYR   A 1 18  ? 31.46097 17.81420  -3.60913  0.557 65.86274  ? 15  TYR   A CG  1 
ATOM   148  C CD1 A TYR   A 1 18  ? 31.20626 7.97305   0.13941   0.443 65.75462  ? 15  TYR   A CD1 1 
ATOM   149  C CD1 B TYR   A 1 18  ? 32.36576 18.24856  -2.65010  0.557 58.00787  ? 15  TYR   A CD1 1 
ATOM   150  C CD2 A TYR   A 1 18  ? 30.21307 9.01250   -1.75989  0.443 69.46817  ? 15  TYR   A CD2 1 
ATOM   151  C CD2 B TYR   A 1 18  ? 30.33244 18.59059  -3.84361  0.557 62.51860  ? 15  TYR   A CD2 1 
ATOM   152  C CE1 A TYR   A 1 18  ? 30.13847 7.09993   0.22569   0.443 67.75847  ? 15  TYR   A CE1 1 
ATOM   153  C CE1 B TYR   A 1 18  ? 32.15333 19.41872  -1.94551  0.557 66.27269  ? 15  TYR   A CE1 1 
ATOM   154  C CE2 A TYR   A 1 18  ? 29.13965 8.14324   -1.68084  0.443 67.12823  ? 15  TYR   A CE2 1 
ATOM   155  C CE2 B TYR   A 1 18  ? 30.11068 19.76103  -3.14386  0.557 59.26601  ? 15  TYR   A CE2 1 
ATOM   156  C CZ  A TYR   A 1 18  ? 29.10845 7.18896   -0.68609  0.443 61.08541  ? 15  TYR   A CZ  1 
ATOM   157  C CZ  B TYR   A 1 18  ? 31.02375 20.17031  -2.19588  0.557 69.81271  ? 15  TYR   A CZ  1 
ATOM   158  O OH  A TYR   A 1 18  ? 28.04298 6.32176   -0.60392  0.443 64.59588  ? 15  TYR   A OH  1 
ATOM   159  O OH  B TYR   A 1 18  ? 30.80697 21.33577  -1.49676  0.557 72.29012  ? 15  TYR   A OH  1 
ATOM   160  N N   A GLY   A 1 19  ? 33.73328 12.91741  -0.63402  0.443 86.44282  ? 16  GLY   A N   1 
ATOM   161  N N   B GLY   A 1 19  ? 32.53301 15.08382  -1.57601  0.557 84.42070  ? 16  GLY   A N   1 
ATOM   162  C CA  A GLY   A 1 19  ? 34.94047 13.64799  -0.98635  0.443 74.20270  ? 16  GLY   A CA  1 
ATOM   163  C CA  B GLY   A 1 19  ? 33.65675 14.63728  -0.77592  0.557 79.56865  ? 16  GLY   A CA  1 
ATOM   164  C C   A GLY   A 1 19  ? 35.02139 15.00392  -0.31432  0.443 72.14310  ? 16  GLY   A C   1 
ATOM   165  C C   B GLY   A 1 19  ? 34.38366 15.79559  -0.12641  0.557 71.77985  ? 16  GLY   A C   1 
ATOM   166  O O   A GLY   A 1 19  ? 34.03700 15.74464  -0.26886  0.443 72.82820  ? 16  GLY   A O   1 
ATOM   167  O O   B GLY   A 1 19  ? 33.77601 16.83555  0.14124   0.557 69.37890  ? 16  GLY   A O   1 
ATOM   168  N N   A VAL   A 1 20  ? 36.20524 15.32040  0.20236   0.443 73.19682  ? 17  VAL   A N   1 
ATOM   169  N N   B VAL   A 1 20  ? 35.67869 15.63817  0.13026   0.557 73.68604  ? 17  VAL   A N   1 
ATOM   170  C CA  A VAL   A 1 20  ? 36.54406 16.65155  0.68980   0.443 64.49122  ? 17  VAL   A CA  1 
ATOM   171  C CA  B VAL   A 1 20  ? 36.49847 16.69110  0.71931   0.557 62.36062  ? 17  VAL   A CA  1 
ATOM   172  C C   A VAL   A 1 20  ? 37.51699 17.26407  -0.30499  0.443 65.88433  ? 17  VAL   A C   1 
ATOM   173  C C   B VAL   A 1 20  ? 37.41833 17.21885  -0.37409  0.557 65.73484  ? 17  VAL   A C   1 
ATOM   174  O O   A VAL   A 1 20  ? 38.52233 16.63767  -0.66125  0.443 65.68420  ? 17  VAL   A O   1 
ATOM   175  O O   B VAL   A 1 20  ? 38.29363 16.49631  -0.86653  0.557 65.11572  ? 17  VAL   A O   1 
ATOM   176  C CB  A VAL   A 1 20  ? 37.15769 16.60151  2.09935   0.443 68.11493  ? 17  VAL   A CB  1 
ATOM   177  C CB  B VAL   A 1 20  ? 37.29696 16.18850  1.92956   0.557 68.55621  ? 17  VAL   A CB  1 
ATOM   178  C CG1 A VAL   A 1 20  ? 37.63882 17.98139  2.51807   0.443 63.79147  ? 17  VAL   A CG1 1 
ATOM   179  C CG1 B VAL   A 1 20  ? 37.74433 17.36003  2.79518   0.557 64.52328  ? 17  VAL   A CG1 1 
ATOM   180  C CG2 A VAL   A 1 20  ? 36.15350 16.05388  3.09800   0.443 68.61290  ? 17  VAL   A CG2 1 
ATOM   181  C CG2 B VAL   A 1 20  ? 36.46771 15.20458  2.73986   0.557 72.85095  ? 17  VAL   A CG2 1 
ATOM   182  N N   . VAL   A 1 21  ? 37.22193 18.47783  -0.75621  1.000 52.63138  ? 18  VAL   A N   1 
ATOM   183  C CA  . VAL   A 1 21  ? 37.98534 19.12081  -1.81966  1.000 59.56083  ? 18  VAL   A CA  1 
ATOM   184  C C   . VAL   A 1 21  ? 38.89401 20.17353  -1.20140  1.000 58.58321  ? 18  VAL   A C   1 
ATOM   185  O O   . VAL   A 1 21  ? 38.42652 21.06858  -0.48609  1.000 55.27158  ? 18  VAL   A O   1 
ATOM   186  C CB  . VAL   A 1 21  ? 37.06139 19.73991  -2.87944  1.000 55.59308  ? 18  VAL   A CB  1 
ATOM   187  C CG1 . VAL   A 1 21  ? 37.87962 20.41096  -3.97587  1.000 49.53280  ? 18  VAL   A CG1 1 
ATOM   188  C CG2 . VAL   A 1 21  ? 36.15020 18.67535  -3.46599  1.000 60.02743  ? 18  VAL   A CG2 1 
ATOM   189  N N   . TYR   A 1 22  ? 40.19032 20.06432  -1.47804  1.000 46.03842  ? 19  TYR   A N   1 
ATOM   190  C CA  . TYR   A 1 22  ? 41.18245 21.03652  -1.04938  1.000 51.97576  ? 19  TYR   A CA  1 
ATOM   191  C C   . TYR   A 1 22  ? 41.77791 21.73738  -2.26260  1.000 61.41000  ? 19  TYR   A C   1 
ATOM   192  O O   . TYR   A 1 22  ? 41.84271 21.17346  -3.35870  1.000 64.06100  ? 19  TYR   A O   1 
ATOM   193  C CB  . TYR   A 1 22  ? 42.31529 20.37736  -0.25213  1.000 60.10439  ? 19  TYR   A CB  1 
ATOM   194  C CG  . TYR   A 1 22  ? 41.88711 19.64227  0.99795   1.000 63.03566  ? 19  TYR   A CG  1 
ATOM   195  C CD1 . TYR   A 1 22  ? 41.80106 20.29812  2.21908   1.000 71.61072  ? 19  TYR   A CD1 1 
ATOM   196  C CD2 . TYR   A 1 22  ? 41.59214 18.28559  0.96073   1.000 69.47312  ? 19  TYR   A CD2 1 
ATOM   197  C CE1 . TYR   A 1 22  ? 41.41956 19.62497  3.36739   1.000 81.15070  ? 19  TYR   A CE1 1 
ATOM   198  C CE2 . TYR   A 1 22  ? 41.21099 17.60474  2.10151   1.000 75.20677  ? 19  TYR   A CE2 1 
ATOM   199  C CZ  . TYR   A 1 22  ? 41.12576 18.27839  3.30158   1.000 75.81072  ? 19  TYR   A CZ  1 
ATOM   200  O OH  . TYR   A 1 22  ? 40.74576 17.60197  4.43832   1.000 82.23339  ? 19  TYR   A OH  1 
ATOM   201  N N   . LYS   A 1 23  ? 42.21422 22.97444  -2.05554  1.000 64.83965  ? 20  LYS   A N   1 
ATOM   202  C CA  . LYS   A 1 23  ? 43.01787 23.68678  -3.03880  1.000 54.85413  ? 20  LYS   A CA  1 
ATOM   203  C C   . LYS   A 1 23  ? 44.48811 23.43281  -2.73067  1.000 57.23988  ? 20  LYS   A C   1 
ATOM   204  O O   . LYS   A 1 23  ? 44.97359 23.80747  -1.65849  1.000 64.33836  ? 20  LYS   A O   1 
ATOM   205  C CB  . LYS   A 1 23  ? 42.70900 25.18245  -3.01484  1.000 56.07792  ? 20  LYS   A CB  1 
ATOM   206  C CG  . LYS   A 1 23  ? 43.60140 26.01493  -3.92272  1.000 56.99253  ? 20  LYS   A CG  1 
ATOM   207  C CD  . LYS   A 1 23  ? 43.30084 27.49735  -3.77095  1.000 64.30312  ? 20  LYS   A CD  1 
ATOM   208  C CE  . LYS   A 1 23  ? 44.21392 28.34153  -4.64172  1.000 68.25283  ? 20  LYS   A CE  1 
ATOM   209  N NZ  . LYS   A 1 23  ? 43.87909 29.78895  -4.54539  1.000 80.94571  ? 20  LYS   A NZ  1 
ATOM   210  N N   . ALA   A 1 24  ? 45.18843 22.78574  -3.65645  1.000 57.61390  ? 21  ALA   A N   1 
ATOM   211  C CA  . ALA   A 1 24  ? 46.59567 22.46063  -3.48486  1.000 59.35104  ? 21  ALA   A CA  1 
ATOM   212  C C   . ALA   A 1 24  ? 47.44339 23.24114  -4.48049  1.000 70.78129  ? 21  ALA   A C   1 
ATOM   213  O O   . ALA   A 1 24  ? 46.94702 23.75956  -5.48411  1.000 70.40804  ? 21  ALA   A O   1 
ATOM   214  C CB  . ALA   A 1 24  ? 46.83974 20.95689  -3.65087  1.000 68.19883  ? 21  ALA   A CB  1 
ATOM   215  N N   . ARG   A 1 25  ? 48.74084 23.31559  -4.19024  1.000 75.30410  ? 22  ARG   A N   1 
ATOM   216  C CA  . ARG   A 1 25  ? 49.67914 24.07382  -5.01015  1.000 69.93533  ? 22  ARG   A CA  1 
ATOM   217  C C   . ARG   A 1 25  ? 50.95311 23.26356  -5.18157  1.000 77.17272  ? 22  ARG   A C   1 
ATOM   218  O O   . ARG   A 1 25  ? 51.58092 22.87728  -4.19129  1.000 84.64744  ? 22  ARG   A O   1 
ATOM   219  C CB  . ARG   A 1 25  ? 49.99064 25.43416  -4.37768  1.000 76.39340  ? 22  ARG   A CB  1 
ATOM   220  C CG  . ARG   A 1 25  ? 50.90544 26.31087  -5.21455  1.000 83.07502  ? 22  ARG   A CG  1 
ATOM   221  C CD  . ARG   A 1 25  ? 51.24542 27.60294  -4.49259  1.000 94.09624  ? 22  ARG   A CD  1 
ATOM   222  N NE  . ARG   A 1 25  ? 52.11213 28.45854  -5.29401  1.000 111.52394 ? 22  ARG   A NE  1 
ATOM   223  C CZ  . ARG   A 1 25  ? 53.43496 28.36825  -5.32261  1.000 118.92946 ? 22  ARG   A CZ  1 
ATOM   224  N NH1 . ARG   A 1 25  ? 54.08182 27.46416  -4.60487  1.000 119.26264 ? 22  ARG   A NH1 1 
ATOM   225  N NH2 . ARG   A 1 25  ? 54.12618 29.20480  -6.09212  1.000 106.62226 ? 22  ARG   A NH2 1 
ATOM   226  N N   . ASN   A 1 26  ? 51.33272 23.00899  -6.43158  1.000 88.33253  ? 23  ASN   A N   1 
ATOM   227  C CA  . ASN   A 1 26  ? 52.58128 22.31039  -6.70417  1.000 88.01189  ? 23  ASN   A CA  1 
ATOM   228  C C   . ASN   A 1 26  ? 53.75976 23.21786  -6.37263  1.000 92.87466  ? 23  ASN   A C   1 
ATOM   229  O O   . ASN   A 1 26  ? 53.82586 24.36102  -6.83353  1.000 97.72471  ? 23  ASN   A O   1 
ATOM   230  C CB  . ASN   A 1 26  ? 52.63788 21.87051  -8.16584  1.000 95.02800  ? 23  ASN   A CB  1 
ATOM   231  C CG  . ASN   A 1 26  ? 53.82137 20.96919  -8.45741  1.000 100.26802 ? 23  ASN   A CG  1 
ATOM   232  O OD1 . ASN   A 1 26  ? 54.94505 21.43841  -8.63767  1.000 95.06538  ? 23  ASN   A OD1 1 
ATOM   233  N ND2 . ASN   A 1 26  ? 53.57292 19.66540  -8.50857  1.000 96.60452  ? 23  ASN   A ND2 1 
ATOM   234  N N   . LYS   A 1 27  ? 54.69203 22.70765  -5.56629  1.000 100.36725 ? 24  LYS   A N   1 
ATOM   235  C CA  . LYS   A 1 27  ? 55.78092 23.54773  -5.07925  1.000 103.76637 ? 24  LYS   A CA  1 
ATOM   236  C C   . LYS   A 1 27  ? 56.83957 23.79106  -6.14804  1.000 107.90103 ? 24  LYS   A C   1 
ATOM   237  O O   . LYS   A 1 27  ? 57.44995 24.86605  -6.17719  1.000 107.57425 ? 24  LYS   A O   1 
ATOM   238  C CB  . LYS   A 1 27  ? 56.40906 22.91618  -3.83659  1.000 114.98222 ? 24  LYS   A CB  1 
ATOM   239  C CG  . LYS   A 1 27  ? 55.52709 22.99317  -2.60047  1.000 117.38971 ? 24  LYS   A CG  1 
ATOM   240  C CD  . LYS   A 1 27  ? 55.96446 21.99951  -1.53659  1.000 123.10935 ? 24  LYS   A CD  1 
ATOM   241  C CE  . LYS   A 1 27  ? 55.65548 20.57128  -1.96050  1.000 119.08337 ? 24  LYS   A CE  1 
ATOM   242  N NZ  . LYS   A 1 27  ? 55.94725 19.58849  -0.88021  1.000 123.04988 ? 24  LYS   A NZ  1 
ATOM   243  N N   . LEU   A 1 28  ? 57.07036 22.81910  -7.03258  1.000 119.77923 ? 25  LEU   A N   1 
ATOM   244  C CA  . LEU   A 1 28  ? 58.11519 22.97351  -8.03953  1.000 126.71208 ? 25  LEU   A CA  1 
ATOM   245  C C   . LEU   A 1 28  ? 57.62289 23.74705  -9.25704  1.000 120.15852 ? 25  LEU   A C   1 
ATOM   246  O O   . LEU   A 1 28  ? 58.33057 24.62403  -9.76573  1.000 116.31742 ? 25  LEU   A O   1 
ATOM   247  C CB  . LEU   A 1 28  ? 58.64377 21.60301  -8.46297  1.000 119.88430 ? 25  LEU   A CB  1 
ATOM   248  C CG  . LEU   A 1 28  ? 59.48772 20.83989  -7.44145  1.000 119.84108 ? 25  LEU   A CG  1 
ATOM   249  C CD1 . LEU   A 1 28  ? 60.01149 19.55200  -8.05410  1.000 111.56308 ? 25  LEU   A CD1 1 
ATOM   250  C CD2 . LEU   A 1 28  ? 60.63420 21.70301  -6.93458  1.000 111.40503 ? 25  LEU   A CD2 1 
ATOM   251  N N   . THR   A 1 29  ? 56.41782 23.43993  -9.73584  1.000 103.84134 ? 26  THR   A N   1 
ATOM   252  C CA  . THR   A 1 29  ? 55.90686 24.02804  -10.96604 1.000 101.08365 ? 26  THR   A CA  1 
ATOM   253  C C   . THR   A 1 29  ? 55.02724 25.24992  -10.74090 1.000 93.99499  ? 26  THR   A C   1 
ATOM   254  O O   . THR   A 1 29  ? 54.78849 26.00189  -11.69208 1.000 94.96517  ? 26  THR   A O   1 
ATOM   255  C CB  . THR   A 1 29  ? 55.10922 22.98461  -11.75938 1.000 90.85220  ? 26  THR   A CB  1 
ATOM   256  O OG1 . THR   A 1 29  ? 53.89022 22.68561  -11.06928 1.000 92.76602  ? 26  THR   A OG1 1 
ATOM   257  C CG2 . THR   A 1 29  ? 55.91604 21.70529  -11.91170 1.000 101.89638 ? 26  THR   A CG2 1 
ATOM   258  N N   . GLY   A 1 30  ? 54.54591 25.47027  -9.52014  1.000 92.45108  ? 27  GLY   A N   1 
ATOM   259  C CA  . GLY   A 1 30  ? 53.61368 26.54506  -9.26045  1.000 94.23990  ? 27  GLY   A CA  1 
ATOM   260  C C   . GLY   A 1 30  ? 52.18112 26.25069  -9.64441  1.000 84.64657  ? 27  GLY   A C   1 
ATOM   261  O O   . GLY   A 1 30  ? 51.31859 27.12056  -9.46481  1.000 84.12159  ? 27  GLY   A O   1 
ATOM   262  N N   . GLU   A 1 31  ? 51.89996 25.05959  -10.16693 1.000 79.70351  ? 28  GLU   A N   1 
ATOM   263  C CA  . GLU   A 1 31  ? 50.53936 24.69547  -10.53466 1.000 81.39276  ? 28  GLU   A CA  1 
ATOM   264  C C   . GLU   A 1 31  ? 49.64970 24.61471  -9.30292  1.000 78.55454  ? 28  GLU   A C   1 
ATOM   265  O O   . GLU   A 1 31  ? 50.07251 24.15105  -8.24014  1.000 75.70190  ? 28  GLU   A O   1 
ATOM   266  C CB  . GLU   A 1 31  ? 50.52455 23.34947  -11.25698 1.000 80.93840  ? 28  GLU   A CB  1 
ATOM   267  C CG  . GLU   A 1 31  ? 51.15314 23.35307  -12.63421 1.000 100.89616 ? 28  GLU   A CG  1 
ATOM   268  C CD  . GLU   A 1 31  ? 51.37217 21.94939  -13.16300 1.000 108.58646 ? 28  GLU   A CD  1 
ATOM   269  O OE1 . GLU   A 1 31  ? 52.08679 21.16836  -12.49732 1.000 95.01725  ? 28  GLU   A OE1 1 
ATOM   270  O OE2 . GLU   A 1 31  ? 50.81951 21.62286  -14.23462 1.000 106.62384 ? 28  GLU   A OE2 1 
ATOM   271  N N   . VAL   A 1 32  ? 48.40839 25.06838  -9.45143  1.000 71.48011  ? 29  VAL   A N   1 
ATOM   272  C CA  . VAL   A 1 32  ? 47.37320 24.87528  -8.44498  1.000 68.99778  ? 29  VAL   A CA  1 
ATOM   273  C C   . VAL   A 1 32  ? 46.34990 23.89958  -9.00357  1.000 65.66802  ? 29  VAL   A C   1 
ATOM   274  O O   . VAL   A 1 32  ? 46.01346 23.94355  -10.19333 1.000 62.39443  ? 29  VAL   A O   1 
ATOM   275  C CB  . VAL   A 1 32  ? 46.70209 26.19761  -8.02168  1.000 63.35468  ? 29  VAL   A CB  1 
ATOM   276  C CG1 . VAL   A 1 32  ? 47.71623 27.11968  -7.36205  1.000 66.82634  ? 29  VAL   A CG1 1 
ATOM   277  C CG2 . VAL   A 1 32  ? 46.03661 26.87345  -9.20926  1.000 72.63973  ? 29  VAL   A CG2 1 
ATOM   278  N N   . VAL   A 1 33  ? 45.87660 22.99860  -8.14511  1.000 60.06308  ? 30  VAL   A N   1 
ATOM   279  C CA  . VAL   A 1 33  ? 44.89972 21.98861  -8.52079  1.000 55.49555  ? 30  VAL   A CA  1 
ATOM   280  C C   . VAL   A 1 33  ? 43.85374 21.90480  -7.42024  1.000 58.48656  ? 30  VAL   A C   1 
ATOM   281  O O   . VAL   A 1 33  ? 44.06003 22.36904  -6.29741  1.000 55.76747  ? 30  VAL   A O   1 
ATOM   282  C CB  . VAL   A 1 33  ? 45.54361 20.60160  -8.74758  1.000 55.90467  ? 30  VAL   A CB  1 
ATOM   283  C CG1 . VAL   A 1 33  ? 46.52550 20.64432  -9.90866  1.000 64.17548  ? 30  VAL   A CG1 1 
ATOM   284  C CG2 . VAL   A 1 33  ? 46.22969 20.12345  -7.47521  1.000 54.64263  ? 30  VAL   A CG2 1 
ATOM   285  N N   . ALA   A 1 34  ? 42.71535 21.31173  -7.76050  1.000 56.04204  ? 31  ALA   A N   1 
ATOM   286  C CA  . ALA   A 1 34  ? 41.68580 20.97804  -6.78719  1.000 52.06077  ? 31  ALA   A CA  1 
ATOM   287  C C   . ALA   A 1 34  ? 41.81266 19.49692  -6.45923  1.000 60.36188  ? 31  ALA   A C   1 
ATOM   288  O O   . ALA   A 1 34  ? 41.74345 18.65043  -7.35716  1.000 63.30467  ? 31  ALA   A O   1 
ATOM   289  C CB  . ALA   A 1 34  ? 40.29352 21.30315  -7.32143  1.000 55.19125  ? 31  ALA   A CB  1 
ATOM   290  N N   . LEU   A 1 35  ? 42.00145 19.18958  -5.18118  1.000 50.47135  ? 32  LEU   A N   1 
ATOM   291  C CA  . LEU   A 1 35  ? 42.33089 17.84435  -4.72558  1.000 48.13396  ? 32  LEU   A CA  1 
ATOM   292  C C   . LEU   A 1 35  ? 41.14687 17.28359  -3.94529  1.000 62.66009  ? 32  LEU   A C   1 
ATOM   293  O O   . LEU   A 1 35  ? 40.84437 17.75505  -2.84360  1.000 63.84694  ? 32  LEU   A O   1 
ATOM   294  C CB  . LEU   A 1 35  ? 43.59547 17.87912  -3.87008  1.000 52.94834  ? 32  LEU   A CB  1 
ATOM   295  C CG  . LEU   A 1 35  ? 44.28325 16.56994  -3.49402  1.000 67.05814  ? 32  LEU   A CG  1 
ATOM   296  C CD1 . LEU   A 1 35  ? 44.71527 15.80955  -4.73530  1.000 67.99839  ? 32  LEU   A CD1 1 
ATOM   297  C CD2 . LEU   A 1 35  ? 45.47652 16.86708  -2.60576  1.000 60.94678  ? 32  LEU   A CD2 1 
ATOM   298  N N   . LYS   A 1 36  ? 40.47812 16.28109  -4.51266  1.000 57.78281  ? 33  LYS   A N   1 
ATOM   299  C CA  . LYS   A 1 36  ? 39.38396 15.60146  -3.82854  1.000 65.73737  ? 33  LYS   A CA  1 
ATOM   300  C C   . LYS   A 1 36  ? 39.93971 14.41048  -3.05568  1.000 65.72637  ? 33  LYS   A C   1 
ATOM   301  O O   . LYS   A 1 36  ? 40.55423 13.51289  -3.64281  1.000 66.98877  ? 33  LYS   A O   1 
ATOM   302  C CB  . LYS   A 1 36  ? 38.30722 15.14796  -4.81322  1.000 54.93998  ? 33  LYS   A CB  1 
ATOM   303  C CG  . LYS   A 1 36  ? 37.12350 14.46047  -4.13773  1.000 63.99807  ? 33  LYS   A CG  1 
ATOM   304  C CD  . LYS   A 1 36  ? 36.09080 13.97592  -5.14389  1.000 67.96028  ? 33  LYS   A CD  1 
ATOM   305  C CE  . LYS   A 1 36  ? 35.42082 15.13505  -5.85982  1.000 66.63650  ? 33  LYS   A CE  1 
ATOM   306  N NZ  . LYS   A 1 36  ? 34.38186 14.66431  -6.81846  1.000 70.09926  ? 33  LYS   A NZ  1 
ATOM   307  N N   . LYS   A 1 37  ? 39.71634 14.40455  -1.74497  1.000 62.12165  ? 34  LYS   A N   1 
ATOM   308  C CA  . LYS   A 1 37  ? 40.24123 13.38297  -0.84883  1.000 65.53527  ? 34  LYS   A CA  1 
ATOM   309  C C   . LYS   A 1 37  ? 39.14425 12.37844  -0.52157  1.000 71.96655  ? 34  LYS   A C   1 
ATOM   310  O O   . LYS   A 1 37  ? 38.03175 12.76635  -0.14939  1.000 76.94992  ? 34  LYS   A O   1 
ATOM   311  C CB  . LYS   A 1 37  ? 40.77527 14.02289  0.43422   1.000 65.40681  ? 34  LYS   A CB  1 
ATOM   312  C CG  . LYS   A 1 37  ? 41.44486 13.06685  1.41093   1.000 85.27861  ? 34  LYS   A CG  1 
ATOM   313  C CD  . LYS   A 1 37  ? 41.61077 13.72982  2.77561   1.000 89.22685  ? 34  LYS   A CD  1 
ATOM   314  C CE  . LYS   A 1 37  ? 42.47482 12.90011  3.71177   1.000 96.28497  ? 34  LYS   A CE  1 
ATOM   315  N NZ  . LYS   A 1 37  ? 43.91090 12.94450  3.32362   1.000 95.44215  ? 34  LYS   A NZ  1 
ATOM   316  N N   . ILE   A 1 38  ? 39.45821 11.09303  -0.66473  1.000 69.60000  ? 35  ILE   A N   1 
ATOM   317  C CA  . ILE   A 1 38  ? 38.53040 10.01078  -0.35642  1.000 73.45907  ? 35  ILE   A CA  1 
ATOM   318  C C   . ILE   A 1 38  ? 39.21122 9.07730   0.63324   1.000 81.46080  ? 35  ILE   A C   1 
ATOM   319  O O   . ILE   A 1 38  ? 40.22114 8.44546   0.30080   1.000 80.31524  ? 35  ILE   A O   1 
ATOM   320  C CB  . ILE   A 1 38  ? 38.09669 9.24078   -1.61421  1.000 72.74625  ? 35  ILE   A CB  1 
ATOM   321  C CG1 . ILE   A 1 38  ? 37.40534 10.17864  -2.60324  1.000 65.04186  ? 35  ILE   A CG1 1 
ATOM   322  C CG2 . ILE   A 1 38  ? 37.17712 8.08774   -1.24211  1.000 65.15909  ? 35  ILE   A CG2 1 
ATOM   323  C CD1 . ILE   A 1 38  ? 36.97806 9.49871   -3.87699  1.000 60.61308  ? 35  ILE   A CD1 1 
ATOM   324  N N   . ARG   A 1 39  ? 38.66342 8.99126   1.84323   1.000 73.79342  ? 36  ARG   A N   1 
ATOM   325  C CA  . ARG   A 1 39  ? 39.20532 8.12832   2.88784   1.000 77.09018  ? 36  ARG   A CA  1 
ATOM   326  C C   . ARG   A 1 39  ? 38.62107 6.73126   2.70732   1.000 76.99024  ? 36  ARG   A C   1 
ATOM   327  O O   . ARG   A 1 39  ? 37.42430 6.51828   2.92700   1.000 86.11868  ? 36  ARG   A O   1 
ATOM   328  C CB  . ARG   A 1 39  ? 38.88333 8.69270   4.26941   1.000 90.18710  ? 36  ARG   A CB  1 
ATOM   329  C CG  . ARG   A 1 39  ? 39.02340 10.20608  4.36241   1.000 96.08144  ? 36  ARG   A CG  1 
ATOM   330  C CD  . ARG   A 1 39  ? 40.09835 10.62687  5.35467   1.000 102.88633 ? 36  ARG   A CD  1 
ATOM   331  N NE  . ARG   A 1 39  ? 39.70452 10.38271  6.73741   1.000 112.35881 ? 36  ARG   A NE  1 
ATOM   332  C CZ  . ARG   A 1 39  ? 40.13376 9.36541   7.47179   1.000 111.88222 ? 36  ARG   A CZ  1 
ATOM   333  N NH1 . ARG   A 1 39  ? 40.98420 8.47419   6.98886   1.000 110.60016 ? 36  ARG   A NH1 1 
ATOM   334  N NH2 . ARG   A 1 39  ? 39.70205 9.24138   8.72362   1.000 109.82462 ? 36  ARG   A NH2 1 
ATOM   335  N N   . LEU   A 1 40  ? 39.46484 5.77826   2.30420   1.000 79.63785  ? 37  LEU   A N   1 
ATOM   336  C CA  . LEU   A 1 40  ? 38.97947 4.43330   2.01351   1.000 83.94887  ? 37  LEU   A CA  1 
ATOM   337  C C   . LEU   A 1 40  ? 38.72028 3.62521   3.27880   1.000 84.26928  ? 37  LEU   A C   1 
ATOM   338  O O   . LEU   A 1 40  ? 37.88495 2.71415   3.26406   1.000 81.64036  ? 37  LEU   A O   1 
ATOM   339  C CB  . LEU   A 1 40  ? 39.97474 3.69546   1.11600   1.000 80.18924  ? 37  LEU   A CB  1 
ATOM   340  C CG  . LEU   A 1 40  ? 40.26169 4.31759   -0.25236  1.000 71.77621  ? 37  LEU   A CG  1 
ATOM   341  C CD1 . LEU   A 1 40  ? 41.31523 3.51215   -0.99466  1.000 77.47791  ? 37  LEU   A CD1 1 
ATOM   342  C CD2 . LEU   A 1 40  ? 38.98772 4.42502   -1.07719  1.000 64.61276  ? 37  LEU   A CD2 1 
ATOM   343  N N   . ASP   A 1 41  ? 39.41714 3.93624   4.37438   1.000 85.11393  ? 38  ASP   A N   1 
ATOM   344  C CA  . ASP   A 1 41  ? 39.19418 3.21753   5.62396   1.000 86.76429  ? 38  ASP   A CA  1 
ATOM   345  C C   . ASP   A 1 41  ? 37.79771 3.45481   6.18554   1.000 85.14374  ? 38  ASP   A C   1 
ATOM   346  O O   . ASP   A 1 41  ? 37.31189 2.63670   6.97423   1.000 79.67651  ? 38  ASP   A O   1 
ATOM   347  C CB  . ASP   A 1 41  ? 40.25445 3.61518   6.65305   1.000 94.68114  ? 38  ASP   A CB  1 
ATOM   348  C CG  . ASP   A 1 41  ? 40.61765 5.08596   6.57799   1.000 99.67703  ? 38  ASP   A CG  1 
ATOM   349  O OD1 . ASP   A 1 41  ? 40.73256 5.61590   5.45207   1.000 99.03349  ? 38  ASP   A OD1 1 
ATOM   350  O OD2 . ASP   A 1 41  ? 40.78857 5.71277   7.64426   1.000 103.90943 ? 38  ASP   A OD2 1 
ATOM   351  N N   . THR   A 1 42  ? 37.14042 4.54834   5.79239   1.000 85.06413  ? 39  THR   A N   1 
ATOM   352  C CA  . THR   A 1 42  ? 35.77837 4.81373   6.24181   1.000 90.03904  ? 39  THR   A CA  1 
ATOM   353  C C   . THR   A 1 42  ? 34.74170 4.10589   5.37462   1.000 92.79131  ? 39  THR   A C   1 
ATOM   354  O O   . THR   A 1 42  ? 33.63820 3.81113   5.84809   1.000 101.13619 ? 39  THR   A O   1 
ATOM   355  C CB  . THR   A 1 42  ? 35.51701 6.32344   6.24745   1.000 95.36938  ? 39  THR   A CB  1 
ATOM   356  O OG1 . THR   A 1 42  ? 36.59019 6.99189   6.92206   1.000 101.70542 ? 39  THR   A OG1 1 
ATOM   357  C CG2 . THR   A 1 42  ? 34.21010 6.64858   6.95885   1.000 103.47505 ? 39  THR   A CG2 1 
ATOM   358  N N   . GLU   A 1 43  ? 35.07729 3.80921   4.12152   1.000 83.59042  ? 40  GLU   A N   1 
ATOM   359  C CA  . GLU   A 1 43  ? 34.12513 3.24711   3.16861   1.000 80.16940  ? 40  GLU   A CA  1 
ATOM   360  C C   . GLU   A 1 43  ? 34.09943 1.72879   3.31265   1.000 86.57020  ? 40  GLU   A C   1 
ATOM   361  O O   . GLU   A 1 43  ? 35.08111 1.04966   2.99228   1.000 84.80967  ? 40  GLU   A O   1 
ATOM   362  C CB  . GLU   A 1 43  ? 34.49459 3.65658   1.74617   1.000 78.34851  ? 40  GLU   A CB  1 
ATOM   363  C CG  . GLU   A 1 43  ? 34.75846 5.14379   1.57353   1.000 82.68055  ? 40  GLU   A CG  1 
ATOM   364  C CD  . GLU   A 1 43  ? 33.52174 5.99161   1.80086   1.000 90.87304  ? 40  GLU   A CD  1 
ATOM   365  O OE1 . GLU   A 1 43  ? 32.39887 5.46398   1.65207   1.000 89.82425  ? 40  GLU   A OE1 1 
ATOM   366  O OE2 . GLU   A 1 43  ? 33.67354 7.18761   2.12881   1.000 91.88881  ? 40  GLU   A OE2 1 
ATOM   367  N N   . THR   A 1 44  ? 32.96918 1.19511   3.78542   1.000 76.47458  ? 41  THR   A N   1 
ATOM   368  C CA  . THR   A 1 44  ? 32.83728 -0.25174  3.92609   1.000 87.30322  ? 41  THR   A CA  1 
ATOM   369  C C   . THR   A 1 44  ? 32.73401 -0.94583  2.57381   1.000 92.99565  ? 41  THR   A C   1 
ATOM   370  O O   . THR   A 1 44  ? 33.18231 -2.08918  2.43051   1.000 81.69994  ? 41  THR   A O   1 
ATOM   371  C CB  . THR   A 1 44  ? 31.61534 -0.59455  4.77880   1.000 87.42873  ? 41  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 44  ? 30.44635 0.00886   4.20909   1.000 95.76235  ? 41  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 44  ? 31.79968 -0.09303  6.19738   1.000 98.54829  ? 41  THR   A CG2 1 
ATOM   374  N N   . GLU   A 1 45  ? 32.14861 -0.28151  1.57778   1.000 74.48655  ? 42  GLU   A N   1 
ATOM   375  C CA  . GLU   A 1 45  ? 31.96184 -0.86156  0.25642   1.000 75.98121  ? 42  GLU   A CA  1 
ATOM   376  C C   . GLU   A 1 45  ? 33.09989 -0.52351  -0.70016  1.000 77.76530  ? 42  GLU   A C   1 
ATOM   377  O O   . GLU   A 1 45  ? 32.89915 -0.54603  -1.91981  1.000 73.67692  ? 42  GLU   A O   1 
ATOM   378  C CB  . GLU   A 1 45  ? 30.62499 -0.40464  -0.33275  1.000 76.15356  ? 42  GLU   A CB  1 
ATOM   379  C CG  . GLU   A 1 45  ? 29.43711 -0.61147  0.59474   1.000 92.60291  ? 42  GLU   A CG  1 
ATOM   380  C CD  . GLU   A 1 45  ? 29.21036 -2.07161  0.93911   1.000 100.59751 ? 42  GLU   A CD  1 
ATOM   381  O OE1 . GLU   A 1 45  ? 29.39542 -2.92832  0.04937   1.000 88.71393  ? 42  GLU   A OE1 1 
ATOM   382  O OE2 . GLU   A 1 45  ? 28.85297 -2.36306  2.10118   1.000 96.99107  ? 42  GLU   A OE2 1 
ATOM   383  N N   . GLY   A 1 46  ? 34.28566 -0.21337  -0.17766  1.000 70.41762  ? 43  GLY   A N   1 
ATOM   384  C CA  . GLY   A 1 46  ? 35.39446 0.13384   -1.04505  1.000 78.14562  ? 43  GLY   A CA  1 
ATOM   385  C C   . GLY   A 1 46  ? 35.20965 1.50205   -1.67943  1.000 68.88738  ? 43  GLY   A C   1 
ATOM   386  O O   . GLY   A 1 46  ? 34.58587 2.40424   -1.11371  1.000 71.27215  ? 43  GLY   A O   1 
ATOM   387  N N   . VAL   A 1 47  ? 35.76477 1.65417   -2.87786  1.000 60.01868  ? 44  VAL   A N   1 
ATOM   388  C CA  . VAL   A 1 47  ? 35.63277 2.92745   -3.59400  1.000 63.13389  ? 44  VAL   A CA  1 
ATOM   389  C C   . VAL   A 1 47  ? 34.15705 3.20177   -3.85594  1.000 64.54458  ? 44  VAL   A C   1 
ATOM   390  O O   . VAL   A 1 47  ? 33.44956 2.32360   -4.38832  1.000 58.80928  ? 44  VAL   A O   1 
ATOM   391  C CB  . VAL   A 1 47  ? 36.42817 2.89382   -4.90966  1.000 59.73541  ? 44  VAL   A CB  1 
ATOM   392  C CG1 . VAL   A 1 47  ? 36.41066 4.26107   -5.57353  1.000 59.61623  ? 44  VAL   A CG1 1 
ATOM   393  C CG2 . VAL   A 1 47  ? 37.85333 2.44416   -4.65232  1.000 65.81964  ? 44  VAL   A CG2 1 
ATOM   394  N N   . PRO   A 1 48  ? 33.63831 4.37523   -3.49262  1.000 62.61163  ? 45  PRO   A N   1 
ATOM   395  C CA  . PRO   A 1 48  ? 32.20862 4.64338   -3.68394  1.000 56.07641  ? 45  PRO   A CA  1 
ATOM   396  C C   . PRO   A 1 48  ? 31.81041 4.55920   -5.14905  1.000 61.44384  ? 45  PRO   A C   1 
ATOM   397  O O   . PRO   A 1 48  ? 32.59497 4.86693   -6.04960  1.000 60.40235  ? 45  PRO   A O   1 
ATOM   398  C CB  . PRO   A 1 48  ? 32.03961 6.06769   -3.14150  1.000 58.19152  ? 45  PRO   A CB  1 
ATOM   399  C CG  . PRO   A 1 48  ? 33.18398 6.25125   -2.20114  1.000 69.40099  ? 45  PRO   A CG  1 
ATOM   400  C CD  . PRO   A 1 48  ? 34.32067 5.47646   -2.79361  1.000 64.42266  ? 45  PRO   A CD  1 
ATOM   401  N N   . SER   A 1 49  ? 30.56721 4.12918   -5.37823  1.000 59.25064  ? 46  SER   A N   1 
ATOM   402  C CA  . SER   A 1 49  ? 30.06617 4.01353   -6.74345  1.000 55.37264  ? 46  SER   A CA  1 
ATOM   403  C C   . SER   A 1 49  ? 30.09524 5.35851   -7.45823  1.000 59.22577  ? 46  SER   A C   1 
ATOM   404  O O   . SER   A 1 49  ? 30.37973 5.42389   -8.65955  1.000 60.27581  ? 46  SER   A O   1 
ATOM   405  C CB  . SER   A 1 49  ? 28.65046 3.43757   -6.73547  1.000 58.89539  ? 46  SER   A CB  1 
ATOM   406  O OG  . SER   A 1 49  ? 27.76766 4.27226   -6.00785  1.000 81.87289  ? 46  SER   A OG  1 
ATOM   407  N N   . THR   A 1 50  ? 29.81300 6.44561   -6.73466  1.000 53.24182  ? 47  THR   A N   1 
ATOM   408  C CA  . THR   A 1 50  ? 29.87191 7.76988   -7.34604  1.000 60.73628  ? 47  THR   A CA  1 
ATOM   409  C C   . THR   A 1 50  ? 31.29111 8.13594   -7.76417  1.000 52.35507  ? 47  THR   A C   1 
ATOM   410  O O   . THR   A 1 50  ? 31.47609 8.87577   -8.73690  1.000 58.65181  ? 47  THR   A O   1 
ATOM   411  C CB  . THR   A 1 50  ? 29.31757 8.82657   -6.38830  1.000 61.67064  ? 47  THR   A CB  1 
ATOM   412  O OG1 . THR   A 1 50  ? 30.02758 8.77106   -5.14366  1.000 60.49178  ? 47  THR   A OG1 1 
ATOM   413  C CG2 . THR   A 1 50  ? 27.83326 8.59622   -6.13702  1.000 62.69832  ? 47  THR   A CG2 1 
ATOM   414  N N   . ALA   A 1 51  ? 32.30035 7.63305   -7.05008  1.000 50.98282  ? 48  ALA   A N   1 
ATOM   415  C CA  . ALA   A 1 51  ? 33.68102 7.92174   -7.42020  1.000 50.99552  ? 48  ALA   A CA  1 
ATOM   416  C C   . ALA   A 1 51  ? 34.12131 7.09112   -8.61802  1.000 59.35394  ? 48  ALA   A C   1 
ATOM   417  O O   . ALA   A 1 51  ? 34.79167 7.60631   -9.51978  1.000 51.76092  ? 48  ALA   A O   1 
ATOM   418  C CB  . ALA   A 1 51  ? 34.61007 7.67706   -6.23100  1.000 54.10840  ? 48  ALA   A CB  1 
ATOM   419  N N   . ILE   A 1 52  ? 33.75349 5.80778   -8.64533  1.000 56.78161  ? 49  ILE   A N   1 
ATOM   420  C CA  . ILE   A 1 52  ? 34.10332 4.96141   -9.78249  1.000 59.87747  ? 49  ILE   A CA  1 
ATOM   421  C C   . ILE   A 1 52  ? 33.45420 5.48663   -11.05659 1.000 47.85829  ? 49  ILE   A C   1 
ATOM   422  O O   . ILE   A 1 52  ? 34.08734 5.53398   -12.11839 1.000 55.34876  ? 49  ILE   A O   1 
ATOM   423  C CB  . ILE   A 1 52  ? 33.70830 3.49992   -9.50491  1.000 54.31760  ? 49  ILE   A CB  1 
ATOM   424  C CG1 . ILE   A 1 52  ? 34.26731 3.04779   -8.15646  1.000 59.85210  ? 49  ILE   A CG1 1 
ATOM   425  C CG2 . ILE   A 1 52  ? 34.22331 2.59852   -10.60779 1.000 59.23599  ? 49  ILE   A CG2 1 
ATOM   426  C CD1 . ILE   A 1 52  ? 33.96531 1.60552   -7.81749  1.000 59.06603  ? 49  ILE   A CD1 1 
ATOM   427  N N   . ARG   A 1 53  ? 32.18592 5.89826   -10.97180 1.000 52.22829  ? 50  ARG   A N   1 
ATOM   428  C CA  . ARG   A 1 53  ? 31.51053 6.46602   -12.13566 1.000 55.69937  ? 50  ARG   A CA  1 
ATOM   429  C C   . ARG   A 1 53  ? 32.18839 7.75207   -12.59106 1.000 50.54530  ? 50  ARG   A C   1 
ATOM   430  O O   . ARG   A 1 53  ? 32.50937 7.91143   -13.77339 1.000 54.71073  ? 50  ARG   A O   1 
ATOM   431  C CB  . ARG   A 1 53  ? 30.03721 6.73260   -11.82183 1.000 64.24067  ? 50  ARG   A CB  1 
ATOM   432  C CG  . ARG   A 1 53  ? 29.15401 5.50134   -11.73284 1.000 76.86094  ? 50  ARG   A CG  1 
ATOM   433  C CD  . ARG   A 1 53  ? 27.71281 5.90917   -11.45445 1.000 81.28340  ? 50  ARG   A CD  1 
ATOM   434  N NE  . ARG   A 1 53  ? 26.82303 4.76439   -11.30308 1.000 73.44840  ? 50  ARG   A NE  1 
ATOM   435  C CZ  . ARG   A 1 53  ? 25.51504 4.85557   -11.10129 1.000 78.54562  ? 50  ARG   A CZ  1 
ATOM   436  N NH1 . ARG   A 1 53  ? 24.90824 6.02920   -11.01257 1.000 58.65137  ? 50  ARG   A NH1 1 
ATOM   437  N NH2 . ARG   A 1 53  ? 24.79684 3.74170   -10.98824 1.000 67.74536  ? 50  ARG   A NH2 1 
ATOM   438  N N   . GLU   A 1 54  ? 32.41522 8.68417   -11.66015 1.000 45.80984  ? 51  GLU   A N   1 
ATOM   439  C CA  . GLU   A 1 54  ? 32.94889 9.99047   -12.03624 1.000 54.10609  ? 51  GLU   A CA  1 
ATOM   440  C C   . GLU   A 1 54  ? 34.33295 9.86943   -12.66121 1.000 48.13335  ? 51  GLU   A C   1 
ATOM   441  O O   . GLU   A 1 54  ? 34.63308 10.54384  -13.65255 1.000 53.02966  ? 51  GLU   A O   1 
ATOM   442  C CB  . GLU   A 1 54  ? 32.99223 10.91552  -10.81960 1.000 53.95426  ? 51  GLU   A CB  1 
ATOM   443  C CG  . GLU   A 1 54  ? 33.52648 12.30544  -11.13269 1.000 60.08806  ? 51  GLU   A CG  1 
ATOM   444  C CD  . GLU   A 1 54  ? 33.49797 13.23160  -9.93309  1.000 68.58903  ? 51  GLU   A CD  1 
ATOM   445  O OE1 . GLU   A 1 54  ? 33.37600 12.73089  -8.79495  1.000 76.00089  ? 51  GLU   A OE1 1 
ATOM   446  O OE2 . GLU   A 1 54  ? 33.59498 14.46261  -10.13116 1.000 68.97046  ? 51  GLU   A OE2 1 
ATOM   447  N N   . ILE   A 1 55  ? 35.18786 9.01329   -12.09853 1.000 46.98694  ? 52  ILE   A N   1 
ATOM   448  C CA  . ILE   A 1 55  ? 36.54112 8.85376   -12.62665 1.000 54.11549  ? 52  ILE   A CA  1 
ATOM   449  C C   . ILE   A 1 55  ? 36.49766 8.30470   -14.04724 1.000 52.12956  ? 52  ILE   A C   1 
ATOM   450  O O   . ILE   A 1 55  ? 37.11392 8.85896   -14.96472 1.000 56.15158  ? 52  ILE   A O   1 
ATOM   451  C CB  . ILE   A 1 55  ? 37.37709 7.95222   -11.70074 1.000 57.13203  ? 52  ILE   A CB  1 
ATOM   452  C CG1 . ILE   A 1 55  ? 37.66745 8.66139   -10.37846 1.000 47.37365  ? 52  ILE   A CG1 1 
ATOM   453  C CG2 . ILE   A 1 55  ? 38.67412 7.54767   -12.38099 1.000 59.05537  ? 52  ILE   A CG2 1 
ATOM   454  C CD1 . ILE   A 1 55  ? 38.37692 7.78572   -9.36005  1.000 49.38524  ? 52  ILE   A CD1 1 
ATOM   455  N N   . SER   A 1 56  ? 35.76047 7.20992   -14.25169 1.000 54.09901  ? 53  SER   A N   1 
ATOM   456  C CA  . SER   A 1 56  ? 35.71829 6.58267   -15.56938 1.000 53.07323  ? 53  SER   A CA  1 
ATOM   457  C C   . SER   A 1 56  ? 35.06665 7.49347   -16.60284 1.000 59.00759  ? 53  SER   A C   1 
ATOM   458  O O   . SER   A 1 56  ? 35.50492 7.53947   -17.75746 1.000 57.45048  ? 53  SER   A O   1 
ATOM   459  C CB  . SER   A 1 56  ? 34.97713 5.25063   -15.49226 1.000 60.09324  ? 53  SER   A CB  1 
ATOM   460  O OG  . SER   A 1 56  ? 33.63767 5.45072   -15.07967 1.000 71.72544  ? 53  SER   A OG  1 
ATOM   461  N N   . LEU   A 1 57  ? 34.01750 8.22344   -16.21438 1.000 49.19261  ? 54  LEU   A N   1 
ATOM   462  C CA  . LEU   A 1 57  ? 33.36786 9.11729   -17.16870 1.000 60.27994  ? 54  LEU   A CA  1 
ATOM   463  C C   . LEU   A 1 57  ? 34.27604 10.28393  -17.54116 1.000 55.11100  ? 54  LEU   A C   1 
ATOM   464  O O   . LEU   A 1 57  ? 34.33744 10.67859  -18.71069 1.000 55.56221  ? 54  LEU   A O   1 
ATOM   465  C CB  . LEU   A 1 57  ? 32.04077 9.62864   -16.60444 1.000 48.74895  ? 54  LEU   A CB  1 
ATOM   466  C CG  . LEU   A 1 57  ? 30.91849 8.59999   -16.42788 1.000 55.07326  ? 54  LEU   A CG  1 
ATOM   467  C CD1 . LEU   A 1 57  ? 29.68876 9.23300   -15.78988 1.000 50.00858  ? 54  LEU   A CD1 1 
ATOM   468  C CD2 . LEU   A 1 57  ? 30.55944 7.94612   -17.75291 1.000 54.35663  ? 54  LEU   A CD2 1 
ATOM   469  N N   . LEU   A 1 58  ? 35.00155 10.84036  -16.56685 1.000 55.85426  ? 55  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 58  ? 35.80866 12.02381  -16.84540 1.000 54.15756  ? 55  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 58  ? 37.08335 11.68256  -17.60784 1.000 58.32195  ? 55  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 58  ? 37.61728 12.53672  -18.32466 1.000 65.50926  ? 55  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 58  ? 36.14155 12.75464  -15.54527 1.000 49.49926  ? 55  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 58  ? 34.97450 13.52464  -14.92105 1.000 57.52812  ? 55  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 58  ? 35.43071 14.28483  -13.69038 1.000 49.71631  ? 55  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 58  ? 34.35270 14.46881  -15.94124 1.000 61.36525  ? 55  LEU   A CD2 1 
ATOM   477  N N   . LYS   A 1 59  ? 37.59014 10.45464  -17.47252 1.000 55.54296  ? 56  LYS   A N   1 
ATOM   478  C CA  . LYS   A 1 59  ? 38.76148 10.06339  -18.24814 1.000 63.39431  ? 56  LYS   A CA  1 
ATOM   479  C C   . LYS   A 1 59  ? 38.45172 9.90376   -19.72996 1.000 70.16938  ? 56  LYS   A C   1 
ATOM   480  O O   . LYS   A 1 59  ? 39.38283 9.75345   -20.52793 1.000 72.54180  ? 56  LYS   A O   1 
ATOM   481  C CB  . LYS   A 1 59  ? 39.36016 8.76779   -17.69681 1.000 67.55203  ? 56  LYS   A CB  1 
ATOM   482  C CG  . LYS   A 1 59  ? 40.00612 8.92517   -16.32834 1.000 67.83183  ? 56  LYS   A CG  1 
ATOM   483  C CD  . LYS   A 1 59  ? 40.81386 7.69792   -15.94519 1.000 75.92862  ? 56  LYS   A CD  1 
ATOM   484  C CE  . LYS   A 1 59  ? 42.29891 7.90307   -16.20465 1.000 91.47047  ? 56  LYS   A CE  1 
ATOM   485  N NZ  . LYS   A 1 59  ? 42.87314 8.96871   -15.33587 1.000 77.43805  ? 56  LYS   A NZ  1 
ATOM   486  N N   . GLU   A 1 60  ? 37.17513 9.93530   -20.11292 1.000 63.92856  ? 57  GLU   A N   1 
ATOM   487  C CA  . GLU   A 1 60  ? 36.77147 9.88808   -21.51145 1.000 66.95813  ? 57  GLU   A CA  1 
ATOM   488  C C   . GLU   A 1 60  ? 35.96215 11.11211  -21.92106 1.000 59.51782  ? 57  GLU   A C   1 
ATOM   489  O O   . GLU   A 1 60  ? 35.40690 11.13384  -23.02594 1.000 66.18637  ? 57  GLU   A O   1 
ATOM   490  C CB  . GLU   A 1 60  ? 35.97678 8.60930   -21.79120 1.000 77.62256  ? 57  GLU   A CB  1 
ATOM   491  C CG  . GLU   A 1 60  ? 36.77499 7.33352   -21.56916 1.000 81.66399  ? 57  GLU   A CG  1 
ATOM   492  C CD  . GLU   A 1 60  ? 36.02874 6.09177   -22.01245 1.000 92.18339  ? 57  GLU   A CD  1 
ATOM   493  O OE1 . GLU   A 1 60  ? 34.81772 6.19408   -22.30103 1.000 97.55208  ? 57  GLU   A OE1 1 
ATOM   494  O OE2 . GLU   A 1 60  ? 36.65549 5.01368   -22.07609 1.000 91.70705  ? 57  GLU   A OE2 1 
ATOM   495  N N   . LEU   A 1 61  ? 35.87821 12.12819  -21.06142 1.000 54.04281  ? 58  LEU   A N   1 
ATOM   496  C CA  . LEU   A 1 61  ? 35.18132 13.36502  -21.39276 1.000 59.82056  ? 58  LEU   A CA  1 
ATOM   497  C C   . LEU   A 1 61  ? 36.13889 14.54894  -21.36294 1.000 65.42342  ? 58  LEU   A C   1 
ATOM   498  O O   . LEU   A 1 61  ? 35.96797 15.47055  -20.55838 1.000 68.25888  ? 58  LEU   A O   1 
ATOM   499  C CB  . LEU   A 1 61  ? 34.01899 13.61049  -20.42767 1.000 57.28810  ? 58  LEU   A CB  1 
ATOM   500  C CG  . LEU   A 1 61  ? 32.76118 12.75612  -20.58374 1.000 62.30032  ? 58  LEU   A CG  1 
ATOM   501  C CD1 . LEU   A 1 61  ? 31.76362 13.07916  -19.47795 1.000 47.78947  ? 58  LEU   A CD1 1 
ATOM   502  C CD2 . LEU   A 1 61  ? 32.13941 12.96600  -21.95147 1.000 53.29711  ? 58  LEU   A CD2 1 
ATOM   503  N N   . ASN   A 1 62  ? 37.14734 14.53526  -22.23081 1.000 59.67321  ? 59  ASN   A N   1 
ATOM   504  C CA  . ASN   A 1 62  ? 38.10621 15.63187  -22.30726 1.000 64.50041  ? 59  ASN   A CA  1 
ATOM   505  C C   . ASN   A 1 62  ? 37.53013 16.71601  -23.20941 1.000 56.63111  ? 59  ASN   A C   1 
ATOM   506  O O   . ASN   A 1 62  ? 37.39654 16.52046  -24.42179 1.000 60.32559  ? 59  ASN   A O   1 
ATOM   507  C CB  . ASN   A 1 62  ? 39.45207 15.13316  -22.82562 1.000 65.39318  ? 59  ASN   A CB  1 
ATOM   508  C CG  . ASN   A 1 62  ? 40.59509 16.06641  -22.47298 1.000 82.64987  ? 59  ASN   A CG  1 
ATOM   509  O OD1 . ASN   A 1 62  ? 41.50416 15.69733  -21.72955 1.000 92.68221  ? 59  ASN   A OD1 1 
ATOM   510  N ND2 . ASN   A 1 62  ? 40.55633 17.28186  -23.00725 1.000 84.90139  ? 59  ASN   A ND2 1 
ATOM   511  N N   . HIS   A 1 63  ? 37.18605 17.85794  -22.62018 1.000 55.48552  ? 60  HIS   A N   1 
ATOM   512  C CA  . HIS   A 1 63  ? 36.57076 18.95835  -23.34570 1.000 55.49529  ? 60  HIS   A CA  1 
ATOM   513  C C   . HIS   A 1 63  ? 36.94115 20.25983  -22.65302 1.000 52.75157  ? 60  HIS   A C   1 
ATOM   514  O O   . HIS   A 1 63  ? 37.09042 20.28302  -21.42553 1.000 53.48534  ? 60  HIS   A O   1 
ATOM   515  C CB  . HIS   A 1 63  ? 35.04336 18.80130  -23.41052 1.000 48.98822  ? 60  HIS   A CB  1 
ATOM   516  C CG  . HIS   A 1 63  ? 34.37905 19.75409  -24.35220 1.000 47.65499  ? 60  HIS   A CG  1 
ATOM   517  N ND1 . HIS   A 1 63  ? 33.88046 20.97343  -23.94781 1.000 52.00855  ? 60  HIS   A ND1 1 
ATOM   518  C CD2 . HIS   A 1 63  ? 34.14522 19.67432  -25.68380 1.000 51.31850  ? 60  HIS   A CD2 1 
ATOM   519  C CE1 . HIS   A 1 63  ? 33.36179 21.60107  -24.98851 1.000 55.94147  ? 60  HIS   A CE1 1 
ATOM   520  N NE2 . HIS   A 1 63  ? 33.50844 20.83386  -26.05377 1.000 48.98725  ? 60  HIS   A NE2 1 
ATOM   521  N N   . PRO   A 1 64  ? 37.11091 21.35131  -23.40503 1.000 51.69570  ? 61  PRO   A N   1 
ATOM   522  C CA  . PRO   A 1 64  ? 37.49039 22.62608  -22.77245 1.000 48.80760  ? 61  PRO   A CA  1 
ATOM   523  C C   . PRO   A 1 64  ? 36.45536 23.17160  -21.80242 1.000 58.04373  ? 61  PRO   A C   1 
ATOM   524  O O   . PRO   A 1 64  ? 36.81088 23.98393  -20.94110 1.000 56.01521  ? 61  PRO   A O   1 
ATOM   525  C CB  . PRO   A 1 64  ? 37.68107 23.56808  -23.96896 1.000 53.68006  ? 61  PRO   A CB  1 
ATOM   526  C CG  . PRO   A 1 64  ? 37.98468 22.66496  -25.11393 1.000 59.18296  ? 61  PRO   A CG  1 
ATOM   527  C CD  . PRO   A 1 64  ? 37.17222 21.42654  -24.87389 1.000 51.60055  ? 61  PRO   A CD  1 
ATOM   528  N N   . ASN   A 1 65  ? 35.19088 22.76502  -21.90720 1.000 55.76252  ? 62  ASN   A N   1 
ATOM   529  C CA  . ASN   A 1 65  ? 34.15286 23.24047  -21.00286 1.000 48.89790  ? 62  ASN   A CA  1 
ATOM   530  C C   . ASN   A 1 65  ? 33.75683 22.19143  -19.96876 1.000 49.30609  ? 62  ASN   A C   1 
ATOM   531  O O   . ASN   A 1 65  ? 32.65108 22.25129  -19.42111 1.000 52.70804  ? 62  ASN   A O   1 
ATOM   532  C CB  . ASN   A 1 65  ? 32.93505 23.70551  -21.80095 1.000 47.71021  ? 62  ASN   A CB  1 
ATOM   533  C CG  . ASN   A 1 65  ? 33.26441 24.85108  -22.74379 1.000 54.63300  ? 62  ASN   A CG  1 
ATOM   534  O OD1 . ASN   A 1 65  ? 33.22138 24.69682  -23.96205 1.000 59.55527  ? 62  ASN   A OD1 1 
ATOM   535  N ND2 . ASN   A 1 65  ? 33.60387 26.00632  -22.18009 1.000 51.14673  ? 62  ASN   A ND2 1 
ATOM   536  N N   . ILE   A 1 66  ? 34.64089 21.23660  -19.68982 1.000 50.68929  ? 63  ILE   A N   1 
ATOM   537  C CA  . ILE   A 1 66  ? 34.44180 20.23631  -18.64798 1.000 48.22156  ? 63  ILE   A CA  1 
ATOM   538  C C   . ILE   A 1 66  ? 35.68230 20.23357  -17.76606 1.000 47.91252  ? 63  ILE   A C   1 
ATOM   539  O O   . ILE   A 1 66  ? 36.80591 20.14958  -18.27497 1.000 55.47555  ? 63  ILE   A O   1 
ATOM   540  C CB  . ILE   A 1 66  ? 34.19244 18.83425  -19.23804 1.000 50.47410  ? 63  ILE   A CB  1 
ATOM   541  C CG1 . ILE   A 1 66  ? 32.96439 18.84397  -20.15122 1.000 48.70503  ? 63  ILE   A CG1 1 
ATOM   542  C CG2 . ILE   A 1 66  ? 34.02906 17.80863  -18.13117 1.000 47.52547  ? 63  ILE   A CG2 1 
ATOM   543  C CD1 . ILE   A 1 66  ? 32.64516 17.49530  -20.75622 1.000 59.29681  ? 63  ILE   A CD1 1 
ATOM   544  N N   . VAL   A 1 67  ? 35.48234 20.33745  -16.45068 1.000 47.62618  ? 64  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 67  ? 36.61273 20.37542  -15.52603 1.000 52.56802  ? 64  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 67  ? 37.38438 19.06879  -15.63230 1.000 51.36732  ? 64  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 67  ? 36.83145 17.98328  -15.41737 1.000 60.49619  ? 64  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 67  ? 36.13675 20.63410  -14.09353 1.000 51.49487  ? 64  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 67  ? 37.31962 20.61784  -13.13571 1.000 53.10097  ? 64  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 67  ? 35.40923 21.96501  -14.01160 1.000 51.59706  ? 64  VAL   A CG2 1 
ATOM   551  N N   . LYS   A 1 68  ? 38.67017 19.16918  -15.95889 1.000 46.74536  ? 65  LYS   A N   1 
ATOM   552  C CA  . LYS   A 1 68  ? 39.47648 17.99534  -16.26173 1.000 59.56550  ? 65  LYS   A CA  1 
ATOM   553  C C   . LYS   A 1 68  ? 39.85265 17.22692  -15.00307 1.000 52.83459  ? 65  LYS   A C   1 
ATOM   554  O O   . LYS   A 1 68  ? 40.16779 17.81494  -13.96448 1.000 58.89259  ? 65  LYS   A O   1 
ATOM   555  C CB  . LYS   A 1 68  ? 40.75318 18.39752  -17.00207 1.000 62.33007  ? 65  LYS   A CB  1 
ATOM   556  C CG  . LYS   A 1 68  ? 40.56438 18.73258  -18.46631 1.000 70.08243  ? 65  LYS   A CG  1 
ATOM   557  C CD  . LYS   A 1 68  ? 41.90762 18.80122  -19.17208 1.000 68.92053  ? 65  LYS   A CD  1 
ATOM   558  C CE  . LYS   A 1 68  ? 42.68232 17.50195  -18.99477 1.000 80.58547  ? 65  LYS   A CE  1 
ATOM   559  N NZ  . LYS   A 1 68  ? 44.02273 17.54718  -19.64579 1.000 99.17572  ? 65  LYS   A NZ  1 
ATOM   560  N N   . LEU   A 1 69  ? 39.83022 15.90085  -15.11110 1.000 58.36040  ? 66  LEU   A N   1 
ATOM   561  C CA  . LEU   A 1 69  ? 40.42472 15.02071  -14.11105 1.000 56.55133  ? 66  LEU   A CA  1 
ATOM   562  C C   . LEU   A 1 69  ? 41.86515 14.75130  -14.53081 1.000 62.79373  ? 66  LEU   A C   1 
ATOM   563  O O   . LEU   A 1 69  ? 42.10953 14.11709  -15.56202 1.000 66.12951  ? 66  LEU   A O   1 
ATOM   564  C CB  . LEU   A 1 69  ? 39.63251 13.72243  -13.98739 1.000 54.14774  ? 66  LEU   A CB  1 
ATOM   565  C CG  . LEU   A 1 69  ? 40.24382 12.63710  -13.09910 1.000 63.26927  ? 66  LEU   A CG  1 
ATOM   566  C CD1 . LEU   A 1 69  ? 40.40804 13.13907  -11.67361 1.000 55.87658  ? 66  LEU   A CD1 1 
ATOM   567  C CD2 . LEU   A 1 69  ? 39.39536 11.37339  -13.13304 1.000 58.50652  ? 66  LEU   A CD2 1 
ATOM   568  N N   . LEU   A 1 70  ? 42.81903 15.23906  -13.73934 1.000 61.19278  ? 67  LEU   A N   1 
ATOM   569  C CA  . LEU   A 1 70  ? 44.22501 15.14679  -14.11223 1.000 63.22239  ? 67  LEU   A CA  1 
ATOM   570  C C   . LEU   A 1 70  ? 44.85664 13.81710  -13.71729 1.000 64.09219  ? 67  LEU   A C   1 
ATOM   571  O O   . LEU   A 1 70  ? 45.58148 13.21980  -14.51923 1.000 78.26060  ? 67  LEU   A O   1 
ATOM   572  C CB  . LEU   A 1 70  ? 45.00881 16.30202  -13.48520 1.000 67.95629  ? 67  LEU   A CB  1 
ATOM   573  C CG  . LEU   A 1 70  ? 44.52299 17.70130  -13.86787 1.000 65.06193  ? 67  LEU   A CG  1 
ATOM   574  C CD1 . LEU   A 1 70  ? 45.33706 18.77156  -13.15822 1.000 64.88521  ? 67  LEU   A CD1 1 
ATOM   575  C CD2 . LEU   A 1 70  ? 44.57713 17.89097  -15.37553 1.000 67.88557  ? 67  LEU   A CD2 1 
ATOM   576  N N   . ASP   A 1 71  ? 44.60044 13.33515  -12.50338 1.000 64.37764  ? 68  ASP   A N   1 
ATOM   577  C CA  . ASP   A 1 71  ? 45.24553 12.11648  -12.03436 1.000 65.20770  ? 68  ASP   A CA  1 
ATOM   578  C C   . ASP   A 1 71  ? 44.39001 11.48076  -10.94727 1.000 67.76641  ? 68  ASP   A C   1 
ATOM   579  O O   . ASP   A 1 71  ? 43.57062 12.14388  -10.30498 1.000 62.45388  ? 68  ASP   A O   1 
ATOM   580  C CB  . ASP   A 1 71  ? 46.66065 12.40465  -11.51403 1.000 75.66050  ? 68  ASP   A CB  1 
ATOM   581  C CG  . ASP   A 1 71  ? 47.50389 11.14906  -11.37275 1.000 84.61484  ? 68  ASP   A CG  1 
ATOM   582  O OD1 . ASP   A 1 71  ? 47.04579 10.06607  -11.79473 1.000 91.86433  ? 68  ASP   A OD1 1 
ATOM   583  O OD2 . ASP   A 1 71  ? 48.62895 11.24783  -10.83844 1.000 88.70887  ? 68  ASP   A OD2 1 
ATOM   584  N N   . VAL   A 1 72  ? 44.58858 10.17770  -10.76009 1.000 69.64618  ? 69  VAL   A N   1 
ATOM   585  C CA  . VAL   A 1 72  ? 43.95929 9.41037   -9.68980  1.000 66.26853  ? 69  VAL   A CA  1 
ATOM   586  C C   . VAL   A 1 72  ? 45.08026 8.69994   -8.94513  1.000 68.82603  ? 69  VAL   A C   1 
ATOM   587  O O   . VAL   A 1 72  ? 45.72690 7.80320   -9.50030  1.000 77.48027  ? 69  VAL   A O   1 
ATOM   588  C CB  . VAL   A 1 72  ? 42.92671 8.40347   -10.21623 1.000 68.59126  ? 69  VAL   A CB  1 
ATOM   589  C CG1 . VAL   A 1 72  ? 42.34553 7.59258   -9.06889  1.000 55.74735  ? 69  VAL   A CG1 1 
ATOM   590  C CG2 . VAL   A 1 72  ? 41.82233 9.12047   -10.98076 1.000 59.67366  ? 69  VAL   A CG2 1 
ATOM   591  N N   . ILE   A 1 73  ? 45.31609 9.09683   -7.69717  1.000 73.78044  ? 70  ILE   A N   1 
ATOM   592  C CA  . ILE   A 1 73  ? 46.44601 8.61330   -6.91360  1.000 72.50725  ? 70  ILE   A CA  1 
ATOM   593  C C   . ILE   A 1 73  ? 45.91900 7.85508   -5.70399  1.000 66.07955  ? 70  ILE   A C   1 
ATOM   594  O O   . ILE   A 1 73  ? 45.12565 8.39316   -4.92318  1.000 71.39577  ? 70  ILE   A O   1 
ATOM   595  C CB  . ILE   A 1 73  ? 47.36577 9.76842   -6.47736  1.000 81.14934  ? 70  ILE   A CB  1 
ATOM   596  C CG1 . ILE   A 1 73  ? 47.81018 10.57808  -7.69737  1.000 67.20334  ? 70  ILE   A CG1 1 
ATOM   597  C CG2 . ILE   A 1 73  ? 48.57226 9.23353   -5.71961  1.000 65.05034  ? 70  ILE   A CG2 1 
ATOM   598  C CD1 . ILE   A 1 73  ? 48.65037 11.78627  -7.35789  1.000 72.96436  ? 70  ILE   A CD1 1 
ATOM   599  N N   . HIS   A 1 74  ? 46.36210 6.60914   -5.55413  1.000 68.27976  ? 71  HIS   A N   1 
ATOM   600  C CA  . HIS   A 1 74  ? 46.05159 5.77368   -4.39845  1.000 79.80199  ? 71  HIS   A CA  1 
ATOM   601  C C   . HIS   A 1 74  ? 47.33459 5.61247   -3.59205  1.000 89.23046  ? 71  HIS   A C   1 
ATOM   602  O O   . HIS   A 1 74  ? 48.27435 4.94658   -4.03943  1.000 93.23293  ? 71  HIS   A O   1 
ATOM   603  C CB  . HIS   A 1 74  ? 45.49434 4.42179   -4.83880  1.000 68.97540  ? 71  HIS   A CB  1 
ATOM   604  C CG  . HIS   A 1 74  ? 45.32409 3.44178   -3.72090  1.000 70.25460  ? 71  HIS   A CG  1 
ATOM   605  N ND1 . HIS   A 1 74  ? 44.70816 3.76709   -2.53173  1.000 87.28347  ? 71  HIS   A ND1 1 
ATOM   606  C CD2 . HIS   A 1 74  ? 45.68406 2.14096   -3.61447  1.000 76.48661  ? 71  HIS   A CD2 1 
ATOM   607  C CE1 . HIS   A 1 74  ? 44.69924 2.71011   -1.73926  1.000 88.82408  ? 71  HIS   A CE1 1 
ATOM   608  N NE2 . HIS   A 1 74  ? 45.28462 1.70987   -2.37275  1.000 86.61005  ? 71  HIS   A NE2 1 
ATOM   609  N N   . THR   A 1 75  ? 47.37480 6.22023   -2.40656  1.000 82.86703  ? 72  THR   A N   1 
ATOM   610  C CA  . THR   A 1 75  ? 48.60407 6.31794   -1.62943  1.000 102.84095 ? 72  THR   A CA  1 
ATOM   611  C C   . THR   A 1 75  ? 48.58243 5.45931   -0.36973  1.000 113.59118 ? 72  THR   A C   1 
ATOM   612  O O   . THR   A 1 75  ? 49.36539 4.51139   -0.25936  1.000 127.42095 ? 72  THR   A O   1 
ATOM   613  C CB  . THR   A 1 75  ? 48.88175 7.79067   -1.28084  1.000 98.83384  ? 72  THR   A CB  1 
ATOM   614  O OG1 . THR   A 1 75  ? 49.81407 7.86602   -0.19508  1.000 128.27698 ? 72  THR   A OG1 1 
ATOM   615  C CG2 . THR   A 1 75  ? 47.59404 8.52087   -0.91245  1.000 93.44197  ? 72  THR   A CG2 1 
ATOM   616  N N   . GLU   A 1 76  ? 47.70277 5.76081   0.59533   1.000 103.47038 ? 73  GLU   A N   1 
ATOM   617  C CA  . GLU   A 1 76  ? 47.73683 5.09506   1.90174   1.000 108.67233 ? 73  GLU   A CA  1 
ATOM   618  C C   . GLU   A 1 76  ? 46.30529 5.04025   2.44355   1.000 100.38632 ? 73  GLU   A C   1 
ATOM   619  O O   . GLU   A 1 76  ? 45.87300 5.88349   3.23437   1.000 102.43121 ? 73  GLU   A O   1 
ATOM   620  C CB  . GLU   A 1 76  ? 48.67308 5.81082   2.87464   1.000 115.09260 ? 73  GLU   A CB  1 
ATOM   621  C CG  . GLU   A 1 76  ? 48.63954 7.32826   2.75124   1.000 113.41491 ? 73  GLU   A CG  1 
ATOM   622  C CD  . GLU   A 1 76  ? 49.08487 8.03163   4.01604   1.000 126.43889 ? 73  GLU   A CD  1 
ATOM   623  O OE1 . GLU   A 1 76  ? 48.73900 7.55292   5.11653   1.000 132.52372 ? 73  GLU   A OE1 1 
ATOM   624  O OE2 . GLU   A 1 76  ? 49.78135 9.06292   3.90978   1.000 133.81981 ? 73  GLU   A OE2 1 
ATOM   625  N N   . ASN   A 1 77  ? 45.56536 4.01910   2.00861   1.000 93.50246  ? 74  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 77  ? 44.15048 3.85596   2.34813   1.000 96.86967  ? 74  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 77  ? 43.33977 5.10074   1.99871   1.000 87.41173  ? 74  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 77  ? 42.28039 5.34937   2.58299   1.000 79.68833  ? 74  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 77  ? 43.96771 3.49441   3.82648   1.000 96.82064  ? 74  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 77  ? 44.79484 2.29237   4.23802   1.000 114.55949 ? 74  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 77  ? 44.45966 1.15255   3.91376   1.000 115.69773 ? 74  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 77  ? 45.88140 2.54139   4.96112   1.000 120.48357 ? 74  ASN   A ND2 1 
ATOM   633  N N   . LYS   A 1 78  ? 43.83725 5.89426   1.05262   1.000 84.00107  ? 75  LYS   A N   1 
ATOM   634  C CA  . LYS   A 1 78  ? 43.16976 7.10366   0.60281   1.000 83.63163  ? 75  LYS   A CA  1 
ATOM   635  C C   . LYS   A 1 78  ? 43.25986 7.18174   -0.91292  1.000 84.55334  ? 75  LYS   A C   1 
ATOM   636  O O   . LYS   A 1 78  ? 44.21673 6.69448   -1.52213  1.000 71.20626  ? 75  LYS   A O   1 
ATOM   637  C CB  . LYS   A 1 78  ? 43.78248 8.36261   1.23205   1.000 87.37791  ? 75  LYS   A CB  1 
ATOM   638  C CG  . LYS   A 1 78  ? 43.62441 8.44575   2.74093   1.000 91.69878  ? 75  LYS   A CG  1 
ATOM   639  C CD  . LYS   A 1 78  ? 44.34318 9.65930   3.30088   1.000 104.41223 ? 75  LYS   A CD  1 
ATOM   640  C CE  . LYS   A 1 78  ? 45.81613 9.64472   2.92570   1.000 104.57064 ? 75  LYS   A CE  1 
ATOM   641  N NZ  . LYS   A 1 78  ? 46.53672 10.84328  3.43554   1.000 101.09304 ? 75  LYS   A NZ  1 
ATOM   642  N N   . LEU   A 1 79  ? 42.24839 7.79801   -1.51553  1.000 72.18555  ? 76  LEU   A N   1 
ATOM   643  C CA  . LEU   A 1 79  ? 42.17123 7.96779   -2.96133  1.000 72.72732  ? 76  LEU   A CA  1 
ATOM   644  C C   . LEU   A 1 79  ? 42.10580 9.46065   -3.25156  1.000 72.14026  ? 76  LEU   A C   1 
ATOM   645  O O   . LEU   A 1 79  ? 41.13722 10.12903  -2.87413  1.000 68.23701  ? 76  LEU   A O   1 
ATOM   646  C CB  . LEU   A 1 79  ? 40.95788 7.23589   -3.53261  1.000 65.47497  ? 76  LEU   A CB  1 
ATOM   647  C CG  . LEU   A 1 79  ? 40.95146 6.97701   -5.03752  1.000 66.02339  ? 76  LEU   A CG  1 
ATOM   648  C CD1 . LEU   A 1 79  ? 42.12114 6.08340   -5.42666  1.000 63.51831  ? 76  LEU   A CD1 1 
ATOM   649  C CD2 . LEU   A 1 79  ? 39.62635 6.35836   -5.46319  1.000 54.81499  ? 76  LEU   A CD2 1 
ATOM   650  N N   . TYR   A 1 80  ? 43.13681 9.98300   -3.90711  1.000 63.84326  ? 77  TYR   A N   1 
ATOM   651  C CA  . TYR   A 1 80  ? 43.20654 11.39355  -4.26090  1.000 67.92042  ? 77  TYR   A CA  1 
ATOM   652  C C   . TYR   A 1 80  ? 42.84622 11.57220  -5.72934  1.000 70.84055  ? 77  TYR   A C   1 
ATOM   653  O O   . TYR   A 1 80  ? 43.41669 10.90643  -6.60010  1.000 69.36309  ? 77  TYR   A O   1 
ATOM   654  C CB  . TYR   A 1 80  ? 44.60032 11.96054  -3.98507  1.000 74.46908  ? 77  TYR   A CB  1 
ATOM   655  C CG  . TYR   A 1 80  ? 44.87556 12.24152  -2.52356  1.000 77.05040  ? 77  TYR   A CG  1 
ATOM   656  C CD1 . TYR   A 1 80  ? 44.36081 13.37413  -1.90753  1.000 75.99710  ? 77  TYR   A CD1 1 
ATOM   657  C CD2 . TYR   A 1 80  ? 45.65805 11.38172  -1.76356  1.000 86.95466  ? 77  TYR   A CD2 1 
ATOM   658  C CE1 . TYR   A 1 80  ? 44.60995 13.64012  -0.57444  1.000 83.36839  ? 77  TYR   A CE1 1 
ATOM   659  C CE2 . TYR   A 1 80  ? 45.91360 11.63945  -0.42840  1.000 85.82740  ? 77  TYR   A CE2 1 
ATOM   660  C CZ  . TYR   A 1 80  ? 45.38671 12.77020  0.16034   1.000 90.87145  ? 77  TYR   A CZ  1 
ATOM   661  O OH  . TYR   A 1 80  ? 45.63672 13.03368  1.48803   1.000 103.14156 ? 77  TYR   A OH  1 
ATOM   662  N N   . LEU   A 1 81  ? 41.89915 12.46705  -5.99766  1.000 64.61760  ? 78  LEU   A N   1 
ATOM   663  C CA  . LEU   A 1 81  ? 41.47440 12.79869  -7.35421  1.000 61.50337  ? 78  LEU   A CA  1 
ATOM   664  C C   . LEU   A 1 81  ? 41.94541 14.21604  -7.65589  1.000 62.82750  ? 78  LEU   A C   1 
ATOM   665  O O   . LEU   A 1 81  ? 41.46571 15.17746  -7.04637  1.000 60.36048  ? 78  LEU   A O   1 
ATOM   666  C CB  . LEU   A 1 81  ? 39.95893 12.67790  -7.50731  1.000 62.15785  ? 78  LEU   A CB  1 
ATOM   667  C CG  . LEU   A 1 81  ? 39.32932 11.29701  -7.71714  1.000 64.59756  ? 78  LEU   A CG  1 
ATOM   668  C CD1 . LEU   A 1 81  ? 39.50470 10.39948  -6.50067  1.000 56.89151  ? 78  LEU   A CD1 1 
ATOM   669  C CD2 . LEU   A 1 81  ? 37.85407 11.44628  -8.06582  1.000 57.29147  ? 78  LEU   A CD2 1 
ATOM   670  N N   . VAL   A 1 82  ? 42.88186 14.34396  -8.58948  1.000 54.73167  ? 79  VAL   A N   1 
ATOM   671  C CA  . VAL   A 1 82  ? 43.47132 15.63425  -8.92855  1.000 56.45885  ? 79  VAL   A CA  1 
ATOM   672  C C   . VAL   A 1 82  ? 42.67800 16.24685  -10.07620 1.000 61.68826  ? 79  VAL   A C   1 
ATOM   673  O O   . VAL   A 1 82  ? 42.65731 15.70631  -11.18766 1.000 58.75240  ? 79  VAL   A O   1 
ATOM   674  C CB  . VAL   A 1 82  ? 44.95492 15.48651  -9.29760  1.000 63.40083  ? 79  VAL   A CB  1 
ATOM   675  C CG1 . VAL   A 1 82  ? 45.57963 16.85099  -9.54951  1.000 60.90110  ? 79  VAL   A CG1 1 
ATOM   676  C CG2 . VAL   A 1 82  ? 45.70190 14.74388  -8.20015  1.000 57.32748  ? 79  VAL   A CG2 1 
ATOM   677  N N   . PHE   A 1 83  ? 42.02503 17.37327  -9.80816  1.000 52.87011  ? 80  PHE   A N   1 
ATOM   678  C CA  . PHE   A 1 83  ? 41.24028 18.08962  -10.80140 1.000 58.23587  ? 80  PHE   A CA  1 
ATOM   679  C C   . PHE   A 1 83  ? 41.92592 19.39421  -11.18756 1.000 59.63446  ? 80  PHE   A C   1 
ATOM   680  O O   . PHE   A 1 83  ? 42.80675 19.89718  -10.48415 1.000 58.25872  ? 80  PHE   A O   1 
ATOM   681  C CB  . PHE   A 1 83  ? 39.83274 18.40610  -10.28222 1.000 55.66041  ? 80  PHE   A CB  1 
ATOM   682  C CG  . PHE   A 1 83  ? 38.95916 17.20158  -10.08407 1.000 53.56004  ? 80  PHE   A CG  1 
ATOM   683  C CD1 . PHE   A 1 83  ? 38.95778 16.52104  -8.87707  1.000 53.14646  ? 80  PHE   A CD1 1 
ATOM   684  C CD2 . PHE   A 1 83  ? 38.11604 16.76813  -11.09359 1.000 50.34198  ? 80  PHE   A CD2 1 
ATOM   685  C CE1 . PHE   A 1 83  ? 38.14410 15.42081  -8.68671  1.000 60.42756  ? 80  PHE   A CE1 1 
ATOM   686  C CE2 . PHE   A 1 83  ? 37.29904 15.66624  -10.90962 1.000 53.31388  ? 80  PHE   A CE2 1 
ATOM   687  C CZ  . PHE   A 1 83  ? 37.31305 14.99242  -9.70521  1.000 48.76069  ? 80  PHE   A CZ  1 
ATOM   688  N N   . GLU   A 1 84  ? 41.49662 19.94190  -12.32071 1.000 56.04335  ? 81  GLU   A N   1 
ATOM   689  C CA  . GLU   A 1 84  ? 41.89082 21.28909  -12.70481 1.000 55.14875  ? 81  GLU   A CA  1 
ATOM   690  C C   . GLU   A 1 84  ? 41.19161 22.30590  -11.80629 1.000 56.56980  ? 81  GLU   A C   1 
ATOM   691  O O   . GLU   A 1 84  ? 40.05318 22.09840  -11.37674 1.000 56.73322  ? 81  GLU   A O   1 
ATOM   692  C CB  . GLU   A 1 84  ? 41.55481 21.52474  -14.18006 1.000 56.98254  ? 81  GLU   A CB  1 
ATOM   693  C CG  . GLU   A 1 84  ? 40.85226 22.83264  -14.49315 1.000 66.64852  ? 81  GLU   A CG  1 
ATOM   694  C CD  . GLU   A 1 84  ? 40.30532 22.87320  -15.90894 1.000 69.95447  ? 81  GLU   A CD  1 
ATOM   695  O OE1 . GLU   A 1 84  ? 39.84206 21.82196  -16.40329 1.000 64.50234  ? 81  GLU   A OE1 1 
ATOM   696  O OE2 . GLU   A 1 84  ? 40.34294 23.95579  -16.53001 1.000 70.05340  ? 81  GLU   A OE2 1 
ATOM   697  N N   . PHE   A 1 85  ? 41.88363 23.40144  -11.50147 1.000 56.55282  ? 82  PHE   A N   1 
ATOM   698  C CA  . PHE   A 1 85  ? 41.39937 24.37959  -10.53373 1.000 53.39668  ? 82  PHE   A CA  1 
ATOM   699  C C   . PHE   A 1 85  ? 40.75934 25.57296  -11.23352 1.000 51.82740  ? 82  PHE   A C   1 
ATOM   700  O O   . PHE   A 1 85  ? 41.33781 26.13934  -12.16758 1.000 57.90477  ? 82  PHE   A O   1 
ATOM   701  C CB  . PHE   A 1 85  ? 42.53321 24.86037  -9.62638  1.000 54.41179  ? 82  PHE   A CB  1 
ATOM   702  C CG  . PHE   A 1 85  ? 42.11592 25.92935  -8.65416  1.000 58.74620  ? 82  PHE   A CG  1 
ATOM   703  C CD1 . PHE   A 1 85  ? 41.41892 25.60266  -7.50201  1.000 52.94816  ? 82  PHE   A CD1 1 
ATOM   704  C CD2 . PHE   A 1 85  ? 42.41721 27.26072  -8.89421  1.000 60.57123  ? 82  PHE   A CD2 1 
ATOM   705  C CE1 . PHE   A 1 85  ? 41.02983 26.58279  -6.60683  1.000 58.39955  ? 82  PHE   A CE1 1 
ATOM   706  C CE2 . PHE   A 1 85  ? 42.03161 28.24538  -8.00123  1.000 59.86975  ? 82  PHE   A CE2 1 
ATOM   707  C CZ  . PHE   A 1 85  ? 41.33715 27.90506  -6.85690  1.000 52.03527  ? 82  PHE   A CZ  1 
ATOM   708  N N   . LEU   A 1 86  ? 39.56867 25.95157  -10.76896 1.000 56.66566  ? 83  LEU   A N   1 
ATOM   709  C CA  . LEU   A 1 86  ? 38.90498 27.18911  -11.15457 1.000 48.35445  ? 83  LEU   A CA  1 
ATOM   710  C C   . LEU   A 1 86  ? 38.53210 27.94118  -9.88477  1.000 52.46999  ? 83  LEU   A C   1 
ATOM   711  O O   . LEU   A 1 86  ? 38.12855 27.33090  -8.89028  1.000 48.11660  ? 83  LEU   A O   1 
ATOM   712  C CB  . LEU   A 1 86  ? 37.65803 26.92950  -12.01435 1.000 55.39901  ? 83  LEU   A CB  1 
ATOM   713  C CG  . LEU   A 1 86  ? 37.88021 26.34373  -13.41396 1.000 62.35609  ? 83  LEU   A CG  1 
ATOM   714  C CD1 . LEU   A 1 86  ? 37.95846 24.82272  -13.37687 1.000 55.23193  ? 83  LEU   A CD1 1 
ATOM   715  C CD2 . LEU   A 1 86  ? 36.79287 26.80382  -14.37296 1.000 52.76519  ? 83  LEU   A CD2 1 
ATOM   716  N N   . HIS   A 1 87  ? 38.66035 29.26734  -9.92158  1.000 49.89295  ? 84  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 87  ? 38.67321 30.04687  -8.68908  1.000 61.31459  ? 84  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 87  ? 37.28786 30.35411  -8.13228  1.000 57.37678  ? 84  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 87  ? 37.19290 30.77810  -6.97518  1.000 66.36471  ? 84  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 87  ? 39.43264 31.35995  -8.90614  1.000 54.69599  ? 84  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 87  ? 38.60817 32.44035  -9.53315  1.000 61.41729  ? 84  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 87  ? 38.07372 32.33077  -10.79881 1.000 69.14812  ? 84  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 87  ? 38.23324 33.65669  -9.07091  1.000 71.68972  ? 84  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 87  ? 37.40128 33.43083  -11.08771 1.000 66.74387  ? 84  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 87  ? 37.48297 34.25174  -10.05606 1.000 70.67101  ? 84  HIS   A NE2 1 
ATOM   726  N N   . GLN   A 1 88  ? 36.21817 30.14973  -8.89787  1.000 60.13375  ? 85  GLN   A N   1 
ATOM   727  C CA  . GLN   A 1 88  ? 34.90767 30.57993  -8.43109  1.000 54.49928  ? 85  GLN   A CA  1 
ATOM   728  C C   . GLN   A 1 88  ? 33.82037 29.78510  -9.13915  1.000 61.40811  ? 85  GLN   A C   1 
ATOM   729  O O   . GLN   A 1 88  ? 33.95414 29.43428  -10.31465 1.000 51.36748  ? 85  GLN   A O   1 
ATOM   730  C CB  . GLN   A 1 88  ? 34.71184 32.08302  -8.66642  1.000 61.71648  ? 85  GLN   A CB  1 
ATOM   731  C CG  . GLN   A 1 88  ? 33.41302 32.65042  -8.12185  1.000 63.24230  ? 85  GLN   A CG  1 
ATOM   732  C CD  . GLN   A 1 88  ? 33.33847 34.15858  -8.25763  1.000 65.44471  ? 85  GLN   A CD  1 
ATOM   733  O OE1 . GLN   A 1 88  ? 32.79376 34.84590  -7.39431  1.000 82.70295  ? 85  GLN   A OE1 1 
ATOM   734  N NE2 . GLN   A 1 88  ? 33.88781 34.68135  -9.34715  1.000 72.33704  ? 85  GLN   A NE2 1 
ATOM   735  N N   . ASP   A 1 89  ? 32.74292 29.51047  -8.40898  1.000 46.92167  ? 86  ASP   A N   1 
ATOM   736  C CA  . ASP   A 1 89  ? 31.55837 28.89714  -8.98537  1.000 53.66617  ? 86  ASP   A CA  1 
ATOM   737  C C   . ASP   A 1 89  ? 30.59400 29.97607  -9.46532  1.000 55.50609  ? 86  ASP   A C   1 
ATOM   738  O O   . ASP   A 1 89  ? 30.68654 31.14429  -9.08122  1.000 53.67758  ? 86  ASP   A O   1 
ATOM   739  C CB  . ASP   A 1 89  ? 30.87065 27.97174  -7.97664  1.000 54.00747  ? 86  ASP   A CB  1 
ATOM   740  C CG  . ASP   A 1 89  ? 30.38799 28.70364  -6.73795  1.000 63.96437  ? 86  ASP   A CG  1 
ATOM   741  O OD1 . ASP   A 1 89  ? 29.31360 29.33829  -6.79932  1.000 69.40377  ? 86  ASP   A OD1 1 
ATOM   742  O OD2 . ASP   A 1 89  ? 31.08169 28.63995  -5.70016  1.000 92.69648  ? 86  ASP   A OD2 1 
ATOM   743  N N   . LEU   A 1 90  ? 29.66026 29.56576  -10.32572 1.000 50.88743  ? 87  LEU   A N   1 
ATOM   744  C CA  . LEU   A 1 90  ? 28.73631 30.52387  -10.92272 1.000 54.35074  ? 87  LEU   A CA  1 
ATOM   745  C C   . LEU   A 1 90  ? 27.80162 31.13767  -9.88635  1.000 54.19189  ? 87  LEU   A C   1 
ATOM   746  O O   . LEU   A 1 90  ? 27.43830 32.31326  -10.00486 1.000 53.04616  ? 87  LEU   A O   1 
ATOM   747  C CB  . LEU   A 1 90  ? 27.92849 29.85278  -12.03341 1.000 48.44225  ? 87  LEU   A CB  1 
ATOM   748  C CG  . LEU   A 1 90  ? 26.94177 30.76990  -12.75692 1.000 45.79099  ? 87  LEU   A CG  1 
ATOM   749  C CD1 . LEU   A 1 90  ? 27.68426 31.89498  -13.46969 1.000 52.99453  ? 87  LEU   A CD1 1 
ATOM   750  C CD2 . LEU   A 1 90  ? 26.06852 29.98459  -13.72288 1.000 47.82298  ? 87  LEU   A CD2 1 
ATOM   751  N N   . LYS   A 1 91  ? 27.41176 30.37185  -8.86429  1.000 55.83343  ? 88  LYS   A N   1 
ATOM   752  C CA  . LYS   A 1 91  ? 26.48433 30.89603  -7.86598  1.000 50.65542  ? 88  LYS   A CA  1 
ATOM   753  C C   . LYS   A 1 91  ? 27.09097 32.07534  -7.11574  1.000 53.83145  ? 88  LYS   A C   1 
ATOM   754  O O   . LYS   A 1 91  ? 26.41389 33.08242  -6.87724  1.000 57.25716  ? 88  LYS   A O   1 
ATOM   755  C CB  . LYS   A 1 91  ? 26.07454 29.78675  -6.89645  1.000 56.01020  ? 88  LYS   A CB  1 
ATOM   756  C CG  . LYS   A 1 91  ? 24.68756 29.96976  -6.29117  1.000 66.21043  ? 88  LYS   A CG  1 
ATOM   757  C CD  . LYS   A 1 91  ? 24.72943 30.74060  -4.98407  1.000 71.01349  ? 88  LYS   A CD  1 
ATOM   758  C CE  . LYS   A 1 91  ? 24.71569 29.80292  -3.78352  1.000 91.88312  ? 88  LYS   A CE  1 
ATOM   759  N NZ  . LYS   A 1 91  ? 25.91202 28.91729  -3.73265  1.000 93.95708  ? 88  LYS   A NZ  1 
ATOM   760  N N   . LYS   A 1 92  ? 28.36953 31.97239  -6.74175  1.000 52.80769  ? 89  LYS   A N   1 
ATOM   761  C CA  . LYS   A 1 92  ? 29.03475 33.08200  -6.06701  1.000 53.40653  ? 89  LYS   A CA  1 
ATOM   762  C C   . LYS   A 1 92  ? 29.22490 34.26871  -7.00436  1.000 61.52037  ? 89  LYS   A C   1 
ATOM   763  O O   . LYS   A 1 92  ? 29.24266 35.41920  -6.55182  1.000 56.63508  ? 89  LYS   A O   1 
ATOM   764  C CB  . LYS   A 1 92  ? 30.38088 32.61917  -5.50136  1.000 61.60365  ? 89  LYS   A CB  1 
ATOM   765  C CG  . LYS   A 1 92  ? 30.97895 33.54602  -4.44994  1.000 81.28731  ? 89  LYS   A CG  1 
ATOM   766  C CD  . LYS   A 1 92  ? 32.21459 32.93518  -3.79079  1.000 86.23441  ? 89  LYS   A CD  1 
ATOM   767  C CE  . LYS   A 1 92  ? 33.45637 33.09896  -4.65418  1.000 84.90882  ? 89  LYS   A CE  1 
ATOM   768  N NZ  . LYS   A 1 92  ? 34.65246 32.41677  -4.07994  1.000 89.13754  ? 89  LYS   A NZ  1 
ATOM   769  N N   . PHE   A 1 93  ? 29.35703 34.01116  -8.30860  1.000 58.71336  ? 90  PHE   A N   1 
ATOM   770  C CA  . PHE   A 1 93  ? 29.51347 35.09682  -9.27123  1.000 55.96129  ? 90  PHE   A CA  1 
ATOM   771  C C   . PHE   A 1 93  ? 28.19078 35.81294  -9.51573  1.000 54.85603  ? 90  PHE   A C   1 
ATOM   772  O O   . PHE   A 1 93  ? 28.16183 37.03957  -9.66613  1.000 57.66937  ? 90  PHE   A O   1 
ATOM   773  C CB  . PHE   A 1 93  ? 30.08632 34.54884  -10.57953 1.000 58.17324  ? 90  PHE   A CB  1 
ATOM   774  C CG  . PHE   A 1 93  ? 30.11645 35.54822  -11.70305 1.000 57.64377  ? 90  PHE   A CG  1 
ATOM   775  C CD1 . PHE   A 1 93  ? 31.09370 36.53020  -11.75243 1.000 60.74505  ? 90  PHE   A CD1 1 
ATOM   776  C CD2 . PHE   A 1 93  ? 29.17637 35.49363  -12.72028 1.000 56.66130  ? 90  PHE   A CD2 1 
ATOM   777  C CE1 . PHE   A 1 93  ? 31.12526 37.44709  -12.78935 1.000 58.20387  ? 90  PHE   A CE1 1 
ATOM   778  C CE2 . PHE   A 1 93  ? 29.20311 36.40584  -13.76022 1.000 69.45009  ? 90  PHE   A CE2 1 
ATOM   779  C CZ  . PHE   A 1 93  ? 30.17843 37.38407  -13.79473 1.000 62.04851  ? 90  PHE   A CZ  1 
ATOM   780  N N   . MET   A 1 94  ? 27.08582 35.06457  -9.56018  1.000 53.72627  ? 91  MET   A N   1 
ATOM   781  C CA  . MET   A 1 94  ? 25.77726 35.68713  -9.73139  1.000 55.69692  ? 91  MET   A CA  1 
ATOM   782  C C   . MET   A 1 94  ? 25.38207 36.49205  -8.49951  1.000 54.62832  ? 91  MET   A C   1 
ATOM   783  O O   . MET   A 1 94  ? 24.75642 37.55182  -8.61897  1.000 57.63965  ? 91  MET   A O   1 
ATOM   784  C CB  . MET   A 1 94  ? 24.72845 34.62054  -10.02931 1.000 57.37820  ? 91  MET   A CB  1 
ATOM   785  C CG  . MET   A 1 94  ? 25.05358 33.75070  -11.22525 1.000 60.42268  ? 91  MET   A CG  1 
ATOM   786  S SD  . MET   A 1 94  ? 24.01342 32.28382  -11.24722 1.000 76.91830  ? 91  MET   A SD  1 
ATOM   787  C CE  . MET   A 1 94  ? 22.45059 33.03715  -11.65083 1.000 65.34066  ? 91  MET   A CE  1 
ATOM   788  N N   . ASP   A 1 95  ? 25.72856 36.00047  -7.30717  1.000 48.40222  ? 92  ASP   A N   1 
ATOM   789  C CA  . ASP   A 1 95  ? 25.44467 36.75335  -6.08881  1.000 63.82290  ? 92  ASP   A CA  1 
ATOM   790  C C   . ASP   A 1 95  ? 26.26875 38.03316  -6.02898  1.000 54.27456  ? 92  ASP   A C   1 
ATOM   791  O O   . ASP   A 1 95  ? 25.75201 39.09438  -5.66039  1.000 62.49566  ? 92  ASP   A O   1 
ATOM   792  C CB  . ASP   A 1 95  ? 25.70958 35.88571  -4.85804  1.000 57.66372  ? 92  ASP   A CB  1 
ATOM   793  C CG  . ASP   A 1 95  ? 24.73529 34.72633  -4.73815  1.000 66.34511  ? 92  ASP   A CG  1 
ATOM   794  O OD1 . ASP   A 1 95  ? 23.78611 34.65616  -5.54804  1.000 68.47904  ? 92  ASP   A OD1 1 
ATOM   795  O OD2 . ASP   A 1 95  ? 24.92144 33.88277  -3.83438  1.000 66.31077  ? 92  ASP   A OD2 1 
ATOM   796  N N   . ALA   A 1 96  ? 27.55190 37.95333  -6.39030  1.000 55.02132  ? 93  ALA   A N   1 
ATOM   797  C CA  . ALA   A 1 96  ? 28.38368 39.15048  -6.43930  1.000 56.52212  ? 93  ALA   A CA  1 
ATOM   798  C C   . ALA   A 1 96  ? 27.90152 40.12946  -7.50220  1.000 57.06045  ? 93  ALA   A C   1 
ATOM   799  O O   . ALA   A 1 96  ? 28.13106 41.33790  -7.37890  1.000 62.74322  ? 93  ALA   A O   1 
ATOM   800  C CB  . ALA   A 1 96  ? 29.84035 38.76708  -6.69418  1.000 53.39499  ? 93  ALA   A CB  1 
ATOM   801  N N   . SER   A 1 97  ? 27.23101 39.63409  -8.54088  1.000 57.77407  ? 94  SER   A N   1 
ATOM   802  C CA  . SER   A 1 97  ? 26.72020 40.46364  -9.62232  1.000 55.46372  ? 94  SER   A CA  1 
ATOM   803  C C   . SER   A 1 97  ? 25.23950 40.78288  -9.46942  1.000 64.37742  ? 94  SER   A C   1 
ATOM   804  O O   . SER   A 1 97  ? 24.63287 41.30524  -10.40736 1.000 69.16277  ? 94  SER   A O   1 
ATOM   805  C CB  . SER   A 1 97  ? 26.95633 39.77677  -10.97064 1.000 60.27044  ? 94  SER   A CB  1 
ATOM   806  O OG  . SER   A 1 97  ? 28.28609 39.30413  -11.08587 1.000 62.73533  ? 94  SER   A OG  1 
ATOM   807  N N   . ALA   A 1 98  ? 24.64514 40.48571  -8.31178  1.000 61.12639  ? 95  ALA   A N   1 
ATOM   808  C CA  . ALA   A 1 98  ? 23.19693 40.60885  -8.17184  1.000 65.80921  ? 95  ALA   A CA  1 
ATOM   809  C C   . ALA   A 1 98  ? 22.73972 42.05929  -8.27183  1.000 64.59065  ? 95  ALA   A C   1 
ATOM   810  O O   . ALA   A 1 98  ? 21.67380 42.34081  -8.83127  1.000 74.55198  ? 95  ALA   A O   1 
ATOM   811  C CB  . ALA   A 1 98  ? 22.74430 39.99604  -6.84823  1.000 70.52066  ? 95  ALA   A CB  1 
ATOM   812  N N   . LEU   A 1 99  ? 23.52284 42.99378  -7.73413  1.000 64.05523  ? 96  LEU   A N   1 
ATOM   813  C CA  . LEU   A 1 99  ? 23.11828 44.39455  -7.77511  1.000 71.71427  ? 96  LEU   A CA  1 
ATOM   814  C C   . LEU   A 1 99  ? 23.34877 44.99855  -9.15480  1.000 79.47359  ? 96  LEU   A C   1 
ATOM   815  O O   . LEU   A 1 99  ? 22.47193 45.68029  -9.69694  1.000 80.02769  ? 96  LEU   A O   1 
ATOM   816  C CB  . LEU   A 1 99  ? 23.86861 45.19349  -6.70839  1.000 73.02144  ? 96  LEU   A CB  1 
ATOM   817  C CG  . LEU   A 1 99  ? 23.62000 44.78564  -5.25603  1.000 75.38289  ? 96  LEU   A CG  1 
ATOM   818  C CD1 . LEU   A 1 99  ? 24.30075 45.76012  -4.30977  1.000 77.80800  ? 96  LEU   A CD1 1 
ATOM   819  C CD2 . LEU   A 1 99  ? 22.12858 44.69826  -4.96335  1.000 70.43421  ? 96  LEU   A CD2 1 
ATOM   820  N N   . THR   A 1 100 ? 24.52262 44.75490  -9.73874  1.000 86.40138  ? 97  THR   A N   1 
ATOM   821  C CA  . THR   A 1 100 ? 24.85727 45.33730  -11.03181 1.000 87.82036  ? 97  THR   A CA  1 
ATOM   822  C C   . THR   A 1 100 ? 24.32305 44.52620  -12.20522 1.000 76.82933  ? 97  THR   A C   1 
ATOM   823  O O   . THR   A 1 100 ? 24.15192 45.08173  -13.29555 1.000 75.85002  ? 97  THR   A O   1 
ATOM   824  C CB  . THR   A 1 100 ? 26.37546 45.48737  -11.16451 1.000 95.94108  ? 97  THR   A CB  1 
ATOM   825  O OG1 . THR   A 1 100 ? 27.00085 44.20706  -11.00819 1.000 96.68437  ? 97  THR   A OG1 1 
ATOM   826  C CG2 . THR   A 1 100 ? 26.91120 46.44014  -10.10375 1.000 101.00882 ? 97  THR   A CG2 1 
ATOM   827  N N   . GLY   A 1 101 ? 24.05253 43.23781  -12.01108 1.000 83.21599  ? 98  GLY   A N   1 
ATOM   828  C CA  . GLY   A 1 101 ? 23.60711 42.38908  -13.09893 1.000 69.12787  ? 98  GLY   A CA  1 
ATOM   829  C C   . GLY   A 1 101 ? 24.75938 41.89490  -13.94788 1.000 67.72957  ? 98  GLY   A C   1 
ATOM   830  O O   . GLY   A 1 101 ? 25.70484 42.64311  -14.21236 1.000 77.17611  ? 98  GLY   A O   1 
ATOM   831  N N   . ILE   A 1 102 ? 24.70323 40.63886  -14.36912 1.000 72.34940  ? 99  ILE   A N   1 
ATOM   832  C CA  . ILE   A 1 102 ? 25.73157 40.11508  -15.27544 1.000 67.13675  ? 99  ILE   A CA  1 
ATOM   833  C C   . ILE   A 1 102 ? 25.52507 40.72138  -16.65914 1.000 68.63241  ? 99  ILE   A C   1 
ATOM   834  O O   . ILE   A 1 102 ? 24.37933 40.77439  -17.14176 1.000 67.56790  ? 99  ILE   A O   1 
ATOM   835  C CB  . ILE   A 1 102 ? 25.66840 38.58781  -15.32865 1.000 71.59959  ? 99  ILE   A CB  1 
ATOM   836  C CG1 . ILE   A 1 102 ? 25.68431 38.00244  -13.91602 1.000 66.17846  ? 99  ILE   A CG1 1 
ATOM   837  C CG2 . ILE   A 1 102 ? 26.83313 38.03198  -16.13572 1.000 64.54230  ? 99  ILE   A CG2 1 
ATOM   838  C CD1 . ILE   A 1 102 ? 25.56030 36.49498  -13.88488 1.000 65.59781  ? 99  ILE   A CD1 1 
ATOM   839  N N   . PRO   A 1 103 ? 26.57562 41.20524  -17.32206 1.000 71.79492  ? 100 PRO   A N   1 
ATOM   840  C CA  . PRO   A 1 103 ? 26.39825 41.77588  -18.66273 1.000 66.43749  ? 100 PRO   A CA  1 
ATOM   841  C C   . PRO   A 1 103 ? 25.83231 40.74977  -19.63418 1.000 66.36652  ? 100 PRO   A C   1 
ATOM   842  O O   . PRO   A 1 103 ? 26.20163 39.57384  -19.61048 1.000 66.92510  ? 100 PRO   A O   1 
ATOM   843  C CB  . PRO   A 1 103 ? 27.81683 42.20288  -19.05650 1.000 78.84459  ? 100 PRO   A CB  1 
ATOM   844  C CG  . PRO   A 1 103 ? 28.52929 42.38841  -17.75986 1.000 65.47979  ? 100 PRO   A CG  1 
ATOM   845  C CD  . PRO   A 1 103 ? 27.95694 41.35710  -16.83382 1.000 62.15525  ? 100 PRO   A CD  1 
ATOM   846  N N   . LEU   A 1 104 ? 24.91851 41.21078  -20.48842 1.000 68.21097  ? 101 LEU   A N   1 
ATOM   847  C CA  . LEU   A 1 104 ? 24.28451 40.31177  -21.44925 1.000 68.69856  ? 101 LEU   A CA  1 
ATOM   848  C C   . LEU   A 1 104 ? 25.27635 39.60761  -22.37085 1.000 71.83401  ? 101 LEU   A C   1 
ATOM   849  O O   . LEU   A 1 104 ? 25.08550 38.40437  -22.62258 1.000 62.30161  ? 101 LEU   A O   1 
ATOM   850  C CB  . LEU   A 1 104 ? 23.23273 41.07968  -22.26216 1.000 70.56417  ? 101 LEU   A CB  1 
ATOM   851  C CG  . LEU   A 1 104 ? 22.48150 40.27320  -23.32580 1.000 82.10282  ? 101 LEU   A CG  1 
ATOM   852  C CD1 . LEU   A 1 104 ? 21.78006 39.07323  -22.70343 1.000 72.48780  ? 101 LEU   A CD1 1 
ATOM   853  C CD2 . LEU   A 1 104 ? 21.48777 41.15197  -24.07248 1.000 91.83430  ? 101 LEU   A CD2 1 
ATOM   854  N N   . PRO   A 1 105 ? 26.31764 40.25791  -22.90805 1.000 70.21555  ? 102 PRO   A N   1 
ATOM   855  C CA  . PRO   A 1 105 ? 27.30407 39.49674  -23.69369 1.000 74.35269  ? 102 PRO   A CA  1 
ATOM   856  C C   . PRO   A 1 105 ? 27.97218 38.38409  -22.90544 1.000 69.36214  ? 102 PRO   A C   1 
ATOM   857  O O   . PRO   A 1 105 ? 28.31742 37.34664  -23.48544 1.000 66.38496  ? 102 PRO   A O   1 
ATOM   858  C CB  . PRO   A 1 105 ? 28.31337 40.57083  -24.12311 1.000 74.13888  ? 102 PRO   A CB  1 
ATOM   859  C CG  . PRO   A 1 105 ? 27.53245 41.83181  -24.12731 1.000 71.25153  ? 102 PRO   A CG  1 
ATOM   860  C CD  . PRO   A 1 105 ? 26.57929 41.70878  -22.97666 1.000 61.56408  ? 102 PRO   A CD  1 
ATOM   861  N N   . LEU   A 1 106 ? 28.16095 38.56393  -21.59697 1.000 58.95185  ? 103 LEU   A N   1 
ATOM   862  C CA  . LEU   A 1 106 ? 28.77355 37.51593  -20.78870 1.000 63.23852  ? 103 LEU   A CA  1 
ATOM   863  C C   . LEU   A 1 106 ? 27.78915 36.38884  -20.49773 1.000 63.46856  ? 103 LEU   A C   1 
ATOM   864  O O   . LEU   A 1 106 ? 28.18446 35.21924  -20.43227 1.000 60.99560  ? 103 LEU   A O   1 
ATOM   865  C CB  . LEU   A 1 106 ? 29.31691 38.10578  -19.48721 1.000 56.84498  ? 103 LEU   A CB  1 
ATOM   866  C CG  . LEU   A 1 106 ? 30.16225 37.16765  -18.62451 1.000 60.69197  ? 103 LEU   A CG  1 
ATOM   867  C CD1 . LEU   A 1 106 ? 31.36300 36.66451  -19.40864 1.000 59.67273  ? 103 LEU   A CD1 1 
ATOM   868  C CD2 . LEU   A 1 106 ? 30.60722 37.87004  -17.35310 1.000 58.21033  ? 103 LEU   A CD2 1 
ATOM   869  N N   . ILE   A 1 107 ? 26.50769 36.71901  -20.31664 1.000 62.87039  ? 104 ILE   A N   1 
ATOM   870  C CA  . ILE   A 1 107 ? 25.49210 35.68091  -20.15824 1.000 67.25085  ? 104 ILE   A CA  1 
ATOM   871  C C   . ILE   A 1 107 ? 25.39773 34.84089  -21.42338 1.000 56.68901  ? 104 ILE   A C   1 
ATOM   872  O O   . ILE   A 1 107 ? 25.32102 33.60718  -21.36708 1.000 52.16443  ? 104 ILE   A O   1 
ATOM   873  C CB  . ILE   A 1 107 ? 24.13262 36.30754  -19.79694 1.000 62.60901  ? 104 ILE   A CB  1 
ATOM   874  C CG1 . ILE   A 1 107 ? 24.20737 37.00468  -18.43835 1.000 70.35417  ? 104 ILE   A CG1 1 
ATOM   875  C CG2 . ILE   A 1 107 ? 23.04044 35.24906  -19.79873 1.000 51.83153  ? 104 ILE   A CG2 1 
ATOM   876  C CD1 . ILE   A 1 107 ? 22.90299 37.63470  -18.00497 1.000 67.45056  ? 104 ILE   A CD1 1 
ATOM   877  N N   . LYS   A 1 108 ? 25.40674 35.49733  -22.58424 1.000 56.90899  ? 105 LYS   A N   1 
ATOM   878  C CA  . LYS   A 1 108 ? 25.35543 34.77432  -23.84903 1.000 66.85412  ? 105 LYS   A CA  1 
ATOM   879  C C   . LYS   A 1 108 ? 26.59628 33.91071  -24.03691 1.000 57.90237  ? 105 LYS   A C   1 
ATOM   880  O O   . LYS   A 1 108 ? 26.50797 32.78325  -24.53570 1.000 60.97558  ? 105 LYS   A O   1 
ATOM   881  C CB  . LYS   A 1 108 ? 25.20137 35.76569  -25.00240 1.000 56.43604  ? 105 LYS   A CB  1 
ATOM   882  C CG  . LYS   A 1 108 ? 24.97458 35.12852  -26.35720 1.000 66.67609  ? 105 LYS   A CG  1 
ATOM   883  C CD  . LYS   A 1 108 ? 24.76104 36.18799  -27.43103 1.000 75.90125  ? 105 LYS   A CD  1 
ATOM   884  C CE  . LYS   A 1 108 ? 23.53295 37.03691  -27.14153 1.000 80.59767  ? 105 LYS   A CE  1 
ATOM   885  N NZ  . LYS   A 1 108 ? 23.24630 37.99392  -28.24797 1.000 92.22541  ? 105 LYS   A NZ  1 
ATOM   886  N N   . SER   A 1 109 ? 27.76169 34.41822  -23.62982 1.000 60.35178  ? 106 SER   A N   1 
ATOM   887  C CA  . SER   A 1 109 ? 28.99081 33.64234  -23.75584 1.000 55.07369  ? 106 SER   A CA  1 
ATOM   888  C C   . SER   A 1 109 ? 28.99769 32.45082  -22.80685 1.000 58.11105  ? 106 SER   A C   1 
ATOM   889  O O   . SER   A 1 109 ? 29.42419 31.35349  -23.18477 1.000 54.31011  ? 106 SER   A O   1 
ATOM   890  C CB  . SER   A 1 109 ? 30.20307 34.53418  -23.49784 1.000 61.17022  ? 106 SER   A CB  1 
ATOM   891  O OG  . SER   A 1 109 ? 31.38638 33.75990  -23.42421 1.000 63.91649  ? 106 SER   A OG  1 
ATOM   892  N N   . TYR   A 1 110 ? 28.53597 32.64658  -21.56996 1.000 54.34549  ? 107 TYR   A N   1 
ATOM   893  C CA  . TYR   A 1 110 ? 28.51484 31.55089  -20.60606 1.000 54.43296  ? 107 TYR   A CA  1 
ATOM   894  C C   . TYR   A 1 110 ? 27.54464 30.45828  -21.03542 1.000 52.12228  ? 107 TYR   A C   1 
ATOM   895  O O   . TYR   A 1 110 ? 27.87946 29.26876  -20.99813 1.000 47.16205  ? 107 TYR   A O   1 
ATOM   896  C CB  . TYR   A 1 110 ? 28.15211 32.07612  -19.21660 1.000 49.00953  ? 107 TYR   A CB  1 
ATOM   897  C CG  . TYR   A 1 110 ? 29.32424 32.63787  -18.44427 1.000 52.87347  ? 107 TYR   A CG  1 
ATOM   898  C CD1 . TYR   A 1 110 ? 30.62954 32.41853  -18.86521 1.000 51.64105  ? 107 TYR   A CD1 1 
ATOM   899  C CD2 . TYR   A 1 110 ? 29.12517 33.37803  -17.28726 1.000 56.95279  ? 107 TYR   A CD2 1 
ATOM   900  C CE1 . TYR   A 1 110 ? 31.70317 32.92692  -18.15704 1.000 56.79756  ? 107 TYR   A CE1 1 
ATOM   901  C CE2 . TYR   A 1 110 ? 30.19006 33.88954  -16.57390 1.000 51.75378  ? 107 TYR   A CE2 1 
ATOM   902  C CZ  . TYR   A 1 110 ? 31.47613 33.66172  -17.01228 1.000 59.12259  ? 107 TYR   A CZ  1 
ATOM   903  O OH  . TYR   A 1 110 ? 32.53605 34.17245  -16.30019 1.000 58.10650  ? 107 TYR   A OH  1 
ATOM   904  N N   . LEU   A 1 111 ? 26.33189 30.84315  -21.44030 1.000 51.92754  ? 108 LEU   A N   1 
ATOM   905  C CA  . LEU   A 1 111 ? 25.35208 29.85297  -21.87435 1.000 56.18004  ? 108 LEU   A CA  1 
ATOM   906  C C   . LEU   A 1 111 ? 25.84400 29.09690  -23.10106 1.000 56.00982  ? 108 LEU   A C   1 
ATOM   907  O O   . LEU   A 1 111 ? 25.66008 27.87821  -23.20502 1.000 53.52464  ? 108 LEU   A O   1 
ATOM   908  C CB  . LEU   A 1 111 ? 24.01391 30.53038  -22.16587 1.000 51.48944  ? 108 LEU   A CB  1 
ATOM   909  C CG  . LEU   A 1 111 ? 22.88375 29.59974  -22.60732 1.000 51.18204  ? 108 LEU   A CG  1 
ATOM   910  C CD1 . LEU   A 1 111 ? 22.46250 28.68866  -21.46130 1.000 46.53898  ? 108 LEU   A CD1 1 
ATOM   911  C CD2 . LEU   A 1 111 ? 21.70110 30.39759  -23.13427 1.000 58.77866  ? 108 LEU   A CD2 1 
ATOM   912  N N   . PHE   A 1 112 ? 26.47606 29.80637  -24.03843 1.000 49.92857  ? 109 PHE   A N   1 
ATOM   913  C CA  . PHE   A 1 112 ? 27.00689 29.16309  -25.23582 1.000 51.87625  ? 109 PHE   A CA  1 
ATOM   914  C C   . PHE   A 1 112 ? 28.03070 28.09439  -24.87340 1.000 53.28565  ? 109 PHE   A C   1 
ATOM   915  O O   . PHE   A 1 112 ? 27.98696 26.97374  -25.39413 1.000 49.57104  ? 109 PHE   A O   1 
ATOM   916  C CB  . PHE   A 1 112 ? 27.62051 30.21838  -26.15808 1.000 55.23430  ? 109 PHE   A CB  1 
ATOM   917  C CG  . PHE   A 1 112 ? 28.06542 29.68247  -27.48691 1.000 56.42060  ? 109 PHE   A CG  1 
ATOM   918  C CD1 . PHE   A 1 112 ? 27.14107 29.39391  -28.47614 1.000 54.78515  ? 109 PHE   A CD1 1 
ATOM   919  C CD2 . PHE   A 1 112 ? 29.40892 29.47843  -27.75161 1.000 60.95798  ? 109 PHE   A CD2 1 
ATOM   920  C CE1 . PHE   A 1 112 ? 27.54619 28.90329  -29.70244 1.000 60.68661  ? 109 PHE   A CE1 1 
ATOM   921  C CE2 . PHE   A 1 112 ? 29.82129 28.99066  -28.97856 1.000 63.77977  ? 109 PHE   A CE2 1 
ATOM   922  C CZ  . PHE   A 1 112 ? 28.88836 28.70221  -29.95395 1.000 64.35415  ? 109 PHE   A CZ  1 
ATOM   923  N N   . GLN   A 1 113 ? 28.95286 28.42098  -23.96341 1.000 48.53900  ? 110 GLN   A N   1 
ATOM   924  C CA  . GLN   A 1 113 ? 29.95786 27.45027  -23.54356 1.000 49.93471  ? 110 GLN   A CA  1 
ATOM   925  C C   . GLN   A 1 113 ? 29.32919 26.28473  -22.79207 1.000 51.44243  ? 110 GLN   A C   1 
ATOM   926  O O   . GLN   A 1 113 ? 29.74979 25.13460  -22.96161 1.000 53.77766  ? 110 GLN   A O   1 
ATOM   927  C CB  . GLN   A 1 113 ? 31.01315 28.12931  -22.67536 1.000 54.09194  ? 110 GLN   A CB  1 
ATOM   928  C CG  . GLN   A 1 113 ? 31.78546 29.22681  -23.37827 1.000 49.82236  ? 110 GLN   A CG  1 
ATOM   929  C CD  . GLN   A 1 113 ? 32.69508 29.96777  -22.42488 1.000 66.72771  ? 110 GLN   A CD  1 
ATOM   930  O OE1 . GLN   A 1 113 ? 33.54920 29.36612  -21.77371 1.000 57.22912  ? 110 GLN   A OE1 1 
ATOM   931  N NE2 . GLN   A 1 113 ? 32.50331 31.27820  -22.31960 1.000 58.29447  ? 110 GLN   A NE2 1 
ATOM   932  N N   . LEU   A 1 114 ? 28.33307 26.56216  -21.94552 1.000 45.56138  ? 111 LEU   A N   1 
ATOM   933  C CA  . LEU   A 1 114 ? 27.66130 25.48828  -21.22021 1.000 50.04273  ? 111 LEU   A CA  1 
ATOM   934  C C   . LEU   A 1 114 ? 26.95849 24.53698  -22.17951 1.000 46.99529  ? 111 LEU   A C   1 
ATOM   935  O O   . LEU   A 1 114 ? 26.98951 23.31569  -21.99006 1.000 45.70820  ? 111 LEU   A O   1 
ATOM   936  C CB  . LEU   A 1 114 ? 26.66218 26.06842  -20.21774 1.000 54.50810  ? 111 LEU   A CB  1 
ATOM   937  C CG  . LEU   A 1 114 ? 27.19132 26.78164  -18.97175 1.000 58.01066  ? 111 LEU   A CG  1 
ATOM   938  C CD1 . LEU   A 1 114 ? 26.04311 27.44523  -18.22850 1.000 50.17152  ? 111 LEU   A CD1 1 
ATOM   939  C CD2 . LEU   A 1 114 ? 27.92877 25.81324  -18.05566 1.000 47.94991  ? 111 LEU   A CD2 1 
ATOM   940  N N   . LEU   A 1 115 ? 26.31810 25.07932  -23.21652 1.000 46.33396  ? 112 LEU   A N   1 
ATOM   941  C CA  . LEU   A 1 115 ? 25.66874 24.23039  -24.20845 1.000 50.76466  ? 112 LEU   A CA  1 
ATOM   942  C C   . LEU   A 1 115 ? 26.68203 23.41603  -25.00327 1.000 49.03285  ? 112 LEU   A C   1 
ATOM   943  O O   . LEU   A 1 115 ? 26.36870 22.30373  -25.44107 1.000 55.76471  ? 112 LEU   A O   1 
ATOM   944  C CB  . LEU   A 1 115 ? 24.81362 25.08055  -25.14780 1.000 47.56217  ? 112 LEU   A CB  1 
ATOM   945  C CG  . LEU   A 1 115 ? 23.52855 25.66951  -24.56771 1.000 49.75655  ? 112 LEU   A CG  1 
ATOM   946  C CD1 . LEU   A 1 115 ? 22.97500 26.72411  -25.49877 1.000 47.20073  ? 112 LEU   A CD1 1 
ATOM   947  C CD2 . LEU   A 1 115 ? 22.50014 24.57466  -24.32429 1.000 46.83718  ? 112 LEU   A CD2 1 
ATOM   948  N N   . GLN   A 1 116 ? 27.89402 23.94488  -25.19832 1.000 49.08439  ? 113 GLN   A N   1 
ATOM   949  C CA  . GLN   A 1 116 ? 28.92793 23.19041  -25.90220 1.000 44.72977  ? 113 GLN   A CA  1 
ATOM   950  C C   . GLN   A 1 116 ? 29.41219 22.01181  -25.06661 1.000 49.07672  ? 113 GLN   A C   1 
ATOM   951  O O   . GLN   A 1 116 ? 29.51393 20.88467  -25.56374 1.000 47.24925  ? 113 GLN   A O   1 
ATOM   952  C CB  . GLN   A 1 116 ? 30.09897 24.10430  -26.26440 1.000 49.63145  ? 113 GLN   A CB  1 
ATOM   953  C CG  . GLN   A 1 116 ? 29.81326 25.07791  -27.39058 1.000 49.06121  ? 113 GLN   A CG  1 
ATOM   954  C CD  . GLN   A 1 116 ? 30.99941 25.96852  -27.69907 1.000 63.95108  ? 113 GLN   A CD  1 
ATOM   955  O OE1 . GLN   A 1 116 ? 31.64114 26.50438  -26.79470 1.000 72.93959  ? 113 GLN   A OE1 1 
ATOM   956  N NE2 . GLN   A 1 116 ? 31.30313 26.12453  -28.98170 1.000 70.44853  ? 113 GLN   A NE2 1 
ATOM   957  N N   . GLY   A 1 117 ? 29.72891 22.25537  -23.79432 1.000 46.44744  ? 114 GLY   A N   1 
ATOM   958  C CA  . GLY   A 1 117 ? 30.11778 21.16305  -22.92107 1.000 51.06327  ? 114 GLY   A CA  1 
ATOM   959  C C   . GLY   A 1 117 ? 29.00842 20.15297  -22.71096 1.000 47.49882  ? 114 GLY   A C   1 
ATOM   960  O O   . GLY   A 1 117 ? 29.27333 18.96166  -22.53653 1.000 52.00049  ? 114 GLY   A O   1 
ATOM   961  N N   . LEU   A 1 118 ? 27.75388 20.60737  -22.72910 1.000 50.13444  ? 115 LEU   A N   1 
ATOM   962  C CA  . LEU   A 1 118 ? 26.63900 19.68386  -22.55237 1.000 56.20316  ? 115 LEU   A CA  1 
ATOM   963  C C   . LEU   A 1 118 ? 26.39445 18.87272  -23.81903 1.000 51.69857  ? 115 LEU   A C   1 
ATOM   964  O O   . LEU   A 1 118 ? 26.08526 17.67696  -23.74729 1.000 53.19411  ? 115 LEU   A O   1 
ATOM   965  C CB  . LEU   A 1 118 ? 25.38043 20.45097  -22.14872 1.000 48.32366  ? 115 LEU   A CB  1 
ATOM   966  C CG  . LEU   A 1 118 ? 24.21518 19.59886  -21.64925 1.000 55.06885  ? 115 LEU   A CG  1 
ATOM   967  C CD1 . LEU   A 1 118 ? 24.63186 18.80158  -20.41998 1.000 50.69763  ? 115 LEU   A CD1 1 
ATOM   968  C CD2 . LEU   A 1 118 ? 23.00806 20.47380  -21.34772 1.000 51.22511  ? 115 LEU   A CD2 1 
ATOM   969  N N   . ALA   A 1 119 ? 26.53092 19.50678  -24.98801 1.000 47.31165  ? 116 ALA   A N   1 
ATOM   970  C CA  . ALA   A 1 119 ? 26.41002 18.78061  -26.24834 1.000 56.84486  ? 116 ALA   A CA  1 
ATOM   971  C C   . ALA   A 1 119 ? 27.50923 17.73924  -26.39701 1.000 51.70171  ? 116 ALA   A C   1 
ATOM   972  O O   . ALA   A 1 119 ? 27.28450 16.67981  -26.99360 1.000 48.99849  ? 116 ALA   A O   1 
ATOM   973  C CB  . ALA   A 1 119 ? 26.44092 19.75640  -27.42451 1.000 51.25826  ? 116 ALA   A CB  1 
ATOM   974  N N   . PHE   A 1 120 ? 28.69967 18.02275  -25.86317 1.000 50.90754  ? 117 PHE   A N   1 
ATOM   975  C CA  . PHE   A 1 120 ? 29.76557 17.02689  -25.84189 1.000 53.14327  ? 117 PHE   A CA  1 
ATOM   976  C C   . PHE   A 1 120 ? 29.41058 15.86083  -24.92530 1.000 49.88798  ? 117 PHE   A C   1 
ATOM   977  O O   . PHE   A 1 120 ? 29.64640 14.69849  -25.27483 1.000 59.73580  ? 117 PHE   A O   1 
ATOM   978  C CB  . PHE   A 1 120 ? 31.07538 17.68483  -25.40562 1.000 57.38997  ? 117 PHE   A CB  1 
ATOM   979  C CG  . PHE   A 1 120 ? 32.27599 16.78315  -25.48899 1.000 53.02636  ? 117 PHE   A CG  1 
ATOM   980  C CD1 . PHE   A 1 120 ? 32.98086 16.65351  -26.67425 1.000 60.29639  ? 117 PHE   A CD1 1 
ATOM   981  C CD2 . PHE   A 1 120 ? 32.71570 16.08670  -24.37441 1.000 56.36563  ? 117 PHE   A CD2 1 
ATOM   982  C CE1 . PHE   A 1 120 ? 34.09393 15.83379  -26.75109 1.000 59.87861  ? 117 PHE   A CE1 1 
ATOM   983  C CE2 . PHE   A 1 120 ? 33.82566 15.26525  -24.44425 1.000 58.42720  ? 117 PHE   A CE2 1 
ATOM   984  C CZ  . PHE   A 1 120 ? 34.51704 15.13950  -25.63315 1.000 50.64875  ? 117 PHE   A CZ  1 
ATOM   985  N N   . CYS   A 1 121 ? 28.84330 16.14984  -23.74849 1.000 43.31232  ? 118 CYS   A N   1 
ATOM   986  C CA  . CYS   A 1 121 ? 28.43198 15.07968  -22.84204 1.000 44.90493  ? 118 CYS   A CA  1 
ATOM   987  C C   . CYS   A 1 121 ? 27.36773 14.19668  -23.47671 1.000 47.18785  ? 118 CYS   A C   1 
ATOM   988  O O   . CYS   A 1 121 ? 27.42484 12.96606  -23.37225 1.000 54.94827  ? 118 CYS   A O   1 
ATOM   989  C CB  . CYS   A 1 121 ? 27.90280 15.66035  -21.53049 1.000 51.08665  ? 118 CYS   A CB  1 
ATOM   990  S SG  . CYS   A 1 121 ? 29.12554 16.45631  -20.48083 1.000 52.23491  ? 118 CYS   A SG  1 
ATOM   991  N N   . HIS   A 1 122 ? 26.38344 14.80871  -24.13409 1.000 44.28612  ? 119 HIS   A N   1 
ATOM   992  C CA  . HIS   A 1 122 ? 25.27795 14.03740  -24.68645 1.000 49.56206  ? 119 HIS   A CA  1 
ATOM   993  C C   . HIS   A 1 122 ? 25.69634 13.24535  -25.91858 1.000 50.01188  ? 119 HIS   A C   1 
ATOM   994  O O   . HIS   A 1 122 ? 25.20211 12.13250  -26.12859 1.000 47.88987  ? 119 HIS   A O   1 
ATOM   995  C CB  . HIS   A 1 122 ? 24.11172 14.96794  -25.00339 1.000 44.95865  ? 119 HIS   A CB  1 
ATOM   996  C CG  . HIS   A 1 122 ? 23.48623 15.57472  -23.78697 1.000 51.44830  ? 119 HIS   A CG  1 
ATOM   997  N ND1 . HIS   A 1 122 ? 22.53121 16.56607  -23.85400 1.000 54.52112  ? 119 HIS   A ND1 1 
ATOM   998  C CD2 . HIS   A 1 122 ? 23.67410 15.32139  -22.46997 1.000 49.65446  ? 119 HIS   A CD2 1 
ATOM   999  C CE1 . HIS   A 1 122 ? 22.15958 16.89889  -22.63086 1.000 55.47025  ? 119 HIS   A CE1 1 
ATOM   1000 N NE2 . HIS   A 1 122 ? 22.83767 16.15817  -21.77266 1.000 49.40618  ? 119 HIS   A NE2 1 
ATOM   1001 N N   . SER   A 1 123 ? 26.60141 13.79046  -26.73849 1.000 48.95528  ? 120 SER   A N   1 
ATOM   1002 C CA  . SER   A 1 123 ? 27.10606 13.03259  -27.87955 1.000 52.58911  ? 120 SER   A CA  1 
ATOM   1003 C C   . SER   A 1 123 ? 27.92803 11.83360  -27.42857 1.000 55.98153  ? 120 SER   A C   1 
ATOM   1004 O O   . SER   A 1 123 ? 28.02731 10.84083  -28.15889 1.000 57.12071  ? 120 SER   A O   1 
ATOM   1005 C CB  . SER   A 1 123 ? 27.94239 13.93162  -28.78835 1.000 51.45607  ? 120 SER   A CB  1 
ATOM   1006 O OG  . SER   A 1 123 ? 29.13154 14.33481  -28.13438 1.000 59.69827  ? 120 SER   A OG  1 
ATOM   1007 N N   . HIS   A 1 124 ? 28.52834 11.91174  -26.24277 1.000 50.53810  ? 121 HIS   A N   1 
ATOM   1008 C CA  . HIS   A 1 124 ? 29.19984 10.78219  -25.61832 1.000 52.90422  ? 121 HIS   A CA  1 
ATOM   1009 C C   . HIS   A 1 124 ? 28.25498 9.94568   -24.76779 1.000 52.65865  ? 121 HIS   A C   1 
ATOM   1010 O O   . HIS   A 1 124 ? 28.71692 9.07208   -24.02627 1.000 55.07363  ? 121 HIS   A O   1 
ATOM   1011 C CB  . HIS   A 1 124 ? 30.37738 11.27018  -24.77012 1.000 52.96502  ? 121 HIS   A CB  1 
ATOM   1012 C CG  . HIS   A 1 124 ? 31.57351 11.66386  -25.57707 1.000 53.87886  ? 121 HIS   A CG  1 
ATOM   1013 N ND1 . HIS   A 1 124 ? 31.53542 12.66409  -26.52432 1.000 58.82029  ? 121 HIS   A ND1 1 
ATOM   1014 C CD2 . HIS   A 1 124 ? 32.83792 11.18038  -25.59085 1.000 57.51036  ? 121 HIS   A CD2 1 
ATOM   1015 C CE1 . HIS   A 1 124 ? 32.72632 12.78311  -27.08375 1.000 57.66896  ? 121 HIS   A CE1 1 
ATOM   1016 N NE2 . HIS   A 1 124 ? 33.53503 11.89530  -26.53439 1.000 65.40624  ? 121 HIS   A NE2 1 
ATOM   1017 N N   . ARG   A 1 125 ? 26.94865 10.20334  -24.85800 1.000 48.65526  ? 122 ARG   A N   1 
ATOM   1018 C CA  . ARG   A 1 125 ? 25.92656 9.43842   -24.14359 1.000 54.25390  ? 122 ARG   A CA  1 
ATOM   1019 C C   . ARG   A 1 125 ? 26.12459 9.51271   -22.62965 1.000 60.25168  ? 122 ARG   A C   1 
ATOM   1020 O O   . ARG   A 1 125 ? 26.10886 8.50017   -21.92832 1.000 54.86931  ? 122 ARG   A O   1 
ATOM   1021 C CB  . ARG   A 1 125 ? 25.89117 7.98444   -24.62285 1.000 56.94933  ? 122 ARG   A CB  1 
ATOM   1022 C CG  . ARG   A 1 125 ? 25.16922 7.77850   -25.94991 1.000 58.14439  ? 122 ARG   A CG  1 
ATOM   1023 C CD  . ARG   A 1 125 ? 25.91023 6.78960   -26.83331 1.000 64.48391  ? 122 ARG   A CD  1 
ATOM   1024 N NE  . ARG   A 1 125 ? 26.74890 5.88377   -26.05737 1.000 75.81109  ? 122 ARG   A NE  1 
ATOM   1025 C CZ  . ARG   A 1 125 ? 26.36104 4.69656   -25.61283 1.000 78.94232  ? 122 ARG   A CZ  1 
ATOM   1026 N NH1 . ARG   A 1 125 ? 25.14810 4.22919   -25.85852 1.000 74.50495  ? 122 ARG   A NH1 1 
ATOM   1027 N NH2 . ARG   A 1 125 ? 27.21108 3.96093   -24.90203 1.000 83.57335  ? 122 ARG   A NH2 1 
ATOM   1028 N N   . VAL   A 1 126 ? 26.30005 10.73127  -22.12160 1.000 50.41639  ? 123 VAL   A N   1 
ATOM   1029 C CA  . VAL   A 1 126 ? 26.46937 10.96590  -20.69095 1.000 44.59765  ? 123 VAL   A CA  1 
ATOM   1030 C C   . VAL   A 1 126 ? 25.46938 12.02497  -20.24718 1.000 47.64858  ? 123 VAL   A C   1 
ATOM   1031 O O   . VAL   A 1 126 ? 25.44188 13.13078  -20.80183 1.000 50.36837  ? 123 VAL   A O   1 
ATOM   1032 C CB  . VAL   A 1 126 ? 27.90081 11.40240  -20.33759 1.000 49.83336  ? 123 VAL   A CB  1 
ATOM   1033 C CG1 . VAL   A 1 126 ? 27.99708 11.73451  -18.85383 1.000 49.69457  ? 123 VAL   A CG1 1 
ATOM   1034 C CG2 . VAL   A 1 126 ? 28.89479 10.31593  -20.70424 1.000 58.95240  ? 123 VAL   A CG2 1 
ATOM   1035 N N   . LEU   A 1 127 ? 24.65314 11.68729  -19.25219 1.000 51.19645  ? 124 LEU   A N   1 
ATOM   1036 C CA  . LEU   A 1 127 ? 23.79089 12.65154  -18.58472 1.000 49.23127  ? 124 LEU   A CA  1 
ATOM   1037 C C   . LEU   A 1 127 ? 24.50738 13.20330  -17.36118 1.000 52.48209  ? 124 LEU   A C   1 
ATOM   1038 O O   . LEU   A 1 127 ? 25.11357 12.44774  -16.59964 1.000 54.08758  ? 124 LEU   A O   1 
ATOM   1039 C CB  . LEU   A 1 127 ? 22.47671 11.99994  -18.15569 1.000 46.82033  ? 124 LEU   A CB  1 
ATOM   1040 C CG  . LEU   A 1 127 ? 21.72958 11.20369  -19.21929 1.000 58.52183  ? 124 LEU   A CG  1 
ATOM   1041 C CD1 . LEU   A 1 127 ? 20.45668 10.61676  -18.64101 1.000 53.28459  ? 124 LEU   A CD1 1 
ATOM   1042 C CD2 . LEU   A 1 127 ? 21.42797 12.09070  -20.40596 1.000 54.00264  ? 124 LEU   A CD2 1 
ATOM   1043 N N   . HIS   A 1 128 ? 24.43617 14.52389  -17.17333 1.000 47.31244  ? 125 HIS   A N   1 
ATOM   1044 C CA  . HIS   A 1 128 ? 25.02788 15.12460  -15.98021 1.000 41.42338  ? 125 HIS   A CA  1 
ATOM   1045 C C   . HIS   A 1 128 ? 24.12487 14.94401  -14.76442 1.000 45.20689  ? 125 HIS   A C   1 
ATOM   1046 O O   . HIS   A 1 128 ? 24.57209 14.46713  -13.71414 1.000 46.91269  ? 125 HIS   A O   1 
ATOM   1047 C CB  . HIS   A 1 128 ? 25.31495 16.60787  -16.21670 1.000 40.35548  ? 125 HIS   A CB  1 
ATOM   1048 C CG  . HIS   A 1 128 ? 26.10243 17.24808  -15.11672 1.000 49.48172  ? 125 HIS   A CG  1 
ATOM   1049 N ND1 . HIS   A 1 128 ? 25.53845 17.61844  -13.91424 1.000 47.03043  ? 125 HIS   A ND1 1 
ATOM   1050 C CD2 . HIS   A 1 128 ? 27.41359 17.57471  -15.03355 1.000 44.05614  ? 125 HIS   A CD2 1 
ATOM   1051 C CE1 . HIS   A 1 128 ? 26.46791 18.14816  -13.13918 1.000 51.76439  ? 125 HIS   A CE1 1 
ATOM   1052 N NE2 . HIS   A 1 128 ? 27.61461 18.13344  -13.79483 1.000 50.44336  ? 125 HIS   A NE2 1 
ATOM   1053 N N   . ARG   A 1 129 ? 22.85752 15.34142  -14.88735 1.000 43.39659  ? 126 ARG   A N   1 
ATOM   1054 C CA  . ARG   A 1 129 ? 21.81348 15.12238  -13.88650 1.000 50.33282  ? 126 ARG   A CA  1 
ATOM   1055 C C   . ARG   A 1 129 ? 22.02014 15.92174  -12.60191 1.000 42.36504  ? 126 ARG   A C   1 
ATOM   1056 O O   . ARG   A 1 129 ? 21.39457 15.61745  -11.58314 1.000 50.27642  ? 126 ARG   A O   1 
ATOM   1057 C CB  . ARG   A 1 129 ? 21.66502 13.63368  -13.54316 1.000 43.09986  ? 126 ARG   A CB  1 
ATOM   1058 C CG  . ARG   A 1 129 ? 21.47003 12.73032  -14.74476 1.000 50.04691  ? 126 ARG   A CG  1 
ATOM   1059 C CD  . ARG   A 1 129 ? 21.07982 11.32576  -14.31859 1.000 52.72107  ? 126 ARG   A CD  1 
ATOM   1060 N NE  . ARG   A 1 129 ? 22.03777 10.74265  -13.38704 1.000 50.51540  ? 126 ARG   A NE  1 
ATOM   1061 C CZ  . ARG   A 1 129 ? 21.90127 9.54695   -12.82913 1.000 68.19028  ? 126 ARG   A CZ  1 
ATOM   1062 N NH1 . ARG   A 1 129 ? 20.85461 8.77995   -13.08696 1.000 59.69684  ? 126 ARG   A NH1 1 
ATOM   1063 N NH2 . ARG   A 1 129 ? 22.83756 9.10956   -11.99144 1.000 62.40592  ? 126 ARG   A NH2 1 
ATOM   1064 N N   . ASP   A 1 130 ? 22.87766 16.94130  -12.60837 1.000 46.37374  ? 127 ASP   A N   1 
ATOM   1065 C CA  . ASP   A 1 130 ? 23.00367 17.80482  -11.43587 1.000 46.46367  ? 127 ASP   A CA  1 
ATOM   1066 C C   . ASP   A 1 130 ? 23.53803 19.17289  -11.83811 1.000 48.20883  ? 127 ASP   A C   1 
ATOM   1067 O O   . ASP   A 1 130 ? 24.45835 19.70016  -11.20495 1.000 48.37206  ? 127 ASP   A O   1 
ATOM   1068 C CB  . ASP   A 1 130 ? 23.91122 17.16866  -10.37820 1.000 40.77811  ? 127 ASP   A CB  1 
ATOM   1069 C CG  . ASP   A 1 130 ? 23.62161 17.67901  -8.96728  1.000 66.24699  ? 127 ASP   A CG  1 
ATOM   1070 O OD1 . ASP   A 1 130 ? 22.53716 18.25931  -8.73968  1.000 51.66820  ? 127 ASP   A OD1 1 
ATOM   1071 O OD2 . ASP   A 1 130 ? 24.48321 17.49936  -8.08093  1.000 71.53400  ? 127 ASP   A OD2 1 
ATOM   1072 N N   . LEU   A 1 131 ? 22.96972 19.75147  -12.89265 1.000 45.68684  ? 128 LEU   A N   1 
ATOM   1073 C CA  . LEU   A 1 131 ? 23.38932 21.06409  -13.37852 1.000 48.80304  ? 128 LEU   A CA  1 
ATOM   1074 C C   . LEU   A 1 131 ? 22.76004 22.13241  -12.49397 1.000 49.50257  ? 128 LEU   A C   1 
ATOM   1075 O O   . LEU   A 1 131 ? 21.56043 22.40447  -12.57858 1.000 61.24301  ? 128 LEU   A O   1 
ATOM   1076 C CB  . LEU   A 1 131 ? 22.99778 21.25049  -14.84018 1.000 45.05654  ? 128 LEU   A CB  1 
ATOM   1077 C CG  . LEU   A 1 131 ? 23.72888 20.37602  -15.85893 1.000 53.97990  ? 128 LEU   A CG  1 
ATOM   1078 C CD1 . LEU   A 1 131 ? 23.23022 20.66326  -17.26694 1.000 57.77386  ? 128 LEU   A CD1 1 
ATOM   1079 C CD2 . LEU   A 1 131 ? 25.22754 20.59745  -15.76955 1.000 46.08056  ? 128 LEU   A CD2 1 
ATOM   1080 N N   . LYS   A 1 132 ? 23.57020 22.72737  -11.63208 1.000 51.06738  ? 129 LYS   A N   1 
ATOM   1081 C CA  . LYS   A 1 132 ? 23.17005 23.82593  -10.76988 1.000 54.89425  ? 129 LYS   A CA  1 
ATOM   1082 C C   . LYS   A 1 132 ? 24.32206 24.81932  -10.73256 1.000 44.86642  ? 129 LYS   A C   1 
ATOM   1083 O O   . LYS   A 1 132 ? 25.46597 24.45334  -11.01630 1.000 50.22840  ? 129 LYS   A O   1 
ATOM   1084 C CB  . LYS   A 1 132 ? 22.82181 23.33868  -9.35575  1.000 47.76822  ? 129 LYS   A CB  1 
ATOM   1085 C CG  . LYS   A 1 132 ? 23.88597 22.46668  -8.71237  1.000 44.54409  ? 129 LYS   A CG  1 
ATOM   1086 C CD  . LYS   A 1 132 ? 23.40642 21.90518  -7.38592  1.000 45.74875  ? 129 LYS   A CD  1 
ATOM   1087 C CE  . LYS   A 1 132 ? 24.46175 21.00676  -6.75753  1.000 57.61400  ? 129 LYS   A CE  1 
ATOM   1088 N NZ  . LYS   A 1 132 ? 24.06295 20.52793  -5.40525  1.000 66.34473  ? 129 LYS   A NZ  1 
ATOM   1089 N N   . PRO   A 1 133 ? 24.04514 26.08630  -10.40740 1.000 49.05591  ? 130 PRO   A N   1 
ATOM   1090 C CA  . PRO   A 1 133 ? 25.12724 27.08664  -10.41625 1.000 47.65129  ? 130 PRO   A CA  1 
ATOM   1091 C C   . PRO   A 1 133 ? 26.31548 26.70776  -9.55112  1.000 44.47566  ? 130 PRO   A C   1 
ATOM   1092 O O   . PRO   A 1 133 ? 27.44681 27.08760  -9.87726  1.000 51.19350  ? 130 PRO   A O   1 
ATOM   1093 C CB  . PRO   A 1 133 ? 24.43157 28.35506  -9.90323  1.000 45.56072  ? 130 PRO   A CB  1 
ATOM   1094 C CG  . PRO   A 1 133 ? 22.99915 28.16132  -10.26181 1.000 60.57853  ? 130 PRO   A CG  1 
ATOM   1095 C CD  . PRO   A 1 133 ? 22.74112 26.69291  -10.09232 1.000 52.66702  ? 130 PRO   A CD  1 
ATOM   1096 N N   . GLN   A 1 134 ? 26.09880 25.95628  -8.46733  1.000 45.82752  ? 131 GLN   A N   1 
ATOM   1097 C CA  . GLN   A 1 134 ? 27.21471 25.52575  -7.63024  1.000 47.41659  ? 131 GLN   A CA  1 
ATOM   1098 C C   . GLN   A 1 134 ? 28.16494 24.60017  -8.38063  1.000 49.30303  ? 131 GLN   A C   1 
ATOM   1099 O O   . GLN   A 1 134 ? 29.35342 24.53100  -8.04616  1.000 50.07341  ? 131 GLN   A O   1 
ATOM   1100 C CB  . GLN   A 1 134 ? 26.69827 24.82882  -6.36948  1.000 53.02323  ? 131 GLN   A CB  1 
ATOM   1101 C CG  . GLN   A 1 134 ? 25.97638 25.73701  -5.38346  1.000 58.78262  ? 131 GLN   A CG  1 
ATOM   1102 C CD  . GLN   A 1 134 ? 24.48835 25.86005  -5.66721  1.000 71.77054  ? 131 GLN   A CD  1 
ATOM   1103 O OE1 . GLN   A 1 134 ? 24.01256 25.50307  -6.74770  1.000 55.16511  ? 131 GLN   A OE1 1 
ATOM   1104 N NE2 . GLN   A 1 134 ? 23.74366 26.36396  -4.68908  1.000 80.19246  ? 131 GLN   A NE2 1 
ATOM   1105 N N   . ASN   A 1 135 ? 27.66842 23.88216  -9.38754  1.000 40.56616  ? 132 ASN   A N   1 
ATOM   1106 C CA  . ASN   A 1 135 ? 28.47427 22.93388  -10.14472 1.000 48.46267  ? 132 ASN   A CA  1 
ATOM   1107 C C   . ASN   A 1 135 ? 29.03816 23.52700  -11.42793 1.000 47.26005  ? 132 ASN   A C   1 
ATOM   1108 O O   . ASN   A 1 135 ? 29.61633 22.79389  -12.23600 1.000 44.96559  ? 132 ASN   A O   1 
ATOM   1109 C CB  . ASN   A 1 135 ? 27.65346 21.68298  -10.46303 1.000 47.76742  ? 132 ASN   A CB  1 
ATOM   1110 C CG  . ASN   A 1 135 ? 27.45267 20.80150  -9.24900  1.000 48.41559  ? 132 ASN   A CG  1 
ATOM   1111 O OD1 . ASN   A 1 135 ? 28.23215 20.85638  -8.29889  1.000 58.28464  ? 132 ASN   A OD1 1 
ATOM   1112 N ND2 . ASN   A 1 135 ? 26.40931 19.98217  -9.27336  1.000 46.87694  ? 132 ASN   A ND2 1 
ATOM   1113 N N   . LEU   A 1 136 ? 28.88185 24.82953  -11.63610 1.000 51.70467  ? 133 LEU   A N   1 
ATOM   1114 C CA  . LEU   A 1 136 ? 29.39843 25.51187  -12.81490 1.000 47.36340  ? 133 LEU   A CA  1 
ATOM   1115 C C   . LEU   A 1 136 ? 30.52210 26.43533  -12.37163 1.000 51.87055  ? 133 LEU   A C   1 
ATOM   1116 O O   . LEU   A 1 136 ? 30.29426 27.36412  -11.58901 1.000 49.15518  ? 133 LEU   A O   1 
ATOM   1117 C CB  . LEU   A 1 136 ? 28.29240 26.29093  -13.52431 1.000 41.89332  ? 133 LEU   A CB  1 
ATOM   1118 C CG  . LEU   A 1 136 ? 27.04882 25.45499  -13.82575 1.000 47.15477  ? 133 LEU   A CG  1 
ATOM   1119 C CD1 . LEU   A 1 136 ? 26.01901 26.27223  -14.58200 1.000 57.06338  ? 133 LEU   A CD1 1 
ATOM   1120 C CD2 . LEU   A 1 136 ? 27.43287 24.21165  -14.61067 1.000 42.83762  ? 133 LEU   A CD2 1 
ATOM   1121 N N   . LEU   A 1 137 ? 31.72854 26.17392  -12.86245 1.000 45.26774  ? 134 LEU   A N   1 
ATOM   1122 C CA  . LEU   A 1 137 ? 32.92700 26.85401  -12.39913 1.000 49.63321  ? 134 LEU   A CA  1 
ATOM   1123 C C   . LEU   A 1 137 ? 33.46521 27.76549  -13.49026 1.000 55.82188  ? 134 LEU   A C   1 
ATOM   1124 O O   . LEU   A 1 137 ? 33.43760 27.41590  -14.67423 1.000 56.23694  ? 134 LEU   A O   1 
ATOM   1125 C CB  . LEU   A 1 137 ? 33.99674 25.84365  -11.98130 1.000 44.19033  ? 134 LEU   A CB  1 
ATOM   1126 C CG  . LEU   A 1 137 ? 33.54314 24.82578  -10.93371 1.000 41.74325  ? 134 LEU   A CG  1 
ATOM   1127 C CD1 . LEU   A 1 137 ? 34.65566 23.83579  -10.64451 1.000 43.84334  ? 134 LEU   A CD1 1 
ATOM   1128 C CD2 . LEU   A 1 137 ? 33.10213 25.53012  -9.66005  1.000 54.75527  ? 134 LEU   A CD2 1 
ATOM   1129 N N   . ILE   A 1 138 ? 33.95493 28.93400  -13.08456 1.000 49.01247  ? 135 ILE   A N   1 
ATOM   1130 C CA  . ILE   A 1 138 ? 34.48302 29.92356  -14.01148 1.000 53.59030  ? 135 ILE   A CA  1 
ATOM   1131 C C   . ILE   A 1 138 ? 35.90570 30.26659  -13.60263 1.000 61.92071  ? 135 ILE   A C   1 
ATOM   1132 O O   . ILE   A 1 138 ? 36.28788 30.13362  -12.43522 1.000 59.42088  ? 135 ILE   A O   1 
ATOM   1133 C CB  . ILE   A 1 138 ? 33.61028 31.19642  -14.06019 1.000 53.10111  ? 135 ILE   A CB  1 
ATOM   1134 C CG1 . ILE   A 1 138 ? 33.64389 31.92041  -12.71400 1.000 61.66121  ? 135 ILE   A CG1 1 
ATOM   1135 C CG2 . ILE   A 1 138 ? 32.17965 30.84760  -14.43201 1.000 51.35473  ? 135 ILE   A CG2 1 
ATOM   1136 C CD1 . ILE   A 1 138 ? 32.78531 33.16258  -12.67258 1.000 66.90434  ? 135 ILE   A CD1 1 
ATOM   1137 N N   . ASN   A 1 139 ? 36.69420 30.70546  -14.57684 1.000 54.34145  ? 136 ASN   A N   1 
ATOM   1138 C CA  . ASN   A 1 139 ? 38.05017 31.17139  -14.33149 1.000 55.87319  ? 136 ASN   A CA  1 
ATOM   1139 C C   . ASN   A 1 139 ? 38.14756 32.65375  -14.67955 1.000 64.12989  ? 136 ASN   A C   1 
ATOM   1140 O O   . ASN   A 1 139 ? 37.15554 33.30350  -15.02220 1.000 59.18434  ? 136 ASN   A O   1 
ATOM   1141 C CB  . ASN   A 1 139 ? 39.07459 30.33826  -15.11337 1.000 62.00339  ? 136 ASN   A CB  1 
ATOM   1142 C CG  . ASN   A 1 139 ? 38.87822 30.40424  -16.62250 1.000 62.71821  ? 136 ASN   A CG  1 
ATOM   1143 O OD1 . ASN   A 1 139 ? 38.05291 31.16140  -17.13333 1.000 62.32254  ? 136 ASN   A OD1 1 
ATOM   1144 N ND2 . ASN   A 1 139 ? 39.65702 29.60717  -17.34490 1.000 61.33094  ? 136 ASN   A ND2 1 
ATOM   1145 N N   . THR   A 1 140 ? 39.36400 33.18415  -14.58755 1.000 60.46419  ? 137 THR   A N   1 
ATOM   1146 C CA  . THR   A 1 140 ? 39.63104 34.59143  -14.84503 1.000 68.18499  ? 137 THR   A CA  1 
ATOM   1147 C C   . THR   A 1 140 ? 39.86266 34.88827  -16.32118 1.000 68.54466  ? 137 THR   A C   1 
ATOM   1148 O O   . THR   A 1 140 ? 40.27676 36.00168  -16.65905 1.000 70.61357  ? 137 THR   A O   1 
ATOM   1149 C CB  . THR   A 1 140 ? 40.84116 35.05330  -14.02821 1.000 64.56026  ? 137 THR   A CB  1 
ATOM   1150 O OG1 . THR   A 1 140 ? 42.00721 34.33974  -14.45711 1.000 77.74281  ? 137 THR   A OG1 1 
ATOM   1151 C CG2 . THR   A 1 140 ? 40.61149 34.78926  -12.54368 1.000 62.19631  ? 137 THR   A CG2 1 
ATOM   1152 N N   . GLU   A 1 141 ? 39.60496 33.92307  -17.20540 1.000 66.10391  ? 138 GLU   A N   1 
ATOM   1153 C CA  . GLU   A 1 141 ? 39.81265 34.09910  -18.63853 1.000 69.84671  ? 138 GLU   A CA  1 
ATOM   1154 C C   . GLU   A 1 141 ? 38.50737 34.01011  -19.42471 1.000 63.52931  ? 138 GLU   A C   1 
ATOM   1155 O O   . GLU   A 1 141 ? 38.53362 33.80299  -20.64115 1.000 63.82546  ? 138 GLU   A O   1 
ATOM   1156 C CB  . GLU   A 1 141 ? 40.82214 33.07292  -19.15987 1.000 67.95137  ? 138 GLU   A CB  1 
ATOM   1157 C CG  . GLU   A 1 141 ? 42.18578 33.14573  -18.48239 1.000 79.34328  ? 138 GLU   A CG  1 
ATOM   1158 C CD  . GLU   A 1 141 ? 43.16034 32.09848  -18.99547 1.000 87.67744  ? 138 GLU   A CD  1 
ATOM   1159 O OE1 . GLU   A 1 141 ? 42.72241 31.16178  -19.69648 1.000 78.86158  ? 138 GLU   A OE1 1 
ATOM   1160 O OE2 . GLU   A 1 141 ? 44.36815 32.21420  -18.69767 1.000 82.41958  ? 138 GLU   A OE2 1 
ATOM   1161 N N   . GLY   A 1 142 ? 37.36589 34.15421  -18.75653 1.000 66.70725  ? 139 GLY   A N   1 
ATOM   1162 C CA  . GLY   A 1 142 ? 36.08495 34.16995  -19.43230 1.000 57.66850  ? 139 GLY   A CA  1 
ATOM   1163 C C   . GLY   A 1 142 ? 35.46304 32.81860  -19.70586 1.000 56.50448  ? 139 GLY   A C   1 
ATOM   1164 O O   . GLY   A 1 142 ? 34.43095 32.76033  -20.38437 1.000 58.30129  ? 139 GLY   A O   1 
ATOM   1165 N N   . ALA   A 1 143 ? 36.04223 31.73508  -19.19909 1.000 51.87701  ? 140 ALA   A N   1 
ATOM   1166 C CA  . ALA   A 1 143 ? 35.53313 30.39425  -19.44152 1.000 60.23035  ? 140 ALA   A CA  1 
ATOM   1167 C C   . ALA   A 1 143 ? 34.63767 29.93671  -18.29485 1.000 56.13205  ? 140 ALA   A C   1 
ATOM   1168 O O   . ALA   A 1 143 ? 34.76562 30.40103  -17.15981 1.000 52.39553  ? 140 ALA   A O   1 
ATOM   1169 C CB  . ALA   A 1 143 ? 36.68453 29.40403  -19.62885 1.000 57.14103  ? 140 ALA   A CB  1 
ATOM   1170 N N   . ILE   A 1 144 ? 33.71934 29.02292  -18.61059 1.000 48.45509  ? 141 ILE   A N   1 
ATOM   1171 C CA  . ILE   A 1 144 ? 32.87297 28.36176  -17.62180 1.000 46.95364  ? 141 ILE   A CA  1 
ATOM   1172 C C   . ILE   A 1 144 ? 32.84000 26.87404  -17.95361 1.000 56.64438  ? 141 ILE   A C   1 
ATOM   1173 O O   . ILE   A 1 144 ? 32.84052 26.49253  -19.12879 1.000 52.99989  ? 141 ILE   A O   1 
ATOM   1174 C CB  . ILE   A 1 144 ? 31.45123 28.96769  -17.58044 1.000 41.93820  ? 141 ILE   A CB  1 
ATOM   1175 C CG1 . ILE   A 1 144 ? 30.62142 28.33140  -16.46192 1.000 49.14344  ? 141 ILE   A CG1 1 
ATOM   1176 C CG2 . ILE   A 1 144 ? 30.75092 28.81927  -18.92507 1.000 51.67197  ? 141 ILE   A CG2 1 
ATOM   1177 C CD1 . ILE   A 1 144 ? 29.28440 29.00434  -16.24333 1.000 49.44910  ? 141 ILE   A CD1 1 
ATOM   1178 N N   . LYS   A 1 145 ? 32.83631 26.02818  -16.91982 1.000 53.01670  ? 142 LYS   A N   1 
ATOM   1179 C CA  . LYS   A 1 145 ? 33.03096 24.59664  -17.11176 1.000 51.46657  ? 142 LYS   A CA  1 
ATOM   1180 C C   . LYS   A 1 145 ? 32.08941 23.79350  -16.22416 1.000 52.39485  ? 142 LYS   A C   1 
ATOM   1181 O O   . LYS   A 1 145 ? 31.77427 24.18999  -15.09807 1.000 47.51746  ? 142 LYS   A O   1 
ATOM   1182 C CB  . LYS   A 1 145 ? 34.48625 24.18875  -16.82571 1.000 43.78036  ? 142 LYS   A CB  1 
ATOM   1183 C CG  . LYS   A 1 145 ? 35.51084 24.96744  -17.64582 1.000 52.74194  ? 142 LYS   A CG  1 
ATOM   1184 C CD  . LYS   A 1 145 ? 36.91794 24.41671  -17.50265 1.000 50.69136  ? 142 LYS   A CD  1 
ATOM   1185 C CE  . LYS   A 1 145 ? 37.90183 25.25329  -18.31302 1.000 45.03901  ? 142 LYS   A CE  1 
ATOM   1186 N NZ  . LYS   A 1 145 ? 39.21142 24.57010  -18.48401 1.000 67.08459  ? 142 LYS   A NZ  1 
ATOM   1187 N N   . LEU   A 1 146 ? 31.65034 22.65028  -16.75051 1.000 44.22207  ? 143 LEU   A N   1 
ATOM   1188 C CA  . LEU   A 1 146 ? 30.84576 21.70502  -15.98941 1.000 43.08523  ? 143 LEU   A CA  1 
ATOM   1189 C C   . LEU   A 1 146 ? 31.71920 20.94272  -15.00406 1.000 45.17223  ? 143 LEU   A C   1 
ATOM   1190 O O   . LEU   A 1 146 ? 32.82717 20.51505  -15.33864 1.000 47.28393  ? 143 LEU   A O   1 
ATOM   1191 C CB  . LEU   A 1 146 ? 30.15039 20.71357  -16.92316 1.000 45.14261  ? 143 LEU   A CB  1 
ATOM   1192 C CG  . LEU   A 1 146 ? 29.26389 21.26664  -18.03669 1.000 52.17144  ? 143 LEU   A CG  1 
ATOM   1193 C CD1 . LEU   A 1 146 ? 28.67985 20.12603  -18.85285 1.000 48.46967  ? 143 LEU   A CD1 1 
ATOM   1194 C CD2 . LEU   A 1 146 ? 28.15991 22.13369  -17.45988 1.000 51.89788  ? 143 LEU   A CD2 1 
ATOM   1195 N N   . ALA   A 1 147 ? 31.20610 20.75669  -13.78921 1.000 44.15383  ? 144 ALA   A N   1 
ATOM   1196 C CA  . ALA   A 1 147 ? 31.94089 20.07336  -12.73676 1.000 41.11888  ? 144 ALA   A CA  1 
ATOM   1197 C C   . ALA   A 1 147 ? 30.99001 19.18284  -11.94928 1.000 58.18185  ? 144 ALA   A C   1 
ATOM   1198 O O   . ALA   A 1 147 ? 29.76813 19.23863  -12.11476 1.000 50.09679  ? 144 ALA   A O   1 
ATOM   1199 C CB  . ALA   A 1 147 ? 32.63708 21.06864  -11.80120 1.000 54.02426  ? 144 ALA   A CB  1 
ATOM   1200 N N   . ASP   A 1 148 ? 31.57852 18.36211  -11.07551 1.000 56.37249  ? 145 ASP   A N   1 
ATOM   1201 C CA  . ASP   A 1 148 ? 30.86172 17.41435  -10.22699 1.000 57.67745  ? 145 ASP   A CA  1 
ATOM   1202 C C   . ASP   A 1 148 ? 30.04563 16.43274  -11.05977 1.000 52.07503  ? 145 ASP   A C   1 
ATOM   1203 O O   . ASP   A 1 148 ? 28.82828 16.58658  -11.20268 1.000 52.20045  ? 145 ASP   A O   1 
ATOM   1204 C CB  . ASP   A 1 148 ? 29.96310 18.14656  -9.22346  1.000 50.69282  ? 145 ASP   A CB  1 
ATOM   1205 C CG  . ASP   A 1 148 ? 29.51563 17.25021  -8.07740  1.000 71.31018  ? 145 ASP   A CG  1 
ATOM   1206 O OD1 . ASP   A 1 148 ? 29.83411 16.04159  -8.10493  1.000 62.79618  ? 145 ASP   A OD1 1 
ATOM   1207 O OD2 . ASP   A 1 148 ? 28.85246 17.75407  -7.14428  1.000 75.96646  ? 145 ASP   A OD2 1 
ATOM   1208 N N   . PHE   A 1 149 ? 30.71344 15.41702  -11.60747 1.000 55.60069  ? 146 PHE   A N   1 
ATOM   1209 C CA  . PHE   A 1 149 ? 30.06322 14.34853  -12.35132 1.000 51.94581  ? 146 PHE   A CA  1 
ATOM   1210 C C   . PHE   A 1 149 ? 29.75921 13.13089  -11.48215 1.000 56.67904  ? 146 PHE   A C   1 
ATOM   1211 O O   . PHE   A 1 149 ? 29.61191 12.02268  -12.01080 1.000 58.04028  ? 146 PHE   A O   1 
ATOM   1212 C CB  . PHE   A 1 149 ? 30.92408 13.94625  -13.55192 1.000 47.80405  ? 146 PHE   A CB  1 
ATOM   1213 C CG  . PHE   A 1 149 ? 30.79032 14.87325  -14.72991 1.000 53.13972  ? 146 PHE   A CG  1 
ATOM   1214 C CD1 . PHE   A 1 149 ? 31.39512 16.11966  -14.72232 1.000 55.66343  ? 146 PHE   A CD1 1 
ATOM   1215 C CD2 . PHE   A 1 149 ? 30.05599 14.49847  -15.84363 1.000 47.48347  ? 146 PHE   A CD2 1 
ATOM   1216 C CE1 . PHE   A 1 149 ? 31.27105 16.97418  -15.80478 1.000 43.45559  ? 146 PHE   A CE1 1 
ATOM   1217 C CE2 . PHE   A 1 149 ? 29.92732 15.34933  -16.92540 1.000 46.34229  ? 146 PHE   A CE2 1 
ATOM   1218 C CZ  . PHE   A 1 149 ? 30.53751 16.58806  -16.90530 1.000 49.17196  ? 146 PHE   A CZ  1 
ATOM   1219 N N   . GLY   A 1 150 ? 29.65701 13.31520  -10.16326 1.000 53.68689  ? 147 GLY   A N   1 
ATOM   1220 C CA  . GLY   A 1 150 ? 29.34900 12.19969  -9.28468  1.000 52.51352  ? 147 GLY   A CA  1 
ATOM   1221 C C   . GLY   A 1 150 ? 27.94843 11.65214  -9.47364  1.000 57.07222  ? 147 GLY   A C   1 
ATOM   1222 O O   . GLY   A 1 150 ? 27.71731 10.45345  -9.28877  1.000 60.80631  ? 147 GLY   A O   1 
ATOM   1223 N N   . LEU   A 1 151 ? 26.99953 12.50894  -9.84206  1.000 55.50330  ? 148 LEU   A N   1 
ATOM   1224 C CA  . LEU   A 1 151 ? 25.63091 12.08910  -10.10579 1.000 51.26033  ? 148 LEU   A CA  1 
ATOM   1225 C C   . LEU   A 1 151 ? 25.38459 11.78994  -11.57815 1.000 51.97916  ? 148 LEU   A C   1 
ATOM   1226 O O   . LEU   A 1 151 ? 24.24060 11.53088  -11.96430 1.000 52.09890  ? 148 LEU   A O   1 
ATOM   1227 C CB  . LEU   A 1 151 ? 24.64793 13.15562  -9.61600  1.000 54.98373  ? 148 LEU   A CB  1 
ATOM   1228 C CG  . LEU   A 1 151 ? 24.58089 13.34820  -8.09674  1.000 66.08648  ? 148 LEU   A CG  1 
ATOM   1229 C CD1 . LEU   A 1 151 ? 23.52838 14.37904  -7.72403  1.000 64.19118  ? 148 LEU   A CD1 1 
ATOM   1230 C CD2 . LEU   A 1 151 ? 24.30234 12.02610  -7.39835  1.000 61.21192  ? 148 LEU   A CD2 1 
ATOM   1231 N N   . ALA   A 1 152 ? 26.42717 11.81634  -12.40174 1.000 51.69308  ? 149 ALA   A N   1 
ATOM   1232 C CA  . ALA   A 1 152 ? 26.28305 11.56669  -13.82437 1.000 50.70872  ? 149 ALA   A CA  1 
ATOM   1233 C C   . ALA   A 1 152 ? 26.14563 10.07231  -14.09913 1.000 46.85371  ? 149 ALA   A C   1 
ATOM   1234 O O   . ALA   A 1 152 ? 26.52307 9.22283   -13.28717 1.000 54.52338  ? 149 ALA   A O   1 
ATOM   1235 C CB  . ALA   A 1 152 ? 27.47779 12.13397  -14.59353 1.000 41.03408  ? 149 ALA   A CB  1 
ATOM   1236 N N   . ARG   A 1 153 ? 25.59576 9.75677   -15.26790 1.000 53.73950  ? 150 ARG   A N   1 
ATOM   1237 C CA  . ARG   A 1 153 ? 25.44800 8.37114   -15.68307 1.000 56.73769  ? 150 ARG   A CA  1 
ATOM   1238 C C   . ARG   A 1 153 ? 25.47259 8.30077   -17.20044 1.000 57.44767  ? 150 ARG   A C   1 
ATOM   1239 O O   . ARG   A 1 153 ? 24.86908 9.13686   -17.87905 1.000 57.60573  ? 150 ARG   A O   1 
ATOM   1240 C CB  . ARG   A 1 153 ? 24.14890 7.75389   -15.15222 1.000 60.91658  ? 150 ARG   A CB  1 
ATOM   1241 C CG  . ARG   A 1 153 ? 24.02908 6.26372   -15.42428 1.000 73.87978  ? 150 ARG   A CG  1 
ATOM   1242 C CD  . ARG   A 1 153 ? 22.60926 5.76201   -15.21596 1.000 78.79123  ? 150 ARG   A CD  1 
ATOM   1243 N NE  . ARG   A 1 153 ? 22.50699 4.32609   -15.44812 1.000 84.54985  ? 150 ARG   A NE  1 
ATOM   1244 C CZ  . ARG   A 1 153 ? 22.57629 3.40572   -14.49575 1.000 87.23966  ? 150 ARG   A CZ  1 
ATOM   1245 N NH1 . ARG   A 1 153 ? 22.72434 3.73672   -13.22357 1.000 89.55586  ? 150 ARG   A NH1 1 
ATOM   1246 N NH2 . ARG   A 1 153 ? 22.49349 2.12057   -14.82798 1.000 91.08311  ? 150 ARG   A NH2 1 
ATOM   1247 N N   . ALA   A 1 154 ? 26.17924 7.30507   -17.72524 1.000 56.65250  ? 151 ALA   A N   1 
ATOM   1248 C CA  . ALA   A 1 154 ? 26.15380 7.04025   -19.15531 1.000 63.61731  ? 151 ALA   A CA  1 
ATOM   1249 C C   . ALA   A 1 154 ? 24.87997 6.28368   -19.50202 1.000 57.63356  ? 151 ALA   A C   1 
ATOM   1250 O O   . ALA   A 1 154 ? 24.54765 5.28657   -18.85428 1.000 67.99959  ? 151 ALA   A O   1 
ATOM   1251 C CB  . ALA   A 1 154 ? 27.38397 6.23839   -19.57828 1.000 47.57615  ? 151 ALA   A CB  1 
ATOM   1252 N N   . PHE   A 1 155 ? 24.15813 6.75956   -20.51049 1.000 57.23389  ? 152 PHE   A N   1 
ATOM   1253 C CA  . PHE   A 1 155 ? 22.92776 6.10174   -20.91817 1.000 57.97997  ? 152 PHE   A CA  1 
ATOM   1254 C C   . PHE   A 1 155 ? 23.16034 5.27490   -22.17479 1.000 64.65777  ? 152 PHE   A C   1 
ATOM   1255 O O   . PHE   A 1 155 ? 23.97616 5.62317   -23.03183 1.000 68.74006  ? 152 PHE   A O   1 
ATOM   1256 C CB  . PHE   A 1 155 ? 21.79274 7.11021   -21.14174 1.000 61.29418  ? 152 PHE   A CB  1 
ATOM   1257 C CG  . PHE   A 1 155 ? 22.00900 8.05375   -22.29850 1.000 60.15095  ? 152 PHE   A CG  1 
ATOM   1258 C CD1 . PHE   A 1 155 ? 21.57758 7.72429   -23.57439 1.000 58.91939  ? 152 PHE   A CD1 1 
ATOM   1259 C CD2 . PHE   A 1 155 ? 22.60449 9.28773   -22.10028 1.000 62.70493  ? 152 PHE   A CD2 1 
ATOM   1260 C CE1 . PHE   A 1 155 ? 21.76168 8.59625   -24.63583 1.000 64.82500  ? 152 PHE   A CE1 1 
ATOM   1261 C CE2 . PHE   A 1 155 ? 22.78323 10.16850  -23.15467 1.000 65.12386  ? 152 PHE   A CE2 1 
ATOM   1262 C CZ  . PHE   A 1 155 ? 22.36525 9.81919   -24.42663 1.000 58.21943  ? 152 PHE   A CZ  1 
ATOM   1263 N N   . GLY   A 1 156 ? 22.44329 4.15809   -22.26307 1.000 62.35646  ? 153 GLY   A N   1 
ATOM   1264 C CA  . GLY   A 1 156 ? 22.50816 3.31790   -23.43694 1.000 74.99125  ? 153 GLY   A CA  1 
ATOM   1265 C C   . GLY   A 1 156 ? 21.55225 3.77310   -24.52069 1.000 85.12759  ? 153 GLY   A C   1 
ATOM   1266 O O   . GLY   A 1 156 ? 20.73307 4.66938   -24.32775 1.000 80.95253  ? 153 GLY   A O   1 
ATOM   1267 N N   . VAL   A 1 157 ? 21.67914 3.14205   -25.67942 1.000 90.89815  ? 154 VAL   A N   1 
ATOM   1268 C CA  . VAL   A 1 157 ? 20.81070 3.38547   -26.82155 1.000 92.46464  ? 154 VAL   A CA  1 
ATOM   1269 C C   . VAL   A 1 157 ? 20.14341 2.06746   -27.19429 1.000 92.93653  ? 154 VAL   A C   1 
ATOM   1270 O O   . VAL   A 1 157 ? 20.74092 1.22441   -27.86318 1.000 95.48519  ? 154 VAL   A O   1 
ATOM   1271 C CB  . VAL   A 1 157 ? 21.59319 3.96905   -28.01239 1.000 90.24682  ? 154 VAL   A CB  1 
ATOM   1272 C CG1 . VAL   A 1 157 ? 20.65858 4.24747   -29.17883 1.000 82.27652  ? 154 VAL   A CG1 1 
ATOM   1273 C CG2 . VAL   A 1 157 ? 22.33025 5.23652   -27.59809 1.000 82.96065  ? 154 VAL   A CG2 1 
ATOM   1274 N N   . PRO   A 1 158 ? 18.89011 1.84981   -26.77368 1.000 86.25917  ? 155 PRO   A N   1 
ATOM   1275 C CA  . PRO   A 1 158 ? 18.01495 2.75983   -26.02341 1.000 87.39506  ? 155 PRO   A CA  1 
ATOM   1276 C C   . PRO   A 1 158 ? 18.31719 2.78084   -24.52779 1.000 84.62668  ? 155 PRO   A C   1 
ATOM   1277 O O   . PRO   A 1 158 ? 19.05333 1.93979   -24.01698 1.000 72.88970  ? 155 PRO   A O   1 
ATOM   1278 C CB  . PRO   A 1 158 ? 16.62275 2.18904   -26.31170 1.000 84.68127  ? 155 PRO   A CB  1 
ATOM   1279 C CG  . PRO   A 1 158 ? 16.86578 0.70828   -26.39125 1.000 83.64275  ? 155 PRO   A CG  1 
ATOM   1280 C CD  . PRO   A 1 158 ? 18.22418 0.56237   -27.04542 1.000 87.22961  ? 155 PRO   A CD  1 
ATOM   1281 N N   . VAL   A 1 159 ? 17.75387 3.74539   -23.80257 1.000 77.60717  ? 156 VAL   A N   1 
ATOM   1282 C CA  . VAL   A 1 159 ? 17.95273 3.84447   -22.36211 1.000 77.11111  ? 156 VAL   A CA  1 
ATOM   1283 C C   . VAL   A 1 159 ? 17.03150 2.85323   -21.66693 1.000 74.54745  ? 156 VAL   A C   1 
ATOM   1284 O O   . VAL   A 1 159 ? 16.13168 2.27925   -22.29059 1.000 74.98583  ? 156 VAL   A O   1 
ATOM   1285 C CB  . VAL   A 1 159 ? 17.69345 5.27545   -21.85512 1.000 73.19425  ? 156 VAL   A CB  1 
ATOM   1286 C CG1 . VAL   A 1 159 ? 18.39650 6.29247   -22.73826 1.000 68.87176  ? 156 VAL   A CG1 1 
ATOM   1287 C CG2 . VAL   A 1 159 ? 16.19457 5.55343   -21.78903 1.000 68.93082  ? 156 VAL   A CG2 1 
ATOM   1288 N N   . ARG   A 1 160 ? 17.25477 2.64123   -20.37427 1.000 75.48270  ? 157 ARG   A N   1 
ATOM   1289 C CA  . ARG   A 1 160 ? 16.33450 1.89807   -19.52818 1.000 77.69591  ? 157 ARG   A CA  1 
ATOM   1290 C C   . ARG   A 1 160 ? 16.00445 2.75713   -18.31284 1.000 71.70289  ? 157 ARG   A C   1 
ATOM   1291 O O   . ARG   A 1 160 ? 16.46730 3.89585   -18.18846 1.000 68.46375  ? 157 ARG   A O   1 
ATOM   1292 C CB  . ARG   A 1 160 ? 16.91561 0.53636   -19.12081 1.000 69.10639  ? 157 ARG   A CB  1 
ATOM   1293 C CG  . ARG   A 1 160 ? 17.99536 0.58730   -18.05315 1.000 78.26125  ? 157 ARG   A CG  1 
ATOM   1294 C CD  . ARG   A 1 160 ? 18.36868 -0.81975  -17.60966 1.000 82.28246  ? 157 ARG   A CD  1 
ATOM   1295 N NE  . ARG   A 1 160 ? 19.07046 -0.82961  -16.33203 1.000 85.68260  ? 157 ARG   A NE  1 
ATOM   1296 C CZ  . ARG   A 1 160 ? 20.38747 -0.89946  -16.19878 1.000 81.43652  ? 157 ARG   A CZ  1 
ATOM   1297 N NH1 . ARG   A 1 160 ? 21.18555 -0.97461  -17.25134 1.000 86.55679  ? 157 ARG   A NH1 1 
ATOM   1298 N NH2 . ARG   A 1 160 ? 20.91677 -0.89712  -14.97834 1.000 77.59911  ? 157 ARG   A NH2 1 
ATOM   1299 N N   . THR   A 1 161 ? 15.18861 2.21012   -17.41466 1.000 64.18599  ? 158 THR   A N   1 
ATOM   1300 C CA  . THR   A 1 161 ? 14.76242 2.95064   -16.23366 1.000 70.69793  ? 158 THR   A CA  1 
ATOM   1301 C C   . THR   A 1 161 ? 15.95698 3.21544   -15.32401 1.000 77.68415  ? 158 THR   A C   1 
ATOM   1302 O O   . THR   A 1 161 ? 16.57096 2.27835   -14.80222 1.000 78.95090  ? 158 THR   A O   1 
ATOM   1303 C CB  . THR   A 1 161 ? 13.67879 2.17787   -15.48666 1.000 66.35483  ? 158 THR   A CB  1 
ATOM   1304 O OG1 . THR   A 1 161 ? 12.57337 1.93736   -16.36589 1.000 76.69780  ? 158 THR   A OG1 1 
ATOM   1305 C CG2 . THR   A 1 161 ? 13.19525 2.97242   -14.28102 1.000 76.37607  ? 158 THR   A CG2 1 
ATOM   1306 N N   . TYR   A 1 162 ? 16.28537 4.48967   -15.13508 1.000 69.43637  ? 159 TYR   A N   1 
ATOM   1307 C CA  . TYR   A 1 162 ? 17.42303 4.87052   -14.30468 1.000 68.75288  ? 159 TYR   A CA  1 
ATOM   1308 C C   . TYR   A 1 162 ? 16.96880 5.36502   -12.93474 1.000 70.66100  ? 159 TYR   A C   1 
ATOM   1309 O O   . TYR   A 1 162 ? 15.78681 5.27917   -12.59916 1.000 67.02405  ? 159 TYR   A O   1 
ATOM   1310 C CB  . TYR   A 1 162 ? 18.25904 5.94149   -15.00730 1.000 70.13191  ? 159 TYR   A CB  1 
ATOM   1311 C CG  . TYR   A 1 162 ? 18.86677 5.47269   -16.30988 1.000 67.46417  ? 159 TYR   A CG  1 
ATOM   1312 C CD1 . TYR   A 1 162 ? 19.25867 4.15020   -16.47822 1.000 66.14978  ? 159 TYR   A CD1 1 
ATOM   1313 C CD2 . TYR   A 1 162 ? 19.04082 6.34881   -17.37395 1.000 73.37537  ? 159 TYR   A CD2 1 
ATOM   1314 C CE1 . TYR   A 1 162 ? 19.81157 3.71384   -17.66713 1.000 73.40104  ? 159 TYR   A CE1 1 
ATOM   1315 C CE2 . TYR   A 1 162 ? 19.59136 5.92170   -18.56816 1.000 62.20916  ? 159 TYR   A CE2 1 
ATOM   1316 C CZ  . TYR   A 1 162 ? 19.97573 4.60310   -18.70894 1.000 73.04847  ? 159 TYR   A CZ  1 
ATOM   1317 O OH  . TYR   A 1 162 ? 20.52548 4.17124   -19.89472 1.000 67.91971  ? 159 TYR   A OH  1 
HETATM 1318 N N   . TPO   A 1 163 ? 17.91551 5.87858   -12.15147 1.000 70.48838  ? 160 TPO   A N   1 
HETATM 1319 C CA  . TPO   A 1 163 ? 17.64229 6.32901   -10.78760 1.000 70.14406  ? 160 TPO   A CA  1 
HETATM 1320 C CB  . TPO   A 1 163 ? 18.93389 6.79795   -10.07844 1.000 71.75418  ? 160 TPO   A CB  1 
HETATM 1321 C CG2 . TPO   A 1 163 ? 18.66393 7.25533   -8.64766  1.000 62.98378  ? 160 TPO   A CG2 1 
HETATM 1322 O OG1 . TPO   A 1 163 ? 19.85728 5.73830   -10.06439 1.000 76.43027  ? 160 TPO   A OG1 1 
HETATM 1323 P P   . TPO   A 1 163 ? 21.35784 5.92989   -10.87567 1.000 68.79486  ? 160 TPO   A P   1 
HETATM 1324 O O1P . TPO   A 1 163 ? 22.03259 4.60586   -10.53190 1.000 78.90590  ? 160 TPO   A O1P 1 
HETATM 1325 O O2P . TPO   A 1 163 ? 20.98001 6.10014   -12.34657 1.000 65.46482  ? 160 TPO   A O2P 1 
HETATM 1326 O O3P . TPO   A 1 163 ? 22.00756 7.16706   -10.25211 1.000 65.26654  ? 160 TPO   A O3P 1 
HETATM 1327 C C   . TPO   A 1 163 ? 16.61748 7.45992   -10.76007 1.000 70.48503  ? 160 TPO   A C   1 
HETATM 1328 O O   . TPO   A 1 163 ? 16.73834 8.44350   -11.49092 1.000 72.69089  ? 160 TPO   A O   1 
ATOM   1329 N N   . HIS   A 1 164 ? 15.60835 7.30360   -9.90974  1.000 62.85593  ? 161 HIS   A N   1 
ATOM   1330 C CA  . HIS   A 1 164 ? 14.53973 8.28564   -9.77189  1.000 85.01366  ? 161 HIS   A CA  1 
ATOM   1331 C C   . HIS   A 1 164 ? 14.94503 9.45326   -8.87262  1.000 86.98998  ? 161 HIS   A C   1 
ATOM   1332 O O   . HIS   A 1 164 ? 15.87846 9.33982   -8.07525  1.000 84.22470  ? 161 HIS   A O   1 
ATOM   1333 C CB  . HIS   A 1 164 ? 13.28305 7.61499   -9.21279  1.000 82.05908  ? 161 HIS   A CB  1 
ATOM   1334 C CG  . HIS   A 1 164 ? 13.45818 7.06620   -7.83039  1.000 92.60089  ? 161 HIS   A CG  1 
ATOM   1335 N ND1 . HIS   A 1 164 ? 13.05738 7.74904   -6.70213  1.000 98.21144  ? 161 HIS   A ND1 1 
ATOM   1336 C CD2 . HIS   A 1 164 ? 13.99989 5.90445   -7.39373  1.000 97.35064  ? 161 HIS   A CD2 1 
ATOM   1337 C CE1 . HIS   A 1 164 ? 13.33855 7.02943   -5.63056  1.000 99.23750  ? 161 HIS   A CE1 1 
ATOM   1338 N NE2 . HIS   A 1 164 ? 13.91096 5.90545   -6.02258  1.000 107.14948 ? 161 HIS   A NE2 1 
ATOM   1339 N N   . GLU   A 1 165 ? 14.22828 10.57147  -9.01473  1.000 96.11554  ? 162 GLU   A N   1 
ATOM   1340 C CA  . GLU   A 1 165 ? 14.40142 11.75107  -8.16281  1.000 94.11902  ? 162 GLU   A CA  1 
ATOM   1341 C C   . GLU   A 1 165 ? 15.84021 12.26708  -8.20444  1.000 82.91476  ? 162 GLU   A C   1 
ATOM   1342 O O   . GLU   A 1 165 ? 16.49002 12.45736  -7.17426  1.000 105.73123 ? 162 GLU   A O   1 
ATOM   1343 C CB  . GLU   A 1 165 ? 13.96265 11.45814  -6.72532  1.000 87.46806  ? 162 GLU   A CB  1 
ATOM   1344 C CG  . GLU   A 1 165 ? 12.50799 11.03667  -6.59682  1.000 89.88691  ? 162 GLU   A CG  1 
ATOM   1345 C CD  . GLU   A 1 165 ? 12.10764 10.75340  -5.16242  1.000 111.37417 ? 162 GLU   A CD  1 
ATOM   1346 O OE1 . GLU   A 1 165 ? 12.81125 11.22342  -4.24355  1.000 120.20708 ? 162 GLU   A OE1 1 
ATOM   1347 O OE2 . GLU   A 1 165 ? 11.09153 10.05727  -4.95378  1.000 117.90182 ? 162 GLU   A OE2 1 
ATOM   1348 N N   . VAL   A 1 166 ? 16.33652 12.49532  -9.41826  1.000 75.48648  ? 163 VAL   A N   1 
ATOM   1349 C CA  . VAL   A 1 166 ? 17.66701 13.05737  -9.61951  1.000 74.62337  ? 163 VAL   A CA  1 
ATOM   1350 C C   . VAL   A 1 166 ? 17.54731 14.56937  -9.76015  1.000 67.75195  ? 163 VAL   A C   1 
ATOM   1351 O O   . VAL   A 1 166 ? 16.43509 15.10826  -9.81031  1.000 70.42896  ? 163 VAL   A O   1 
ATOM   1352 C CB  . VAL   A 1 166 ? 18.35495 12.43500  -10.84845 1.000 71.63373  ? 163 VAL   A CB  1 
ATOM   1353 C CG1 . VAL   A 1 166 ? 18.70467 10.97939  -10.57820 1.000 75.16501  ? 163 VAL   A CG1 1 
ATOM   1354 C CG2 . VAL   A 1 166 ? 17.45627 12.54786  -12.07047 1.000 48.06764  ? 163 VAL   A CG2 1 
ATOM   1355 N N   . VAL   A 1 167 ? 18.69434 15.25480  -9.81865  1.000 55.99981  ? 164 VAL   A N   1 
ATOM   1356 C CA  . VAL   A 1 167 ? 18.79809 16.70681  -9.97969  1.000 64.02245  ? 164 VAL   A CA  1 
ATOM   1357 C C   . VAL   A 1 167 ? 18.30053 17.43068  -8.73142  1.000 56.21089  ? 164 VAL   A C   1 
ATOM   1358 O O   . VAL   A 1 167 ? 17.28481 17.04978  -8.13788  1.000 49.58863  ? 164 VAL   A O   1 
ATOM   1359 C CB  . VAL   A 1 167 ? 18.04266 17.20114  -11.23163 1.000 54.99678  ? 164 VAL   A CB  1 
ATOM   1360 C CG1 . VAL   A 1 167 ? 18.33830 18.67227  -11.48161 1.000 55.03749  ? 164 VAL   A CG1 1 
ATOM   1361 C CG2 . VAL   A 1 167 ? 18.40163 16.36370  -12.45763 1.000 55.12729  ? 164 VAL   A CG2 1 
ATOM   1362 N N   . THR   A 1 168 ? 19.01796 18.47999  -8.32642  1.000 53.04482  ? 165 THR   A N   1 
ATOM   1363 C CA  . THR   A 1 168 ? 18.56082 19.33487  -7.23722  1.000 49.36849  ? 165 THR   A CA  1 
ATOM   1364 C C   . THR   A 1 168 ? 17.17857 19.89769  -7.55892  1.000 54.14934  ? 165 THR   A C   1 
ATOM   1365 O O   . THR   A 1 168 ? 16.83764 20.13800  -8.72058  1.000 55.86006  ? 165 THR   A O   1 
ATOM   1366 C CB  . THR   A 1 168 ? 19.56187 20.47000  -6.99968  1.000 56.39582  ? 165 THR   A CB  1 
ATOM   1367 O OG1 . THR   A 1 168 ? 20.88146 19.92244  -6.88502  1.000 58.23123  ? 165 THR   A OG1 1 
ATOM   1368 C CG2 . THR   A 1 168 ? 19.23195 21.23736  -5.72310  1.000 47.76805  ? 165 THR   A CG2 1 
ATOM   1369 N N   . LEU   A 1 169 ? 16.38450 20.11580  -6.50708  1.000 44.43489  ? 166 LEU   A N   1 
ATOM   1370 C CA  . LEU   A 1 169 ? 14.95338 20.36337  -6.67431  1.000 53.34327  ? 166 LEU   A CA  1 
ATOM   1371 C C   . LEU   A 1 169 ? 14.67888 21.57932  -7.55701  1.000 57.47192  ? 166 LEU   A C   1 
ATOM   1372 O O   . LEU   A 1 169 ? 13.82943 21.52592  -8.45486  1.000 48.18333  ? 166 LEU   A O   1 
ATOM   1373 C CB  . LEU   A 1 169 ? 14.29765 20.53132  -5.30521  1.000 47.04542  ? 166 LEU   A CB  1 
ATOM   1374 C CG  . LEU   A 1 169 ? 12.77285 20.61281  -5.30614  1.000 55.86422  ? 166 LEU   A CG  1 
ATOM   1375 C CD1 . LEU   A 1 169 ? 12.17989 19.38422  -5.97591  1.000 50.11514  ? 166 LEU   A CD1 1 
ATOM   1376 C CD2 . LEU   A 1 169 ? 12.24902 20.76385  -3.88821  1.000 49.56064  ? 166 LEU   A CD2 1 
ATOM   1377 N N   . TRP   A 1 170 ? 15.38936 22.68664  -7.31992  1.000 48.12098  ? 167 TRP   A N   1 
ATOM   1378 C CA  . TRP   A 1 170 ? 15.11483 23.92035  -8.05367  1.000 45.29325  ? 167 TRP   A CA  1 
ATOM   1379 C C   . TRP   A 1 170 ? 15.35295 23.78184  -9.55218  1.000 51.16976  ? 167 TRP   A C   1 
ATOM   1380 O O   . TRP   A 1 170 ? 14.75881 24.53129  -10.33574 1.000 46.03258  ? 167 TRP   A O   1 
ATOM   1381 C CB  . TRP   A 1 170 ? 15.97129 25.06484  -7.51156  1.000 46.14526  ? 167 TRP   A CB  1 
ATOM   1382 C CG  . TRP   A 1 170 ? 15.55355 25.56081  -6.16501  1.000 52.51430  ? 167 TRP   A CG  1 
ATOM   1383 C CD1 . TRP   A 1 170 ? 14.57651 25.04488  -5.36398  1.000 49.72893  ? 167 TRP   A CD1 1 
ATOM   1384 C CD2 . TRP   A 1 170 ? 16.09921 26.68296  -5.46187  1.000 51.62606  ? 167 TRP   A CD2 1 
ATOM   1385 N NE1 . TRP   A 1 170 ? 14.48301 25.77499  -4.20308  1.000 54.77389  ? 167 TRP   A NE1 1 
ATOM   1386 C CE2 . TRP   A 1 170 ? 15.40765 26.78626  -4.23922  1.000 55.81980  ? 167 TRP   A CE2 1 
ATOM   1387 C CE3 . TRP   A 1 170 ? 17.10779 27.60931  -5.74792  1.000 51.81409  ? 167 TRP   A CE3 1 
ATOM   1388 C CZ2 . TRP   A 1 170 ? 15.69050 27.77972  -3.30436  1.000 56.53350  ? 167 TRP   A CZ2 1 
ATOM   1389 C CZ3 . TRP   A 1 170 ? 17.38609 28.59263  -4.82083  1.000 57.60834  ? 167 TRP   A CZ3 1 
ATOM   1390 C CH2 . TRP   A 1 170 ? 16.68114 28.67030  -3.61330  1.000 59.35607  ? 167 TRP   A CH2 1 
ATOM   1391 N N   . TYR   A 1 171 ? 16.20119 22.84400  -9.96899  1.000 38.74234  ? 168 TYR   A N   1 
ATOM   1392 C CA  . TYR   A 1 171 ? 16.56328 22.67597  -11.36965 1.000 47.63031  ? 168 TYR   A CA  1 
ATOM   1393 C C   . TYR   A 1 171 ? 16.07170 21.34718  -11.93479 1.000 48.58062  ? 168 TYR   A C   1 
ATOM   1394 O O   . TYR   A 1 171 ? 16.57564 20.88629  -12.96447 1.000 43.14244  ? 168 TYR   A O   1 
ATOM   1395 C CB  . TYR   A 1 171 ? 18.07896 22.82014  -11.52291 1.000 43.21169  ? 168 TYR   A CB  1 
ATOM   1396 C CG  . TYR   A 1 171 ? 18.58355 24.07588  -10.84860 1.000 49.16759  ? 168 TYR   A CG  1 
ATOM   1397 C CD1 . TYR   A 1 171 ? 18.54962 25.29904  -11.50486 1.000 45.69515  ? 168 TYR   A CD1 1 
ATOM   1398 C CD2 . TYR   A 1 171 ? 19.05395 24.04685  -9.54125  1.000 44.32339  ? 168 TYR   A CD2 1 
ATOM   1399 C CE1 . TYR   A 1 171 ? 18.98507 26.45398  -10.88746 1.000 51.47293  ? 168 TYR   A CE1 1 
ATOM   1400 C CE2 . TYR   A 1 171 ? 19.49144 25.20064  -8.91316  1.000 48.47596  ? 168 TYR   A CE2 1 
ATOM   1401 C CZ  . TYR   A 1 171 ? 19.45260 26.39969  -9.59149  1.000 52.37024  ? 168 TYR   A CZ  1 
ATOM   1402 O OH  . TYR   A 1 171 ? 19.88799 27.54961  -8.97678  1.000 54.29709  ? 168 TYR   A OH  1 
ATOM   1403 N N   . ARG   A 1 172 ? 15.08161 20.73550  -11.28846 1.000 39.19140  ? 169 ARG   A N   1 
ATOM   1404 C CA  . ARG   A 1 172 ? 14.58816 19.41968  -11.67006 1.000 47.51980  ? 169 ARG   A CA  1 
ATOM   1405 C C   . ARG   A 1 172 ? 13.47856 19.55416  -12.70637 1.000 42.42874  ? 169 ARG   A C   1 
ATOM   1406 O O   . ARG   A 1 172 ? 12.54213 20.33977  -12.52757 1.000 45.61212  ? 169 ARG   A O   1 
ATOM   1407 C CB  . ARG   A 1 172 ? 14.07903 18.66262  -10.44140 1.000 46.18297  ? 169 ARG   A CB  1 
ATOM   1408 C CG  . ARG   A 1 172 ? 13.68873 17.21805  -10.72157 1.000 49.08817  ? 169 ARG   A CG  1 
ATOM   1409 C CD  . ARG   A 1 172 ? 13.25852 16.50622  -9.45184  1.000 48.87977  ? 169 ARG   A CD  1 
ATOM   1410 N NE  . ARG   A 1 172 ? 14.26965 16.59573  -8.40612  1.000 47.75648  ? 169 ARG   A NE  1 
ATOM   1411 C CZ  . ARG   A 1 172 ? 14.08834 16.19537  -7.15535  1.000 60.65177  ? 169 ARG   A CZ  1 
ATOM   1412 N NH1 . ARG   A 1 172 ? 12.94880 15.65014  -6.76329  1.000 44.48668  ? 169 ARG   A NH1 1 
ATOM   1413 N NH2 . ARG   A 1 172 ? 15.07310 16.35129  -6.27479  1.000 51.05717  ? 169 ARG   A NH2 1 
ATOM   1414 N N   . ALA   A 1 173 ? 13.58462 18.77570  -13.77950 1.000 46.38053  ? 170 ALA   A N   1 
ATOM   1415 C CA  . ALA   A 1 173 ? 12.63587 18.86448  -14.87510 1.000 39.14912  ? 170 ALA   A CA  1 
ATOM   1416 C C   . ALA   A 1 173 ? 11.25443 18.37613  -14.43604 1.000 48.68190  ? 170 ALA   A C   1 
ATOM   1417 O O   . ALA   A 1 173 ? 11.13624 17.57390  -13.50538 1.000 51.06499  ? 170 ALA   A O   1 
ATOM   1418 C CB  . ALA   A 1 173 ? 13.13045 18.04601  -16.06414 1.000 45.81031  ? 170 ALA   A CB  1 
ATOM   1419 N N   . PRO   A 1 174 ? 10.18830 18.84990  -15.09013 1.000 48.52364  ? 171 PRO   A N   1 
ATOM   1420 C CA  . PRO   A 1 174 ? 8.84297  18.42869  -14.67306 1.000 42.76994  ? 171 PRO   A CA  1 
ATOM   1421 C C   . PRO   A 1 174 ? 8.56527  16.95603  -14.91927 1.000 51.24173  ? 171 PRO   A C   1 
ATOM   1422 O O   . PRO   A 1 174 ? 7.76475  16.36493  -14.18416 1.000 48.38776  ? 171 PRO   A O   1 
ATOM   1423 C CB  . PRO   A 1 174 ? 7.91863  19.32751  -15.50724 1.000 51.54838  ? 171 PRO   A CB  1 
ATOM   1424 C CG  . PRO   A 1 174 ? 8.73307  19.69000  -16.70458 1.000 43.68093  ? 171 PRO   A CG  1 
ATOM   1425 C CD  . PRO   A 1 174 ? 10.14218 19.81633  -16.20186 1.000 45.86321  ? 171 PRO   A CD  1 
ATOM   1426 N N   . GLU   A 1 175 ? 9.19617  16.33899  -15.92403 1.000 45.65547  ? 172 GLU   A N   1 
ATOM   1427 C CA  . GLU   A 1 175 ? 8.96807  14.91412  -16.14603 1.000 53.24848  ? 172 GLU   A CA  1 
ATOM   1428 C C   . GLU   A 1 175 ? 9.52182  14.07526  -15.00133 1.000 53.05716  ? 172 GLU   A C   1 
ATOM   1429 O O   . GLU   A 1 175 ? 8.97672  13.00730  -14.70072 1.000 53.53535  ? 172 GLU   A O   1 
ATOM   1430 C CB  . GLU   A 1 175 ? 9.57486  14.46601  -17.47806 1.000 49.71976  ? 172 GLU   A CB  1 
ATOM   1431 C CG  . GLU   A 1 175 ? 11.08551 14.62411  -17.58458 1.000 51.23304  ? 172 GLU   A CG  1 
ATOM   1432 C CD  . GLU   A 1 175 ? 11.49058 15.95934  -18.17277 1.000 49.92213  ? 172 GLU   A CD  1 
ATOM   1433 O OE1 . GLU   A 1 175 ? 10.69579 16.91739  -18.07627 1.000 50.53775  ? 172 GLU   A OE1 1 
ATOM   1434 O OE2 . GLU   A 1 175 ? 12.60250 16.05010  -18.73750 1.000 44.83336  ? 172 GLU   A OE2 1 
ATOM   1435 N N   . ILE   A 1 176 ? 10.58995 14.54030  -14.34787 1.000 47.48986  ? 173 ILE   A N   1 
ATOM   1436 C CA  . ILE   A 1 176 ? 11.08918 13.84740  -13.16427 1.000 45.26568  ? 173 ILE   A CA  1 
ATOM   1437 C C   . ILE   A 1 176 ? 10.11744 14.01462  -12.00300 1.000 51.63564  ? 173 ILE   A C   1 
ATOM   1438 O O   . ILE   A 1 176 ? 9.81503  13.05364  -11.28476 1.000 51.21773  ? 173 ILE   A O   1 
ATOM   1439 C CB  . ILE   A 1 176 ? 12.49686 14.35121  -12.79754 1.000 41.43842  ? 173 ILE   A CB  1 
ATOM   1440 C CG1 . ILE   A 1 176 ? 13.44317 14.22157  -13.99229 1.000 48.22623  ? 173 ILE   A CG1 1 
ATOM   1441 C CG2 . ILE   A 1 176 ? 13.04175 13.58333  -11.59966 1.000 46.23654  ? 173 ILE   A CG2 1 
ATOM   1442 C CD1 . ILE   A 1 176 ? 13.62373 12.80172  -14.47567 1.000 58.89116  ? 173 ILE   A CD1 1 
ATOM   1443 N N   . LEU   A 1 177 ? 9.60874  15.23459  -11.80335 1.000 46.30275  ? 174 LEU   A N   1 
ATOM   1444 C CA  . LEU   A 1 177 ? 8.67653  15.48360  -10.70720 1.000 50.97541  ? 174 LEU   A CA  1 
ATOM   1445 C C   . LEU   A 1 177 ? 7.37421  14.71128  -10.88178 1.000 56.27422  ? 174 LEU   A C   1 
ATOM   1446 O O   . LEU   A 1 177 ? 6.70030  14.40391  -9.89296  1.000 53.79881  ? 174 LEU   A O   1 
ATOM   1447 C CB  . LEU   A 1 177 ? 8.38959  16.98074  -10.59545 1.000 57.21232  ? 174 LEU   A CB  1 
ATOM   1448 C CG  . LEU   A 1 177 ? 9.56793  17.89084  -10.25164 1.000 49.97956  ? 174 LEU   A CG  1 
ATOM   1449 C CD1 . LEU   A 1 177 ? 9.21868  19.33648  -10.55132 1.000 47.66486  ? 174 LEU   A CD1 1 
ATOM   1450 C CD2 . LEU   A 1 177 ? 9.94091  17.72584  -8.78648  1.000 52.90293  ? 174 LEU   A CD2 1 
ATOM   1451 N N   . LEU   A 1 178 ? 6.99805  14.39687  -12.11981 1.000 62.35370  ? 175 LEU   A N   1 
ATOM   1452 C CA  . LEU   A 1 178 ? 5.78751  13.63215  -12.38796 1.000 58.71759  ? 175 LEU   A CA  1 
ATOM   1453 C C   . LEU   A 1 178 ? 6.03526  12.13005  -12.45236 1.000 65.24241  ? 175 LEU   A C   1 
ATOM   1454 O O   . LEU   A 1 178 ? 5.09378  11.37307  -12.71127 1.000 64.87856  ? 175 LEU   A O   1 
ATOM   1455 C CB  . LEU   A 1 178 ? 5.13732  14.10831  -13.69124 1.000 62.99818  ? 175 LEU   A CB  1 
ATOM   1456 C CG  . LEU   A 1 178 ? 4.44837  15.47306  -13.62840 1.000 67.19069  ? 175 LEU   A CG  1 
ATOM   1457 C CD1 . LEU   A 1 178 ? 3.96066  15.89759  -15.00171 1.000 61.54082  ? 175 LEU   A CD1 1 
ATOM   1458 C CD2 . LEU   A 1 178 ? 3.29339  15.43550  -12.64420 1.000 52.01499  ? 175 LEU   A CD2 1 
ATOM   1459 N N   . GLY   A 1 179 ? 7.27127  11.68477  -12.23504 1.000 63.03957  ? 176 GLY   A N   1 
ATOM   1460 C CA  . GLY   A 1 179 ? 7.56875  10.27012  -12.11402 1.000 63.16884  ? 176 GLY   A CA  1 
ATOM   1461 C C   . GLY   A 1 179 ? 7.64302  9.50126   -13.41767 1.000 60.37110  ? 176 GLY   A C   1 
ATOM   1462 O O   . GLY   A 1 179 ? 7.06937  8.41467   -13.53052 1.000 69.83790  ? 176 GLY   A O   1 
ATOM   1463 N N   . CYS   A 1 180 ? 8.35181  10.04121  -14.40488 1.000 53.54884  ? 177 CYS   A N   1 
ATOM   1464 C CA  . CYS   A 1 180 ? 8.51869  9.34157   -15.67122 1.000 64.71899  ? 177 CYS   A CA  1 
ATOM   1465 C C   . CYS   A 1 180 ? 9.38551  8.09951   -15.49284 1.000 63.58214  ? 177 CYS   A C   1 
ATOM   1466 O O   . CYS   A 1 180 ? 10.32750 8.08644   -14.69583 1.000 58.10520  ? 177 CYS   A O   1 
ATOM   1467 C CB  . CYS   A 1 180 ? 9.14302  10.27004  -16.71229 1.000 62.09641  ? 177 CYS   A CB  1 
ATOM   1468 S SG  . CYS   A 1 180 ? 10.77613 10.89819  -16.25074 1.000 68.92128  ? 177 CYS   A SG  1 
ATOM   1469 N N   . LYS   A 1 181 ? 9.05848  7.04646   -16.24487 1.000 65.86317  ? 178 LYS   A N   1 
ATOM   1470 C CA  . LYS   A 1 181 ? 9.84672  5.81854   -16.18913 1.000 67.70084  ? 178 LYS   A CA  1 
ATOM   1471 C C   . LYS   A 1 181 ? 11.23987 6.03551   -16.76763 1.000 65.66569  ? 178 LYS   A C   1 
ATOM   1472 O O   . LYS   A 1 181 ? 12.25114 5.80167   -16.09526 1.000 75.07298  ? 178 LYS   A O   1 
ATOM   1473 C CB  . LYS   A 1 181 ? 9.12595  4.69365   -16.93477 1.000 72.35871  ? 178 LYS   A CB  1 
ATOM   1474 C CG  . LYS   A 1 181 ? 8.02242  4.01578   -16.14062 1.000 89.07156  ? 178 LYS   A CG  1 
ATOM   1475 C CD  . LYS   A 1 181 ? 7.32209  2.95058   -16.97149 1.000 95.51080  ? 178 LYS   A CD  1 
ATOM   1476 C CE  . LYS   A 1 181 ? 8.31979  1.98414   -17.59332 1.000 100.41181 ? 178 LYS   A CE  1 
ATOM   1477 N NZ  . LYS   A 1 181 ? 9.15186  1.29417   -16.56950 1.000 95.86818  ? 178 LYS   A NZ  1 
ATOM   1478 N N   . TYR   A 1 182 ? 11.31121 6.48015   -18.01780 1.000 61.53710  ? 179 TYR   A N   1 
ATOM   1479 C CA  . TYR   A 1 182 ? 12.57329 6.71455   -18.69972 1.000 65.37492  ? 179 TYR   A CA  1 
ATOM   1480 C C   . TYR   A 1 182 ? 12.83802 8.20905   -18.81568 1.000 71.14113  ? 179 TYR   A C   1 
ATOM   1481 O O   . TYR   A 1 182 ? 11.90928 9.02038   -18.86663 1.000 78.60352  ? 179 TYR   A O   1 
ATOM   1482 C CB  . TYR   A 1 182 ? 12.57545 6.09268   -20.10046 1.000 63.15426  ? 179 TYR   A CB  1 
ATOM   1483 C CG  . TYR   A 1 182 ? 12.06318 4.67257   -20.15903 1.000 68.34603  ? 179 TYR   A CG  1 
ATOM   1484 C CD1 . TYR   A 1 182 ? 12.75474 3.63698   -19.54420 1.000 64.20907  ? 179 TYR   A CD1 1 
ATOM   1485 C CD2 . TYR   A 1 182 ? 10.89717 4.36453   -20.84771 1.000 71.41616  ? 179 TYR   A CD2 1 
ATOM   1486 C CE1 . TYR   A 1 182 ? 12.29227 2.33619   -19.60285 1.000 73.84255  ? 179 TYR   A CE1 1 
ATOM   1487 C CE2 . TYR   A 1 182 ? 10.42702 3.06698   -20.91243 1.000 71.06802  ? 179 TYR   A CE2 1 
ATOM   1488 C CZ  . TYR   A 1 182 ? 11.12855 2.05642   -20.28894 1.000 76.88958  ? 179 TYR   A CZ  1 
ATOM   1489 O OH  . TYR   A 1 182 ? 10.66406 0.76252   -20.35102 1.000 77.37314  ? 179 TYR   A OH  1 
ATOM   1490 N N   . TYR   A 1 183 ? 14.11930 8.56468   -18.85925 1.000 65.29110  ? 180 TYR   A N   1 
ATOM   1491 C CA  . TYR   A 1 183 ? 14.52166 9.93518   -19.13327 1.000 69.73118  ? 180 TYR   A CA  1 
ATOM   1492 C C   . TYR   A 1 183 ? 15.92119 9.91998   -19.72530 1.000 57.85038  ? 180 TYR   A C   1 
ATOM   1493 O O   . TYR   A 1 183 ? 16.66934 8.95023   -19.57519 1.000 64.53920  ? 180 TYR   A O   1 
ATOM   1494 C CB  . TYR   A 1 183 ? 14.46934 10.81365  -17.87454 1.000 67.99088  ? 180 TYR   A CB  1 
ATOM   1495 C CG  . TYR   A 1 183 ? 15.41187 10.39963  -16.76438 1.000 66.54145  ? 180 TYR   A CG  1 
ATOM   1496 C CD1 . TYR   A 1 183 ? 16.72865 10.84489  -16.73986 1.000 55.60170  ? 180 TYR   A CD1 1 
ATOM   1497 C CD2 . TYR   A 1 183 ? 14.97873 9.58181   -15.72986 1.000 63.46559  ? 180 TYR   A CD2 1 
ATOM   1498 C CE1 . TYR   A 1 183 ? 17.58881 10.47437  -15.72687 1.000 66.67216  ? 180 TYR   A CE1 1 
ATOM   1499 C CE2 . TYR   A 1 183 ? 15.83258 9.20819   -14.70984 1.000 58.98017  ? 180 TYR   A CE2 1 
ATOM   1500 C CZ  . TYR   A 1 183 ? 17.13568 9.65731   -14.71333 1.000 61.41581  ? 180 TYR   A CZ  1 
ATOM   1501 O OH  . TYR   A 1 183 ? 17.99028 9.28805   -13.70011 1.000 61.08158  ? 180 TYR   A OH  1 
ATOM   1502 N N   . SER   A 1 184 ? 16.26824 11.00976  -20.40632 1.000 55.13052  ? 181 SER   A N   1 
ATOM   1503 C CA  . SER   A 1 184 ? 17.59857 11.12182  -20.98981 1.000 66.78328  ? 181 SER   A CA  1 
ATOM   1504 C C   . SER   A 1 184 ? 18.08984 12.56407  -20.97997 1.000 56.76566  ? 181 SER   A C   1 
ATOM   1505 O O   . SER   A 1 184 ? 18.09326 13.21974  -19.93313 1.000 59.92283  ? 181 SER   A O   1 
ATOM   1506 C CB  . SER   A 1 184 ? 17.61138 10.56418  -22.41612 1.000 63.09956  ? 181 SER   A CB  1 
ATOM   1507 O OG  . SER   A 1 184 ? 16.83526 11.36423  -23.29037 1.000 73.61909  ? 181 SER   A OG  1 
ATOM   1508 N N   . THR   A 1 185 ? 18.49299 13.06595  -22.14909 1.000 57.85589  ? 182 THR   A N   1 
ATOM   1509 C CA  . THR   A 1 185 ? 19.22737 14.32377  -22.22851 1.000 52.63642  ? 182 THR   A CA  1 
ATOM   1510 C C   . THR   A 1 185 ? 18.36817 15.54385  -21.92531 1.000 48.30635  ? 182 THR   A C   1 
ATOM   1511 O O   . THR   A 1 185 ? 18.91918 16.60624  -21.61907 1.000 55.09596  ? 182 THR   A O   1 
ATOM   1512 C CB  . THR   A 1 185 ? 19.85227 14.47117  -23.61501 1.000 50.40738  ? 182 THR   A CB  1 
ATOM   1513 O OG1 . THR   A 1 185 ? 18.82249 14.42622  -24.61036 1.000 55.73918  ? 182 THR   A OG1 1 
ATOM   1514 C CG2 . THR   A 1 185 ? 20.84384 13.34474  -23.87048 1.000 52.26465  ? 182 THR   A CG2 1 
ATOM   1515 N N   . ALA   A 1 186 ? 17.04125 15.42353  -21.99752 1.000 49.08007  ? 183 ALA   A N   1 
ATOM   1516 C CA  . ALA   A 1 186 ? 16.18499 16.58869  -21.80561 1.000 47.63458  ? 183 ALA   A CA  1 
ATOM   1517 C C   . ALA   A 1 186 ? 16.25973 17.15232  -20.39081 1.000 52.10965  ? 183 ALA   A C   1 
ATOM   1518 O O   . ALA   A 1 186 ? 15.97523 18.33976  -20.19959 1.000 46.38290  ? 183 ALA   A O   1 
ATOM   1519 C CB  . ALA   A 1 186 ? 14.73635 16.24177  -22.14870 1.000 43.32583  ? 183 ALA   A CB  1 
ATOM   1520 N N   . VAL   A 1 187 ? 16.64144 16.34207  -19.39896 1.000 46.88089  ? 184 VAL   A N   1 
ATOM   1521 C CA  . VAL   A 1 187 ? 16.65427 16.83795  -18.02518 1.000 47.32380  ? 184 VAL   A CA  1 
ATOM   1522 C C   . VAL   A 1 187 ? 17.77298 17.85396  -17.81962 1.000 44.68741  ? 184 VAL   A C   1 
ATOM   1523 O O   . VAL   A 1 187 ? 17.63387 18.78033  -17.01164 1.000 46.63235  ? 184 VAL   A O   1 
ATOM   1524 C CB  . VAL   A 1 187 ? 16.75544 15.67081  -17.02268 1.000 55.06051  ? 184 VAL   A CB  1 
ATOM   1525 C CG1 . VAL   A 1 187 ? 15.59200 14.70394  -17.21207 1.000 49.14484  ? 184 VAL   A CG1 1 
ATOM   1526 C CG2 . VAL   A 1 187 ? 18.08712 14.94772  -17.15809 1.000 58.67286  ? 184 VAL   A CG2 1 
ATOM   1527 N N   . ASP   A 1 188 ? 18.88899 17.71204  -18.54174 1.000 47.71348  ? 185 ASP   A N   1 
ATOM   1528 C CA  . ASP   A 1 188 ? 19.97410 18.68168  -18.42303 1.000 50.89459  ? 185 ASP   A CA  1 
ATOM   1529 C C   . ASP   A 1 188 ? 19.62758 20.00199  -19.10001 1.000 47.79681  ? 185 ASP   A C   1 
ATOM   1530 O O   . ASP   A 1 188 ? 20.04026 21.06611  -18.62381 1.000 49.33055  ? 185 ASP   A O   1 
ATOM   1531 C CB  . ASP   A 1 188 ? 21.26513 18.11455  -19.01814 1.000 50.15280  ? 185 ASP   A CB  1 
ATOM   1532 C CG  . ASP   A 1 188 ? 21.83224 16.96347  -18.20668 1.000 49.62791  ? 185 ASP   A CG  1 
ATOM   1533 O OD1 . ASP   A 1 188 ? 21.52879 16.86979  -16.99688 1.000 45.46201  ? 185 ASP   A OD1 1 
ATOM   1534 O OD2 . ASP   A 1 188 ? 22.59373 16.15533  -18.78165 1.000 47.85877  ? 185 ASP   A OD2 1 
ATOM   1535 N N   . ILE   A 1 189 ? 18.88598 19.95498  -20.21035 1.000 45.14435  ? 186 ILE   A N   1 
ATOM   1536 C CA  . ILE   A 1 189 ? 18.49701 21.18234  -20.89959 1.000 41.52992  ? 186 ILE   A CA  1 
ATOM   1537 C C   . ILE   A 1 189 ? 17.55574 22.00945  -20.03147 1.000 47.76586  ? 186 ILE   A C   1 
ATOM   1538 O O   . ILE   A 1 189 ? 17.65612 23.24214  -19.98619 1.000 48.10402  ? 186 ILE   A O   1 
ATOM   1539 C CB  . ILE   A 1 189 ? 17.86872 20.85233  -22.26521 1.000 45.00265  ? 186 ILE   A CB  1 
ATOM   1540 C CG1 . ILE   A 1 189 ? 18.88855 20.15314  -23.16338 1.000 55.38625  ? 186 ILE   A CG1 1 
ATOM   1541 C CG2 . ILE   A 1 189 ? 17.35820 22.11587  -22.93966 1.000 46.00159  ? 186 ILE   A CG2 1 
ATOM   1542 C CD1 . ILE   A 1 189 ? 20.05778 21.03168  -23.54783 1.000 55.80287  ? 186 ILE   A CD1 1 
ATOM   1543 N N   . TRP   A 1 190 ? 16.62766 21.34974  -19.33092 1.000 40.53767  ? 187 TRP   A N   1 
ATOM   1544 C CA  . TRP   A 1 190 ? 15.75180 22.06200  -18.40481 1.000 45.82121  ? 187 TRP   A CA  1 
ATOM   1545 C C   . TRP   A 1 190 ? 16.56148 22.79046  -17.34073 1.000 44.78625  ? 187 TRP   A C   1 
ATOM   1546 O O   . TRP   A 1 190 ? 16.34084 23.97936  -17.07986 1.000 42.12385  ? 187 TRP   A O   1 
ATOM   1547 C CB  . TRP   A 1 190 ? 14.76836 21.09174  -17.74985 1.000 42.68924  ? 187 TRP   A CB  1 
ATOM   1548 C CG  . TRP   A 1 190 ? 13.83329 21.76599  -16.78571 1.000 43.48859  ? 187 TRP   A CG  1 
ATOM   1549 C CD1 . TRP   A 1 190 ? 14.06963 22.04688  -15.46879 1.000 43.53579  ? 187 TRP   A CD1 1 
ATOM   1550 C CD2 . TRP   A 1 190 ? 12.51520 22.24841  -17.06712 1.000 45.85811  ? 187 TRP   A CD2 1 
ATOM   1551 N NE1 . TRP   A 1 190 ? 12.97953 22.67419  -14.91487 1.000 43.69182  ? 187 TRP   A NE1 1 
ATOM   1552 C CE2 . TRP   A 1 190 ? 12.01175 22.80947  -15.87598 1.000 44.28475  ? 187 TRP   A CE2 1 
ATOM   1553 C CE3 . TRP   A 1 190 ? 11.71058 22.25895  -18.21046 1.000 48.94603  ? 187 TRP   A CE3 1 
ATOM   1554 C CZ2 . TRP   A 1 190 ? 10.74172 23.37299  -15.79632 1.000 40.70748  ? 187 TRP   A CZ2 1 
ATOM   1555 C CZ3 . TRP   A 1 190 ? 10.44813 22.81992  -18.12765 1.000 52.00569  ? 187 TRP   A CZ3 1 
ATOM   1556 C CH2 . TRP   A 1 190 ? 9.97727  23.36770  -16.92972 1.000 43.67722  ? 187 TRP   A CH2 1 
ATOM   1557 N N   . SER   A 1 191 ? 17.50389 22.08391  -16.71168 1.000 40.57514  ? 188 SER   A N   1 
ATOM   1558 C CA  . SER   A 1 191 ? 18.35695 22.70488  -15.70419 1.000 43.86298  ? 188 SER   A CA  1 
ATOM   1559 C C   . SER   A 1 191 ? 19.08651 23.91486  -16.26997 1.000 46.94401  ? 188 SER   A C   1 
ATOM   1560 O O   . SER   A 1 191 ? 19.17256 24.95938  -15.61463 1.000 47.39018  ? 188 SER   A O   1 
ATOM   1561 C CB  . SER   A 1 191 ? 19.35700 21.68302  -15.16593 1.000 41.22374  ? 188 SER   A CB  1 
ATOM   1562 O OG  . SER   A 1 191 ? 18.69074 20.55123  -14.63632 1.000 47.27024  ? 188 SER   A OG  1 
ATOM   1563 N N   . LEU   A 1 192 ? 19.60525 23.79743  -17.49425 1.000 38.57492  ? 189 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 192 ? 20.31479 24.91477  -18.10376 1.000 45.81138  ? 189 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 192 ? 19.37588 26.06992  -18.41918 1.000 45.09074  ? 189 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 192 ? 19.77813 27.23506  -18.32631 1.000 49.74306  ? 189 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 192 ? 21.03412 24.44866  -19.36656 1.000 41.30947  ? 189 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 192 ? 22.51376 24.80830  -19.43775 1.000 60.45734  ? 189 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 192 ? 23.23052 24.30638  -18.19265 1.000 58.64382  ? 189 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 192 ? 23.13568 24.22599  -20.69358 1.000 59.93306  ? 189 LEU   A CD2 1 
ATOM   1571 N N   . GLY   A 1 193 ? 18.13088 25.77149  -18.79363 1.000 45.69206  ? 190 GLY   A N   1 
ATOM   1572 C CA  . GLY   A 1 193 ? 17.15592 26.83178  -18.98675 1.000 48.40759  ? 190 GLY   A CA  1 
ATOM   1573 C C   . GLY   A 1 193 ? 16.85357 27.57857  -17.70180 1.000 49.51184  ? 190 GLY   A C   1 
ATOM   1574 O O   . GLY   A 1 193 ? 16.70928 28.80371  -17.70293 1.000 46.31224  ? 190 GLY   A O   1 
ATOM   1575 N N   . CYS   A 1 194 ? 16.75405 26.85088  -16.58656 1.000 40.10275  ? 191 CYS   A N   1 
ATOM   1576 C CA  . CYS   A 1 194 ? 16.58732 27.50531  -15.29255 1.000 48.19204  ? 191 CYS   A CA  1 
ATOM   1577 C C   . CYS   A 1 194 ? 17.79927 28.36388  -14.95498 1.000 48.44221  ? 191 CYS   A C   1 
ATOM   1578 O O   . CYS   A 1 194 ? 17.65754 29.48374  -14.44980 1.000 47.73114  ? 191 CYS   A O   1 
ATOM   1579 C CB  . CYS   A 1 194 ? 16.35296 26.46141  -14.20065 1.000 45.25994  ? 191 CYS   A CB  1 
ATOM   1580 S SG  . CYS   A 1 194 ? 14.86141 25.47133  -14.41475 1.000 46.96408  ? 191 CYS   A SG  1 
ATOM   1581 N N   . ILE   A 1 195 ? 19.00074 27.85345  -15.23118 1.000 45.85699  ? 192 ILE   A N   1 
ATOM   1582 C CA  . ILE   A 1 195 ? 20.21843 28.61706  -14.97910 1.000 55.35829  ? 192 ILE   A CA  1 
ATOM   1583 C C   . ILE   A 1 195 ? 20.28328 29.83567  -15.89230 1.000 49.64496  ? 192 ILE   A C   1 
ATOM   1584 O O   . ILE   A 1 195 ? 20.73126 30.91446  -15.48168 1.000 51.93553  ? 192 ILE   A O   1 
ATOM   1585 C CB  . ILE   A 1 195 ? 21.44782 27.70522  -15.14604 1.000 50.00236  ? 192 ILE   A CB  1 
ATOM   1586 C CG1 . ILE   A 1 195 ? 21.44053 26.61602  -14.07070 1.000 52.45159  ? 192 ILE   A CG1 1 
ATOM   1587 C CG2 . ILE   A 1 195 ? 22.73536 28.51196  -15.09335 1.000 49.35228  ? 192 ILE   A CG2 1 
ATOM   1588 C CD1 . ILE   A 1 195 ? 22.48555 25.54542  -14.27793 1.000 57.60168  ? 192 ILE   A CD1 1 
ATOM   1589 N N   . PHE   A 1 196 ? 19.83144 29.68280  -17.14045 1.000 52.55729  ? 193 PHE   A N   1 
ATOM   1590 C CA  . PHE   A 1 196 ? 19.78604 30.80223  -18.07770 1.000 48.54787  ? 193 PHE   A CA  1 
ATOM   1591 C C   . PHE   A 1 196 ? 18.93349 31.93967  -17.52503 1.000 50.17729  ? 193 PHE   A C   1 
ATOM   1592 O O   . PHE   A 1 196 ? 19.39342 33.08324  -17.42067 1.000 50.15245  ? 193 PHE   A O   1 
ATOM   1593 C CB  . PHE   A 1 196 ? 19.24815 30.30904  -19.42624 1.000 45.53611  ? 193 PHE   A CB  1 
ATOM   1594 C CG  . PHE   A 1 196 ? 19.25039 31.34702  -20.52276 1.000 50.32997  ? 193 PHE   A CG  1 
ATOM   1595 C CD1 . PHE   A 1 196 ? 20.04182 32.48319  -20.44348 1.000 55.92598  ? 193 PHE   A CD1 1 
ATOM   1596 C CD2 . PHE   A 1 196 ? 18.45079 31.17399  -21.64333 1.000 52.44298  ? 193 PHE   A CD2 1 
ATOM   1597 C CE1 . PHE   A 1 196 ? 20.03027 33.42757  -21.46017 1.000 54.81243  ? 193 PHE   A CE1 1 
ATOM   1598 C CE2 . PHE   A 1 196 ? 18.43616 32.11266  -22.66162 1.000 53.11441  ? 193 PHE   A CE2 1 
ATOM   1599 C CZ  . PHE   A 1 196 ? 19.22672 33.24049  -22.56894 1.000 46.26508  ? 193 PHE   A CZ  1 
ATOM   1600 N N   . ALA   A 1 197 ? 17.68511 31.63925  -17.15629 1.000 53.46030  ? 194 ALA   A N   1 
ATOM   1601 C CA  . ALA   A 1 197 ? 16.80846 32.66524  -16.60180 1.000 49.79236  ? 194 ALA   A CA  1 
ATOM   1602 C C   . ALA   A 1 197 ? 17.34967 33.21713  -15.29115 1.000 52.95634  ? 194 ALA   A C   1 
ATOM   1603 O O   . ALA   A 1 197 ? 17.15895 34.40076  -14.99045 1.000 58.23376  ? 194 ALA   A O   1 
ATOM   1604 C CB  . ALA   A 1 197 ? 15.40247 32.10203  -16.39684 1.000 55.44288  ? 194 ALA   A CB  1 
ATOM   1605 N N   . GLU   A 1 198 ? 18.02849 32.38189  -14.50199 1.000 48.57099  ? 195 GLU   A N   1 
ATOM   1606 C CA  . GLU   A 1 198 ? 18.57076 32.85327  -13.23478 1.000 58.32977  ? 195 GLU   A CA  1 
ATOM   1607 C C   . GLU   A 1 198 ? 19.69172 33.86217  -13.44961 1.000 61.44864  ? 195 GLU   A C   1 
ATOM   1608 O O   . GLU   A 1 198 ? 19.82896 34.80799  -12.66633 1.000 58.91668  ? 195 GLU   A O   1 
ATOM   1609 C CB  . GLU   A 1 198 ? 19.05859 31.66872  -12.40017 1.000 53.66303  ? 195 GLU   A CB  1 
ATOM   1610 C CG  . GLU   A 1 198 ? 19.20401 31.97755  -10.92143 1.000 55.44006  ? 195 GLU   A CG  1 
ATOM   1611 C CD  . GLU   A 1 198 ? 19.61270 30.76524  -10.10803 1.000 60.44839  ? 195 GLU   A CD  1 
ATOM   1612 O OE1 . GLU   A 1 198 ? 19.16804 29.64355  -10.43781 1.000 55.37637  ? 195 GLU   A OE1 1 
ATOM   1613 O OE2 . GLU   A 1 198 ? 20.38397 30.93492  -9.14103  1.000 54.77161  ? 195 GLU   A OE2 1 
ATOM   1614 N N   . MET   A 1 199 ? 20.49910 33.68280  -14.49866 1.000 54.06288  ? 196 MET   A N   1 
ATOM   1615 C CA  . MET   A 1 199 ? 21.50865 34.68449  -14.82795 1.000 56.93947  ? 196 MET   A CA  1 
ATOM   1616 C C   . MET   A 1 199 ? 20.87627 35.99339  -15.28552 1.000 57.77142  ? 196 MET   A C   1 
ATOM   1617 O O   . MET   A 1 199 ? 21.44752 37.06643  -15.06275 1.000 56.58198  ? 196 MET   A O   1 
ATOM   1618 C CB  . MET   A 1 199 ? 22.45213 34.15623  -15.90905 1.000 57.52094  ? 196 MET   A CB  1 
ATOM   1619 C CG  . MET   A 1 199 ? 23.43128 33.09407  -15.43636 1.000 51.24210  ? 196 MET   A CG  1 
ATOM   1620 S SD  . MET   A 1 199 ? 24.68145 32.72165  -16.68548 1.000 62.13486  ? 196 MET   A SD  1 
ATOM   1621 C CE  . MET   A 1 199 ? 23.68790 31.94074  -17.95641 1.000 50.17353  ? 196 MET   A CE  1 
ATOM   1622 N N   . VAL   A 1 200 ? 19.70543 35.92832  -15.91972 1.000 58.00988  ? 197 VAL   A N   1 
ATOM   1623 C CA  . VAL   A 1 200 ? 19.06300 37.13392  -16.43362 1.000 63.41541  ? 197 VAL   A CA  1 
ATOM   1624 C C   . VAL   A 1 200 ? 18.37722 37.90336  -15.31182 1.000 70.12040  ? 197 VAL   A C   1 
ATOM   1625 O O   . VAL   A 1 200 ? 18.49859 39.12988  -15.21593 1.000 65.08897  ? 197 VAL   A O   1 
ATOM   1626 C CB  . VAL   A 1 200 ? 18.07129 36.77177  -17.55482 1.000 60.01763  ? 197 VAL   A CB  1 
ATOM   1627 C CG1 . VAL   A 1 200 ? 17.31274 38.00758  -18.01498 1.000 63.99206  ? 197 VAL   A CG1 1 
ATOM   1628 C CG2 . VAL   A 1 200 ? 18.80133 36.12149  -18.71952 1.000 56.03848  ? 197 VAL   A CG2 1 
ATOM   1629 N N   . THR   A 1 201 ? 17.64837 37.19838  -14.44805 1.000 64.93534  ? 198 THR   A N   1 
ATOM   1630 C CA  . THR   A 1 201 ? 16.86471 37.83364  -13.39821 1.000 63.25545  ? 198 THR   A CA  1 
ATOM   1631 C C   . THR   A 1 201 ? 17.59687 37.92126  -12.06508 1.000 66.71238  ? 198 THR   A C   1 
ATOM   1632 O O   . THR   A 1 201 ? 17.06880 38.53489  -11.13164 1.000 71.00981  ? 198 THR   A O   1 
ATOM   1633 C CB  . THR   A 1 201 ? 15.54425 37.08022  -13.20058 1.000 68.08134  ? 198 THR   A CB  1 
ATOM   1634 O OG1 . THR   A 1 201 ? 15.81633 35.73029  -12.80375 1.000 71.63576  ? 198 THR   A OG1 1 
ATOM   1635 C CG2 . THR   A 1 201 ? 14.74489 37.06636  -14.49212 1.000 61.04247  ? 198 THR   A CG2 1 
ATOM   1636 N N   . ARG   A 1 202 ? 18.79088 37.33167  -11.95766 1.000 71.45174  ? 199 ARG   A N   1 
ATOM   1637 C CA  . ARG   A 1 202 ? 19.55747 37.28525  -10.70901 1.000 75.59734  ? 199 ARG   A CA  1 
ATOM   1638 C C   . ARG   A 1 202 ? 18.75139 36.66600  -9.56882  1.000 70.09894  ? 199 ARG   A C   1 
ATOM   1639 O O   . ARG   A 1 202 ? 18.92329 37.02663  -8.40201  1.000 70.99100  ? 199 ARG   A O   1 
ATOM   1640 C CB  . ARG   A 1 202 ? 20.07370 38.67288  -10.31329 1.000 86.72522  ? 199 ARG   A CB  1 
ATOM   1641 C CG  . ARG   A 1 202 ? 21.25812 39.14934  -11.14404 1.000 89.79848  ? 199 ARG   A CG  1 
ATOM   1642 C CD  . ARG   A 1 202 ? 20.82239 39.99888  -12.32737 1.000 81.23681  ? 199 ARG   A CD  1 
ATOM   1643 N NE  . ARG   A 1 202 ? 20.61305 41.39153  -11.94898 1.000 82.50443  ? 199 ARG   A NE  1 
ATOM   1644 C CZ  . ARG   A 1 202 ? 19.43308 41.92565  -11.66580 1.000 88.12734  ? 199 ARG   A CZ  1 
ATOM   1645 N NH1 . ARG   A 1 202 ? 18.32025 41.21204  -11.71870 1.000 96.53995  ? 199 ARG   A NH1 1 
ATOM   1646 N NH2 . ARG   A 1 202 ? 19.36776 43.20934  -11.32380 1.000 90.89689  ? 199 ARG   A NH2 1 
ATOM   1647 N N   . ARG   A 1 203 ? 17.87774 35.71864  -9.90021  1.000 64.66924  ? 200 ARG   A N   1 
ATOM   1648 C CA  . ARG   A 1 203 ? 17.01292 35.07709  -8.92145  1.000 68.30503  ? 200 ARG   A CA  1 
ATOM   1649 C C   . ARG   A 1 203 ? 16.55823 33.74170  -9.49087  1.000 66.19432  ? 200 ARG   A C   1 
ATOM   1650 O O   . ARG   A 1 203 ? 16.28935 33.63762  -10.69066 1.000 60.50550  ? 200 ARG   A O   1 
ATOM   1651 C CB  . ARG   A 1 203 ? 15.81345 35.97183  -8.57917  1.000 63.65023  ? 200 ARG   A CB  1 
ATOM   1652 C CG  . ARG   A 1 203 ? 14.58007 35.24163  -8.07495  1.000 78.35820  ? 200 ARG   A CG  1 
ATOM   1653 C CD  . ARG   A 1 203 ? 13.53635 36.22410  -7.56056  1.000 89.85679  ? 200 ARG   A CD  1 
ATOM   1654 N NE  . ARG   A 1 203 ? 13.48399 37.44214  -8.36175  1.000 100.42732 ? 200 ARG   A NE  1 
ATOM   1655 C CZ  . ARG   A 1 203 ? 12.72835 37.60346  -9.43975  1.000 96.82919  ? 200 ARG   A CZ  1 
ATOM   1656 N NH1 . ARG   A 1 203 ? 11.94199 36.63691  -9.88458  1.000 92.25278  ? 200 ARG   A NH1 1 
ATOM   1657 N NH2 . ARG   A 1 203 ? 12.76344 38.76407  -10.08852 1.000 101.38685 ? 200 ARG   A NH2 1 
ATOM   1658 N N   . ALA   A 1 204 ? 16.49609 32.72525  -8.63081  1.000 60.07348  ? 201 ALA   A N   1 
ATOM   1659 C CA  . ALA   A 1 204 ? 16.10159 31.39484  -9.07447  1.000 56.19256  ? 201 ALA   A CA  1 
ATOM   1660 C C   . ALA   A 1 204 ? 14.73528 31.43791  -9.74407  1.000 50.42633  ? 201 ALA   A C   1 
ATOM   1661 O O   . ALA   A 1 204 ? 13.81305 32.11013  -9.27420  1.000 54.53805  ? 201 ALA   A O   1 
ATOM   1662 C CB  . ALA   A 1 204 ? 16.08169 30.42036  -7.89619  1.000 49.95557  ? 201 ALA   A CB  1 
ATOM   1663 N N   . LEU   A 1 205 ? 14.61344 30.71375  -10.85730 1.000 45.16101  ? 202 LEU   A N   1 
ATOM   1664 C CA  . LEU   A 1 205 ? 13.37480 30.73853  -11.62751 1.000 42.73077  ? 202 LEU   A CA  1 
ATOM   1665 C C   . LEU   A 1 205 ? 12.24693 30.03254  -10.88394 1.000 48.69820  ? 202 LEU   A C   1 
ATOM   1666 O O   . LEU   A 1 205 ? 11.13667 30.56481  -10.77172 1.000 52.50565  ? 202 LEU   A O   1 
ATOM   1667 C CB  . LEU   A 1 205 ? 13.60708 30.10333  -12.99870 1.000 45.66863  ? 202 LEU   A CB  1 
ATOM   1668 C CG  . LEU   A 1 205 ? 12.45455 30.13542  -14.00016 1.000 54.94619  ? 202 LEU   A CG  1 
ATOM   1669 C CD1 . LEU   A 1 205 ? 11.97220 31.56057  -14.22451 1.000 51.61323  ? 202 LEU   A CD1 1 
ATOM   1670 C CD2 . LEU   A 1 205 ? 12.89280 29.50110  -15.31046 1.000 45.09752  ? 202 LEU   A CD2 1 
ATOM   1671 N N   . PHE   A 1 206 ? 12.51041 28.83050  -10.37083 1.000 45.44998  ? 203 PHE   A N   1 
ATOM   1672 C CA  . PHE   A 1 206 ? 11.51686 28.03414  -9.64885  1.000 46.55252  ? 203 PHE   A CA  1 
ATOM   1673 C C   . PHE   A 1 206 ? 12.10725 27.60366  -8.31211  1.000 52.07098  ? 203 PHE   A C   1 
ATOM   1674 O O   . PHE   A 1 206 ? 12.57209 26.46520  -8.16575  1.000 55.09818  ? 203 PHE   A O   1 
ATOM   1675 C CB  . PHE   A 1 206 ? 11.08583 26.80597  -10.45266 1.000 46.83346  ? 203 PHE   A CB  1 
ATOM   1676 C CG  . PHE   A 1 206 ? 10.66062 27.10340  -11.86368 1.000 48.85199  ? 203 PHE   A CG  1 
ATOM   1677 C CD1 . PHE   A 1 206 ? 9.53799  27.87259  -12.12075 1.000 52.89921  ? 203 PHE   A CD1 1 
ATOM   1678 C CD2 . PHE   A 1 206 ? 11.36237 26.57252  -12.93379 1.000 50.39524  ? 203 PHE   A CD2 1 
ATOM   1679 C CE1 . PHE   A 1 206 ? 9.13925  28.12940  -13.42035 1.000 53.92366  ? 203 PHE   A CE1 1 
ATOM   1680 C CE2 . PHE   A 1 206 ? 10.96755 26.82270  -14.23515 1.000 48.38196  ? 203 PHE   A CE2 1 
ATOM   1681 C CZ  . PHE   A 1 206 ? 9.85712  27.60354  -14.47887 1.000 53.10993  ? 203 PHE   A CZ  1 
ATOM   1682 N N   . PRO   A 1 207 ? 12.10622 28.48743  -7.31052  1.000 48.52122  ? 204 PRO   A N   1 
ATOM   1683 C CA  . PRO   A 1 207 ? 12.69068 28.13431  -5.99790  1.000 52.81517  ? 204 PRO   A CA  1 
ATOM   1684 C C   . PRO   A 1 207 ? 11.70368 27.39837  -5.09786  1.000 65.30922  ? 204 PRO   A C   1 
ATOM   1685 O O   . PRO   A 1 207 ? 11.16650 27.92939  -4.11798  1.000 64.05354  ? 204 PRO   A O   1 
ATOM   1686 C CB  . PRO   A 1 207 ? 13.08483 29.50554  -5.44157  1.000 60.73653  ? 204 PRO   A CB  1 
ATOM   1687 C CG  . PRO   A 1 207 ? 12.03081 30.41853  -5.98205  1.000 56.68957  ? 204 PRO   A CG  1 
ATOM   1688 C CD  . PRO   A 1 207 ? 11.68440 29.89895  -7.36150  1.000 52.31492  ? 204 PRO   A CD  1 
ATOM   1689 N N   . GLY   A 1 208 ? 11.45159 26.13072  -5.42279  1.000 52.15439  ? 205 GLY   A N   1 
ATOM   1690 C CA  . GLY   A 1 208 ? 10.50534 25.35257  -4.65473  1.000 59.48064  ? 205 GLY   A CA  1 
ATOM   1691 C C   . GLY   A 1 208 ? 11.11476 24.73960  -3.40789  1.000 55.47979  ? 205 GLY   A C   1 
ATOM   1692 O O   . GLY   A 1 208 ? 12.32591 24.55939  -3.29099  1.000 61.63140  ? 205 GLY   A O   1 
ATOM   1693 N N   . ASP   A 1 209 ? 10.23896 24.41305  -2.45462  1.000 65.82140  ? 206 ASP   A N   1 
ATOM   1694 C CA  . ASP   A 1 209 ? 10.64706 23.79982  -1.19862  1.000 67.62809  ? 206 ASP   A CA  1 
ATOM   1695 C C   . ASP   A 1 209 ? 10.21783 22.34698  -1.05737  1.000 59.63010  ? 206 ASP   A C   1 
ATOM   1696 O O   . ASP   A 1 209 ? 10.73989 21.64942  -0.18325  1.000 72.70662  ? 206 ASP   A O   1 
ATOM   1697 C CB  . ASP   A 1 209 ? 10.09096 24.59972  -0.01195  1.000 66.75891  ? 206 ASP   A CB  1 
ATOM   1698 C CG  . ASP   A 1 209 ? 8.62747  24.94540  -0.18174  1.000 76.11909  ? 206 ASP   A CG  1 
ATOM   1699 O OD1 . ASP   A 1 209 ? 7.78757  24.02259  -0.12890  1.000 78.38105  ? 206 ASP   A OD1 1 
ATOM   1700 O OD2 . ASP   A 1 209 ? 8.31733  26.14051  -0.37434  1.000 94.13507  ? 206 ASP   A OD2 1 
ATOM   1701 N N   . SER   A 1 210 ? 9.28210  21.88156  -1.87935  1.000 64.97827  ? 207 SER   A N   1 
ATOM   1702 C CA  . SER   A 1 210 ? 8.87493  20.48570  -1.90245  1.000 65.53225  ? 207 SER   A CA  1 
ATOM   1703 C C   . SER   A 1 210 ? 8.67257  20.07609  -3.35271  1.000 59.06172  ? 207 SER   A C   1 
ATOM   1704 O O   . SER   A 1 210 ? 8.73418  20.90408  -4.26439  1.000 55.75643  ? 207 SER   A O   1 
ATOM   1705 C CB  . SER   A 1 210 ? 7.59569  20.25220  -1.08947  1.000 65.98766  ? 207 SER   A CB  1 
ATOM   1706 O OG  . SER   A 1 210 ? 6.47366  20.83339  -1.73192  1.000 63.70712  ? 207 SER   A OG  1 
ATOM   1707 N N   . GLU   A 1 211 ? 8.42972  18.78110  -3.56670  1.000 55.21988  ? 208 GLU   A N   1 
ATOM   1708 C CA  . GLU   A 1 211 ? 8.21526  18.29983  -4.92791  1.000 56.04303  ? 208 GLU   A CA  1 
ATOM   1709 C C   . GLU   A 1 211 ? 6.93402  18.87216  -5.52206  1.000 54.35423  ? 208 GLU   A C   1 
ATOM   1710 O O   . GLU   A 1 211 ? 6.91036  19.26584  -6.69373  1.000 59.94178  ? 208 GLU   A O   1 
ATOM   1711 C CB  . GLU   A 1 211 ? 8.18169  16.77234  -4.95469  1.000 60.30796  ? 208 GLU   A CB  1 
ATOM   1712 C CG  . GLU   A 1 211 ? 9.52347  16.11044  -4.69857  1.000 57.56151  ? 208 GLU   A CG  1 
ATOM   1713 C CD  . GLU   A 1 211 ? 9.51216  14.63169  -5.04056  1.000 90.83512  ? 208 GLU   A CD  1 
ATOM   1714 O OE1 . GLU   A 1 211 ? 8.97139  14.26995  -6.10764  1.000 87.30396  ? 208 GLU   A OE1 1 
ATOM   1715 O OE2 . GLU   A 1 211 ? 10.03705 13.83014  -4.23961  1.000 110.97441 ? 208 GLU   A OE2 1 
ATOM   1716 N N   . ILE   A 1 212 ? 5.85971  18.93116  -4.73096  1.000 56.94625  ? 209 ILE   A N   1 
ATOM   1717 C CA  . ILE   A 1 212 ? 4.60617  19.47753  -5.23923  1.000 57.27072  ? 209 ILE   A CA  1 
ATOM   1718 C C   . ILE   A 1 212 ? 4.69183  20.99513  -5.37091  1.000 63.32638  ? 209 ILE   A C   1 
ATOM   1719 O O   . ILE   A 1 212 ? 4.10884  21.57709  -6.29414  1.000 64.63271  ? 209 ILE   A O   1 
ATOM   1720 C CB  . ILE   A 1 212 ? 3.42819  19.03924  -4.34463  1.000 60.30456  ? 209 ILE   A CB  1 
ATOM   1721 C CG1 . ILE   A 1 212 ? 2.09160  19.40764  -4.99291  1.000 68.41353  ? 209 ILE   A CG1 1 
ATOM   1722 C CG2 . ILE   A 1 212 ? 3.54067  19.63593  -2.94548  1.000 61.43133  ? 209 ILE   A CG2 1 
ATOM   1723 C CD1 . ILE   A 1 212 ? 1.84828  18.71426  -6.31799  1.000 70.98595  ? 209 ILE   A CD1 1 
ATOM   1724 N N   . ASP   A 1 213 ? 5.42500  21.66059  -4.47280  1.000 55.75865  ? 210 ASP   A N   1 
ATOM   1725 C CA  . ASP   A 1 213 ? 5.58315  23.10801  -4.57718  1.000 49.70684  ? 210 ASP   A CA  1 
ATOM   1726 C C   . ASP   A 1 213 ? 6.48408  23.47876  -5.74785  1.000 59.27546  ? 210 ASP   A C   1 
ATOM   1727 O O   . ASP   A 1 213 ? 6.27310  24.50839  -6.39886  1.000 57.66062  ? 210 ASP   A O   1 
ATOM   1728 C CB  . ASP   A 1 213 ? 6.14106  23.67469  -3.27200  1.000 53.63763  ? 210 ASP   A CB  1 
ATOM   1729 C CG  . ASP   A 1 213 ? 6.30621  25.18380  -3.31485  1.000 68.66577  ? 210 ASP   A CG  1 
ATOM   1730 O OD1 . ASP   A 1 213 ? 5.27839  25.89730  -3.32214  1.000 63.22427  ? 210 ASP   A OD1 1 
ATOM   1731 O OD2 . ASP   A 1 213 ? 7.46402  25.65612  -3.34145  1.000 62.51211  ? 210 ASP   A OD2 1 
ATOM   1732 N N   . GLN   A 1 214 ? 7.50111  22.65811  -6.02203  1.000 50.06690  ? 211 GLN   A N   1 
ATOM   1733 C CA  . GLN   A 1 214 ? 8.32747  22.87472  -7.20438  1.000 45.82856  ? 211 GLN   A CA  1 
ATOM   1734 C C   . GLN   A 1 214 ? 7.50131  22.74091  -8.47493  1.000 52.83349  ? 211 GLN   A C   1 
ATOM   1735 O O   . GLN   A 1 214 ? 7.65087  23.53303  -9.41272  1.000 52.19282  ? 211 GLN   A O   1 
ATOM   1736 C CB  . GLN   A 1 214 ? 9.48879  21.88222  -7.22148  1.000 47.24753  ? 211 GLN   A CB  1 
ATOM   1737 C CG  . GLN   A 1 214 ? 10.43473 22.05779  -8.39517  1.000 47.85787  ? 211 GLN   A CG  1 
ATOM   1738 C CD  . GLN   A 1 214 ? 11.33679 23.26185  -8.23022  1.000 57.82605  ? 211 GLN   A CD  1 
ATOM   1739 O OE1 . GLN   A 1 214 ? 11.58995 23.71084  -7.11262  1.000 50.88844  ? 211 GLN   A OE1 1 
ATOM   1740 N NE2 . GLN   A 1 214 ? 11.83100 23.79005  -9.34330  1.000 52.50145  ? 211 GLN   A NE2 1 
ATOM   1741 N N   . LEU   A 1 215 ? 6.61941  21.74160  -8.51822  1.000 55.65537  ? 212 LEU   A N   1 
ATOM   1742 C CA  . LEU   A 1 215 ? 5.79028  21.52268  -9.69639  1.000 55.12202  ? 212 LEU   A CA  1 
ATOM   1743 C C   . LEU   A 1 215 ? 4.78803  22.65540  -9.88478  1.000 62.03171  ? 212 LEU   A C   1 
ATOM   1744 O O   . LEU   A 1 215 ? 4.56295  23.11177  -11.01173 1.000 57.01289  ? 212 LEU   A O   1 
ATOM   1745 C CB  . LEU   A 1 215 ? 5.07420  20.17876  -9.57278  1.000 56.57095  ? 212 LEU   A CB  1 
ATOM   1746 C CG  . LEU   A 1 215 ? 4.43995  19.58706  -10.82730 1.000 64.55111  ? 212 LEU   A CG  1 
ATOM   1747 C CD1 . LEU   A 1 215 ? 5.50630  19.22626  -11.84996 1.000 52.53570  ? 212 LEU   A CD1 1 
ATOM   1748 C CD2 . LEU   A 1 215 ? 3.60495  18.37307  -10.46368 1.000 67.01526  ? 212 LEU   A CD2 1 
ATOM   1749 N N   . PHE   A 1 216 ? 4.17937  23.12621  -8.79288  1.000 55.46811  ? 213 PHE   A N   1 
ATOM   1750 C CA  . PHE   A 1 216 ? 3.20678  24.20829  -8.90428  1.000 59.36886  ? 213 PHE   A CA  1 
ATOM   1751 C C   . PHE   A 1 216 ? 3.87115  25.52804  -9.27448  1.000 59.63733  ? 213 PHE   A C   1 
ATOM   1752 O O   . PHE   A 1 216 ? 3.25455  26.35924  -9.95068  1.000 66.36983  ? 213 PHE   A O   1 
ATOM   1753 C CB  . PHE   A 1 216 ? 2.42044  24.35501  -7.60076  1.000 59.35596  ? 213 PHE   A CB  1 
ATOM   1754 C CG  . PHE   A 1 216 ? 1.38547  23.28306  -7.38987  1.000 60.13304  ? 213 PHE   A CG  1 
ATOM   1755 C CD1 . PHE   A 1 216 ? 1.17741  22.30039  -8.34471  1.000 69.19658  ? 213 PHE   A CD1 1 
ATOM   1756 C CD2 . PHE   A 1 216 ? 0.61222  23.26634  -6.24113  1.000 62.64538  ? 213 PHE   A CD2 1 
ATOM   1757 C CE1 . PHE   A 1 216 ? 0.22403  21.31774  -8.15336  1.000 76.61630  ? 213 PHE   A CE1 1 
ATOM   1758 C CE2 . PHE   A 1 216 ? -0.34547 22.28642  -6.04446  1.000 64.66072  ? 213 PHE   A CE2 1 
ATOM   1759 C CZ  . PHE   A 1 216 ? -0.53898 21.31169  -7.00132  1.000 70.01954  ? 213 PHE   A CZ  1 
ATOM   1760 N N   . ARG   A 1 217 ? 5.11708  25.74328  -8.84389  1.000 50.42165  ? 214 ARG   A N   1 
ATOM   1761 C CA  . ARG   A 1 217 ? 5.84298  26.93260  -9.27887  1.000 55.20059  ? 214 ARG   A CA  1 
ATOM   1762 C C   . ARG   A 1 217 ? 6.11601  26.88882  -10.77570 1.000 57.22672  ? 214 ARG   A C   1 
ATOM   1763 O O   . ARG   A 1 217 ? 6.06447  27.92249  -11.45264 1.000 57.78561  ? 214 ARG   A O   1 
ATOM   1764 C CB  . ARG   A 1 217 ? 7.14714  27.07514  -8.49578  1.000 47.31257  ? 214 ARG   A CB  1 
ATOM   1765 C CG  . ARG   A 1 217 ? 6.94822  27.56747  -7.07452  1.000 61.67644  ? 214 ARG   A CG  1 
ATOM   1766 C CD  . ARG   A 1 217 ? 8.26829  27.73521  -6.35087  1.000 61.05526  ? 214 ARG   A CD  1 
ATOM   1767 N NE  . ARG   A 1 217 ? 8.06887  28.19751  -4.98317  1.000 68.11802  ? 214 ARG   A NE  1 
ATOM   1768 C CZ  . ARG   A 1 217 ? 7.95753  29.47155  -4.63363  1.000 76.83190  ? 214 ARG   A CZ  1 
ATOM   1769 N NH1 . ARG   A 1 217 ? 8.02636  30.44300  -5.52996  1.000 72.29169  ? 214 ARG   A NH1 1 
ATOM   1770 N NH2 . ARG   A 1 217 ? 7.77200  29.77870  -3.35317  1.000 73.21102  ? 214 ARG   A NH2 1 
ATOM   1771 N N   . ILE   A 1 218 ? 6.40659  25.70038  -11.30897 1.000 52.76543  ? 215 ILE   A N   1 
ATOM   1772 C CA  . ILE   A 1 218 ? 6.55473  25.55152  -12.75203 1.000 52.67503  ? 215 ILE   A CA  1 
ATOM   1773 C C   . ILE   A 1 218 ? 5.22099  25.79088  -13.44776 1.000 55.13954  ? 215 ILE   A C   1 
ATOM   1774 O O   . ILE   A 1 218 ? 5.15336  26.49317  -14.46316 1.000 56.51156  ? 215 ILE   A O   1 
ATOM   1775 C CB  . ILE   A 1 218 ? 7.13424  24.16440  -13.08771 1.000 54.66624  ? 215 ILE   A CB  1 
ATOM   1776 C CG1 . ILE   A 1 218 ? 8.55073  24.02743  -12.52613 1.000 47.10434  ? 215 ILE   A CG1 1 
ATOM   1777 C CG2 . ILE   A 1 218 ? 7.13540  23.92955  -14.58897 1.000 56.62922  ? 215 ILE   A CG2 1 
ATOM   1778 C CD1 . ILE   A 1 218 ? 9.10470  22.62053  -12.59756 1.000 42.54927  ? 215 ILE   A CD1 1 
ATOM   1779 N N   . PHE   A 1 219 ? 4.13737  25.22644  -12.90496 1.000 58.38963  ? 216 PHE   A N   1 
ATOM   1780 C CA  . PHE   A 1 219 ? 2.81914  25.42460  -13.50082 1.000 56.95391  ? 216 PHE   A CA  1 
ATOM   1781 C C   . PHE   A 1 219 ? 2.39852  26.88714  -13.45904 1.000 68.19097  ? 216 PHE   A C   1 
ATOM   1782 O O   . PHE   A 1 219 ? 1.71838  27.36255  -14.37453 1.000 64.61451  ? 216 PHE   A O   1 
ATOM   1783 C CB  . PHE   A 1 219 ? 1.76625  24.57472  -12.78451 1.000 55.82757  ? 216 PHE   A CB  1 
ATOM   1784 C CG  . PHE   A 1 219 ? 1.91932  23.09277  -12.98805 1.000 54.52618  ? 216 PHE   A CG  1 
ATOM   1785 C CD1 . PHE   A 1 219 ? 2.92649  22.57814  -13.78514 1.000 47.96084  ? 216 PHE   A CD1 1 
ATOM   1786 C CD2 . PHE   A 1 219 ? 1.03581  22.21234  -12.38205 1.000 57.54415  ? 216 PHE   A CD2 1 
ATOM   1787 C CE1 . PHE   A 1 219 ? 3.05940  21.21410  -13.96395 1.000 55.85517  ? 216 PHE   A CE1 1 
ATOM   1788 C CE2 . PHE   A 1 219 ? 1.15968  20.84875  -12.56088 1.000 56.01749  ? 216 PHE   A CE2 1 
ATOM   1789 C CZ  . PHE   A 1 219 ? 2.17180  20.34917  -13.35534 1.000 59.61052  ? 216 PHE   A CZ  1 
ATOM   1790 N N   . ARG   A 1 220 ? 2.78166  27.61171  -12.40444 1.000 62.81581  ? 217 ARG   A N   1 
ATOM   1791 C CA  . ARG   A 1 220 ? 2.35603  29.00046  -12.26450 1.000 63.98475  ? 217 ARG   A CA  1 
ATOM   1792 C C   . ARG   A 1 220 ? 2.98827  29.89813  -13.31831 1.000 62.27765  ? 217 ARG   A C   1 
ATOM   1793 O O   . ARG   A 1 220 ? 2.42328  30.94365  -13.65923 1.000 75.28236  ? 217 ARG   A O   1 
ATOM   1794 C CB  . ARG   A 1 220 ? 2.69426  29.51419  -10.86563 1.000 70.69671  ? 217 ARG   A CB  1 
ATOM   1795 C CG  . ARG   A 1 220 ? 1.56276  29.38044  -9.86070  1.000 80.39390  ? 217 ARG   A CG  1 
ATOM   1796 C CD  . ARG   A 1 220 ? 1.98075  29.88649  -8.48779  1.000 87.56499  ? 217 ARG   A CD  1 
ATOM   1797 N NE  . ARG   A 1 220 ? 2.90113  31.01557  -8.57027  1.000 99.69069  ? 217 ARG   A NE  1 
ATOM   1798 C CZ  . ARG   A 1 220 ? 2.54125  32.26634  -8.82742  1.000 101.03889 ? 217 ARG   A CZ  1 
ATOM   1799 N NH1 . ARG   A 1 220 ? 1.27937  32.59010  -9.06039  1.000 89.90747  ? 217 ARG   A NH1 1 
ATOM   1800 N NH2 . ARG   A 1 220 ? 3.47273  33.21543  -8.85897  1.000 97.36260  ? 217 ARG   A NH2 1 
ATOM   1801 N N   . THR   A 1 221 ? 4.14896  29.51192  -13.84244 1.000 56.38040  ? 218 THR   A N   1 
ATOM   1802 C CA  . THR   A 1 221 ? 4.88156  30.31060  -14.81608 1.000 66.00839  ? 218 THR   A CA  1 
ATOM   1803 C C   . THR   A 1 221 ? 4.63625  29.85499  -16.24935 1.000 64.24251  ? 218 THR   A C   1 
ATOM   1804 O O   . THR   A 1 221 ? 4.38638  30.68137  -17.13127 1.000 63.14436  ? 218 THR   A O   1 
ATOM   1805 C CB  . THR   A 1 221 ? 6.38160  30.25875  -14.50349 1.000 63.59710  ? 218 THR   A CB  1 
ATOM   1806 O OG1 . THR   A 1 221 ? 6.59831  30.64272  -13.14025 1.000 61.23324  ? 218 THR   A OG1 1 
ATOM   1807 C CG2 . THR   A 1 221 ? 7.15179  31.19466  -15.42115 1.000 70.79874  ? 218 THR   A CG2 1 
ATOM   1808 N N   . LEU   A 1 222 ? 4.69845  28.54958  -16.49756 1.000 60.97862  ? 219 LEU   A N   1 
ATOM   1809 C CA  . LEU   A 1 222 ? 4.56417  27.99834  -17.83680 1.000 59.65000  ? 219 LEU   A CA  1 
ATOM   1810 C C   . LEU   A 1 222 ? 3.16463  27.48152  -18.13031 1.000 60.06778  ? 219 LEU   A C   1 
ATOM   1811 O O   . LEU   A 1 222 ? 2.92613  26.97566  -19.23011 1.000 63.74871  ? 219 LEU   A O   1 
ATOM   1812 C CB  . LEU   A 1 222 ? 5.58074  26.87223  -18.04082 1.000 58.05094  ? 219 LEU   A CB  1 
ATOM   1813 C CG  . LEU   A 1 222 ? 7.04569  27.25474  -17.83893 1.000 51.97326  ? 219 LEU   A CG  1 
ATOM   1814 C CD1 . LEU   A 1 222 ? 7.92215  26.02025  -17.91779 1.000 53.59144  ? 219 LEU   A CD1 1 
ATOM   1815 C CD2 . LEU   A 1 222 ? 7.47687  28.28848  -18.87049 1.000 65.86126  ? 219 LEU   A CD2 1 
ATOM   1816 N N   . GLY   A 1 223 ? 2.23832  27.59472  -17.18187 1.000 56.93948  ? 220 GLY   A N   1 
ATOM   1817 C CA  . GLY   A 1 223 ? 0.89835  27.07747  -17.36994 1.000 53.27733  ? 220 GLY   A CA  1 
ATOM   1818 C C   . GLY   A 1 223 ? 0.78894  25.60441  -17.03821 1.000 52.43550  ? 220 GLY   A C   1 
ATOM   1819 O O   . GLY   A 1 223 ? 1.73255  24.83990  -17.25610 1.000 55.82159  ? 220 GLY   A O   1 
ATOM   1820 N N   . THR   A 1 224 ? -0.35246 25.19661  -16.50545 1.000 54.95145  ? 221 THR   A N   1 
ATOM   1821 C CA  . THR   A 1 224 ? -0.59368 23.78506  -16.23651 1.000 62.08602  ? 221 THR   A CA  1 
ATOM   1822 C C   . THR   A 1 224 ? -0.65913 23.02105  -17.55298 1.000 55.73770  ? 221 THR   A C   1 
ATOM   1823 O O   . THR   A 1 224 ? -1.53453 23.30552  -18.38021 1.000 58.52048  ? 221 THR   A O   1 
ATOM   1824 C CB  . THR   A 1 224 ? -1.88925 23.60183  -15.45280 1.000 55.78592  ? 221 THR   A CB  1 
ATOM   1825 O OG1 . THR   A 1 224 ? -1.82688 24.35927  -14.23835 1.000 65.24878  ? 221 THR   A OG1 1 
ATOM   1826 C CG2 . THR   A 1 224 ? -2.10251 22.13393  -15.11598 1.000 65.14817  ? 221 THR   A CG2 1 
ATOM   1827 N N   . PRO   A 1 225 ? 0.22411  22.05546  -17.78880 1.000 58.59345  ? 222 PRO   A N   1 
ATOM   1828 C CA  . PRO   A 1 225 ? 0.24725  21.38197  -19.09027 1.000 63.60117  ? 222 PRO   A CA  1 
ATOM   1829 C C   . PRO   A 1 225 ? -0.91762 20.41968  -19.25514 1.000 63.75416  ? 222 PRO   A C   1 
ATOM   1830 O O   . PRO   A 1 225 ? -1.47990 19.90870  -18.28359 1.000 65.88595  ? 222 PRO   A O   1 
ATOM   1831 C CB  . PRO   A 1 225 ? 1.58557  20.63555  -19.07553 1.000 61.27191  ? 222 PRO   A CB  1 
ATOM   1832 C CG  . PRO   A 1 225 ? 1.83441  20.36666  -17.62653 1.000 64.30004  ? 222 PRO   A CG  1 
ATOM   1833 C CD  . PRO   A 1 225 ? 1.26391  21.54613  -16.87823 1.000 50.76785  ? 222 PRO   A CD  1 
ATOM   1834 N N   . ASP   A 1 226 ? -1.28023 20.18200  -20.51577 1.000 64.01099  ? 223 ASP   A N   1 
ATOM   1835 C CA  . ASP   A 1 226 ? -2.31964 19.21537  -20.84843 1.000 60.62318  ? 223 ASP   A CA  1 
ATOM   1836 C C   . ASP   A 1 226 ? -1.83647 18.28568  -21.95582 1.000 61.53285  ? 223 ASP   A C   1 
ATOM   1837 O O   . ASP   A 1 226 ? -0.65978 18.32267  -22.33044 1.000 59.82024  ? 223 ASP   A O   1 
ATOM   1838 C CB  . ASP   A 1 226 ? -3.61279 19.92780  -21.25534 1.000 56.99074  ? 223 ASP   A CB  1 
ATOM   1839 C CG  . ASP   A 1 226 ? -3.40781 20.92572  -22.38522 1.000 65.64418  ? 223 ASP   A CG  1 
ATOM   1840 O OD1 . ASP   A 1 226 ? -2.25373 21.11432  -22.82564 1.000 74.46577  ? 223 ASP   A OD1 1 
ATOM   1841 O OD2 . ASP   A 1 226 ? -4.40882 21.52596  -22.83198 1.000 78.94211  ? 223 ASP   A OD2 1 
ATOM   1842 N N   . GLU   A 1 227 ? -2.73484 17.45124  -22.48667 1.000 56.87738  ? 224 GLU   A N   1 
ATOM   1843 C CA  . GLU   A 1 227 ? -2.33144 16.46883  -23.48840 1.000 60.03149  ? 224 GLU   A CA  1 
ATOM   1844 C C   . GLU   A 1 227 ? -1.87158 17.12658  -24.78261 1.000 66.64244  ? 224 GLU   A C   1 
ATOM   1845 O O   . GLU   A 1 227 ? -1.05843 16.54807  -25.51248 1.000 66.40994  ? 224 GLU   A O   1 
ATOM   1846 C CB  . GLU   A 1 227 ? -3.48012 15.49946  -23.77077 1.000 57.44353  ? 224 GLU   A CB  1 
ATOM   1847 C CG  . GLU   A 1 227 ? -3.66325 14.42431  -22.71131 1.000 66.84068  ? 224 GLU   A CG  1 
ATOM   1848 C CD  . GLU   A 1 227 ? -2.51975 13.42508  -22.68834 1.000 77.21503  ? 224 GLU   A CD  1 
ATOM   1849 O OE1 . GLU   A 1 227 ? -1.83763 13.27242  -23.72479 1.000 76.69628  ? 224 GLU   A OE1 1 
ATOM   1850 O OE2 . GLU   A 1 227 ? -2.30183 12.79290  -21.63265 1.000 74.13576  ? 224 GLU   A OE2 1 
ATOM   1851 N N   . VAL   A 1 228 ? -2.37146 18.32523  -25.08507 1.000 63.70778  ? 225 VAL   A N   1 
ATOM   1852 C CA  . VAL   A 1 228 ? -1.98439 18.99429  -26.32337 1.000 66.20012  ? 225 VAL   A CA  1 
ATOM   1853 C C   . VAL   A 1 228 ? -0.53600 19.46185  -26.25072 1.000 63.86642  ? 225 VAL   A C   1 
ATOM   1854 O O   . VAL   A 1 228 ? 0.27748  19.15246  -27.12828 1.000 65.70573  ? 225 VAL   A O   1 
ATOM   1855 C CB  . VAL   A 1 228 ? -2.93656 20.16285  -26.62607 1.000 74.83385  ? 225 VAL   A CB  1 
ATOM   1856 C CG1 . VAL   A 1 228 ? -2.41014 20.95791  -27.80058 1.000 74.70836  ? 225 VAL   A CG1 1 
ATOM   1857 C CG2 . VAL   A 1 228 ? -4.33646 19.64413  -26.91055 1.000 63.28875  ? 225 VAL   A CG2 1 
ATOM   1858 N N   . VAL   A 1 229 ? -0.18982 20.21665  -25.20718 1.000 64.57197  ? 226 VAL   A N   1 
ATOM   1859 C CA  . VAL   A 1 229 ? 1.17477  20.71706  -25.09755 1.000 66.47740  ? 226 VAL   A CA  1 
ATOM   1860 C C   . VAL   A 1 229 ? 2.15137  19.62815  -24.67281 1.000 67.91567  ? 226 VAL   A C   1 
ATOM   1861 O O   . VAL   A 1 229 ? 3.36518  19.79302  -24.84877 1.000 65.88899  ? 226 VAL   A O   1 
ATOM   1862 C CB  . VAL   A 1 229 ? 1.24151  21.90271  -24.12106 1.000 61.22442  ? 226 VAL   A CB  1 
ATOM   1863 C CG1 . VAL   A 1 229 ? 0.14420  22.90793  -24.43739 1.000 77.80116  ? 226 VAL   A CG1 1 
ATOM   1864 C CG2 . VAL   A 1 229 ? 1.12805  21.41311  -22.68744 1.000 73.42306  ? 226 VAL   A CG2 1 
ATOM   1865 N N   . TRP   A 1 230 ? 1.65943  18.51677  -24.12832 1.000 61.79492  ? 227 TRP   A N   1 
ATOM   1866 C CA  . TRP   A 1 230 ? 2.52565  17.46519  -23.59633 1.000 59.39424  ? 227 TRP   A CA  1 
ATOM   1867 C C   . TRP   A 1 230 ? 1.76318  16.15355  -23.65700 1.000 61.65489  ? 227 TRP   A C   1 
ATOM   1868 O O   . TRP   A 1 230 ? 1.07076  15.77022  -22.70368 1.000 57.75750  ? 227 TRP   A O   1 
ATOM   1869 C CB  . TRP   A 1 230 ? 2.97410  17.77509  -22.16852 1.000 56.44067  ? 227 TRP   A CB  1 
ATOM   1870 C CG  . TRP   A 1 230 ? 3.96742  16.79856  -21.58998 1.000 60.74957  ? 227 TRP   A CG  1 
ATOM   1871 C CD1 . TRP   A 1 230 ? 4.47650  15.68287  -22.19041 1.000 63.82916  ? 227 TRP   A CD1 1 
ATOM   1872 C CD2 . TRP   A 1 230 ? 4.57277  16.86437  -20.29330 1.000 55.91551  ? 227 TRP   A CD2 1 
ATOM   1873 N NE1 . TRP   A 1 230 ? 5.35619  15.05022  -21.34740 1.000 62.59396  ? 227 TRP   A NE1 1 
ATOM   1874 C CE2 . TRP   A 1 230 ? 5.43392  15.75562  -20.17646 1.000 55.24475  ? 227 TRP   A CE2 1 
ATOM   1875 C CE3 . TRP   A 1 230 ? 4.46918  17.75454  -19.21888 1.000 57.07267  ? 227 TRP   A CE3 1 
ATOM   1876 C CZ2 . TRP   A 1 230 ? 6.18797  15.51300  -19.02986 1.000 56.77839  ? 227 TRP   A CZ2 1 
ATOM   1877 C CZ3 . TRP   A 1 230 ? 5.21593  17.51156  -18.08067 1.000 57.34176  ? 227 TRP   A CZ3 1 
ATOM   1878 C CH2 . TRP   A 1 230 ? 6.06525  16.39934  -17.99512 1.000 63.25510  ? 227 TRP   A CH2 1 
ATOM   1879 N N   . PRO   A 1 231 ? 1.87333  15.42973  -24.76790 1.000 64.82004  ? 228 PRO   A N   1 
ATOM   1880 C CA  . PRO   A 1 231 ? 1.13154  14.17041  -24.91241 1.000 60.56867  ? 228 PRO   A CA  1 
ATOM   1881 C C   . PRO   A 1 231 ? 1.56239  13.14655  -23.87162 1.000 60.39079  ? 228 PRO   A C   1 
ATOM   1882 O O   . PRO   A 1 231 ? 2.74747  12.83751  -23.72878 1.000 63.10676  ? 228 PRO   A O   1 
ATOM   1883 C CB  . PRO   A 1 231 ? 1.48154  13.71573  -26.33479 1.000 66.04295  ? 228 PRO   A CB  1 
ATOM   1884 C CG  . PRO   A 1 231 ? 1.92441  14.97928  -27.03572 1.000 60.35189  ? 228 PRO   A CG  1 
ATOM   1885 C CD  . PRO   A 1 231 ? 2.60444  15.79331  -25.99001 1.000 64.83844  ? 228 PRO   A CD  1 
ATOM   1886 N N   . GLY   A 1 232 ? 0.58302  12.62621  -23.13583 1.000 67.90631  ? 229 GLY   A N   1 
ATOM   1887 C CA  . GLY   A 1 232 ? 0.83005  11.62720  -22.12201 1.000 65.52626  ? 229 GLY   A CA  1 
ATOM   1888 C C   . GLY   A 1 232 ? 0.99997  12.15812  -20.71628 1.000 62.31107  ? 229 GLY   A C   1 
ATOM   1889 O O   . GLY   A 1 232 ? 1.22483  11.35949  -19.79718 1.000 72.05416  ? 229 GLY   A O   1 
ATOM   1890 N N   . VAL   A 1 233 ? 0.89655  13.47459  -20.51418 1.000 61.75967  ? 230 VAL   A N   1 
ATOM   1891 C CA  . VAL   A 1 233 ? 1.11559  14.03588  -19.18442 1.000 61.79841  ? 230 VAL   A CA  1 
ATOM   1892 C C   . VAL   A 1 233 ? 0.02964  13.58381  -18.21563 1.000 71.05348  ? 230 VAL   A C   1 
ATOM   1893 O O   . VAL   A 1 233 ? 0.30159  13.37148  -17.02742 1.000 57.07892  ? 230 VAL   A O   1 
ATOM   1894 C CB  . VAL   A 1 233 ? 1.20813  15.57363  -19.25604 1.000 61.37030  ? 230 VAL   A CB  1 
ATOM   1895 C CG1 . VAL   A 1 233 ? -0.10639 16.18001  -19.72734 1.000 55.52702  ? 230 VAL   A CG1 1 
ATOM   1896 C CG2 . VAL   A 1 233 ? 1.60560  16.14843  -17.90707 1.000 57.10243  ? 230 VAL   A CG2 1 
ATOM   1897 N N   . THR   A 1 234 ? -1.20548 13.41102  -18.69681 1.000 63.26971  ? 231 THR   A N   1 
ATOM   1898 C CA  . THR   A 1 234 ? -2.30196 13.00360  -17.82646 1.000 66.45057  ? 231 THR   A CA  1 
ATOM   1899 C C   . THR   A 1 234 ? -2.19579 11.54942  -17.38920 1.000 67.02309  ? 231 THR   A C   1 
ATOM   1900 O O   . THR   A 1 234 ? -2.91343 11.14485  -16.46864 1.000 75.45042  ? 231 THR   A O   1 
ATOM   1901 C CB  . THR   A 1 234 ? -3.65109 13.23331  -18.51922 1.000 75.14398  ? 231 THR   A CB  1 
ATOM   1902 O OG1 . THR   A 1 234 ? -3.68192 12.53136  -19.76869 1.000 70.08860  ? 231 THR   A OG1 1 
ATOM   1903 C CG2 . THR   A 1 234 ? -3.88321 14.71752  -18.76923 1.000 71.47314  ? 231 THR   A CG2 1 
ATOM   1904 N N   . SER   A 1 235 ? -1.32503 10.76181  -18.01608 1.000 67.86723  ? 232 SER   A N   1 
ATOM   1905 C CA  . SER   A 1 235 ? -1.14140 9.36210   -17.66215 1.000 76.75368  ? 232 SER   A CA  1 
ATOM   1906 C C   . SER   A 1 235 ? 0.07735  9.12878   -16.78000 1.000 76.33659  ? 232 SER   A C   1 
ATOM   1907 O O   . SER   A 1 235 ? 0.34380  7.98290   -16.40523 1.000 73.65531  ? 232 SER   A O   1 
ATOM   1908 C CB  . SER   A 1 235 ? -1.03193 8.51033   -18.93114 1.000 71.15455  ? 232 SER   A CB  1 
ATOM   1909 O OG  . SER   A 1 235 ? -2.18973 8.65172   -19.73712 1.000 76.21481  ? 232 SER   A OG  1 
ATOM   1910 N N   . MET   A 1 236 ? 0.81496  10.17997  -16.43530 1.000 64.46643  ? 233 MET   A N   1 
ATOM   1911 C CA  . MET   A 1 236 ? 2.02213  10.01352  -15.64656 1.000 66.69836  ? 233 MET   A CA  1 
ATOM   1912 C C   . MET   A 1 236 ? 1.67069  9.68014   -14.19559 1.000 70.22272  ? 233 MET   A C   1 
ATOM   1913 O O   . MET   A 1 236 ? 0.61797  10.08567  -13.69426 1.000 74.82977  ? 233 MET   A O   1 
ATOM   1914 C CB  . MET   A 1 236 ? 2.87496  11.27586  -15.72006 1.000 66.03918  ? 233 MET   A CB  1 
ATOM   1915 C CG  . MET   A 1 236 ? 3.20550  11.66837  -17.15228 1.000 68.43482  ? 233 MET   A CG  1 
ATOM   1916 S SD  . MET   A 1 236 ? 4.50225  12.90422  -17.29817 1.000 76.17766  ? 233 MET   A SD  1 
ATOM   1917 C CE  . MET   A 1 236 ? 5.90262  12.00648  -16.62883 1.000 69.81918  ? 233 MET   A CE  1 
ATOM   1918 N N   . PRO   A 1 237 ? 2.53721  8.93004   -13.50327 1.000 72.07753  ? 234 PRO   A N   1 
ATOM   1919 C CA  . PRO   A 1 237 ? 2.15971  8.41551   -12.17264 1.000 79.03569  ? 234 PRO   A CA  1 
ATOM   1920 C C   . PRO   A 1 237 ? 1.83414  9.49482   -11.15500 1.000 64.28226  ? 234 PRO   A C   1 
ATOM   1921 O O   . PRO   A 1 237 ? 0.91061  9.31855   -10.35118 1.000 74.93798  ? 234 PRO   A O   1 
ATOM   1922 C CB  . PRO   A 1 237 ? 3.39296  7.60107   -11.75572 1.000 73.07372  ? 234 PRO   A CB  1 
ATOM   1923 C CG  . PRO   A 1 237 ? 4.06177  7.23847   -13.04001 1.000 74.50677  ? 234 PRO   A CG  1 
ATOM   1924 C CD  . PRO   A 1 237 ? 3.83905  8.40551   -13.95087 1.000 65.65975  ? 234 PRO   A CD  1 
ATOM   1925 N N   . ASP   A 1 238 ? 2.56331  10.60610  -11.15858 1.000 67.61363  ? 235 ASP   A N   1 
ATOM   1926 C CA  . ASP   A 1 238 ? 2.34422  11.65938  -10.17743 1.000 70.33554  ? 235 ASP   A CA  1 
ATOM   1927 C C   . ASP   A 1 238 ? 1.38940  12.74217  -10.66196 1.000 70.56628  ? 235 ASP   A C   1 
ATOM   1928 O O   . ASP   A 1 238 ? 1.19357  13.73436  -9.95262  1.000 69.60845  ? 235 ASP   A O   1 
ATOM   1929 C CB  . ASP   A 1 238 ? 3.67923  12.29311  -9.77408  1.000 66.76200  ? 235 ASP   A CB  1 
ATOM   1930 C CG  . ASP   A 1 238 ? 4.59400  11.31867  -9.05706  1.000 82.95475  ? 235 ASP   A CG  1 
ATOM   1931 O OD1 . ASP   A 1 238 ? 4.07849  10.37247  -8.42490  1.000 87.55410  ? 235 ASP   A OD1 1 
ATOM   1932 O OD2 . ASP   A 1 238 ? 5.82855  11.50144  -9.12207  1.000 88.57746  ? 235 ASP   A OD2 1 
ATOM   1933 N N   . TYR   A 1 239 ? 0.79268  12.58587  -11.84023 1.000 70.83399  ? 236 TYR   A N   1 
ATOM   1934 C CA  . TYR   A 1 239 ? -0.17475 13.56287  -12.31543 1.000 72.20083  ? 236 TYR   A CA  1 
ATOM   1935 C C   . TYR   A 1 239 ? -1.50029 13.38929  -11.58709 1.000 63.91198  ? 236 TYR   A C   1 
ATOM   1936 O O   . TYR   A 1 239 ? -1.97995 12.26863  -11.39400 1.000 71.78041  ? 236 TYR   A O   1 
ATOM   1937 C CB  . TYR   A 1 239 ? -0.38978 13.43363  -13.82458 1.000 72.42105  ? 236 TYR   A CB  1 
ATOM   1938 C CG  . TYR   A 1 239 ? -1.37747 14.44226  -14.37801 1.000 73.57650  ? 236 TYR   A CG  1 
ATOM   1939 C CD1 . TYR   A 1 239 ? -0.95547 15.69744  -14.79761 1.000 73.22795  ? 236 TYR   A CD1 1 
ATOM   1940 C CD2 . TYR   A 1 239 ? -2.73328 14.14312  -14.47072 1.000 70.90875  ? 236 TYR   A CD2 1 
ATOM   1941 C CE1 . TYR   A 1 239 ? -1.85346 16.62418  -15.29716 1.000 63.96415  ? 236 TYR   A CE1 1 
ATOM   1942 C CE2 . TYR   A 1 239 ? -3.63736 15.06421  -14.96781 1.000 73.11683  ? 236 TYR   A CE2 1 
ATOM   1943 C CZ  . TYR   A 1 239 ? -3.19100 16.30252  -15.38001 1.000 72.17025  ? 236 TYR   A CZ  1 
ATOM   1944 O OH  . TYR   A 1 239 ? -4.08468 17.22355  -15.87688 1.000 82.61518  ? 236 TYR   A OH  1 
ATOM   1945 N N   . LYS   A 1 240 ? -2.09114 14.50984  -11.18343 1.000 70.37771  ? 237 LYS   A N   1 
ATOM   1946 C CA  . LYS   A 1 240 ? -3.39343 14.52020  -10.54748 1.000 73.83725  ? 237 LYS   A CA  1 
ATOM   1947 C C   . LYS   A 1 240 ? -4.34270 15.41013  -11.33764 1.000 80.53723  ? 237 LYS   A C   1 
ATOM   1948 O O   . LYS   A 1 240 ? -3.96525 16.52970  -11.71313 1.000 72.07903  ? 237 LYS   A O   1 
ATOM   1949 C CB  . LYS   A 1 240 ? -3.30144 15.02024  -9.09386  1.000 82.37360  ? 237 LYS   A CB  1 
ATOM   1950 C CG  . LYS   A 1 240 ? -3.08602 13.92859  -8.05408  1.000 85.95361  ? 237 LYS   A CG  1 
ATOM   1951 C CD  . LYS   A 1 240 ? -1.68424 13.34730  -8.11839  1.000 85.62000  ? 237 LYS   A CD  1 
ATOM   1952 C CE  . LYS   A 1 240 ? -1.44822 12.36865  -6.97972  1.000 93.35790  ? 237 LYS   A CE  1 
ATOM   1953 N NZ  . LYS   A 1 240 ? -1.67918 13.00519  -5.65171  1.000 99.24177  ? 237 LYS   A NZ  1 
ATOM   1954 N N   . PRO   A 1 241 ? -5.56633 14.95657  -11.62022 1.000 78.78680  ? 238 PRO   A N   1 
ATOM   1955 C CA  . PRO   A 1 241 ? -6.54811 15.84944  -12.25725 1.000 84.71241  ? 238 PRO   A CA  1 
ATOM   1956 C C   . PRO   A 1 241 ? -6.90312 17.05436  -11.40603 1.000 86.43272  ? 238 PRO   A C   1 
ATOM   1957 O O   . PRO   A 1 241 ? -7.43470 18.03661  -11.93873 1.000 84.31074  ? 238 PRO   A O   1 
ATOM   1958 C CB  . PRO   A 1 241 ? -7.76662 14.93963  -12.47242 1.000 75.43450  ? 238 PRO   A CB  1 
ATOM   1959 C CG  . PRO   A 1 241 ? -7.21847 13.54698  -12.44135 1.000 90.45608  ? 238 PRO   A CG  1 
ATOM   1960 C CD  . PRO   A 1 241 ? -6.07665 13.58408  -11.47198 1.000 81.63288  ? 238 PRO   A CD  1 
ATOM   1961 N N   . SER   A 1 242 ? -6.62563 17.01229  -10.10341 1.000 82.60151  ? 239 SER   A N   1 
ATOM   1962 C CA  . SER   A 1 242 ? -6.92339 18.11736  -9.20253  1.000 79.20735  ? 239 SER   A CA  1 
ATOM   1963 C C   . SER   A 1 242 ? -5.88436 19.23033  -9.25504  1.000 73.82885  ? 239 SER   A C   1 
ATOM   1964 O O   . SER   A 1 242 ? -5.99871 20.19118  -8.48635  1.000 83.19976  ? 239 SER   A O   1 
ATOM   1965 C CB  . SER   A 1 242 ? -7.04960 17.60063  -7.76650  1.000 89.82811  ? 239 SER   A CB  1 
ATOM   1966 O OG  . SER   A 1 242 ? -5.85782 16.95508  -7.35109  1.000 97.50426  ? 239 SER   A OG  1 
ATOM   1967 N N   . PHE   A 1 243 ? -4.88131 19.12489  -10.12228 1.000 68.31448  ? 240 PHE   A N   1 
ATOM   1968 C CA  . PHE   A 1 243 ? -3.89844 20.19086  -10.25708 1.000 74.54504  ? 240 PHE   A CA  1 
ATOM   1969 C C   . PHE   A 1 243 ? -4.59559 21.48535  -10.66601 1.000 75.80674  ? 240 PHE   A C   1 
ATOM   1970 O O   . PHE   A 1 243 ? -5.43558 21.46989  -11.57710 1.000 82.99259  ? 240 PHE   A O   1 
ATOM   1971 C CB  . PHE   A 1 243 ? -2.83239 19.82307  -11.29147 1.000 72.52293  ? 240 PHE   A CB  1 
ATOM   1972 C CG  . PHE   A 1 243 ? -1.83770 18.80032  -10.81159 1.000 75.53388  ? 240 PHE   A CG  1 
ATOM   1973 C CD1 . PHE   A 1 243 ? -1.69364 18.52884  -9.46084  1.000 72.83170  ? 240 PHE   A CD1 1 
ATOM   1974 C CD2 . PHE   A 1 243 ? -1.03825 18.11660  -11.71601 1.000 77.87930  ? 240 PHE   A CD2 1 
ATOM   1975 C CE1 . PHE   A 1 243 ? -0.77624 17.59031  -9.02131  1.000 71.58739  ? 240 PHE   A CE1 1 
ATOM   1976 C CE2 . PHE   A 1 243 ? -0.11849 17.17718  -11.28216 1.000 73.99936  ? 240 PHE   A CE2 1 
ATOM   1977 C CZ  . PHE   A 1 243 ? 0.01187  16.91436  -9.93266  1.000 76.01445  ? 240 PHE   A CZ  1 
ATOM   1978 N N   . PRO   A 1 244 ? -4.29703 22.60994  -10.01753 1.000 73.21361  ? 241 PRO   A N   1 
ATOM   1979 C CA  . PRO   A 1 244 ? -4.91813 23.87605  -10.42045 1.000 71.36601  ? 241 PRO   A CA  1 
ATOM   1980 C C   . PRO   A 1 244 ? -4.50269 24.27532  -11.82880 1.000 77.61169  ? 241 PRO   A C   1 
ATOM   1981 O O   . PRO   A 1 244 ? -3.42497 23.91756  -12.31116 1.000 72.30103  ? 241 PRO   A O   1 
ATOM   1982 C CB  . PRO   A 1 244 ? -4.39902 24.87497  -9.37887  1.000 74.26700  ? 241 PRO   A CB  1 
ATOM   1983 C CG  . PRO   A 1 244 ? -3.99069 24.03013  -8.21049  1.000 81.75357  ? 241 PRO   A CG  1 
ATOM   1984 C CD  . PRO   A 1 244 ? -3.47070 22.75957  -8.80884  1.000 78.04107  ? 241 PRO   A CD  1 
ATOM   1985 N N   . LYS   A 1 245 ? -5.38039 25.02679  -12.49055 1.000 68.44959  ? 242 LYS   A N   1 
ATOM   1986 C CA  . LYS   A 1 245 ? -5.15719 25.48542  -13.85745 1.000 69.33445  ? 242 LYS   A CA  1 
ATOM   1987 C C   . LYS   A 1 245 ? -4.62615 26.91488  -13.81608 1.000 73.84057  ? 242 LYS   A C   1 
ATOM   1988 O O   . LYS   A 1 245 ? -5.37713 27.85649  -13.54008 1.000 82.42799  ? 242 LYS   A O   1 
ATOM   1989 C CB  . LYS   A 1 245 ? -6.44455 25.40244  -14.67629 1.000 66.51699  ? 242 LYS   A CB  1 
ATOM   1990 C CG  . LYS   A 1 245 ? -7.01136 23.99717  -14.81341 1.000 65.90365  ? 242 LYS   A CG  1 
ATOM   1991 C CD  . LYS   A 1 245 ? -6.01124 23.06059  -15.47207 1.000 68.16352  ? 242 LYS   A CD  1 
ATOM   1992 C CE  . LYS   A 1 245 ? -6.59130 21.66657  -15.65597 1.000 68.91419  ? 242 LYS   A CE  1 
ATOM   1993 N NZ  . LYS   A 1 245 ? -5.60852 20.73892  -16.28328 1.000 88.86658  ? 242 LYS   A NZ  1 
ATOM   1994 N N   . TRP   A 1 246 ? -3.33361 27.07254  -14.08253 1.000 61.57431  ? 243 TRP   A N   1 
ATOM   1995 C CA  . TRP   A 1 246 ? -2.70436 28.37708  -14.21059 1.000 68.06984  ? 243 TRP   A CA  1 
ATOM   1996 C C   . TRP   A 1 246 ? -2.42043 28.66923  -15.67775 1.000 74.61341  ? 243 TRP   A C   1 
ATOM   1997 O O   . TRP   A 1 246 ? -2.12178 27.76406  -16.46206 1.000 72.15668  ? 243 TRP   A O   1 
ATOM   1998 C CB  . TRP   A 1 246 ? -1.39679 28.45346  -13.41461 1.000 64.45408  ? 243 TRP   A CB  1 
ATOM   1999 C CG  . TRP   A 1 246 ? -1.57500 28.48935  -11.92857 1.000 76.14339  ? 243 TRP   A CG  1 
ATOM   2000 C CD1 . TRP   A 1 246 ? -1.98849 29.55085  -11.17788 1.000 68.42512  ? 243 TRP   A CD1 1 
ATOM   2001 C CD2 . TRP   A 1 246 ? -1.32244 27.42136  -11.00850 1.000 75.46747  ? 243 TRP   A CD2 1 
ATOM   2002 N NE1 . TRP   A 1 246 ? -2.01963 29.20695  -9.84845  1.000 76.85351  ? 243 TRP   A NE1 1 
ATOM   2003 C CE2 . TRP   A 1 246 ? -1.61482 27.90458  -9.71751  1.000 82.79425  ? 243 TRP   A CE2 1 
ATOM   2004 C CE3 . TRP   A 1 246 ? -0.88439 26.10160  -11.15163 1.000 72.32654  ? 243 TRP   A CE3 1 
ATOM   2005 C CZ2 . TRP   A 1 246 ? -1.48125 27.11513  -8.57640  1.000 75.99361  ? 243 TRP   A CZ2 1 
ATOM   2006 C CZ3 . TRP   A 1 246 ? -0.75099 25.31939  -10.01743 1.000 83.07937  ? 243 TRP   A CZ3 1 
ATOM   2007 C CH2 . TRP   A 1 246 ? -1.04777 25.82921  -8.74668  1.000 76.23819  ? 243 TRP   A CH2 1 
ATOM   2008 N N   . ALA   A 1 247 ? -2.51419 29.94314  -16.04145 1.000 70.09536  ? 244 ALA   A N   1 
ATOM   2009 C CA  . ALA   A 1 247 ? -2.22671 30.37549  -17.39945 1.000 74.67311  ? 244 ALA   A CA  1 
ATOM   2010 C C   . ALA   A 1 247 ? -0.74440 30.68927  -17.55021 1.000 63.96100  ? 244 ALA   A C   1 
ATOM   2011 O O   . ALA   A 1 247 ? -0.09461 31.17236  -16.61910 1.000 75.74884  ? 244 ALA   A O   1 
ATOM   2012 C CB  . ALA   A 1 247 ? -3.06138 31.60311  -17.76679 1.000 71.10220  ? 244 ALA   A CB  1 
ATOM   2013 N N   . ARG   A 1 248 ? -0.21169 30.40248  -18.73627 1.000 66.09677  ? 245 ARG   A N   1 
ATOM   2014 C CA  . ARG   A 1 248 ? 1.19304  30.67662  -19.00781 1.000 68.30290  ? 245 ARG   A CA  1 
ATOM   2015 C C   . ARG   A 1 248 ? 1.44732  32.17812  -18.97583 1.000 72.73634  ? 245 ARG   A C   1 
ATOM   2016 O O   . ARG   A 1 248 ? 0.71215  32.95721  -19.58950 1.000 80.22441  ? 245 ARG   A O   1 
ATOM   2017 C CB  . ARG   A 1 248 ? 1.60042  30.09946  -20.36314 1.000 70.92034  ? 245 ARG   A CB  1 
ATOM   2018 C CG  . ARG   A 1 248 ? 3.07514  30.28682  -20.69702 1.000 67.42068  ? 245 ARG   A CG  1 
ATOM   2019 C CD  . ARG   A 1 248 ? 3.38288  29.83709  -22.11650 1.000 79.17221  ? 245 ARG   A CD  1 
ATOM   2020 N NE  . ARG   A 1 248 ? 4.80284  29.94131  -22.43372 1.000 77.04241  ? 245 ARG   A NE  1 
ATOM   2021 C CZ  . ARG   A 1 248 ? 5.66578  28.93818  -22.34418 1.000 77.10358  ? 245 ARG   A CZ  1 
ATOM   2022 N NH1 . ARG   A 1 248 ? 5.28838  27.73534  -21.94169 1.000 71.49238  ? 245 ARG   A NH1 1 
ATOM   2023 N NH2 . ARG   A 1 248 ? 6.93822  29.14525  -22.67208 1.000 74.76564  ? 245 ARG   A NH2 1 
ATOM   2024 N N   . GLN   A 1 249 ? 2.48550  32.58382  -18.25342 1.000 74.46581  ? 246 GLN   A N   1 
ATOM   2025 C CA  . GLN   A 1 249 ? 2.82634  33.99307  -18.15735 1.000 81.67730  ? 246 GLN   A CA  1 
ATOM   2026 C C   . GLN   A 1 249 ? 3.64000  34.43383  -19.36735 1.000 82.63831  ? 246 GLN   A C   1 
ATOM   2027 O O   . GLN   A 1 249 ? 4.43335  33.66886  -19.92428 1.000 76.96931  ? 246 GLN   A O   1 
ATOM   2028 C CB  . GLN   A 1 249 ? 3.60830  34.27146  -16.87404 1.000 82.89713  ? 246 GLN   A CB  1 
ATOM   2029 C CG  . GLN   A 1 249 ? 2.81299  34.03690  -15.60153 1.000 91.27286  ? 246 GLN   A CG  1 
ATOM   2030 C CD  . GLN   A 1 249 ? 3.59801  34.38820  -14.35410 1.000 101.73101 ? 246 GLN   A CD  1 
ATOM   2031 O OE1 . GLN   A 1 249 ? 4.75099  34.81352  -14.43135 1.000 107.54125 ? 246 GLN   A OE1 1 
ATOM   2032 N NE2 . GLN   A 1 249 ? 2.97573  34.21227  -13.19424 1.000 107.20571 ? 246 GLN   A NE2 1 
ATOM   2033 N N   . ASP   A 1 250 ? 3.42580  35.68266  -19.77584 1.000 84.28281  ? 247 ASP   A N   1 
ATOM   2034 C CA  . ASP   A 1 250 ? 4.19605  36.25628  -20.87002 1.000 80.55778  ? 247 ASP   A CA  1 
ATOM   2035 C C   . ASP   A 1 250 ? 5.66323  36.35019  -20.47316 1.000 81.66524  ? 247 ASP   A C   1 
ATOM   2036 O O   . ASP   A 1 250 ? 5.99887  36.88343  -19.41162 1.000 91.84289  ? 247 ASP   A O   1 
ATOM   2037 C CB  . ASP   A 1 250 ? 3.64711  37.63919  -21.23027 1.000 86.56922  ? 247 ASP   A CB  1 
ATOM   2038 C CG  . ASP   A 1 250 ? 4.08842  38.11045  -22.60790 1.000 101.00758 ? 247 ASP   A CG  1 
ATOM   2039 O OD1 . ASP   A 1 250 ? 5.20642  37.75954  -23.04051 1.000 104.48080 ? 247 ASP   A OD1 1 
ATOM   2040 O OD2 . ASP   A 1 250 ? 3.31025  38.83771  -23.26134 1.000 110.47557 ? 247 ASP   A OD2 1 
ATOM   2041 N N   . PHE   A 1 251 ? 6.54119  35.82696  -21.33167 1.000 76.83293  ? 248 PHE   A N   1 
ATOM   2042 C CA  . PHE   A 1 251 ? 7.96913  35.83825  -21.03689 1.000 82.71242  ? 248 PHE   A CA  1 
ATOM   2043 C C   . PHE   A 1 251 ? 8.54634  37.24440  -20.96045 1.000 90.09181  ? 248 PHE   A C   1 
ATOM   2044 O O   . PHE   A 1 251 ? 9.68568  37.40179  -20.50770 1.000 88.65178  ? 248 PHE   A O   1 
ATOM   2045 C CB  . PHE   A 1 251 ? 8.72510  35.01302  -22.07815 1.000 79.29018  ? 248 PHE   A CB  1 
ATOM   2046 C CG  . PHE   A 1 251 ? 8.92592  33.57998  -21.67837 1.000 70.42484  ? 248 PHE   A CG  1 
ATOM   2047 C CD1 . PHE   A 1 251 ? 7.88711  32.85103  -21.12312 1.000 74.15087  ? 248 PHE   A CD1 1 
ATOM   2048 C CD2 . PHE   A 1 251 ? 10.15092 32.96109  -21.85881 1.000 66.88720  ? 248 PHE   A CD2 1 
ATOM   2049 C CE1 . PHE   A 1 251 ? 8.06747  31.53295  -20.75117 1.000 75.26814  ? 248 PHE   A CE1 1 
ATOM   2050 C CE2 . PHE   A 1 251 ? 10.33739 31.64174  -21.49115 1.000 66.02347  ? 248 PHE   A CE2 1 
ATOM   2051 C CZ  . PHE   A 1 251 ? 9.29383  30.92697  -20.93699 1.000 76.54024  ? 248 PHE   A CZ  1 
ATOM   2052 N N   . SER   A 1 252 ? 7.79790  38.26386  -21.38850 1.000 98.82763  ? 249 SER   A N   1 
ATOM   2053 C CA  . SER   A 1 252 ? 8.21154  39.63980  -21.14760 1.000 98.43489  ? 249 SER   A CA  1 
ATOM   2054 C C   . SER   A 1 252 ? 8.19664  39.98663  -19.66518 1.000 101.81499 ? 249 SER   A C   1 
ATOM   2055 O O   . SER   A 1 252 ? 8.89030  40.92195  -19.25250 1.000 106.41940 ? 249 SER   A O   1 
ATOM   2056 C CB  . SER   A 1 252 ? 7.31039  40.60444  -21.91915 1.000 106.62152 ? 249 SER   A CB  1 
ATOM   2057 O OG  . SER   A 1 252 ? 7.36610  40.34844  -23.31162 1.000 126.55181 ? 249 SER   A OG  1 
ATOM   2058 N N   . LYS   A 1 253 ? 7.42162  39.25929  -18.86071 1.000 95.24722  ? 250 LYS   A N   1 
ATOM   2059 C CA  . LYS   A 1 253 ? 7.41105  39.43981  -17.41512 1.000 95.95214  ? 250 LYS   A CA  1 
ATOM   2060 C C   . LYS   A 1 253 ? 8.29023  38.43634  -16.68470 1.000 92.10792  ? 250 LYS   A C   1 
ATOM   2061 O O   . LYS   A 1 253 ? 8.79157  38.74489  -15.59850 1.000 98.52990  ? 250 LYS   A O   1 
ATOM   2062 C CB  . LYS   A 1 253 ? 5.98032  39.33650  -16.87271 1.000 97.09373  ? 250 LYS   A CB  1 
ATOM   2063 C CG  . LYS   A 1 253 ? 4.98234  40.26502  -17.54860 1.000 110.50682 ? 250 LYS   A CG  1 
ATOM   2064 C CD  . LYS   A 1 253 ? 3.66699  40.31786  -16.78225 1.000 118.46927 ? 250 LYS   A CD  1 
ATOM   2065 C CE  . LYS   A 1 253 ? 3.08146  38.92861  -16.57116 1.000 121.05838 ? 250 LYS   A CE  1 
ATOM   2066 N NZ  . LYS   A 1 253 ? 2.75151  38.25180  -17.85594 1.000 109.58659 ? 250 LYS   A NZ  1 
ATOM   2067 N N   . VAL   A 1 254 ? 8.48634  37.24479  -17.25266 1.000 84.95077  ? 251 VAL   A N   1 
ATOM   2068 C CA  . VAL   A 1 254 ? 9.34452  36.24807  -16.61865 1.000 80.60399  ? 251 VAL   A CA  1 
ATOM   2069 C C   . VAL   A 1 254 ? 10.80727 36.65787  -16.73449 1.000 80.03751  ? 251 VAL   A C   1 
ATOM   2070 O O   . VAL   A 1 254 ? 11.54447 36.68162  -15.74221 1.000 83.38957  ? 251 VAL   A O   1 
ATOM   2071 C CB  . VAL   A 1 254 ? 9.09675  34.85913  -17.23336 1.000 77.35282  ? 251 VAL   A CB  1 
ATOM   2072 C CG1 . VAL   A 1 254 ? 10.00679 33.82367  -16.59104 1.000 67.21223  ? 251 VAL   A CG1 1 
ATOM   2073 C CG2 . VAL   A 1 254 ? 7.63655  34.46561  -17.07978 1.000 79.30861  ? 251 VAL   A CG2 1 
ATOM   2074 N N   . VAL   A 1 255 ? 11.24755 36.98529  -17.94491 1.000 81.48378  ? 252 VAL   A N   1 
ATOM   2075 C CA  . VAL   A 1 255 ? 12.60496 37.47262  -18.17530 1.000 73.75355  ? 252 VAL   A CA  1 
ATOM   2076 C C   . VAL   A 1 255 ? 12.52423 38.82324  -18.87923 1.000 82.48979  ? 252 VAL   A C   1 
ATOM   2077 O O   . VAL   A 1 255 ? 12.66862 38.89335  -20.10870 1.000 84.93576  ? 252 VAL   A O   1 
ATOM   2078 C CB  . VAL   A 1 255 ? 13.43195 36.45701  -18.97865 1.000 71.33347  ? 252 VAL   A CB  1 
ATOM   2079 C CG1 . VAL   A 1 255 ? 14.02870 35.41866  -18.04494 1.000 74.23408  ? 252 VAL   A CG1 1 
ATOM   2080 C CG2 . VAL   A 1 255 ? 12.56493 35.77823  -20.03120 1.000 71.38213  ? 252 VAL   A CG2 1 
ATOM   2081 N N   . PRO   A 1 256 ? 12.28591 39.90937  -18.14781 1.000 82.86744  ? 253 PRO   A N   1 
ATOM   2082 C CA  . PRO   A 1 256 ? 12.14028 41.23114  -18.78031 1.000 83.43021  ? 253 PRO   A CA  1 
ATOM   2083 C C   . PRO   A 1 256 ? 13.35891 41.63555  -19.59771 1.000 86.13490  ? 253 PRO   A C   1 
ATOM   2084 O O   . PRO   A 1 256 ? 13.19696 42.08889  -20.74084 1.000 87.57583  ? 253 PRO   A O   1 
ATOM   2085 C CB  . PRO   A 1 256 ? 11.92091 42.17129  -17.58432 1.000 88.52438  ? 253 PRO   A CB  1 
ATOM   2086 C CG  . PRO   A 1 256 ? 11.29912 41.29766  -16.54596 1.000 84.21343  ? 253 PRO   A CG  1 
ATOM   2087 C CD  . PRO   A 1 256 ? 11.92488 39.93876  -16.71792 1.000 82.32880  ? 253 PRO   A CD  1 
ATOM   2088 N N   . PRO   A 1 257 ? 14.59154 41.50862  -19.07857 1.000 81.18544  ? 254 PRO   A N   1 
ATOM   2089 C CA  . PRO   A 1 257 ? 15.74395 42.00770  -19.85170 1.000 81.50574  ? 254 PRO   A CA  1 
ATOM   2090 C C   . PRO   A 1 257 ? 16.02056 41.23532  -21.13217 1.000 88.31523  ? 254 PRO   A C   1 
ATOM   2091 O O   . PRO   A 1 257 ? 16.81383 41.71081  -21.95530 1.000 84.72543  ? 254 PRO   A O   1 
ATOM   2092 C CB  . PRO   A 1 257 ? 16.91881 41.87026  -18.87079 1.000 79.33390  ? 254 PRO   A CB  1 
ATOM   2093 C CG  . PRO   A 1 257 ? 16.29847 41.72538  -17.53068 1.000 81.70656  ? 254 PRO   A CG  1 
ATOM   2094 C CD  . PRO   A 1 257 ? 15.04360 40.97091  -17.78131 1.000 75.78893  ? 254 PRO   A CD  1 
ATOM   2095 N N   . LEU   A 1 258 ? 15.39727 40.07809  -21.33392 1.000 85.08962  ? 255 LEU   A N   1 
ATOM   2096 C CA  . LEU   A 1 258 ? 15.73470 39.22064  -22.46120 1.000 80.33919  ? 255 LEU   A CA  1 
ATOM   2097 C C   . LEU   A 1 258 ? 15.01541 39.68311  -23.72378 1.000 83.17743  ? 255 LEU   A C   1 
ATOM   2098 O O   . LEU   A 1 258 ? 13.81652 39.97930  -23.69547 1.000 87.04530  ? 255 LEU   A O   1 
ATOM   2099 C CB  . LEU   A 1 258 ? 15.37538 37.77070  -22.13894 1.000 76.65309  ? 255 LEU   A CB  1 
ATOM   2100 C CG  . LEU   A 1 258 ? 16.34041 36.69318  -22.63416 1.000 78.37693  ? 255 LEU   A CG  1 
ATOM   2101 C CD1 . LEU   A 1 258 ? 17.77839 37.06028  -22.29782 1.000 65.68053  ? 255 LEU   A CD1 1 
ATOM   2102 C CD2 . LEU   A 1 258 ? 15.97883 35.34614  -22.02772 1.000 65.01218  ? 255 LEU   A CD2 1 
ATOM   2103 N N   . ASP   A 1 259 ? 15.75236 39.74358  -24.83119 1.000 81.71373  ? 256 ASP   A N   1 
ATOM   2104 C CA  . ASP   A 1 259 ? 15.18613 40.12473  -26.11552 1.000 85.40928  ? 256 ASP   A CA  1 
ATOM   2105 C C   . ASP   A 1 259 ? 14.41614 38.95093  -26.71927 1.000 85.49233  ? 256 ASP   A C   1 
ATOM   2106 O O   . ASP   A 1 259 ? 14.30093 37.87565  -26.12483 1.000 72.97526  ? 256 ASP   A O   1 
ATOM   2107 C CB  . ASP   A 1 259 ? 16.28551 40.61129  -27.05722 1.000 90.04542  ? 256 ASP   A CB  1 
ATOM   2108 C CG  . ASP   A 1 259 ? 17.41546 39.61050  -27.20106 1.000 98.95296  ? 256 ASP   A CG  1 
ATOM   2109 O OD1 . ASP   A 1 259 ? 17.76760 38.95915  -26.19448 1.000 100.15323 ? 256 ASP   A OD1 1 
ATOM   2110 O OD2 . ASP   A 1 259 ? 17.95125 39.47424  -28.32115 1.000 104.30595 ? 256 ASP   A OD2 1 
ATOM   2111 N N   . GLU   A 1 260 ? 13.88716 39.15421  -27.92953 1.000 90.87849  ? 257 GLU   A N   1 
ATOM   2112 C CA  . GLU   A 1 260 ? 13.01289 38.14683  -28.52322 1.000 89.74435  ? 257 GLU   A CA  1 
ATOM   2113 C C   . GLU   A 1 260 ? 13.78144 36.89637  -28.93537 1.000 83.98975  ? 257 GLU   A C   1 
ATOM   2114 O O   . GLU   A 1 260 ? 13.20203 35.80506  -28.97878 1.000 75.47215  ? 257 GLU   A O   1 
ATOM   2115 C CB  . GLU   A 1 260 ? 12.25639 38.73836  -29.71503 1.000 83.82786  ? 257 GLU   A CB  1 
ATOM   2116 C CG  . GLU   A 1 260 ? 13.05696 38.85235  -31.00176 1.000 111.02636 ? 257 GLU   A CG  1 
ATOM   2117 C CD  . GLU   A 1 260 ? 12.66664 37.79780  -32.02163 1.000 122.34187 ? 257 GLU   A CD  1 
ATOM   2118 O OE1 . GLU   A 1 260 ? 12.22533 36.70355  -31.60943 1.000 115.57471 ? 257 GLU   A OE1 1 
ATOM   2119 O OE2 . GLU   A 1 260 ? 12.79149 38.06695  -33.23563 1.000 116.04543 ? 257 GLU   A OE2 1 
ATOM   2120 N N   . ASP   A 1 261 ? 15.07628 37.02550  -29.23622 1.000 81.63307  ? 258 ASP   A N   1 
ATOM   2121 C CA  . ASP   A 1 261 ? 15.87970 35.83949  -29.51571 1.000 69.39848  ? 258 ASP   A CA  1 
ATOM   2122 C C   . ASP   A 1 261 ? 16.15004 35.05062  -28.24073 1.000 73.36601  ? 258 ASP   A C   1 
ATOM   2123 O O   . ASP   A 1 261 ? 16.15934 33.81390  -28.25773 1.000 60.64565  ? 258 ASP   A O   1 
ATOM   2124 C CB  . ASP   A 1 261 ? 17.19154 36.23423  -30.19504 1.000 78.06187  ? 258 ASP   A CB  1 
ATOM   2125 C CG  . ASP   A 1 261 ? 17.00674 36.59946  -31.65850 1.000 94.11102  ? 258 ASP   A CG  1 
ATOM   2126 O OD1 . ASP   A 1 261 ? 15.86765 36.49867  -32.16085 1.000 98.87142  ? 258 ASP   A OD1 1 
ATOM   2127 O OD2 . ASP   A 1 261 ? 18.00247 36.98441  -32.30807 1.000 85.24078  ? 258 ASP   A OD2 1 
ATOM   2128 N N   . GLY   A 1 262 ? 16.36484 35.74796  -27.12396 1.000 69.26295  ? 259 GLY   A N   1 
ATOM   2129 C CA  . GLY   A 1 262 ? 16.58085 35.05622  -25.86478 1.000 66.88777  ? 259 GLY   A CA  1 
ATOM   2130 C C   . GLY   A 1 262 ? 15.32663 34.37912  -25.34632 1.000 60.33281  ? 259 GLY   A C   1 
ATOM   2131 O O   . GLY   A 1 262 ? 15.38109 33.24783  -24.85564 1.000 55.22326  ? 259 GLY   A O   1 
ATOM   2132 N N   . ARG   A 1 263 ? 14.17987 35.05962  -25.44692 1.000 61.80540  ? 260 ARG   A N   1 
ATOM   2133 C CA  . ARG   A 1 263 ? 12.92452 34.46858  -24.99396 1.000 65.38443  ? 260 ARG   A CA  1 
ATOM   2134 C C   . ARG   A 1 263 ? 12.56474 33.23109  -25.80337 1.000 61.67264  ? 260 ARG   A C   1 
ATOM   2135 O O   . ARG   A 1 263 ? 11.98828 32.28104  -25.26078 1.000 60.54760  ? 260 ARG   A O   1 
ATOM   2136 C CB  . ARG   A 1 263 ? 11.79228 35.49429  -25.07569 1.000 71.08506  ? 260 ARG   A CB  1 
ATOM   2137 C CG  . ARG   A 1 263 ? 12.01720 36.75517  -24.25772 1.000 69.55311  ? 260 ARG   A CG  1 
ATOM   2138 C CD  . ARG   A 1 263 ? 10.75061 37.59724  -24.19097 1.000 85.90262  ? 260 ARG   A CD  1 
ATOM   2139 N NE  . ARG   A 1 263 ? 10.10469 37.72803  -25.49264 1.000 87.41287  ? 260 ARG   A NE  1 
ATOM   2140 C CZ  . ARG   A 1 263 ? 10.30359 38.73420  -26.33345 1.000 89.40131  ? 260 ARG   A CZ  1 
ATOM   2141 N NH1 . ARG   A 1 263 ? 11.13015 39.72535  -26.04238 1.000 97.27211  ? 260 ARG   A NH1 1 
ATOM   2142 N NH2 . ARG   A 1 263 ? 9.65649  38.74643  -27.49584 1.000 89.93762  ? 260 ARG   A NH2 1 
ATOM   2143 N N   . SER   A 1 264 ? 12.89113 33.22455  -27.09778 1.000 61.72001  ? 261 SER   A N   1 
ATOM   2144 C CA  . SER   A 1 264 ? 12.62353 32.05452  -27.92783 1.000 61.57919  ? 261 SER   A CA  1 
ATOM   2145 C C   . SER   A 1 264 ? 13.46385 30.86416  -27.48502 1.000 57.33444  ? 261 SER   A C   1 
ATOM   2146 O O   . SER   A 1 264 ? 12.94773 29.75164  -27.32694 1.000 59.44685  ? 261 SER   A O   1 
ATOM   2147 C CB  . SER   A 1 264 ? 12.89033 32.38015  -29.39649 1.000 57.85710  ? 261 SER   A CB  1 
ATOM   2148 O OG  . SER   A 1 264 ? 12.85429 31.20398  -30.18598 1.000 67.90367  ? 261 SER   A OG  1 
ATOM   2149 N N   . LEU   A 1 265 ? 14.76671 31.07955  -27.28555 1.000 57.79078  ? 262 LEU   A N   1 
ATOM   2150 C CA  . LEU   A 1 265 ? 15.63396 29.99640  -26.83547 1.000 50.98208  ? 262 LEU   A CA  1 
ATOM   2151 C C   . LEU   A 1 265 ? 15.20759 29.48207  -25.46763 1.000 53.23055  ? 262 LEU   A C   1 
ATOM   2152 O O   . LEU   A 1 265 ? 15.15549 28.26740  -25.24376 1.000 49.44715  ? 262 LEU   A O   1 
ATOM   2153 C CB  . LEU   A 1 265 ? 17.08922 30.46452  -26.80024 1.000 53.87352  ? 262 LEU   A CB  1 
ATOM   2154 C CG  . LEU   A 1 265 ? 18.09864 29.45823  -26.24073 1.000 50.98959  ? 262 LEU   A CG  1 
ATOM   2155 C CD1 . LEU   A 1 265 ? 18.08845 28.17572  -27.06265 1.000 48.73715  ? 262 LEU   A CD1 1 
ATOM   2156 C CD2 . LEU   A 1 265 ? 19.49357 30.05828  -26.19662 1.000 46.96398  ? 262 LEU   A CD2 1 
ATOM   2157 N N   . LEU   A 1 266 ? 14.89350 30.39288  -24.54154 1.000 48.74259  ? 263 LEU   A N   1 
ATOM   2158 C CA  . LEU   A 1 266 ? 14.49143 29.97822  -23.20107 1.000 54.69588  ? 263 LEU   A CA  1 
ATOM   2159 C C   . LEU   A 1 266 ? 13.20460 29.16360  -23.23638 1.000 51.79358  ? 263 LEU   A C   1 
ATOM   2160 O O   . LEU   A 1 266 ? 13.06838 28.17588  -22.50569 1.000 50.98207  ? 263 LEU   A O   1 
ATOM   2161 C CB  . LEU   A 1 266 ? 14.32848 31.20128  -22.29851 1.000 52.49902  ? 263 LEU   A CB  1 
ATOM   2162 C CG  . LEU   A 1 266 ? 13.91921 30.91598  -20.85176 1.000 53.82589  ? 263 LEU   A CG  1 
ATOM   2163 C CD1 . LEU   A 1 266 ? 14.98389 30.09054  -20.14507 1.000 51.30135  ? 263 LEU   A CD1 1 
ATOM   2164 C CD2 . LEU   A 1 266 ? 13.65040 32.21030  -20.09839 1.000 55.69031  ? 263 LEU   A CD2 1 
ATOM   2165 N N   . SER   A 1 267 ? 12.24913 29.55988  -24.08202 1.000 50.36837  ? 264 SER   A N   1 
ATOM   2166 C CA  . SER   A 1 267 ? 11.00687 28.80152  -24.19863 1.000 55.54520  ? 264 SER   A CA  1 
ATOM   2167 C C   . SER   A 1 267 ? 11.27048 27.38085  -24.68039 1.000 55.49494  ? 264 SER   A C   1 
ATOM   2168 O O   . SER   A 1 267 ? 10.67328 26.42406  -24.17322 1.000 54.30592  ? 264 SER   A O   1 
ATOM   2169 C CB  . SER   A 1 267 ? 10.03931 29.51245  -25.14588 1.000 53.32752  ? 264 SER   A CB  1 
ATOM   2170 O OG  . SER   A 1 267 ? 9.65177  30.77343  -24.63155 1.000 73.67218  ? 264 SER   A OG  1 
ATOM   2171 N N   . GLN   A 1 268 ? 12.16890 27.22240  -25.65543 1.000 50.00843  ? 265 GLN   A N   1 
ATOM   2172 C CA  . GLN   A 1 268 ? 12.44281 25.89614  -26.19700 1.000 52.03890  ? 265 GLN   A CA  1 
ATOM   2173 C C   . GLN   A 1 268 ? 13.22082 25.03334  -25.21317 1.000 46.55690  ? 265 GLN   A C   1 
ATOM   2174 O O   . GLN   A 1 268 ? 13.10005 23.80364  -25.24381 1.000 55.42456  ? 265 GLN   A O   1 
ATOM   2175 C CB  . GLN   A 1 268 ? 13.19785 26.01756  -27.51885 1.000 51.09056  ? 265 GLN   A CB  1 
ATOM   2176 C CG  . GLN   A 1 268 ? 12.44304 26.80542  -28.57896 1.000 45.36150  ? 265 GLN   A CG  1 
ATOM   2177 C CD  . GLN   A 1 268 ? 13.21232 26.90927  -29.87845 1.000 54.48627  ? 265 GLN   A CD  1 
ATOM   2178 O OE1 . GLN   A 1 268 ? 13.43404 28.00358  -30.39570 1.000 61.37168  ? 265 GLN   A OE1 1 
ATOM   2179 N NE2 . GLN   A 1 268 ? 13.62193 25.76604  -30.41619 1.000 56.30123  ? 265 GLN   A NE2 1 
ATOM   2180 N N   . MET   A 1 269 ? 14.02020 25.64987  -24.33946 1.000 52.82466  ? 266 MET   A N   1 
ATOM   2181 C CA  . MET   A 1 269 ? 14.69635 24.90328  -23.28585 1.000 48.64695  ? 266 MET   A CA  1 
ATOM   2182 C C   . MET   A 1 269 ? 13.76259 24.53761  -22.14017 1.000 49.17278  ? 266 MET   A C   1 
ATOM   2183 O O   . MET   A 1 269 ? 14.08740 23.63841  -21.35725 1.000 49.27201  ? 266 MET   A O   1 
ATOM   2184 C CB  . MET   A 1 269 ? 15.88062 25.70427  -22.73744 1.000 44.46408  ? 266 MET   A CB  1 
ATOM   2185 C CG  . MET   A 1 269 ? 16.92955 26.06975  -23.77553 1.000 47.22723  ? 266 MET   A CG  1 
ATOM   2186 S SD  . MET   A 1 269 ? 18.26725 27.06001  -23.07851 1.000 53.50415  ? 266 MET   A SD  1 
ATOM   2187 C CE  . MET   A 1 269 ? 19.19025 25.80388  -22.19868 1.000 45.75500  ? 266 MET   A CE  1 
ATOM   2188 N N   . LEU   A 1 270 ? 12.61910 25.21469  -22.02235 1.000 49.34807  ? 267 LEU   A N   1 
ATOM   2189 C CA  . LEU   A 1 270 ? 11.65709 24.96737  -20.95611 1.000 46.05888  ? 267 LEU   A CA  1 
ATOM   2190 C C   . LEU   A 1 270 ? 10.37017 24.33709  -21.47665 1.000 51.80746  ? 267 LEU   A C   1 
ATOM   2191 O O   . LEU   A 1 270 ? 9.33220  24.41125  -20.81107 1.000 48.11298  ? 267 LEU   A O   1 
ATOM   2192 C CB  . LEU   A 1 270 ? 11.35183 26.26527  -20.20649 1.000 42.53945  ? 267 LEU   A CB  1 
ATOM   2193 C CG  . LEU   A 1 270 ? 12.52922 26.87986  -19.44701 1.000 51.43258  ? 267 LEU   A CG  1 
ATOM   2194 C CD1 . LEU   A 1 270 ? 12.10504 28.14942  -18.72393 1.000 47.45085  ? 267 LEU   A CD1 1 
ATOM   2195 C CD2 . LEU   A 1 270 ? 13.11313 25.87067  -18.46849 1.000 45.70826  ? 267 LEU   A CD2 1 
ATOM   2196 N N   . HIS   A 1 271 ? 10.41900 23.72471  -22.65733 1.000 50.56602  ? 268 HIS   A N   1 
ATOM   2197 C CA  . HIS   A 1 271 ? 9.26566  23.00659  -23.17892 1.000 50.49501  ? 268 HIS   A CA  1 
ATOM   2198 C C   . HIS   A 1 271 ? 8.90075  21.85314  -22.25019 1.000 59.23002  ? 268 HIS   A C   1 
ATOM   2199 O O   . HIS   A 1 271 ? 9.77292  21.12297  -21.76833 1.000 50.11380  ? 268 HIS   A O   1 
ATOM   2200 C CB  . HIS   A 1 271 ? 9.57111  22.48311  -24.58290 1.000 54.90266  ? 268 HIS   A CB  1 
ATOM   2201 C CG  . HIS   A 1 271 ? 8.35836  22.30503  -25.44111 1.000 65.81262  ? 268 HIS   A CG  1 
ATOM   2202 N ND1 . HIS   A 1 271 ? 7.41538  21.32732  -25.20611 1.000 65.85306  ? 268 HIS   A ND1 1 
ATOM   2203 C CD2 . HIS   A 1 271 ? 7.93651  22.97920  -26.53700 1.000 67.20004  ? 268 HIS   A CD2 1 
ATOM   2204 C CE1 . HIS   A 1 271 ? 6.46331  21.40888  -26.11846 1.000 78.60834  ? 268 HIS   A CE1 1 
ATOM   2205 N NE2 . HIS   A 1 271 ? 6.75599  22.40235  -26.93842 1.000 79.10721  ? 268 HIS   A NE2 1 
ATOM   2206 N N   . TYR   A 1 272 ? 7.59910  21.70116  -21.98634 1.000 52.10081  ? 269 TYR   A N   1 
ATOM   2207 C CA  . TYR   A 1 272 ? 7.13978  20.62046  -21.11750 1.000 49.94126  ? 269 TYR   A CA  1 
ATOM   2208 C C   . TYR   A 1 272 ? 7.48986  19.25719  -21.70073 1.000 55.59857  ? 269 TYR   A C   1 
ATOM   2209 O O   . TYR   A 1 272 ? 8.03222  18.39130  -21.00445 1.000 57.29413  ? 269 TYR   A O   1 
ATOM   2210 C CB  . TYR   A 1 272 ? 5.63176  20.72502  -20.88921 1.000 48.37198  ? 269 TYR   A CB  1 
ATOM   2211 C CG  . TYR   A 1 272 ? 5.22946  21.65706  -19.77067 1.000 54.80836  ? 269 TYR   A CG  1 
ATOM   2212 C CD1 . TYR   A 1 272 ? 5.65851  21.43620  -18.46706 1.000 52.56868  ? 269 TYR   A CD1 1 
ATOM   2213 C CD2 . TYR   A 1 272 ? 4.40228  22.74661  -20.01290 1.000 54.84860  ? 269 TYR   A CD2 1 
ATOM   2214 C CE1 . TYR   A 1 272 ? 5.28557  22.28453  -17.43790 1.000 54.26632  ? 269 TYR   A CE1 1 
ATOM   2215 C CE2 . TYR   A 1 272 ? 4.02415  23.59890  -18.99182 1.000 52.56494  ? 269 TYR   A CE2 1 
ATOM   2216 C CZ  . TYR   A 1 272 ? 4.46722  23.36287  -17.70728 1.000 57.86004  ? 269 TYR   A CZ  1 
ATOM   2217 O OH  . TYR   A 1 272 ? 4.08930  24.21061  -16.69243 1.000 55.38808  ? 269 TYR   A OH  1 
ATOM   2218 N N   . ASP   A 1 273 ? 7.18423  19.05092  -22.97381 1.000 50.16281  ? 270 ASP   A N   1 
ATOM   2219 C CA  . ASP   A 1 273 ? 7.40634  17.76166  -23.61850 1.000 53.34004  ? 270 ASP   A CA  1 
ATOM   2220 C C   . ASP   A 1 273 ? 8.89956  17.50346  -23.76825 1.000 55.26853  ? 270 ASP   A C   1 
ATOM   2221 O O   . ASP   A 1 273 ? 9.57609  18.24525  -24.49268 1.000 49.73126  ? 270 ASP   A O   1 
ATOM   2222 C CB  . ASP   A 1 273 ? 6.71634  17.73486  -24.98181 1.000 56.11768  ? 270 ASP   A CB  1 
ATOM   2223 C CG  . ASP   A 1 273 ? 6.70500  16.34993  -25.61236 1.000 64.33055  ? 270 ASP   A CG  1 
ATOM   2224 O OD1 . ASP   A 1 273 ? 7.34896  15.42745  -25.06782 1.000 58.67252  ? 270 ASP   A OD1 1 
ATOM   2225 O OD2 . ASP   A 1 273 ? 6.04121  16.18259  -26.65826 1.000 69.77651  ? 270 ASP   A OD2 1 
ATOM   2226 N N   . PRO   A 1 274 ? 9.45314  16.47740  -23.11492 1.000 57.17127  ? 271 PRO   A N   1 
ATOM   2227 C CA  . PRO   A 1 274 ? 10.89280 16.20920  -23.26408 1.000 53.07379  ? 271 PRO   A CA  1 
ATOM   2228 C C   . PRO   A 1 274 ? 11.29004 15.84142  -24.68106 1.000 57.31453  ? 271 PRO   A C   1 
ATOM   2229 O O   . PRO   A 1 274 ? 12.44798 16.05301  -25.06439 1.000 54.43142  ? 271 PRO   A O   1 
ATOM   2230 C CB  . PRO   A 1 274 ? 11.13829 15.04613  -22.29052 1.000 43.53343  ? 271 PRO   A CB  1 
ATOM   2231 C CG  . PRO   A 1 274 ? 9.96559  15.05216  -21.36243 1.000 51.92834  ? 271 PRO   A CG  1 
ATOM   2232 C CD  . PRO   A 1 274 ? 8.81071  15.55253  -22.16724 1.000 46.70425  ? 271 PRO   A CD  1 
ATOM   2233 N N   . ASN   A 1 275 ? 10.36210 15.29464  -25.47165 1.000 61.54239  ? 272 ASN   A N   1 
ATOM   2234 C CA  . ASN   A 1 275 ? 10.66306 14.97135  -26.86226 1.000 53.18871  ? 272 ASN   A CA  1 
ATOM   2235 C C   . ASN   A 1 275 ? 10.74007 16.22166  -27.72750 1.000 58.71702  ? 272 ASN   A C   1 
ATOM   2236 O O   . ASN   A 1 275 ? 11.42691 16.22177  -28.75506 1.000 66.28100  ? 272 ASN   A O   1 
ATOM   2237 C CB  . ASN   A 1 275 ? 9.61020  14.01264  -27.41551 1.000 53.21794  ? 272 ASN   A CB  1 
ATOM   2238 C CG  . ASN   A 1 275 ? 9.48768  12.74754  -26.59173 1.000 77.52261  ? 272 ASN   A CG  1 
ATOM   2239 O OD1 . ASN   A 1 275 ? 10.47906 12.23276  -26.07322 1.000 73.15519  ? 272 ASN   A OD1 1 
ATOM   2240 N ND2 . ASN   A 1 275 ? 8.26639  12.24244  -26.46001 1.000 87.06364  ? 272 ASN   A ND2 1 
ATOM   2241 N N   . LYS   A 1 276 ? 10.04179 17.28768  -27.34025 1.000 54.73706  ? 273 LYS   A N   1 
ATOM   2242 C CA  . LYS   A 1 276 ? 10.07507 18.53613  -28.08839 1.000 58.20927  ? 273 LYS   A CA  1 
ATOM   2243 C C   . LYS   A 1 276 ? 11.08208 19.53297  -27.53861 1.000 57.67597  ? 273 LYS   A C   1 
ATOM   2244 O O   . LYS   A 1 276 ? 11.39988 20.50955  -28.22590 1.000 50.83097  ? 273 LYS   A O   1 
ATOM   2245 C CB  . LYS   A 1 276 ? 8.68671  19.18751  -28.10218 1.000 59.58973  ? 273 LYS   A CB  1 
ATOM   2246 C CG  . LYS   A 1 276 ? 7.60389  18.34232  -28.75785 1.000 68.07360  ? 273 LYS   A CG  1 
ATOM   2247 C CD  . LYS   A 1 276 ? 7.86690  18.16276  -30.24279 1.000 69.38362  ? 273 LYS   A CD  1 
ATOM   2248 C CE  . LYS   A 1 276 ? 6.70571  17.46163  -30.92867 1.000 79.54884  ? 273 LYS   A CE  1 
ATOM   2249 N NZ  . LYS   A 1 276 ? 6.92058  17.35448  -32.39900 1.000 91.30968  ? 273 LYS   A NZ  1 
ATOM   2250 N N   . ARG   A 1 277 ? 11.58169 19.31294  -26.32447 1.000 48.63390  ? 274 ARG   A N   1 
ATOM   2251 C CA  . ARG   A 1 277 ? 12.52461 20.24242  -25.72045 1.000 47.54748  ? 274 ARG   A CA  1 
ATOM   2252 C C   . ARG   A 1 277 ? 13.79073 20.31191  -26.56376 1.000 51.40132  ? 274 ARG   A C   1 
ATOM   2253 O O   . ARG   A 1 277 ? 14.30900 19.28470  -27.01209 1.000 53.85845  ? 274 ARG   A O   1 
ATOM   2254 C CB  . ARG   A 1 277 ? 12.84134 19.80348  -24.28862 1.000 43.35383  ? 274 ARG   A CB  1 
ATOM   2255 C CG  . ARG   A 1 277 ? 13.48088 20.87416  -23.41042 1.000 43.61731  ? 274 ARG   A CG  1 
ATOM   2256 C CD  . ARG   A 1 277 ? 13.58287 20.39127  -21.96753 1.000 45.12475  ? 274 ARG   A CD  1 
ATOM   2257 N NE  . ARG   A 1 277 ? 12.27568 20.03210  -21.42798 1.000 47.96227  ? 274 ARG   A NE  1 
ATOM   2258 C CZ  . ARG   A 1 277 ? 12.08170 19.14904  -20.45730 1.000 46.93215  ? 274 ARG   A CZ  1 
ATOM   2259 N NH1 . ARG   A 1 277 ? 13.09263 18.50872  -19.89314 1.000 40.60245  ? 274 ARG   A NH1 1 
ATOM   2260 N NH2 . ARG   A 1 277 ? 10.84129 18.89366  -20.04991 1.000 42.46892  ? 274 ARG   A NH2 1 
ATOM   2261 N N   . ILE   A 1 278 ? 14.27596 21.53422  -26.79528 1.000 52.00677  ? 275 ILE   A N   1 
ATOM   2262 C CA  . ILE   A 1 278 ? 15.39634 21.72460  -27.70570 1.000 47.52684  ? 275 ILE   A CA  1 
ATOM   2263 C C   . ILE   A 1 278 ? 16.62839 20.99337  -27.17729 1.000 54.91757  ? 275 ILE   A C   1 
ATOM   2264 O O   . ILE   A 1 278 ? 16.84170 20.87388  -25.96465 1.000 45.98927  ? 275 ILE   A O   1 
ATOM   2265 C CB  . ILE   A 1 278 ? 15.67840 23.22389  -27.91128 1.000 51.40594  ? 275 ILE   A CB  1 
ATOM   2266 C CG1 . ILE   A 1 278 ? 16.62010 23.44104  -29.09896 1.000 51.64170  ? 275 ILE   A CG1 1 
ATOM   2267 C CG2 . ILE   A 1 278 ? 16.25164 23.84995  -26.64099 1.000 44.66714  ? 275 ILE   A CG2 1 
ATOM   2268 C CD1 . ILE   A 1 278 ? 16.75460 24.89030  -29.52632 1.000 45.95437  ? 275 ILE   A CD1 1 
ATOM   2269 N N   . SER   A 1 279 ? 17.43099 20.47243  -28.09682 1.000 55.11548  ? 276 SER   A N   1 
ATOM   2270 C CA  . SER   A 1 279 ? 18.65348 19.78106  -27.72391 1.000 54.25655  ? 276 SER   A CA  1 
ATOM   2271 C C   . SER   A 1 279 ? 19.80269 20.77142  -27.58101 1.000 53.24571  ? 276 SER   A C   1 
ATOM   2272 O O   . SER   A 1 279 ? 19.74578 21.90188  -28.06935 1.000 47.44455  ? 276 SER   A O   1 
ATOM   2273 C CB  . SER   A 1 279 ? 19.01118 18.72110  -28.76069 1.000 56.99123  ? 276 SER   A CB  1 
ATOM   2274 O OG  . SER   A 1 279 ? 19.41794 19.32654  -29.97448 1.000 52.02866  ? 276 SER   A OG  1 
ATOM   2275 N N   . ALA   A 1 280 ? 20.86176 20.32334  -26.90240 1.000 40.89046  ? 277 ALA   A N   1 
ATOM   2276 C CA  . ALA   A 1 280 ? 22.02776 21.17826  -26.70888 1.000 55.72796  ? 277 ALA   A CA  1 
ATOM   2277 C C   . ALA   A 1 280 ? 22.64407 21.58445  -28.04225 1.000 57.07487  ? 277 ALA   A C   1 
ATOM   2278 O O   . ALA   A 1 280 ? 22.98471 22.75642  -28.24522 1.000 55.21331  ? 277 ALA   A O   1 
ATOM   2279 C CB  . ALA   A 1 280 ? 23.05803 20.47081  -25.82897 1.000 47.18710  ? 277 ALA   A CB  1 
ATOM   2280 N N   . LYS   A 1 281 ? 22.78311 20.63441  -28.97092 1.000 58.44897  ? 278 LYS   A N   1 
ATOM   2281 C CA  . LYS   A 1 281 ? 23.36366 20.96484  -30.26790 1.000 53.43783  ? 278 LYS   A CA  1 
ATOM   2282 C C   . LYS   A 1 281 ? 22.47471 21.93084  -31.04292 1.000 60.10637  ? 278 LYS   A C   1 
ATOM   2283 O O   . LYS   A 1 281 ? 22.97172 22.88386  -31.65389 1.000 53.79389  ? 278 LYS   A O   1 
ATOM   2284 C CB  . LYS   A 1 281 ? 23.61326 19.69488  -31.08155 1.000 62.04533  ? 278 LYS   A CB  1 
ATOM   2285 C CG  . LYS   A 1 281 ? 24.47290 19.94044  -32.31377 1.000 61.79117  ? 278 LYS   A CG  1 
ATOM   2286 C CD  . LYS   A 1 281 ? 24.59489 18.71168  -33.19720 1.000 72.62907  ? 278 LYS   A CD  1 
ATOM   2287 C CE  . LYS   A 1 281 ? 25.51787 18.99676  -34.37377 1.000 88.41457  ? 278 LYS   A CE  1 
ATOM   2288 N NZ  . LYS   A 1 281 ? 25.44713 17.95001  -35.42524 1.000 103.30111 ? 278 LYS   A NZ  1 
ATOM   2289 N N   . ALA   A 1 282 ? 21.15807 21.70623  -31.02796 1.000 53.97701  ? 279 ALA   A N   1 
ATOM   2290 C CA  . ALA   A 1 282 ? 20.25173 22.61416  -31.72401 1.000 55.60590  ? 279 ALA   A CA  1 
ATOM   2291 C C   . ALA   A 1 282 ? 20.24271 23.99577  -31.08404 1.000 58.34900  ? 279 ALA   A C   1 
ATOM   2292 O O   . ALA   A 1 282 ? 20.11559 25.00354  -31.78883 1.000 59.85684  ? 279 ALA   A O   1 
ATOM   2293 C CB  . ALA   A 1 282 ? 18.83790 22.03343  -31.75164 1.000 49.52346  ? 279 ALA   A CB  1 
ATOM   2294 N N   . ALA   A 1 283 ? 20.37821 24.06479  -29.75771 1.000 55.75200  ? 280 ALA   A N   1 
ATOM   2295 C CA  . ALA   A 1 283 ? 20.42113 25.36120  -29.09130 1.000 64.18159  ? 280 ALA   A CA  1 
ATOM   2296 C C   . ALA   A 1 283 ? 21.63169 26.17315  -29.52973 1.000 54.49890  ? 280 ALA   A C   1 
ATOM   2297 O O   . ALA   A 1 283 ? 21.56458 27.40598  -29.58294 1.000 60.89701  ? 280 ALA   A O   1 
ATOM   2298 C CB  . ALA   A 1 283 ? 20.42130 25.17373  -27.57405 1.000 52.17034  ? 280 ALA   A CB  1 
ATOM   2299 N N   . LEU   A 1 284 ? 22.74083 25.50315  -29.85315 1.000 58.20664  ? 281 LEU   A N   1 
ATOM   2300 C CA  . LEU   A 1 284 ? 23.91980 26.20892  -30.34273 1.000 56.03030  ? 281 LEU   A CA  1 
ATOM   2301 C C   . LEU   A 1 284 ? 23.65998 26.87475  -31.68885 1.000 59.79479  ? 281 LEU   A C   1 
ATOM   2302 O O   . LEU   A 1 284 ? 24.29954 27.88173  -32.01429 1.000 61.85799  ? 281 LEU   A O   1 
ATOM   2303 C CB  . LEU   A 1 284 ? 25.10107 25.24325  -30.44145 1.000 57.99602  ? 281 LEU   A CB  1 
ATOM   2304 C CG  . LEU   A 1 284 ? 25.62149 24.69953  -29.10742 1.000 55.57338  ? 281 LEU   A CG  1 
ATOM   2305 C CD1 . LEU   A 1 284 ? 26.62388 23.57839  -29.32799 1.000 61.80356  ? 281 LEU   A CD1 1 
ATOM   2306 C CD2 . LEU   A 1 284 ? 26.24928 25.81813  -28.29569 1.000 53.05065  ? 281 LEU   A CD2 1 
ATOM   2307 N N   . ALA   A 1 285 ? 22.73063 26.33708  -32.47582 1.000 59.48097  ? 282 ALA   A N   1 
ATOM   2308 C CA  . ALA   A 1 285 ? 22.37516 26.89901  -33.77092 1.000 54.83967  ? 282 ALA   A CA  1 
ATOM   2309 C C   . ALA   A 1 285 ? 21.27040 27.94561  -33.68554 1.000 60.73436  ? 282 ALA   A C   1 
ATOM   2310 O O   . ALA   A 1 285 ? 20.87412 28.49115  -34.72052 1.000 63.87031  ? 282 ALA   A O   1 
ATOM   2311 C CB  . ALA   A 1 285 ? 21.95126 25.78066  -34.72854 1.000 62.42307  ? 282 ALA   A CB  1 
ATOM   2312 N N   . HIS   A 1 286 ? 20.77371 28.23955  -32.48795 1.000 62.68759  ? 283 HIS   A N   1 
ATOM   2313 C CA  . HIS   A 1 286 ? 19.69603 29.20617  -32.33711 1.000 68.09172  ? 283 HIS   A CA  1 
ATOM   2314 C C   . HIS   A 1 286 ? 20.19172 30.61186  -32.67780 1.000 66.25102  ? 283 HIS   A C   1 
ATOM   2315 O O   . HIS   A 1 286 ? 21.34938 30.94622  -32.40349 1.000 68.84014  ? 283 HIS   A O   1 
ATOM   2316 C CB  . HIS   A 1 286 ? 19.15141 29.17066  -30.90704 1.000 62.59931  ? 283 HIS   A CB  1 
ATOM   2317 C CG  . HIS   A 1 286 ? 17.86132 29.90844  -30.73273 1.000 61.74803  ? 283 HIS   A CG  1 
ATOM   2318 N ND1 . HIS   A 1 286 ? 17.80722 31.25750  -30.45763 1.000 58.29684  ? 283 HIS   A ND1 1 
ATOM   2319 C CD2 . HIS   A 1 286 ? 16.57641 29.48702  -30.80388 1.000 63.90596  ? 283 HIS   A CD2 1 
ATOM   2320 C CE1 . HIS   A 1 286 ? 16.54478 31.63492  -30.36350 1.000 68.87558  ? 283 HIS   A CE1 1 
ATOM   2321 N NE2 . HIS   A 1 286 ? 15.77770 30.57952  -30.56901 1.000 64.50418  ? 283 HIS   A NE2 1 
ATOM   2322 N N   . PRO   A 1 287 ? 19.33560 31.46200  -33.27674 1.000 71.24595  ? 284 PRO   A N   1 
ATOM   2323 C CA  . PRO   A 1 287 ? 19.76297 32.82085  -33.64903 1.000 74.06672  ? 284 PRO   A CA  1 
ATOM   2324 C C   . PRO   A 1 287 ? 20.17216 33.69010  -32.46840 1.000 73.82864  ? 284 PRO   A C   1 
ATOM   2325 O O   . PRO   A 1 287 ? 20.63171 34.81972  -32.65949 1.000 81.90543  ? 284 PRO   A O   1 
ATOM   2326 C CB  . PRO   A 1 287 ? 18.52517 33.39285  -34.35331 1.000 72.05624  ? 284 PRO   A CB  1 
ATOM   2327 C CG  . PRO   A 1 287 ? 17.79967 32.20032  -34.86248 1.000 71.98882  ? 284 PRO   A CG  1 
ATOM   2328 C CD  . PRO   A 1 287 ? 18.01234 31.13106  -33.83168 1.000 69.44914  ? 284 PRO   A CD  1 
ATOM   2329 N N   . PHE   A 1 288 ? 19.99928 33.19006  -31.24492 1.000 71.23615  ? 285 PHE   A N   1 
ATOM   2330 C CA  . PHE   A 1 288 ? 20.49980 33.91260  -30.08338 1.000 75.54451  ? 285 PHE   A CA  1 
ATOM   2331 C C   . PHE   A 1 288 ? 22.02187 33.97435  -30.06340 1.000 69.18095  ? 285 PHE   A C   1 
ATOM   2332 O O   . PHE   A 1 288 ? 22.58358 34.90068  -29.47058 1.000 67.47514  ? 285 PHE   A O   1 
ATOM   2333 C CB  . PHE   A 1 288 ? 19.97794 33.26889  -28.79617 1.000 64.04195  ? 285 PHE   A CB  1 
ATOM   2334 C CG  . PHE   A 1 288 ? 20.33092 34.03098  -27.54842 1.000 61.42653  ? 285 PHE   A CG  1 
ATOM   2335 C CD1 . PHE   A 1 288 ? 19.81264 35.29616  -27.32458 1.000 68.81388  ? 285 PHE   A CD1 1 
ATOM   2336 C CD2 . PHE   A 1 288 ? 21.16929 33.47845  -26.59391 1.000 54.82978  ? 285 PHE   A CD2 1 
ATOM   2337 C CE1 . PHE   A 1 288 ? 20.13190 36.00056  -26.17729 1.000 68.89051  ? 285 PHE   A CE1 1 
ATOM   2338 C CE2 . PHE   A 1 288 ? 21.49270 34.17801  -25.44243 1.000 60.77909  ? 285 PHE   A CE2 1 
ATOM   2339 C CZ  . PHE   A 1 288 ? 20.97268 35.44026  -25.23431 1.000 63.95715  ? 285 PHE   A CZ  1 
ATOM   2340 N N   . PHE   A 1 289 ? 22.69807 33.02122  -30.70660 1.000 73.39118  ? 286 PHE   A N   1 
ATOM   2341 C CA  . PHE   A 1 289 ? 24.15397 32.99427  -30.77642 1.000 81.77878  ? 286 PHE   A CA  1 
ATOM   2342 C C   . PHE   A 1 289 ? 24.67945 33.30097  -32.17173 1.000 94.29525  ? 286 PHE   A C   1 
ATOM   2343 O O   . PHE   A 1 289 ? 25.86473 33.07558  -32.43440 1.000 101.12085 ? 286 PHE   A O   1 
ATOM   2344 C CB  . PHE   A 1 289 ? 24.69374 31.63449  -30.32127 1.000 69.53457  ? 286 PHE   A CB  1 
ATOM   2345 C CG  . PHE   A 1 289 ? 24.18104 31.18861  -28.98149 1.000 61.67482  ? 286 PHE   A CG  1 
ATOM   2346 C CD1 . PHE   A 1 289 ? 24.62778 31.78868  -27.81603 1.000 56.25414  ? 286 PHE   A CD1 1 
ATOM   2347 C CD2 . PHE   A 1 289 ? 23.26742 30.15207  -28.88813 1.000 52.70547  ? 286 PHE   A CD2 1 
ATOM   2348 C CE1 . PHE   A 1 289 ? 24.16056 31.37286  -26.58459 1.000 60.65532  ? 286 PHE   A CE1 1 
ATOM   2349 C CE2 . PHE   A 1 289 ? 22.79729 29.73036  -27.66109 1.000 56.56072  ? 286 PHE   A CE2 1 
ATOM   2350 C CZ  . PHE   A 1 289 ? 23.24318 30.34108  -26.50725 1.000 56.72526  ? 286 PHE   A CZ  1 
ATOM   2351 N N   . GLN   A 1 290 ? 23.83080 33.80829  -33.07150 1.000 98.36226  ? 287 GLN   A N   1 
ATOM   2352 C CA  . GLN   A 1 290 ? 24.25040 34.04188  -34.45038 1.000 106.48076 ? 287 GLN   A CA  1 
ATOM   2353 C C   . GLN   A 1 290 ? 25.37919 35.05906  -34.54935 1.000 125.11944 ? 287 GLN   A C   1 
ATOM   2354 O O   . GLN   A 1 290 ? 26.11868 35.05470  -35.54013 1.000 127.17280 ? 287 GLN   A O   1 
ATOM   2355 C CB  . GLN   A 1 290 ? 23.05862 34.50044  -35.29441 1.000 100.60472 ? 287 GLN   A CB  1 
ATOM   2356 C CG  . GLN   A 1 290 ? 22.51901 35.87346  -34.92567 1.000 107.92067 ? 287 GLN   A CG  1 
ATOM   2357 C CD  . GLN   A 1 290 ? 21.23562 36.20973  -35.65996 1.000 125.76190 ? 287 GLN   A CD  1 
ATOM   2358 O OE1 . GLN   A 1 290 ? 20.95370 35.65986  -36.72505 1.000 139.94848 ? 287 GLN   A OE1 1 
ATOM   2359 N NE2 . GLN   A 1 290 ? 20.44600 37.11244  -35.08898 1.000 121.89844 ? 287 GLN   A NE2 1 
ATOM   2360 N N   . ASP   A 1 291 ? 25.52669 35.92852  -33.55103 1.000 123.49561 ? 288 ASP   A N   1 
ATOM   2361 C CA  . ASP   A 1 291 ? 26.64481 36.85849  -33.50305 1.000 122.63581 ? 288 ASP   A CA  1 
ATOM   2362 C C   . ASP   A 1 291 ? 27.88092 36.26139  -32.84609 1.000 131.39361 ? 288 ASP   A C   1 
ATOM   2363 O O   . ASP   A 1 291 ? 28.98209 36.79138  -33.03297 1.000 141.62437 ? 288 ASP   A O   1 
ATOM   2364 C CB  . ASP   A 1 291 ? 26.23797 38.13440  -32.75828 1.000 125.54446 ? 288 ASP   A CB  1 
ATOM   2365 C CG  . ASP   A 1 291 ? 25.59388 37.84544  -31.41459 1.000 122.16732 ? 288 ASP   A CG  1 
ATOM   2366 O OD1 . ASP   A 1 291 ? 25.30788 36.66256  -31.13123 1.000 117.74008 ? 288 ASP   A OD1 1 
ATOM   2367 O OD2 . ASP   A 1 291 ? 25.37421 38.80125  -30.64075 1.000 115.56711 ? 288 ASP   A OD2 1 
ATOM   2368 N N   . VAL   A 1 292 ? 27.72680 35.17502  -32.09181 1.000 126.03531 ? 289 VAL   A N   1 
ATOM   2369 C CA  . VAL   A 1 292 ? 28.86233 34.56060  -31.41429 1.000 122.62815 ? 289 VAL   A CA  1 
ATOM   2370 C C   . VAL   A 1 292 ? 29.50264 33.45932  -32.25755 1.000 125.81546 ? 289 VAL   A C   1 
ATOM   2371 O O   . VAL   A 1 292 ? 30.70523 33.20564  -32.13123 1.000 129.25404 ? 289 VAL   A O   1 
ATOM   2372 C CB  . VAL   A 1 292 ? 28.42600 34.02037  -30.04070 1.000 115.43595 ? 289 VAL   A CB  1 
ATOM   2373 C CG1 . VAL   A 1 292 ? 29.63452 33.60472  -29.21300 1.000 107.70794 ? 289 VAL   A CG1 1 
ATOM   2374 C CG2 . VAL   A 1 292 ? 27.60611 35.06091  -29.30193 1.000 112.33223 ? 289 VAL   A CG2 1 
ATOM   2375 N N   . THR   A 1 293 ? 28.73235 32.80407  -33.12364 1.000 119.33473 ? 290 THR   A N   1 
ATOM   2376 C CA  . THR   A 1 293 ? 29.24321 31.69939  -33.92031 1.000 118.39852 ? 290 THR   A CA  1 
ATOM   2377 C C   . THR   A 1 293 ? 28.76483 31.83335  -35.35851 1.000 127.08830 ? 290 THR   A C   1 
ATOM   2378 O O   . THR   A 1 293 ? 27.76304 32.49279  -35.64759 1.000 128.39467 ? 290 THR   A O   1 
ATOM   2379 C CB  . THR   A 1 293 ? 28.80608 30.33995  -33.35493 1.000 109.57951 ? 290 THR   A CB  1 
ATOM   2380 O OG1 . THR   A 1 293 ? 29.34530 29.28778  -34.16427 1.000 108.28780 ? 290 THR   A OG1 1 
ATOM   2381 C CG2 . THR   A 1 293 ? 27.28800 30.23013  -33.34158 1.000 99.31445  ? 290 THR   A CG2 1 
ATOM   2382 N N   . LYS   A 1 294 ? 29.50738 31.19539  -36.26206 1.000 127.49712 ? 291 LYS   A N   1 
ATOM   2383 C CA  . LYS   A 1 294 ? 29.13515 31.06721  -37.65705 1.000 132.22949 ? 291 LYS   A CA  1 
ATOM   2384 C C   . LYS   A 1 294 ? 29.01314 29.59302  -38.02154 1.000 134.55015 ? 291 LYS   A C   1 
ATOM   2385 O O   . LYS   A 1 294 ? 29.87084 28.78914  -37.63916 1.000 134.03674 ? 291 LYS   A O   1 
ATOM   2386 C CB  . LYS   A 1 294 ? 30.16312 31.74494  -38.57661 1.000 135.26366 ? 291 LYS   A CB  1 
ATOM   2387 C CG  . LYS   A 1 294 ? 29.60927 32.93391  -39.34717 1.000 131.72598 ? 291 LYS   A CG  1 
ATOM   2388 C CD  . LYS   A 1 294 ? 28.97730 33.95146  -38.40924 1.000 137.94521 ? 291 LYS   A CD  1 
ATOM   2389 C CE  . LYS   A 1 294 ? 28.32169 35.08687  -39.17966 1.000 137.31203 ? 291 LYS   A CE  1 
ATOM   2390 N NZ  . LYS   A 1 294 ? 27.63919 36.05067  -38.27128 1.000 127.07128 ? 291 LYS   A NZ  1 
ATOM   2391 N N   . PRO   A 1 295 ? 27.96601 29.20689  -38.74644 1.000 134.06806 ? 292 PRO   A N   1 
ATOM   2392 C CA  . PRO   A 1 295 ? 27.74334 27.78259  -39.01374 1.000 132.16071 ? 292 PRO   A CA  1 
ATOM   2393 C C   . PRO   A 1 295 ? 28.79636 27.20522  -39.94566 1.000 135.21079 ? 292 PRO   A C   1 
ATOM   2394 O O   . PRO   A 1 295 ? 29.38060 27.90305  -40.77835 1.000 123.20682 ? 292 PRO   A O   1 
ATOM   2395 C CB  . PRO   A 1 295 ? 26.35448 27.75746  -39.66153 1.000 118.11150 ? 292 PRO   A CB  1 
ATOM   2396 C CG  . PRO   A 1 295 ? 26.21212 29.10704  -40.28067 1.000 123.39172 ? 292 PRO   A CG  1 
ATOM   2397 C CD  . PRO   A 1 295 ? 26.93349 30.05690  -39.36428 1.000 126.91841 ? 292 PRO   A CD  1 
ATOM   2398 N N   . VAL   A 1 296 ? 29.03593 25.90737  -39.78849 1.000 153.18682 ? 293 VAL   A N   1 
ATOM   2399 C CA  . VAL   A 1 296 ? 29.98466 25.18130  -40.62775 1.000 143.10762 ? 293 VAL   A CA  1 
ATOM   2400 C C   . VAL   A 1 296 ? 29.24920 24.69188  -41.86974 1.000 139.66095 ? 293 VAL   A C   1 
ATOM   2401 O O   . VAL   A 1 296 ? 28.02880 24.47831  -41.81948 1.000 152.44927 ? 293 VAL   A O   1 
ATOM   2402 C CB  . VAL   A 1 296 ? 30.63064 24.01519  -39.86110 1.000 139.22039 ? 293 VAL   A CB  1 
ATOM   2403 C CG1 . VAL   A 1 296 ? 31.28053 24.51888  -38.58595 1.000 133.31757 ? 293 VAL   A CG1 1 
ATOM   2404 C CG2 . VAL   A 1 296 ? 29.59960 22.93896  -39.54748 1.000 133.16869 ? 293 VAL   A CG2 1 
ATOM   2405 N N   . PRO   A 1 297 ? 29.93029 24.52030  -43.00258 1.000 123.13740 ? 294 PRO   A N   1 
ATOM   2406 C CA  . PRO   A 1 297 ? 29.25959 23.95524  -44.18140 1.000 121.45676 ? 294 PRO   A CA  1 
ATOM   2407 C C   . PRO   A 1 297 ? 28.89093 22.49897  -43.93912 1.000 117.73542 ? 294 PRO   A C   1 
ATOM   2408 O O   . PRO   A 1 297 ? 29.72437 21.69486  -43.51650 1.000 124.50400 ? 294 PRO   A O   1 
ATOM   2409 C CB  . PRO   A 1 297 ? 30.30562 24.10041  -45.29337 1.000 116.67142 ? 294 PRO   A CB  1 
ATOM   2410 C CG  . PRO   A 1 297 ? 31.61230 24.17794  -44.57521 1.000 119.60270 ? 294 PRO   A CG  1 
ATOM   2411 C CD  . PRO   A 1 297 ? 31.32876 24.88697  -43.28253 1.000 123.15205 ? 294 PRO   A CD  1 
ATOM   2412 N N   . HIS   A 1 298 ? 27.63115 22.16646  -44.20446 1.000 112.79281 ? 295 HIS   A N   1 
ATOM   2413 C CA  . HIS   A 1 298 ? 27.11369 20.82885  -43.94948 1.000 123.41915 ? 295 HIS   A CA  1 
ATOM   2414 C C   . HIS   A 1 298 ? 27.21294 19.98991  -45.21763 1.000 116.36803 ? 295 HIS   A C   1 
ATOM   2415 O O   . HIS   A 1 298 ? 26.66883 20.36536  -46.26180 1.000 118.86853 ? 295 HIS   A O   1 
ATOM   2416 C CB  . HIS   A 1 298 ? 25.66775 20.89293  -43.45893 1.000 131.16410 ? 295 HIS   A CB  1 
ATOM   2417 C CG  . HIS   A 1 298 ? 25.51964 21.46643  -42.08387 1.000 135.92829 ? 295 HIS   A CG  1 
ATOM   2418 N ND1 . HIS   A 1 298 ? 26.58427 21.61812  -41.22161 1.000 141.32697 ? 295 HIS   A ND1 1 
ATOM   2419 C CD2 . HIS   A 1 298 ? 24.43127 21.92548  -41.42165 1.000 139.85484 ? 295 HIS   A CD2 1 
ATOM   2420 C CE1 . HIS   A 1 298 ? 26.15856 22.14552  -40.08764 1.000 142.67288 ? 295 HIS   A CE1 1 
ATOM   2421 N NE2 . HIS   A 1 298 ? 24.85583 22.34199  -40.18312 1.000 142.03415 ? 295 HIS   A NE2 1 
ATOM   2422 N N   . LEU   A 1 299 ? 27.91013 18.85953  -45.12483 1.000 118.28088 ? 296 LEU   A N   1 
ATOM   2423 C CA  . LEU   A 1 299 ? 27.97601 17.90676  -46.22781 1.000 115.29183 ? 296 LEU   A CA  1 
ATOM   2424 C C   . LEU   A 1 299 ? 26.63200 17.20111  -46.35520 1.000 125.75339 ? 296 LEU   A C   1 
ATOM   2425 O O   . LEU   A 1 299 ? 26.23965 16.43075  -45.47292 1.000 119.87061 ? 296 LEU   A O   1 
ATOM   2426 C CB  . LEU   A 1 299 ? 29.10157 16.90329  -45.99544 1.000 103.37442 ? 296 LEU   A CB  1 
ATOM   2427 C CG  . LEU   A 1 299 ? 29.20169 15.74293  -46.98952 1.000 107.62073 ? 296 LEU   A CG  1 
ATOM   2428 C CD1 . LEU   A 1 299 ? 29.59556 16.23708  -48.37533 1.000 97.78051  ? 296 LEU   A CD1 1 
ATOM   2429 C CD2 . LEU   A 1 299 ? 30.18000 14.69122  -46.49286 1.000 98.69687  ? 296 LEU   A CD2 1 
ATOM   2430 N N   . ARG   A 1 300 ? 25.92053 17.46533  -47.44994 1.000 147.48422 ? 297 ARG   A N   1 
ATOM   2431 C CA  . ARG   A 1 300 ? 24.59887 16.87903  -47.67394 1.000 147.94529 ? 297 ARG   A CA  1 
ATOM   2432 C C   . ARG   A 1 300 ? 24.74151 15.59818  -48.49730 1.000 145.29735 ? 297 ARG   A C   1 
ATOM   2433 O O   . ARG   A 1 300 ? 24.30928 15.49426  -49.64677 1.000 146.39268 ? 297 ARG   A O   1 
ATOM   2434 C CB  . ARG   A 1 300 ? 23.67807 17.88887  -48.34658 1.000 154.70473 ? 297 ARG   A CB  1 
ATOM   2435 C CG  . ARG   A 1 300 ? 23.46606 19.15498  -47.53255 1.000 160.13150 ? 297 ARG   A CG  1 
ATOM   2436 C CD  . ARG   A 1 300 ? 22.49294 20.10515  -48.20918 1.000 170.76560 ? 297 ARG   A CD  1 
ATOM   2437 N NE  . ARG   A 1 300 ? 22.25146 21.29384  -47.39993 1.000 185.04614 ? 297 ARG   A NE  1 
ATOM   2438 C CZ  . ARG   A 1 300 ? 21.41370 22.26774  -47.72821 1.000 185.25304 ? 297 ARG   A CZ  1 
ATOM   2439 N NH1 . ARG   A 1 300 ? 20.71462 22.22909  -48.85066 1.000 178.43858 ? 297 ARG   A NH1 1 
ATOM   2440 N NH2 . ARG   A 1 300 ? 21.27298 23.30615  -46.90901 1.000 188.05265 ? 297 ARG   A NH2 1 
ATOM   2441 N N   . LEU   A 1 301 ? 25.36736 14.60664  -47.87126 1.000 126.60356 ? 298 LEU   A N   1 
ATOM   2442 C CA  . LEU   A 1 301 ? 25.58552 13.31212  -48.50521 1.000 135.68960 ? 298 LEU   A CA  1 
ATOM   2443 C C   . LEU   A 1 301 ? 25.07453 12.17797  -47.62289 1.000 147.43616 ? 298 LEU   A C   1 
ATOM   2444 O O   . LEU   A 1 301 ? 24.36995 12.41187  -46.64080 1.000 148.67718 ? 298 LEU   A O   1 
ATOM   2445 C CB  . LEU   A 1 301 ? 27.06985 13.11064  -48.81547 1.000 130.22120 ? 298 LEU   A CB  1 
ATOM   2446 C CG  . LEU   A 1 301 ? 27.46100 11.75848  -49.41373 1.000 126.27899 ? 298 LEU   A CG  1 
ATOM   2447 C CD1 . LEU   A 1 301 ? 26.70522 11.50234  -50.70881 1.000 133.67326 ? 298 LEU   A CD1 1 
ATOM   2448 C CD2 . LEU   A 1 301 ? 28.96159 11.69498  -49.64391 1.000 119.48931 ? 298 LEU   A CD2 1 
ATOM   2449 N N   . GLY   B 2 9   ? 29.64975 1.75162   -42.03903 1.000 88.80823  ? 102 GLY   B N   1 
ATOM   2450 C CA  . GLY   B 2 9   ? 28.43486 2.54312   -42.11398 1.000 106.00149 ? 102 GLY   B CA  1 
ATOM   2451 C C   . GLY   B 2 9   ? 27.79725 2.79898   -40.76157 1.000 105.60480 ? 102 GLY   B C   1 
ATOM   2452 O O   . GLY   B 2 9   ? 28.18836 2.20011   -39.76010 1.000 101.05731 ? 102 GLY   B O   1 
ATOM   2453 N N   . SER   B 2 10  ? 26.80966 3.69133   -40.73250 1.000 104.29098 ? 103 SER   B N   1 
ATOM   2454 C CA  . SER   B 2 10  ? 26.11015 4.05155   -39.50442 1.000 99.69648  ? 103 SER   B CA  1 
ATOM   2455 C C   . SER   B 2 10  ? 24.63744 3.68474   -39.62869 1.000 112.69981 ? 103 SER   B C   1 
ATOM   2456 O O   . SER   B 2 10  ? 23.95119 4.19724   -40.53013 1.000 112.54845 ? 103 SER   B O   1 
ATOM   2457 C CB  . SER   B 2 10  ? 26.26491 5.54522   -39.20597 1.000 109.37471 ? 103 SER   B CB  1 
ATOM   2458 O OG  . SER   B 2 10  ? 25.57118 5.90358   -38.02220 1.000 101.89229 ? 103 SER   B OG  1 
ATOM   2459 N N   . PRO   B 2 11  ? 24.10597 2.81387   -38.76574 1.000 98.98862  ? 104 PRO   B N   1 
ATOM   2460 C CA  . PRO   B 2 11  ? 22.69064 2.43947   -38.85317 1.000 92.01999  ? 104 PRO   B CA  1 
ATOM   2461 C C   . PRO   B 2 11  ? 21.74774 3.30738   -38.03629 1.000 88.04582  ? 104 PRO   B C   1 
ATOM   2462 O O   . PRO   B 2 11  ? 20.52669 3.12701   -38.14570 1.000 81.52110  ? 104 PRO   B O   1 
ATOM   2463 C CB  . PRO   B 2 11  ? 22.70066 1.00642   -38.30886 1.000 85.10733  ? 104 PRO   B CB  1 
ATOM   2464 C CG  . PRO   B 2 11  ? 23.76800 1.04576   -37.26188 1.000 88.24407  ? 104 PRO   B CG  1 
ATOM   2465 C CD  . PRO   B 2 11  ? 24.82498 2.00823   -37.76322 1.000 89.17455  ? 104 PRO   B CD  1 
ATOM   2466 N N   . LEU   B 2 12  ? 22.26723 4.22611   -37.22872 1.000 90.15443  ? 105 LEU   B N   1 
ATOM   2467 C CA  . LEU   B 2 12  ? 21.40974 5.03488   -36.37609 1.000 89.33452  ? 105 LEU   B CA  1 
ATOM   2468 C C   . LEU   B 2 12  ? 20.59205 6.01175   -37.21892 1.000 87.69947  ? 105 LEU   B C   1 
ATOM   2469 O O   . LEU   B 2 12  ? 21.08604 6.53079   -38.22486 1.000 96.13052  ? 105 LEU   B O   1 
ATOM   2470 C CB  . LEU   B 2 12  ? 22.24425 5.80554   -35.35383 1.000 79.23697  ? 105 LEU   B CB  1 
ATOM   2471 C CG  . LEU   B 2 12  ? 23.09393 4.97901   -34.38748 1.000 78.71302  ? 105 LEU   B CG  1 
ATOM   2472 C CD1 . LEU   B 2 12  ? 23.90941 5.88917   -33.48118 1.000 69.59817  ? 105 LEU   B CD1 1 
ATOM   2473 C CD2 . LEU   B 2 12  ? 22.21843 4.04455   -33.56731 1.000 84.66603  ? 105 LEU   B CD2 1 
ATOM   2474 N N   . PRO   B 2 13  ? 19.34916 6.28086   -36.84003 1.000 85.55742  ? 106 PRO   B N   1 
ATOM   2475 C CA  . PRO   B 2 13  ? 18.54447 7.28259   -37.54275 1.000 84.88484  ? 106 PRO   B CA  1 
ATOM   2476 C C   . PRO   B 2 13  ? 18.99232 8.68658   -37.15065 1.000 91.31334  ? 106 PRO   B C   1 
ATOM   2477 O O   . PRO   B 2 13  ? 19.87971 8.87256   -36.31973 1.000 90.92336  ? 106 PRO   B O   1 
ATOM   2478 C CB  . PRO   B 2 13  ? 17.12647 6.98729   -37.05467 1.000 91.19622  ? 106 PRO   B CB  1 
ATOM   2479 C CG  . PRO   B 2 13  ? 17.33115 6.46993   -35.67289 1.000 93.48888  ? 106 PRO   B CG  1 
ATOM   2480 C CD  . PRO   B 2 13  ? 18.60936 5.66696   -35.72309 1.000 92.56000  ? 106 PRO   B CD  1 
ATOM   2481 N N   . VAL   B 2 14  ? 18.35291 9.68253   -37.76577 1.000 91.16011  ? 107 VAL   B N   1 
ATOM   2482 C CA  . VAL   B 2 14  ? 18.65178 11.07223  -37.43670 1.000 92.61331  ? 107 VAL   B CA  1 
ATOM   2483 C C   . VAL   B 2 14  ? 18.31966 11.31647  -35.97105 1.000 85.46148  ? 107 VAL   B C   1 
ATOM   2484 O O   . VAL   B 2 14  ? 17.18924 11.08606  -35.52353 1.000 79.32589  ? 107 VAL   B O   1 
ATOM   2485 C CB  . VAL   B 2 14  ? 17.88988 12.02603  -38.36367 1.000 89.60312  ? 107 VAL   B CB  1 
ATOM   2486 C CG1 . VAL   B 2 14  ? 18.57737 12.10428  -39.72054 1.000 86.93380  ? 107 VAL   B CG1 1 
ATOM   2487 C CG2 . VAL   B 2 14  ? 16.44462 11.57373  -38.52862 1.000 98.45357  ? 107 VAL   B CG2 1 
ATOM   2488 N N   . LEU   B 2 15  ? 19.31178 11.76753  -35.21111 1.000 83.00036  ? 108 LEU   B N   1 
ATOM   2489 C CA  . LEU   B 2 15  ? 19.16156 12.00306  -33.78235 1.000 90.68696  ? 108 LEU   B CA  1 
ATOM   2490 C C   . LEU   B 2 15  ? 18.93017 13.48651  -33.53290 1.000 88.81376  ? 108 LEU   B C   1 
ATOM   2491 O O   . LEU   B 2 15  ? 19.63889 14.33292  -34.08768 1.000 94.66346  ? 108 LEU   B O   1 
ATOM   2492 C CB  . LEU   B 2 15  ? 20.39633 11.52176  -33.01921 1.000 85.60260  ? 108 LEU   B CB  1 
ATOM   2493 C CG  . LEU   B 2 15  ? 20.80329 10.06998  -33.27574 1.000 91.65246  ? 108 LEU   B CG  1 
ATOM   2494 C CD1 . LEU   B 2 15  ? 22.02687 9.69203   -32.45402 1.000 80.89357  ? 108 LEU   B CD1 1 
ATOM   2495 C CD2 . LEU   B 2 15  ? 19.64301 9.13487   -32.98109 1.000 88.57207  ? 108 LEU   B CD2 1 
ATOM   2496 N N   . SER   B 2 16  ? 17.93509 13.79668  -32.70128 1.000 82.81040  ? 109 SER   B N   1 
ATOM   2497 C CA  . SER   B 2 16  ? 17.64096 15.18899  -32.38752 1.000 94.58992  ? 109 SER   B CA  1 
ATOM   2498 C C   . SER   B 2 16  ? 18.63468 15.77524  -31.39326 1.000 102.30250 ? 109 SER   B C   1 
ATOM   2499 O O   . SER   B 2 16  ? 18.86957 16.98869  -31.40476 1.000 101.19576 ? 109 SER   B O   1 
ATOM   2500 C CB  . SER   B 2 16  ? 16.21888 15.31537  -31.83937 1.000 94.98630  ? 109 SER   B CB  1 
ATOM   2501 O OG  . SER   B 2 16  ? 16.07181 14.58056  -30.63680 1.000 101.58763 ? 109 SER   B OG  1 
ATOM   2502 N N   . TRP   B 2 17  ? 19.23177 14.93979  -30.54266 1.000 86.49765  ? 110 TRP   B N   1 
ATOM   2503 C CA  . TRP   B 2 17  ? 20.10874 15.41063  -29.47847 1.000 83.85876  ? 110 TRP   B CA  1 
ATOM   2504 C C   . TRP   B 2 17  ? 21.57137 15.52312  -29.89280 1.000 78.98016  ? 110 TRP   B C   1 
ATOM   2505 O O   . TRP   B 2 17  ? 22.34825 16.16544  -29.17808 1.000 83.02891  ? 110 TRP   B O   1 
ATOM   2506 C CB  . TRP   B 2 17  ? 19.99004 14.49759  -28.24937 1.000 78.05005  ? 110 TRP   B CB  1 
ATOM   2507 C CG  . TRP   B 2 17  ? 19.79167 13.04154  -28.56609 1.000 77.77213  ? 110 TRP   B CG  1 
ATOM   2508 C CD1 . TRP   B 2 17  ? 18.62759 12.43596  -28.94782 1.000 87.97483  ? 110 TRP   B CD1 1 
ATOM   2509 C CD2 . TRP   B 2 17  ? 20.77958 12.00469  -28.50364 1.000 79.26429  ? 110 TRP   B CD2 1 
ATOM   2510 N NE1 . TRP   B 2 17  ? 18.83308 11.09111  -29.13959 1.000 81.24068  ? 110 TRP   B NE1 1 
ATOM   2511 C CE2 . TRP   B 2 17  ? 20.14482 10.80002  -28.87210 1.000 80.13006  ? 110 TRP   B CE2 1 
ATOM   2512 C CE3 . TRP   B 2 17  ? 22.13969 11.97831  -28.17777 1.000 71.63194  ? 110 TRP   B CE3 1 
ATOM   2513 C CZ2 . TRP   B 2 17  ? 20.82307 9.58326   -28.92362 1.000 74.10563  ? 110 TRP   B CZ2 1 
ATOM   2514 C CZ3 . TRP   B 2 17  ? 22.81141 10.76798  -28.22929 1.000 66.94512  ? 110 TRP   B CZ3 1 
ATOM   2515 C CH2 . TRP   B 2 17  ? 22.15191 9.58758   -28.59943 1.000 66.92440  ? 110 TRP   B CH2 1 
ATOM   2516 N N   . ALA   B 2 18  ? 21.96550 14.93151  -31.01628 1.000 82.12266  ? 111 ALA   B N   1 
ATOM   2517 C CA  . ALA   B 2 18  ? 23.33565 15.04183  -31.50311 1.000 87.20992  ? 111 ALA   B CA  1 
ATOM   2518 C C   . ALA   B 2 18  ? 23.36929 14.55919  -32.94544 1.000 93.03074  ? 111 ALA   B C   1 
ATOM   2519 O O   . ALA   B 2 18  ? 22.38649 14.02324  -33.46375 1.000 99.80747  ? 111 ALA   B O   1 
ATOM   2520 C CB  . ALA   B 2 18  ? 24.31379 14.24293  -30.63763 1.000 85.97127  ? 111 ALA   B CB  1 
ATOM   2521 N N   . ASN   B 2 19  ? 24.51512 14.76268  -33.59072 1.000 91.65725  ? 112 ASN   B N   1 
ATOM   2522 C CA  . ASN   B 2 19  ? 24.70706 14.25334  -34.94095 1.000 102.50555 ? 112 ASN   B CA  1 
ATOM   2523 C C   . ASN   B 2 19  ? 24.71374 12.73084  -34.91490 1.000 100.29568 ? 112 ASN   B C   1 
ATOM   2524 O O   . ASN   B 2 19  ? 25.47737 12.11716  -34.16282 1.000 100.30296 ? 112 ASN   B O   1 
ATOM   2525 C CB  . ASN   B 2 19  ? 26.01259 14.78378  -35.53291 1.000 109.03503 ? 112 ASN   B CB  1 
ATOM   2526 C CG  . ASN   B 2 19  ? 26.19497 14.39775  -36.99100 1.000 124.75697 ? 112 ASN   B CG  1 
ATOM   2527 O OD1 . ASN   B 2 19  ? 25.22816 14.09884  -37.69317 1.000 122.98198 ? 112 ASN   B OD1 1 
ATOM   2528 N ND2 . ASN   B 2 19  ? 27.44086 14.40542  -37.45374 1.000 119.11985 ? 112 ASN   B ND2 1 
ATOM   2529 N N   . ARG   B 2 20  ? 23.84628 12.12341  -35.72903 1.000 100.65934 ? 113 ARG   B N   1 
ATOM   2530 C CA  . ARG   B 2 20  ? 23.76031 10.66683  -35.77188 1.000 94.23730  ? 113 ARG   B CA  1 
ATOM   2531 C C   . ARG   B 2 20  ? 25.10449 10.04201  -36.12263 1.000 99.91682  ? 113 ARG   B C   1 
ATOM   2532 O O   . ARG   B 2 20  ? 25.46760 8.98936   -35.58518 1.000 86.51920  ? 113 ARG   B O   1 
ATOM   2533 C CB  . ARG   B 2 20  ? 22.68983 10.23709  -36.77396 1.000 99.24777  ? 113 ARG   B CB  1 
ATOM   2534 C CG  . ARG   B 2 20  ? 22.77821 10.94557  -38.11709 1.000 105.81425 ? 113 ARG   B CG  1 
ATOM   2535 C CD  . ARG   B 2 20  ? 21.86815 10.29911  -39.14807 1.000 103.67198 ? 113 ARG   B CD  1 
ATOM   2536 N NE  . ARG   B 2 20  ? 22.18990 8.89046   -39.34215 1.000 104.51008 ? 113 ARG   B NE  1 
ATOM   2537 C CZ  . ARG   B 2 20  ? 23.14913 8.44419   -40.14155 1.000 109.70525 ? 113 ARG   B CZ  1 
ATOM   2538 N NH1 . ARG   B 2 20  ? 23.90574 9.27248   -40.84282 1.000 113.32979 ? 113 ARG   B NH1 1 
ATOM   2539 N NH2 . ARG   B 2 20  ? 23.35639 7.13393   -40.23761 1.000 106.75719 ? 113 ARG   B NH2 1 
ATOM   2540 N N   . GLU   B 2 21  ? 25.85923 10.67808  -37.02088 1.000 129.87166 ? 114 GLU   B N   1 
ATOM   2541 C CA  . GLU   B 2 21  ? 27.18727 10.17564  -37.35344 1.000 123.16032 ? 114 GLU   B CA  1 
ATOM   2542 C C   . GLU   B 2 21  ? 28.15474 10.37103  -36.19430 1.000 117.41941 ? 114 GLU   B C   1 
ATOM   2543 O O   . GLU   B 2 21  ? 28.98044 9.49505   -35.91460 1.000 119.17031 ? 114 GLU   B O   1 
ATOM   2544 C CB  . GLU   B 2 21  ? 27.71363 10.86858  -38.60978 1.000 132.02819 ? 114 GLU   B CB  1 
ATOM   2545 C CG  . GLU   B 2 21  ? 26.87772 10.62840  -39.85441 1.000 147.73911 ? 114 GLU   B CG  1 
ATOM   2546 C CD  . GLU   B 2 21  ? 27.40682 11.37881  -41.06129 1.000 166.13895 ? 114 GLU   B CD  1 
ATOM   2547 O OE1 . GLU   B 2 21  ? 28.33996 12.19310  -40.89501 1.000 164.71710 ? 114 GLU   B OE1 1 
ATOM   2548 O OE2 . GLU   B 2 21  ? 26.89070 11.15392  -42.17620 1.000 168.82182 ? 114 GLU   B OE2 1 
ATOM   2549 N N   . GLU   B 2 22  ? 28.06319 11.51127  -35.50508 1.000 108.10783 ? 115 GLU   B N   1 
ATOM   2550 C CA  . GLU   B 2 22  ? 28.98894 11.79316  -34.41262 1.000 100.53173 ? 115 GLU   B CA  1 
ATOM   2551 C C   . GLU   B 2 22  ? 28.82690 10.79240  -33.27500 1.000 80.91409  ? 115 GLU   B C   1 
ATOM   2552 O O   . GLU   B 2 22  ? 29.82010 10.28242  -32.74356 1.000 81.40073  ? 115 GLU   B O   1 
ATOM   2553 C CB  . GLU   B 2 22  ? 28.78263 13.22065  -33.90749 1.000 104.88013 ? 115 GLU   B CB  1 
ATOM   2554 C CG  . GLU   B 2 22  ? 29.77030 13.65296  -32.83846 1.000 103.41411 ? 115 GLU   B CG  1 
ATOM   2555 C CD  . GLU   B 2 22  ? 29.52520 15.07059  -32.36085 1.000 110.79976 ? 115 GLU   B CD  1 
ATOM   2556 O OE1 . GLU   B 2 22  ? 28.46057 15.63569  -32.69152 1.000 113.49618 ? 115 GLU   B OE1 1 
ATOM   2557 O OE2 . GLU   B 2 22  ? 30.39825 15.62025  -31.65648 1.000 105.59140 ? 115 GLU   B OE2 1 
ATOM   2558 N N   . VAL   B 2 23  ? 27.58272 10.49557  -32.88972 1.000 76.98401  ? 116 VAL   B N   1 
ATOM   2559 C CA  . VAL   B 2 23  ? 27.34640 9.53290   -31.81580 1.000 73.78520  ? 116 VAL   B CA  1 
ATOM   2560 C C   . VAL   B 2 23  ? 27.88500 8.16195   -32.20122 1.000 79.29093  ? 116 VAL   B C   1 
ATOM   2561 O O   . VAL   B 2 23  ? 28.47283 7.45249   -31.37471 1.000 63.07592  ? 116 VAL   B O   1 
ATOM   2562 C CB  . VAL   B 2 23  ? 25.84724 9.47395   -31.47010 1.000 66.87398  ? 116 VAL   B CB  1 
ATOM   2563 C CG1 . VAL   B 2 23  ? 25.58231 8.40499   -30.41979 1.000 62.35509  ? 116 VAL   B CG1 1 
ATOM   2564 C CG2 . VAL   B 2 23  ? 25.36554 10.82681  -30.98408 1.000 63.88903  ? 116 VAL   B CG2 1 
ATOM   2565 N N   . TRP   B 2 24  ? 27.70552 7.77401   -33.46555 1.000 73.43717  ? 117 TRP   B N   1 
ATOM   2566 C CA  . TRP   B 2 24  ? 28.17146 6.46699   -33.91566 1.000 77.41882  ? 117 TRP   B CA  1 
ATOM   2567 C C   . TRP   B 2 24  ? 29.69313 6.41743   -33.99762 1.000 79.91019  ? 117 TRP   B C   1 
ATOM   2568 O O   . TRP   B 2 24  ? 30.30680 5.42001   -33.60037 1.000 67.81648  ? 117 TRP   B O   1 
ATOM   2569 C CB  . TRP   B 2 24  ? 27.54064 6.12897   -35.26769 1.000 76.89363  ? 117 TRP   B CB  1 
ATOM   2570 C CG  . TRP   B 2 24  ? 27.84854 4.74695   -35.75807 1.000 74.64577  ? 117 TRP   B CG  1 
ATOM   2571 C CD1 . TRP   B 2 24  ? 28.71027 4.40474   -36.75995 1.000 90.90461  ? 117 TRP   B CD1 1 
ATOM   2572 C CD2 . TRP   B 2 24  ? 27.29569 3.51957   -35.26802 1.000 74.02088  ? 117 TRP   B CD2 1 
ATOM   2573 N NE1 . TRP   B 2 24  ? 28.72677 3.04039   -36.92508 1.000 86.69988  ? 117 TRP   B NE1 1 
ATOM   2574 C CE2 . TRP   B 2 24  ? 27.86795 2.47367   -36.02059 1.000 75.79412  ? 117 TRP   B CE2 1 
ATOM   2575 C CE3 . TRP   B 2 24  ? 26.37311 3.20329   -34.26590 1.000 69.13108  ? 117 TRP   B CE3 1 
ATOM   2576 C CZ2 . TRP   B 2 24  ? 27.54937 1.13482   -35.80158 1.000 75.37161  ? 117 TRP   B CZ2 1 
ATOM   2577 C CZ3 . TRP   B 2 24  ? 26.05641 1.87316   -34.05122 1.000 74.27527  ? 117 TRP   B CZ3 1 
ATOM   2578 C CH2 . TRP   B 2 24  ? 26.64251 0.85574   -34.81646 1.000 71.93539  ? 117 TRP   B CH2 1 
ATOM   2579 N N   . LYS   B 2 25  ? 30.32046 7.48207   -34.50862 1.000 82.05364  ? 118 LYS   B N   1 
ATOM   2580 C CA  . LYS   B 2 25  ? 31.77868 7.51034   -34.58486 1.000 74.85259  ? 118 LYS   B CA  1 
ATOM   2581 C C   . LYS   B 2 25  ? 32.40406 7.47737   -33.19644 1.000 70.43786  ? 118 LYS   B C   1 
ATOM   2582 O O   . LYS   B 2 25  ? 33.45541 6.85840   -32.99706 1.000 74.90539  ? 118 LYS   B O   1 
ATOM   2583 C CB  . LYS   B 2 25  ? 32.24985 8.74760   -35.35138 1.000 91.74235  ? 118 LYS   B CB  1 
ATOM   2584 C CG  . LYS   B 2 25  ? 31.84869 8.78150   -36.82021 1.000 110.36024 ? 118 LYS   B CG  1 
ATOM   2585 C CD  . LYS   B 2 25  ? 32.39080 7.58862   -37.58960 1.000 113.60641 ? 118 LYS   B CD  1 
ATOM   2586 C CE  . LYS   B 2 25  ? 31.93451 7.62623   -39.04067 1.000 116.32904 ? 118 LYS   B CE  1 
ATOM   2587 N NZ  . LYS   B 2 25  ? 32.42197 6.45212   -39.81582 1.000 127.97779 ? 118 LYS   B NZ  1 
ATOM   2588 N N   . ILE   B 2 26  ? 31.77350 8.14063   -32.22337 1.000 69.78635  ? 119 ILE   B N   1 
ATOM   2589 C CA  . ILE   B 2 26  ? 32.28444 8.11769   -30.85436 1.000 72.82487  ? 119 ILE   B CA  1 
ATOM   2590 C C   . ILE   B 2 26  ? 32.21909 6.70649   -30.28692 1.000 64.23884  ? 119 ILE   B C   1 
ATOM   2591 O O   . ILE   B 2 26  ? 33.16744 6.23335   -29.64759 1.000 66.73553  ? 119 ILE   B O   1 
ATOM   2592 C CB  . ILE   B 2 26  ? 31.51018 9.11963   -29.97720 1.000 73.04666  ? 119 ILE   B CB  1 
ATOM   2593 C CG1 . ILE   B 2 26  ? 31.86973 10.55479  -30.36565 1.000 74.82658  ? 119 ILE   B CG1 1 
ATOM   2594 C CG2 . ILE   B 2 26  ? 31.79209 8.87541   -28.50183 1.000 61.66968  ? 119 ILE   B CG2 1 
ATOM   2595 C CD1 . ILE   B 2 26  ? 30.94507 11.59197  -29.77626 1.000 79.13680  ? 119 ILE   B CD1 1 
ATOM   2596 N N   . MET   B 2 27  ? 31.10163 6.01021   -30.51551 1.000 58.66068  ? 120 MET   B N   1 
ATOM   2597 C CA  . MET   B 2 27  ? 30.99261 4.62105   -30.08199 1.000 64.38716  ? 120 MET   B CA  1 
ATOM   2598 C C   . MET   B 2 27  ? 32.02289 3.74243   -30.78209 1.000 68.30401  ? 120 MET   B C   1 
ATOM   2599 O O   . MET   B 2 27  ? 32.56070 2.80489   -30.18116 1.000 65.14150  ? 120 MET   B O   1 
ATOM   2600 C CB  . MET   B 2 27  ? 29.57704 4.10181   -30.33980 1.000 67.64155  ? 120 MET   B CB  1 
ATOM   2601 C CG  . MET   B 2 27  ? 28.49419 4.80049   -29.52884 1.000 59.66362  ? 120 MET   B CG  1 
ATOM   2602 S SD  . MET   B 2 27  ? 26.82561 4.33335   -30.03921 1.000 69.35463  ? 120 MET   B SD  1 
ATOM   2603 C CE  . MET   B 2 27  ? 26.82680 2.58652   -29.64591 1.000 78.83400  ? 120 MET   B CE  1 
ATOM   2604 N N   . LEU   B 2 28  ? 32.31481 4.03141   -32.05335 1.000 65.03115  ? 121 LEU   B N   1 
ATOM   2605 C CA  . LEU   B 2 28  ? 33.32235 3.25511   -32.76951 1.000 69.36474  ? 121 LEU   B CA  1 
ATOM   2606 C C   . LEU   B 2 28  ? 34.73099 3.62609   -32.32397 1.000 71.84627  ? 121 LEU   B C   1 
ATOM   2607 O O   . LEU   B 2 28  ? 35.59719 2.75227   -32.20302 1.000 79.58238  ? 121 LEU   B O   1 
ATOM   2608 C CB  . LEU   B 2 28  ? 33.17664 3.45768   -34.27800 1.000 71.23528  ? 121 LEU   B CB  1 
ATOM   2609 C CG  . LEU   B 2 28  ? 31.90678 2.93380   -34.95102 1.000 73.92893  ? 121 LEU   B CG  1 
ATOM   2610 C CD1 . LEU   B 2 28  ? 31.97287 3.17551   -36.45020 1.000 77.44773  ? 121 LEU   B CD1 1 
ATOM   2611 C CD2 . LEU   B 2 28  ? 31.70377 1.45870   -34.64819 1.000 74.67342  ? 121 LEU   B CD2 1 
ATOM   2612 N N   . ASN   B 2 29  ? 34.98037 4.91657   -32.07773 1.000 72.66966  ? 122 ASN   B N   1 
ATOM   2613 C CA  . ASN   B 2 29  ? 36.33005 5.35754   -31.73673 1.000 89.57910  ? 122 ASN   B CA  1 
ATOM   2614 C C   . ASN   B 2 29  ? 36.78172 4.82363   -30.38395 1.000 83.47893  ? 122 ASN   B C   1 
ATOM   2615 O O   . ASN   B 2 29  ? 37.97002 4.53572   -30.20164 1.000 91.78834  ? 122 ASN   B O   1 
ATOM   2616 C CB  . ASN   B 2 29  ? 36.41209 6.88469   -31.75622 1.000 89.27229  ? 122 ASN   B CB  1 
ATOM   2617 C CG  . ASN   B 2 29  ? 36.59983 7.44192   -33.15598 1.000 100.82934 ? 122 ASN   B CG  1 
ATOM   2618 O OD1 . ASN   B 2 29  ? 36.23802 6.80519   -34.14602 1.000 96.30728  ? 122 ASN   B OD1 1 
ATOM   2619 N ND2 . ASN   B 2 29  ? 37.17622 8.63583   -33.24399 1.000 110.98065 ? 122 ASN   B ND2 1 
ATOM   2620 N N   . LYS   B 2 30  ? 35.86409 4.68464   -29.42516 1.000 93.09834  ? 123 LYS   B N   1 
ATOM   2621 C CA  . LYS   B 2 30  ? 36.25789 4.15056   -28.12816 1.000 97.97282  ? 123 LYS   B CA  1 
ATOM   2622 C C   . LYS   B 2 30  ? 36.52111 2.65242   -28.18390 1.000 94.97076  ? 123 LYS   B C   1 
ATOM   2623 O O   . LYS   B 2 30  ? 37.19621 2.12156   -27.29596 1.000 97.16041  ? 123 LYS   B O   1 
ATOM   2624 C CB  . LYS   B 2 30  ? 35.19417 4.45723   -27.07366 1.000 96.27582  ? 123 LYS   B CB  1 
ATOM   2625 C CG  . LYS   B 2 30  ? 34.03030 3.48540   -27.05021 1.000 93.72203  ? 123 LYS   B CG  1 
ATOM   2626 C CD  . LYS   B 2 30  ? 33.53658 3.27894   -25.62774 1.000 83.10748  ? 123 LYS   B CD  1 
ATOM   2627 C CE  . LYS   B 2 30  ? 33.22209 4.60441   -24.95713 1.000 75.54197  ? 123 LYS   B CE  1 
ATOM   2628 N NZ  . LYS   B 2 30  ? 32.82694 4.42008   -23.53760 1.000 70.97708  ? 123 LYS   B NZ  1 
ATOM   2629 N N   . GLU   B 2 31  ? 36.00916 1.96191   -29.20602 1.000 96.35802  ? 124 GLU   B N   1 
ATOM   2630 C CA  . GLU   B 2 31  ? 36.32095 0.54631   -29.36755 1.000 107.06293 ? 124 GLU   B CA  1 
ATOM   2631 C C   . GLU   B 2 31  ? 37.80568 0.33626   -29.63282 1.000 111.85963 ? 124 GLU   B C   1 
ATOM   2632 O O   . GLU   B 2 31  ? 38.35158 -0.72528  -29.31081 1.000 119.15986 ? 124 GLU   B O   1 
ATOM   2633 C CB  . GLU   B 2 31  ? 35.48100 -0.04690  -30.49928 1.000 122.89702 ? 124 GLU   B CB  1 
ATOM   2634 C CG  . GLU   B 2 31  ? 35.39198 -1.56477  -30.49463 1.000 136.41714 ? 124 GLU   B CG  1 
ATOM   2635 C CD  . GLU   B 2 31  ? 33.96135 -2.05936  -30.37741 1.000 125.89041 ? 124 GLU   B CD  1 
ATOM   2636 O OE1 . GLU   B 2 31  ? 33.13297 -1.34397  -29.77448 1.000 99.89852  ? 124 GLU   B OE1 1 
ATOM   2637 O OE2 . GLU   B 2 31  ? 33.66285 -3.15810  -30.89334 1.000 104.24795 ? 124 GLU   B OE2 1 
ATOM   2638 N N   . LYS   B 2 32  ? 38.47304 1.33428   -30.21614 1.000 118.19476 ? 125 LYS   B N   1 
ATOM   2639 C CA  . LYS   B 2 32  ? 39.91898 1.28992   -30.38669 1.000 100.98385 ? 125 LYS   B CA  1 
ATOM   2640 C C   . LYS   B 2 32  ? 40.66389 1.63942   -29.10675 1.000 101.71996 ? 125 LYS   B C   1 
ATOM   2641 O O   . LYS   B 2 32  ? 41.84666 1.30580   -28.98175 1.000 111.56532 ? 125 LYS   B O   1 
ATOM   2642 C CB  . LYS   B 2 32  ? 40.34248 2.23879   -31.51001 1.000 115.39639 ? 125 LYS   B CB  1 
ATOM   2643 C CG  . LYS   B 2 32  ? 39.80458 1.84658   -32.87599 1.000 117.79042 ? 125 LYS   B CG  1 
ATOM   2644 C CD  . LYS   B 2 32  ? 39.33290 3.05865   -33.66142 1.000 114.63076 ? 125 LYS   B CD  1 
ATOM   2645 C CE  . LYS   B 2 32  ? 38.72299 2.64274   -34.99084 1.000 127.52167 ? 125 LYS   B CE  1 
ATOM   2646 N NZ  . LYS   B 2 32  ? 38.10732 3.79174   -35.71076 1.000 132.24282 ? 125 LYS   B NZ  1 
ATOM   2647 N N   . THR   B 2 33  ? 40.00135 2.30505   -28.15904 1.000 101.40916 ? 126 THR   B N   1 
ATOM   2648 C CA  . THR   B 2 33  ? 40.62963 2.58030   -26.87189 1.000 97.14128  ? 126 THR   B CA  1 
ATOM   2649 C C   . THR   B 2 33  ? 40.71602 1.31694   -26.02450 1.000 93.32318  ? 126 THR   B C   1 
ATOM   2650 O O   . THR   B 2 33  ? 41.69019 1.11805   -25.28924 1.000 100.65100 ? 126 THR   B O   1 
ATOM   2651 C CB  . THR   B 2 33  ? 39.85085 3.67024   -26.13293 1.000 100.99455 ? 126 THR   B CB  1 
ATOM   2652 O OG1 . THR   B 2 33  ? 39.72460 4.82318   -26.97467 1.000 93.97832  ? 126 THR   B OG1 1 
ATOM   2653 C CG2 . THR   B 2 33  ? 40.56122 4.06342   -24.84166 1.000 104.23779 ? 126 THR   B CG2 1 
ATOM   2654 N N   . TYR   B 2 34  ? 39.71241 0.44972   -26.12172 1.000 94.75408  ? 127 TYR   B N   1 
ATOM   2655 C CA  . TYR   B 2 34  ? 39.64235 -0.77604  -25.33530 1.000 87.84312  ? 127 TYR   B CA  1 
ATOM   2656 C C   . TYR   B 2 34  ? 40.17578 -1.92901  -26.17816 1.000 90.11305  ? 127 TYR   B C   1 
ATOM   2657 O O   . TYR   B 2 34  ? 39.51864 -2.37073  -27.12620 1.000 94.23137  ? 127 TYR   B O   1 
ATOM   2658 C CB  . TYR   B 2 34  ? 38.20914 -1.03862  -24.87820 1.000 86.04446  ? 127 TYR   B CB  1 
ATOM   2659 C CG  . TYR   B 2 34  ? 37.70600 -0.04715  -23.85167 1.000 82.42149  ? 127 TYR   B CG  1 
ATOM   2660 C CD1 . TYR   B 2 34  ? 37.20720 1.19187   -24.23519 1.000 72.16091  ? 127 TYR   B CD1 1 
ATOM   2661 C CD2 . TYR   B 2 34  ? 37.73116 -0.35121  -22.49803 1.000 67.84511  ? 127 TYR   B CD2 1 
ATOM   2662 C CE1 . TYR   B 2 34  ? 36.74994 2.10019   -23.29602 1.000 76.11524  ? 127 TYR   B CE1 1 
ATOM   2663 C CE2 . TYR   B 2 34  ? 37.27621 0.54818   -21.55298 1.000 73.17178  ? 127 TYR   B CE2 1 
ATOM   2664 C CZ  . TYR   B 2 34  ? 36.78676 1.77147   -21.95545 1.000 70.57230  ? 127 TYR   B CZ  1 
ATOM   2665 O OH  . TYR   B 2 34  ? 36.33279 2.66424   -21.01029 1.000 58.72745  ? 127 TYR   B OH  1 
ATOM   2666 N N   . LEU   B 2 35  ? 41.36311 -2.41390  -25.82963 1.000 91.68602  ? 128 LEU   B N   1 
ATOM   2667 C CA  . LEU   B 2 35  ? 42.00461 -3.49713  -26.55805 1.000 84.93570  ? 128 LEU   B CA  1 
ATOM   2668 C C   . LEU   B 2 35  ? 41.66224 -4.84558  -25.93757 1.000 89.38468  ? 128 LEU   B C   1 
ATOM   2669 O O   . LEU   B 2 35  ? 41.48831 -4.96878  -24.72228 1.000 107.74302 ? 128 LEU   B O   1 
ATOM   2670 C CB  . LEU   B 2 35  ? 43.52392 -3.31331  -26.57914 1.000 87.69835  ? 128 LEU   B CB  1 
ATOM   2671 C CG  . LEU   B 2 35  ? 44.13847 -2.48281  -27.70930 1.000 92.82476  ? 128 LEU   B CG  1 
ATOM   2672 C CD1 . LEU   B 2 35  ? 43.64999 -1.04365  -27.67874 1.000 92.72665  ? 128 LEU   B CD1 1 
ATOM   2673 C CD2 . LEU   B 2 35  ? 45.65782 -2.53643  -27.63744 1.000 96.69376  ? 128 LEU   B CD2 1 
ATOM   2674 N N   . ARG   B 2 36  ? 41.56558 -5.86120  -26.79259 1.000 100.41692 ? 129 ARG   B N   1 
ATOM   2675 C CA  . ARG   B 2 36  ? 41.36738 -7.23794  -26.36462 1.000 108.85772 ? 129 ARG   B CA  1 
ATOM   2676 C C   . ARG   B 2 36  ? 42.31061 -8.14604  -27.13723 1.000 104.30681 ? 129 ARG   B C   1 
ATOM   2677 O O   . ARG   B 2 36  ? 42.52946 -7.95447  -28.33717 1.000 113.68447 ? 129 ARG   B O   1 
ATOM   2678 C CB  . ARG   B 2 36  ? 39.91833 -7.70030  -26.56892 1.000 108.45103 ? 129 ARG   B CB  1 
ATOM   2679 C CG  . ARG   B 2 36  ? 38.93071 -7.11887  -25.57200 1.000 109.28511 ? 129 ARG   B CG  1 
ATOM   2680 C CD  . ARG   B 2 36  ? 38.33979 -5.81320  -26.07071 1.000 117.03223 ? 129 ARG   B CD  1 
ATOM   2681 N NE  . ARG   B 2 36  ? 37.48595 -5.18543  -25.06996 1.000 104.85757 ? 129 ARG   B NE  1 
ATOM   2682 C CZ  . ARG   B 2 36  ? 36.69709 -4.14631  -25.30557 1.000 102.46849 ? 129 ARG   B CZ  1 
ATOM   2683 N NH1 . ARG   B 2 36  ? 36.61393 -3.60018  -26.50792 1.000 114.94162 ? 129 ARG   B NH1 1 
ATOM   2684 N NH2 . ARG   B 2 36  ? 35.97144 -3.64391  -24.31064 1.000 99.52766  ? 129 ARG   B NH2 1 
ATOM   2685 N N   . ASP   B 2 37  ? 42.86729 -9.13269  -26.44102 1.000 107.09410 ? 130 ASP   B N   1 
ATOM   2686 C CA  . ASP   B 2 37  ? 43.78008 -10.10492 -27.02799 1.000 117.69708 ? 130 ASP   B CA  1 
ATOM   2687 C C   . ASP   B 2 37  ? 43.20391 -11.49314 -26.79562 1.000 110.21021 ? 130 ASP   B C   1 
ATOM   2688 O O   . ASP   B 2 37  ? 43.03233 -11.90959 -25.64572 1.000 100.64630 ? 130 ASP   B O   1 
ATOM   2689 C CB  . ASP   B 2 37  ? 45.17772 -9.98336  -26.41367 1.000 116.94851 ? 130 ASP   B CB  1 
ATOM   2690 C CG  . ASP   B 2 37  ? 46.25542 -10.62784 -27.26926 1.000 127.06392 ? 130 ASP   B CG  1 
ATOM   2691 O OD1 . ASP   B 2 37  ? 45.95363 -11.60365 -27.98901 1.000 120.62698 ? 130 ASP   B OD1 1 
ATOM   2692 O OD2 . ASP   B 2 37  ? 47.41046 -10.15420 -27.22025 1.000 127.70342 ? 130 ASP   B OD2 1 
ATOM   2693 N N   . GLN   B 2 38  ? 42.90483 -12.20691 -27.88243 1.000 106.50770 ? 131 GLN   B N   1 
ATOM   2694 C CA  . GLN   B 2 38  ? 42.32869 -13.54140 -27.75462 1.000 107.85613 ? 131 GLN   B CA  1 
ATOM   2695 C C   . GLN   B 2 38  ? 43.32104 -14.57214 -27.23222 1.000 110.61289 ? 131 GLN   B C   1 
ATOM   2696 O O   . GLN   B 2 38  ? 42.92536 -15.72162 -27.00637 1.000 105.25994 ? 131 GLN   B O   1 
ATOM   2697 C CB  . GLN   B 2 38  ? 41.76142 -14.00856 -29.09876 1.000 109.86199 ? 131 GLN   B CB  1 
ATOM   2698 C CG  . GLN   B 2 38  ? 42.79524 -14.20155 -30.20168 1.000 112.68373 ? 131 GLN   B CG  1 
ATOM   2699 C CD  . GLN   B 2 38  ? 43.10078 -12.92005 -30.95546 1.000 117.76593 ? 131 GLN   B CD  1 
ATOM   2700 O OE1 . GLN   B 2 38  ? 42.89416 -11.81853 -30.44433 1.000 117.76818 ? 131 GLN   B OE1 1 
ATOM   2701 N NE2 . GLN   B 2 38  ? 43.58865 -13.05943 -32.18320 1.000 104.37347 ? 131 GLN   B NE2 1 
ATOM   2702 N N   . HIS   B 2 39  ? 44.58209 -14.19851 -27.02905 1.000 107.83308 ? 132 HIS   B N   1 
ATOM   2703 C CA  . HIS   B 2 39  ? 45.61512 -15.10573 -26.54574 1.000 110.10791 ? 132 HIS   B CA  1 
ATOM   2704 C C   . HIS   B 2 39  ? 46.33946 -14.51095 -25.34711 1.000 112.03422 ? 132 HIS   B C   1 
ATOM   2705 O O   . HIS   B 2 39  ? 47.55060 -14.68695 -25.18191 1.000 112.24147 ? 132 HIS   B O   1 
ATOM   2706 C CB  . HIS   B 2 39  ? 46.60762 -15.44458 -27.65609 1.000 119.20733 ? 132 HIS   B CB  1 
ATOM   2707 C CG  . HIS   B 2 39  ? 45.99748 -16.17434 -28.81164 1.000 108.15488 ? 132 HIS   B CG  1 
ATOM   2708 N ND1 . HIS   B 2 39  ? 46.40120 -15.97484 -30.11429 1.000 119.88005 ? 132 HIS   B ND1 1 
ATOM   2709 C CD2 . HIS   B 2 39  ? 45.01675 -17.10666 -28.86049 1.000 119.88119 ? 132 HIS   B CD2 1 
ATOM   2710 C CE1 . HIS   B 2 39  ? 45.69303 -16.74989 -30.91622 1.000 117.29313 ? 132 HIS   B CE1 1 
ATOM   2711 N NE2 . HIS   B 2 39  ? 44.84597 -17.44701 -30.18051 1.000 119.15339 ? 132 HIS   B NE2 1 
ATOM   2712 N N   . PHE   B 2 40  ? 45.61111 -13.79342 -24.48553 1.000 107.64358 ? 133 PHE   B N   1 
ATOM   2713 C CA  . PHE   B 2 40  ? 46.23971 -13.23137 -23.29498 1.000 106.21676 ? 133 PHE   B CA  1 
ATOM   2714 C C   . PHE   B 2 40  ? 46.62927 -14.30678 -22.29034 1.000 104.35585 ? 133 PHE   B C   1 
ATOM   2715 O O   . PHE   B 2 40  ? 47.46096 -14.04645 -21.41438 1.000 107.87899 ? 133 PHE   B O   1 
ATOM   2716 C CB  . PHE   B 2 40  ? 45.32146 -12.19686 -22.63033 1.000 95.65202  ? 133 PHE   B CB  1 
ATOM   2717 C CG  . PHE   B 2 40  ? 44.05326 -12.77303 -22.05193 1.000 92.30467  ? 133 PHE   B CG  1 
ATOM   2718 C CD1 . PHE   B 2 40  ? 44.03439 -13.31674 -20.77734 1.000 92.69671  ? 133 PHE   B CD1 1 
ATOM   2719 C CD2 . PHE   B 2 40  ? 42.87334 -12.74428 -22.77409 1.000 105.63007 ? 133 PHE   B CD2 1 
ATOM   2720 C CE1 . PHE   B 2 40  ? 42.86956 -13.83833 -20.24661 1.000 92.77320  ? 133 PHE   B CE1 1 
ATOM   2721 C CE2 . PHE   B 2 40  ? 41.70526 -13.26115 -22.24691 1.000 99.38923  ? 133 PHE   B CE2 1 
ATOM   2722 C CZ  . PHE   B 2 40  ? 41.70357 -13.80764 -20.98146 1.000 84.77984  ? 133 PHE   B CZ  1 
ATOM   2723 N N   . LEU   B 2 41  ? 46.04687 -15.50325 -22.39431 1.000 104.26633 ? 134 LEU   B N   1 
ATOM   2724 C CA  . LEU   B 2 41  ? 46.39748 -16.59566 -21.49645 1.000 109.65131 ? 134 LEU   B CA  1 
ATOM   2725 C C   . LEU   B 2 41  ? 47.78172 -17.16452 -21.77297 1.000 113.03962 ? 134 LEU   B C   1 
ATOM   2726 O O   . LEU   B 2 41  ? 48.29266 -17.92767 -20.94700 1.000 114.14926 ? 134 LEU   B O   1 
ATOM   2727 C CB  . LEU   B 2 41  ? 45.34886 -17.70407 -21.58625 1.000 103.63444 ? 134 LEU   B CB  1 
ATOM   2728 C CG  . LEU   B 2 41  ? 43.99464 -17.34946 -20.97136 1.000 104.13773 ? 134 LEU   B CG  1 
ATOM   2729 C CD1 . LEU   B 2 41  ? 42.98944 -18.45786 -21.21352 1.000 106.91079 ? 134 LEU   B CD1 1 
ATOM   2730 C CD2 . LEU   B 2 41  ? 44.14440 -17.07478 -19.48196 1.000 98.19286  ? 134 LEU   B CD2 1 
ATOM   2731 N N   . GLU   B 2 42  ? 48.39576 -16.82326 -22.90810 1.000 113.88493 ? 135 GLU   B N   1 
ATOM   2732 C CA  . GLU   B 2 42  ? 49.79332 -17.17543 -23.12123 1.000 115.30301 ? 135 GLU   B CA  1 
ATOM   2733 C C   . GLU   B 2 42  ? 50.71721 -16.40533 -22.18788 1.000 121.61178 ? 135 GLU   B C   1 
ATOM   2734 O O   . GLU   B 2 42  ? 51.84900 -16.84291 -21.95330 1.000 121.17087 ? 135 GLU   B O   1 
ATOM   2735 C CB  . GLU   B 2 42  ? 50.18380 -16.92874 -24.57869 1.000 116.25067 ? 135 GLU   B CB  1 
ATOM   2736 C CG  . GLU   B 2 42  ? 49.46767 -17.83450 -25.56809 1.000 119.38133 ? 135 GLU   B CG  1 
ATOM   2737 C CD  . GLU   B 2 42  ? 49.80047 -17.50379 -27.00881 1.000 122.78361 ? 135 GLU   B CD  1 
ATOM   2738 O OE1 . GLU   B 2 42  ? 50.40994 -16.44091 -27.24973 1.000 116.42239 ? 135 GLU   B OE1 1 
ATOM   2739 O OE2 . GLU   B 2 42  ? 49.45318 -18.30680 -27.90047 1.000 137.25859 ? 135 GLU   B OE2 1 
ATOM   2740 N N   . GLN   B 2 43  ? 50.25845 -15.26943 -21.65404 1.000 114.00588 ? 136 GLN   B N   1 
ATOM   2741 C CA  . GLN   B 2 43  ? 51.00176 -14.56932 -20.61429 1.000 115.77146 ? 136 GLN   B CA  1 
ATOM   2742 C C   . GLN   B 2 43  ? 50.90317 -15.27699 -19.27046 1.000 106.42265 ? 136 GLN   B C   1 
ATOM   2743 O O   . GLN   B 2 43  ? 51.70643 -14.99720 -18.37468 1.000 105.34451 ? 136 GLN   B O   1 
ATOM   2744 C CB  . GLN   B 2 43  ? 50.49471 -13.13188 -20.47880 1.000 112.95830 ? 136 GLN   B CB  1 
ATOM   2745 C CG  . GLN   B 2 43  ? 50.53959 -12.32664 -21.76726 1.000 111.40833 ? 136 GLN   B CG  1 
ATOM   2746 C CD  . GLN   B 2 43  ? 49.94717 -10.93995 -21.60775 1.000 113.64792 ? 136 GLN   B CD  1 
ATOM   2747 O OE1 . GLN   B 2 43  ? 50.01408 -10.11505 -22.51921 1.000 115.83407 ? 136 GLN   B OE1 1 
ATOM   2748 N NE2 . GLN   B 2 43  ? 49.36043 -10.67684 -20.44512 1.000 109.74469 ? 136 GLN   B NE2 1 
ATOM   2749 N N   . HIS   B 2 44  ? 49.93295 -16.18078 -19.11178 1.000 109.82853 ? 137 HIS   B N   1 
ATOM   2750 C CA  . HIS   B 2 44  ? 49.73545 -16.95924 -17.89144 1.000 98.98763  ? 137 HIS   B CA  1 
ATOM   2751 C C   . HIS   B 2 44  ? 49.82457 -18.43424 -18.26625 1.000 116.51587 ? 137 HIS   B C   1 
ATOM   2752 O O   . HIS   B 2 44  ? 48.79449 -19.10270 -18.44370 1.000 117.76950 ? 137 HIS   B O   1 
ATOM   2753 C CB  . HIS   B 2 44  ? 48.39437 -16.63635 -17.23491 1.000 102.46808 ? 137 HIS   B CB  1 
ATOM   2754 C CG  . HIS   B 2 44  ? 48.12643 -15.17014 -17.09636 1.000 100.01113 ? 137 HIS   B CG  1 
ATOM   2755 N ND1 . HIS   B 2 44  ? 48.37767 -14.47361 -15.93380 1.000 99.14146  ? 137 HIS   B ND1 1 
ATOM   2756 C CD2 . HIS   B 2 44  ? 47.62900 -14.26792 -17.97523 1.000 105.81831 ? 137 HIS   B CD2 1 
ATOM   2757 C CE1 . HIS   B 2 44  ? 48.04656 -13.20578 -16.10220 1.000 95.11303  ? 137 HIS   B CE1 1 
ATOM   2758 N NE2 . HIS   B 2 44  ? 47.58909 -13.05454 -17.33212 1.000 105.84479 ? 137 HIS   B NE2 1 
ATOM   2759 N N   . PRO   B 2 45  ? 51.03879 -18.97601 -18.39756 1.000 126.95028 ? 138 PRO   B N   1 
ATOM   2760 C CA  . PRO   B 2 45  ? 51.17733 -20.36903 -18.85821 1.000 126.67186 ? 138 PRO   B CA  1 
ATOM   2761 C C   . PRO   B 2 45  ? 50.53056 -21.39121 -17.93907 1.000 120.41703 ? 138 PRO   B C   1 
ATOM   2762 O O   . PRO   B 2 45  ? 50.19750 -22.48990 -18.40016 1.000 121.32867 ? 138 PRO   B O   1 
ATOM   2763 C CB  . PRO   B 2 45  ? 52.69901 -20.56673 -18.92768 1.000 127.64981 ? 138 PRO   B CB  1 
ATOM   2764 C CG  . PRO   B 2 45  ? 53.26641 -19.18189 -19.01424 1.000 124.48836 ? 138 PRO   B CG  1 
ATOM   2765 C CD  . PRO   B 2 45  ? 52.34439 -18.32328 -18.20498 1.000 121.10408 ? 138 PRO   B CD  1 
ATOM   2766 N N   . LEU   B 2 46  ? 50.33789 -21.06976 -16.65993 1.000 120.18473 ? 139 LEU   B N   1 
ATOM   2767 C CA  . LEU   B 2 46  ? 49.74066 -22.00792 -15.71862 1.000 122.38334 ? 139 LEU   B CA  1 
ATOM   2768 C C   . LEU   B 2 46  ? 48.23620 -22.16479 -15.90721 1.000 121.48869 ? 139 LEU   B C   1 
ATOM   2769 O O   . LEU   B 2 46  ? 47.65851 -23.11915 -15.37490 1.000 117.00404 ? 139 LEU   B O   1 
ATOM   2770 C CB  . LEU   B 2 46  ? 50.03932 -21.56340 -14.28259 1.000 130.03189 ? 139 LEU   B CB  1 
ATOM   2771 C CG  . LEU   B 2 46  ? 49.96062 -22.62638 -13.18410 1.000 130.81277 ? 139 LEU   B CG  1 
ATOM   2772 C CD1 . LEU   B 2 46  ? 50.96031 -23.74103 -13.44852 1.000 114.16135 ? 139 LEU   B CD1 1 
ATOM   2773 C CD2 . LEU   B 2 46  ? 50.19562 -22.00519 -11.81547 1.000 118.97130 ? 139 LEU   B CD2 1 
ATOM   2774 N N   . LEU   B 2 47  ? 47.59461 -21.26926 -16.65039 1.000 114.29223 ? 140 LEU   B N   1 
ATOM   2775 C CA  . LEU   B 2 47  ? 46.15363 -21.29420 -16.84824 1.000 109.79894 ? 140 LEU   B CA  1 
ATOM   2776 C C   . LEU   B 2 47  ? 45.79875 -21.94673 -18.17890 1.000 112.55948 ? 140 LEU   B C   1 
ATOM   2777 O O   . LEU   B 2 47  ? 46.59174 -21.96651 -19.12318 1.000 115.53351 ? 140 LEU   B O   1 
ATOM   2778 C CB  . LEU   B 2 47  ? 45.57498 -19.87742 -16.79813 1.000 102.87160 ? 140 LEU   B CB  1 
ATOM   2779 C CG  . LEU   B 2 47  ? 45.75550 -19.09642 -15.49615 1.000 105.09945 ? 140 LEU   B CG  1 
ATOM   2780 C CD1 . LEU   B 2 47  ? 45.15816 -17.70480 -15.63013 1.000 97.46565  ? 140 LEU   B CD1 1 
ATOM   2781 C CD2 . LEU   B 2 47  ? 45.12871 -19.84342 -14.32929 1.000 104.49206 ? 140 LEU   B CD2 1 
ATOM   2782 N N   . GLN   B 2 48  ? 44.58020 -22.47947 -18.24120 1.000 114.39341 ? 141 GLN   B N   1 
ATOM   2783 C CA  . GLN   B 2 48  ? 44.03519 -23.07672 -19.44746 1.000 113.30143 ? 141 GLN   B CA  1 
ATOM   2784 C C   . GLN   B 2 48  ? 42.76320 -22.34544 -19.86326 1.000 114.89645 ? 141 GLN   B C   1 
ATOM   2785 O O   . GLN   B 2 48  ? 42.07542 -21.76347 -19.01811 1.000 112.26605 ? 141 GLN   B O   1 
ATOM   2786 C CB  . GLN   B 2 48  ? 43.73134 -24.56689 -19.24122 1.000 119.53238 ? 141 GLN   B CB  1 
ATOM   2787 C CG  . GLN   B 2 48  ? 44.95596 -25.40470 -18.90061 1.000 117.93558 ? 141 GLN   B CG  1 
ATOM   2788 C CD  . GLN   B 2 48  ? 46.02527 -25.34422 -19.97632 1.000 118.53623 ? 141 GLN   B CD  1 
ATOM   2789 O OE1 . GLN   B 2 48  ? 45.72355 -25.21366 -21.16330 1.000 132.07811 ? 141 GLN   B OE1 1 
ATOM   2790 N NE2 . GLN   B 2 48  ? 47.28447 -25.43458 -19.56375 1.000 121.03292 ? 141 GLN   B NE2 1 
ATOM   2791 N N   . PRO   B 2 49  ? 42.43234 -22.34340 -21.15812 1.000 112.00332 ? 142 PRO   B N   1 
ATOM   2792 C CA  . PRO   B 2 49  ? 41.24072 -21.60373 -21.60994 1.000 107.63946 ? 142 PRO   B CA  1 
ATOM   2793 C C   . PRO   B 2 49  ? 39.93863 -22.08402 -20.99230 1.000 102.87695 ? 142 PRO   B C   1 
ATOM   2794 O O   . PRO   B 2 49  ? 38.98596 -21.29844 -20.91487 1.000 97.54685  ? 142 PRO   B O   1 
ATOM   2795 C CB  . PRO   B 2 49  ? 41.25074 -21.82018 -23.12934 1.000 102.77833 ? 142 PRO   B CB  1 
ATOM   2796 C CG  . PRO   B 2 49  ? 42.68025 -22.09054 -23.45820 1.000 108.44349 ? 142 PRO   B CG  1 
ATOM   2797 C CD  . PRO   B 2 49  ? 43.21904 -22.86358 -22.28973 1.000 114.47970 ? 142 PRO   B CD  1 
ATOM   2798 N N   . LYS   B 2 50  ? 39.86139 -23.34113 -20.54918 1.000 102.45052 ? 143 LYS   B N   1 
ATOM   2799 C CA  . LYS   B 2 50  ? 38.61972 -23.83673 -19.96402 1.000 104.36131 ? 143 LYS   B CA  1 
ATOM   2800 C C   . LYS   B 2 50  ? 38.33807 -23.19490 -18.61119 1.000 106.66378 ? 143 LYS   B C   1 
ATOM   2801 O O   . LYS   B 2 50  ? 37.17089 -23.00506 -18.24856 1.000 96.61287  ? 143 LYS   B O   1 
ATOM   2802 C CB  . LYS   B 2 50  ? 38.67019 -25.36035 -19.83695 1.000 117.16824 ? 143 LYS   B CB  1 
ATOM   2803 C CG  . LYS   B 2 50  ? 37.42976 -25.97729 -19.20726 1.000 114.76725 ? 143 LYS   B CG  1 
ATOM   2804 C CD  . LYS   B 2 50  ? 37.13639 -27.34899 -19.78914 1.000 119.58711 ? 143 LYS   B CD  1 
ATOM   2805 C CE  . LYS   B 2 50  ? 36.78368 -27.25130 -21.26544 1.000 134.40907 ? 143 LYS   B CE  1 
ATOM   2806 N NZ  . LYS   B 2 50  ? 36.45334 -28.58016 -21.84987 1.000 129.54451 ? 143 LYS   B NZ  1 
ATOM   2807 N N   . MET   B 2 51  ? 39.38562 -22.84709 -17.85886 1.000 103.42351 ? 144 MET   B N   1 
ATOM   2808 C CA  . MET   B 2 51  ? 39.18583 -22.20320 -16.56461 1.000 103.54972 ? 144 MET   B CA  1 
ATOM   2809 C C   . MET   B 2 51  ? 38.44475 -20.87950 -16.70494 1.000 93.17029  ? 144 MET   B C   1 
ATOM   2810 O O   . MET   B 2 51  ? 37.64162 -20.52320 -15.83491 1.000 94.83049  ? 144 MET   B O   1 
ATOM   2811 C CB  . MET   B 2 51  ? 40.53269 -21.98925 -15.87326 1.000 97.45878  ? 144 MET   B CB  1 
ATOM   2812 C CG  . MET   B 2 51  ? 41.39337 -23.24029 -15.79648 1.000 112.39832 ? 144 MET   B CG  1 
ATOM   2813 S SD  . MET   B 2 51  ? 42.99704 -22.93919 -15.03044 1.000 113.58698 ? 144 MET   B SD  1 
ATOM   2814 C CE  . MET   B 2 51  ? 43.77938 -24.53680 -15.24388 1.000 116.60858 ? 144 MET   B CE  1 
ATOM   2815 N N   . ARG   B 2 52  ? 38.69348 -20.14305 -17.79110 1.000 96.57411  ? 145 ARG   B N   1 
ATOM   2816 C CA  . ARG   B 2 52  ? 37.98735 -18.88443 -18.01004 1.000 95.92007  ? 145 ARG   B CA  1 
ATOM   2817 C C   . ARG   B 2 52  ? 36.49564 -19.11646 -18.21642 1.000 89.25535  ? 145 ARG   B C   1 
ATOM   2818 O O   . ARG   B 2 52  ? 35.66792 -18.32728 -17.74590 1.000 89.76588  ? 145 ARG   B O   1 
ATOM   2819 C CB  . ARG   B 2 52  ? 38.58913 -18.14774 -19.20663 1.000 90.19758  ? 145 ARG   B CB  1 
ATOM   2820 C CG  . ARG   B 2 52  ? 37.89860 -16.83732 -19.54379 1.000 86.32481  ? 145 ARG   B CG  1 
ATOM   2821 C CD  . ARG   B 2 52  ? 38.54408 -16.16960 -20.74678 1.000 90.67569  ? 145 ARG   B CD  1 
ATOM   2822 N NE  . ARG   B 2 52  ? 37.81959 -14.97464 -21.16184 1.000 83.95468  ? 145 ARG   B NE  1 
ATOM   2823 C CZ  . ARG   B 2 52  ? 36.80729 -14.97411 -22.01796 1.000 82.73601  ? 145 ARG   B CZ  1 
ATOM   2824 N NH1 . ARG   B 2 52  ? 36.37126 -16.09328 -22.57266 1.000 85.45069  ? 145 ARG   B NH1 1 
ATOM   2825 N NH2 . ARG   B 2 52  ? 36.21632 -13.82222 -22.32358 1.000 80.37434  ? 145 ARG   B NH2 1 
ATOM   2826 N N   . ALA   B 2 53  ? 36.13363 -20.19646 -18.91254 1.000 93.76908  ? 146 ALA   B N   1 
ATOM   2827 C CA  . ALA   B 2 53  ? 34.72235 -20.50493 -19.11758 1.000 84.47573  ? 146 ALA   B CA  1 
ATOM   2828 C C   . ALA   B 2 53  ? 34.04003 -20.87577 -17.80672 1.000 91.91020  ? 146 ALA   B C   1 
ATOM   2829 O O   . ALA   B 2 53  ? 32.89640 -20.47466 -17.56108 1.000 85.87125  ? 146 ALA   B O   1 
ATOM   2830 C CB  . ALA   B 2 53  ? 34.57536 -21.63273 -20.13801 1.000 84.48456  ? 146 ALA   B CB  1 
ATOM   2831 N N   . ILE   B 2 54  ? 34.72746 -21.63770 -16.95254 1.000 92.50572  ? 147 ILE   B N   1 
ATOM   2832 C CA  . ILE   B 2 54  ? 34.14724 -22.04282 -15.67483 1.000 90.08176  ? 147 ILE   B CA  1 
ATOM   2833 C C   . ILE   B 2 54  ? 33.91381 -20.82830 -14.78524 1.000 93.58353  ? 147 ILE   B C   1 
ATOM   2834 O O   . ILE   B 2 54  ? 32.91592 -20.75410 -14.05713 1.000 89.53344  ? 147 ILE   B O   1 
ATOM   2835 C CB  . ILE   B 2 54  ? 35.05170 -23.08315 -14.98784 1.000 101.53288 ? 147 ILE   B CB  1 
ATOM   2836 C CG1 . ILE   B 2 54  ? 35.31755 -24.26023 -15.92858 1.000 99.73082  ? 147 ILE   B CG1 1 
ATOM   2837 C CG2 . ILE   B 2 54  ? 34.42523 -23.56561 -13.68689 1.000 104.77308 ? 147 ILE   B CG2 1 
ATOM   2838 C CD1 . ILE   B 2 54  ? 36.30969 -25.26399 -15.38623 1.000 116.92036 ? 147 ILE   B CD1 1 
ATOM   2839 N N   . LEU   B 2 55  ? 34.82519 -19.85510 -14.83236 1.000 89.75512  ? 148 LEU   B N   1 
ATOM   2840 C CA  . LEU   B 2 55  ? 34.67150 -18.66016 -14.00979 1.000 91.01528  ? 148 LEU   B CA  1 
ATOM   2841 C C   . LEU   B 2 55  ? 33.54061 -17.77834 -14.52613 1.000 87.66332  ? 148 LEU   B C   1 
ATOM   2842 O O   . LEU   B 2 55  ? 32.68695 -17.32990 -13.75150 1.000 86.17485  ? 148 LEU   B O   1 
ATOM   2843 C CB  . LEU   B 2 55  ? 35.98505 -17.88002 -13.96432 1.000 83.19079  ? 148 LEU   B CB  1 
ATOM   2844 C CG  . LEU   B 2 55  ? 35.94783 -16.62353 -13.09259 1.000 89.59186  ? 148 LEU   B CG  1 
ATOM   2845 C CD1 . LEU   B 2 55  ? 35.68863 -16.99313 -11.63881 1.000 84.25047  ? 148 LEU   B CD1 1 
ATOM   2846 C CD2 . LEU   B 2 55  ? 37.23598 -15.83155 -13.22915 1.000 97.98368  ? 148 LEU   B CD2 1 
ATOM   2847 N N   . LEU   B 2 56  ? 33.52015 -17.51417 -15.83531 1.000 87.34812  ? 149 LEU   B N   1 
ATOM   2848 C CA  . LEU   B 2 56  ? 32.46852 -16.67319 -16.39804 1.000 79.50148  ? 149 LEU   B CA  1 
ATOM   2849 C C   . LEU   B 2 56  ? 31.09808 -17.31418 -16.22232 1.000 82.71253  ? 149 LEU   B C   1 
ATOM   2850 O O   . LEU   B 2 56  ? 30.11357 -16.62169 -15.93954 1.000 81.96945  ? 149 LEU   B O   1 
ATOM   2851 C CB  . LEU   B 2 56  ? 32.75109 -16.39328 -17.87373 1.000 81.83471  ? 149 LEU   B CB  1 
ATOM   2852 C CG  . LEU   B 2 56  ? 34.00588 -15.56655 -18.16255 1.000 74.92131  ? 149 LEU   B CG  1 
ATOM   2853 C CD1 . LEU   B 2 56  ? 34.17056 -15.33446 -19.65500 1.000 82.34931  ? 149 LEU   B CD1 1 
ATOM   2854 C CD2 . LEU   B 2 56  ? 33.96276 -14.24556 -17.41207 1.000 75.68491  ? 149 LEU   B CD2 1 
ATOM   2855 N N   . ASP   B 2 57  ? 31.01580 -18.63870 -16.37534 1.000 84.16270  ? 150 ASP   B N   1 
ATOM   2856 C CA  . ASP   B 2 57  ? 29.75029 -19.32836 -16.14456 1.000 86.97397  ? 150 ASP   B CA  1 
ATOM   2857 C C   . ASP   B 2 57  ? 29.31099 -19.19960 -14.69112 1.000 93.08271  ? 150 ASP   B C   1 
ATOM   2858 O O   . ASP   B 2 57  ? 28.11365 -19.08037 -14.40427 1.000 89.38983  ? 150 ASP   B O   1 
ATOM   2859 C CB  . ASP   B 2 57  ? 29.87178 -20.79955 -16.54012 1.000 94.34126  ? 150 ASP   B CB  1 
ATOM   2860 C CG  . ASP   B 2 57  ? 28.57801 -21.56434 -16.34211 1.000 109.45901 ? 150 ASP   B CG  1 
ATOM   2861 O OD1 . ASP   B 2 57  ? 27.63658 -21.35795 -17.13635 1.000 119.03726 ? 150 ASP   B OD1 1 
ATOM   2862 O OD2 . ASP   B 2 57  ? 28.50164 -22.37046 -15.39125 1.000 116.39544 ? 150 ASP   B OD2 1 
ATOM   2863 N N   . TRP   B 2 58  ? 30.26683 -19.22058 -13.75864 1.000 90.72193  ? 151 TRP   B N   1 
ATOM   2864 C CA  . TRP   B 2 58  ? 29.92842 -19.03154 -12.35195 1.000 79.13551  ? 151 TRP   B CA  1 
ATOM   2865 C C   . TRP   B 2 58  ? 29.41144 -17.62162 -12.09589 1.000 86.27366  ? 151 TRP   B C   1 
ATOM   2866 O O   . TRP   B 2 58  ? 28.43387 -17.43671 -11.36163 1.000 84.65472  ? 151 TRP   B O   1 
ATOM   2867 C CB  . TRP   B 2 58  ? 31.14525 -19.33215 -11.47620 1.000 98.59618  ? 151 TRP   B CB  1 
ATOM   2868 C CG  . TRP   B 2 58  ? 30.95227 -18.99142 -10.02808 1.000 102.92672 ? 151 TRP   B CG  1 
ATOM   2869 C CD1 . TRP   B 2 58  ? 30.07516 -19.57212 -9.15855  1.000 105.99756 ? 151 TRP   B CD1 1 
ATOM   2870 C CD2 . TRP   B 2 58  ? 31.66386 -17.99947 -9.27719  1.000 97.13630  ? 151 TRP   B CD2 1 
ATOM   2871 N NE1 . TRP   B 2 58  ? 30.19044 -18.99771 -7.91571  1.000 109.42914 ? 151 TRP   B NE1 1 
ATOM   2872 C CE2 . TRP   B 2 58  ? 31.15962 -18.03021 -7.96180  1.000 105.14656 ? 151 TRP   B CE2 1 
ATOM   2873 C CE3 . TRP   B 2 58  ? 32.67602 -17.08697 -9.59017  1.000 101.05556 ? 151 TRP   B CE3 1 
ATOM   2874 C CZ2 . TRP   B 2 58  ? 31.63265 -17.18368 -6.96076  1.000 103.33038 ? 151 TRP   B CZ2 1 
ATOM   2875 C CZ3 . TRP   B 2 58  ? 33.14435 -16.24703 -8.59431  1.000 92.41749  ? 151 TRP   B CZ3 1 
ATOM   2876 C CH2 . TRP   B 2 58  ? 32.62241 -16.30145 -7.29647  1.000 98.16811  ? 151 TRP   B CH2 1 
ATOM   2877 N N   . LEU   B 2 59  ? 30.04688 -16.61584 -12.70270 1.000 88.86359  ? 152 LEU   B N   1 
ATOM   2878 C CA  . LEU   B 2 59  ? 29.58506 -15.24196 -12.53674 1.000 79.73172  ? 152 LEU   B CA  1 
ATOM   2879 C C   . LEU   B 2 59  ? 28.18678 -15.04360 -13.10916 1.000 81.93418  ? 152 LEU   B C   1 
ATOM   2880 O O   . LEU   B 2 59  ? 27.42383 -14.21379 -12.60087 1.000 80.68239  ? 152 LEU   B O   1 
ATOM   2881 C CB  . LEU   B 2 59  ? 30.57125 -14.27427 -13.19088 1.000 73.32672  ? 152 LEU   B CB  1 
ATOM   2882 C CG  . LEU   B 2 59  ? 31.99426 -14.27281 -12.62929 1.000 79.13559  ? 152 LEU   B CG  1 
ATOM   2883 C CD1 . LEU   B 2 59  ? 32.87372 -13.30968 -13.40872 1.000 83.10149  ? 152 LEU   B CD1 1 
ATOM   2884 C CD2 . LEU   B 2 59  ? 31.98892 -13.91807 -11.15143 1.000 71.80400  ? 152 LEU   B CD2 1 
ATOM   2885 N N   . MET   B 2 60  ? 27.83271 -15.78629 -14.16270 1.000 76.64565  ? 153 MET   B N   1 
ATOM   2886 C CA  . MET   B 2 60  ? 26.47578 -15.70996 -14.69795 1.000 79.39397  ? 153 MET   B CA  1 
ATOM   2887 C C   . MET   B 2 60  ? 25.45780 -16.17461 -13.66619 1.000 80.49761  ? 153 MET   B C   1 
ATOM   2888 O O   . MET   B 2 60  ? 24.44053 -15.51061 -13.43454 1.000 79.83042  ? 153 MET   B O   1 
ATOM   2889 C CB  . MET   B 2 60  ? 26.35119 -16.55051 -15.96972 1.000 84.03514  ? 153 MET   B CB  1 
ATOM   2890 C CG  . MET   B 2 60  ? 27.12432 -16.03884 -17.16735 1.000 84.79783  ? 153 MET   B CG  1 
ATOM   2891 S SD  . MET   B 2 60  ? 26.59284 -16.86636 -18.68060 1.000 90.95323  ? 153 MET   B SD  1 
ATOM   2892 C CE  . MET   B 2 60  ? 27.99010 -16.56157 -19.75469 1.000 83.31117  ? 153 MET   B CE  1 
ATOM   2893 N N   . GLU   B 2 61  ? 25.71414 -17.32692 -13.04237 1.000 86.46254  ? 154 GLU   B N   1 
ATOM   2894 C CA  . GLU   B 2 61  ? 24.79813 -17.84208 -12.03118 1.000 90.05511  ? 154 GLU   B CA  1 
ATOM   2895 C C   . GLU   B 2 61  ? 24.69973 -16.89002 -10.84630 1.000 86.16096  ? 154 GLU   B C   1 
ATOM   2896 O O   . GLU   B 2 61  ? 23.61554 -16.69807 -10.28321 1.000 84.10261  ? 154 GLU   B O   1 
ATOM   2897 C CB  . GLU   B 2 61  ? 25.25084 -19.23064 -11.57863 1.000 96.59820  ? 154 GLU   B CB  1 
ATOM   2898 C CG  . GLU   B 2 61  ? 24.21184 -20.00354 -10.78317 1.000 107.71399 ? 154 GLU   B CG  1 
ATOM   2899 C CD  . GLU   B 2 61  ? 24.63583 -21.43543 -10.51162 1.000 116.92133 ? 154 GLU   B CD  1 
ATOM   2900 O OE1 . GLU   B 2 61  ? 25.76375 -21.80740 -10.89962 1.000 111.82478 ? 154 GLU   B OE1 1 
ATOM   2901 O OE2 . GLU   B 2 61  ? 23.84067 -22.19011 -9.91285  1.000 127.54648 ? 154 GLU   B OE2 1 
ATOM   2902 N N   . VAL   B 2 62  ? 25.82145 -16.27470 -10.46221 1.000 82.20722  ? 155 VAL   B N   1 
ATOM   2903 C CA  . VAL   B 2 62  ? 25.80416 -15.29894 -9.37536  1.000 74.06690  ? 155 VAL   B CA  1 
ATOM   2904 C C   . VAL   B 2 62  ? 24.91916 -14.11280 -9.73870  1.000 82.92505  ? 155 VAL   B C   1 
ATOM   2905 O O   . VAL   B 2 62  ? 24.18256 -13.58701 -8.89490  1.000 80.14633  ? 155 VAL   B O   1 
ATOM   2906 C CB  . VAL   B 2 62  ? 27.24025 -14.85633 -9.03303  1.000 81.17057  ? 155 VAL   B CB  1 
ATOM   2907 C CG1 . VAL   B 2 62  ? 27.22754 -13.71982 -8.02296  1.000 79.08322  ? 155 VAL   B CG1 1 
ATOM   2908 C CG2 . VAL   B 2 62  ? 28.04376 -16.03084 -8.49700  1.000 85.31028  ? 155 VAL   B CG2 1 
ATOM   2909 N N   . CYS   B 2 63  ? 24.96199 -13.68457 -11.00372 1.000 82.33392  ? 156 CYS   B N   1 
ATOM   2910 C CA  . CYS   B 2 63  ? 24.14522 -12.55264 -11.43052 1.000 79.12392  ? 156 CYS   B CA  1 
ATOM   2911 C C   . CYS   B 2 63  ? 22.65881 -12.87701 -11.36092 1.000 77.04051  ? 156 CYS   B C   1 
ATOM   2912 O O   . CYS   B 2 63  ? 21.85114 -12.02235 -10.97719 1.000 72.79106  ? 156 CYS   B O   1 
ATOM   2913 C CB  . CYS   B 2 63  ? 24.52940 -12.12896 -12.84760 1.000 70.05589  ? 156 CYS   B CB  1 
ATOM   2914 S SG  . CYS   B 2 63  ? 26.13386 -11.31812 -12.97251 1.000 75.90551  ? 156 CYS   B SG  1 
ATOM   2915 N N   . GLU   B 2 64  ? 22.27581 -14.10129 -11.73304 1.000 74.54739  ? 157 GLU   B N   1 
ATOM   2916 C CA  . GLU   B 2 64  ? 20.86048 -14.45770 -11.72540 1.000 84.29318  ? 157 GLU   B CA  1 
ATOM   2917 C C   . GLU   B 2 64  ? 20.31959 -14.55438 -10.30350 1.000 84.54366  ? 157 GLU   B C   1 
ATOM   2918 O O   . GLU   B 2 64  ? 19.16572 -14.18975 -10.04859 1.000 87.77767  ? 157 GLU   B O   1 
ATOM   2919 C CB  . GLU   B 2 64  ? 20.64184 -15.77270 -12.47737 1.000 86.77591  ? 157 GLU   B CB  1 
ATOM   2920 C CG  . GLU   B 2 64  ? 19.17740 -16.17352 -12.60998 1.000 92.82264  ? 157 GLU   B CG  1 
ATOM   2921 C CD  . GLU   B 2 64  ? 18.98845 -17.48806 -13.34656 1.000 106.42995 ? 157 GLU   B CD  1 
ATOM   2922 O OE1 . GLU   B 2 64  ? 19.98456 -18.03182 -13.86773 1.000 106.53041 ? 157 GLU   B OE1 1 
ATOM   2923 O OE2 . GLU   B 2 64  ? 17.84060 -17.97926 -13.40292 1.000 111.14197 ? 157 GLU   B OE2 1 
ATOM   2924 N N   . VAL   B 2 65  ? 21.13764 -15.03656 -9.36505  1.000 90.98180  ? 158 VAL   B N   1 
ATOM   2925 C CA  . VAL   B 2 65  ? 20.68919 -15.17043 -7.98051  1.000 90.33449  ? 158 VAL   B CA  1 
ATOM   2926 C C   . VAL   B 2 65  ? 20.34181 -13.80438 -7.40062  1.000 85.60675  ? 158 VAL   B C   1 
ATOM   2927 O O   . VAL   B 2 65  ? 19.28726 -13.62185 -6.78103  1.000 88.24506  ? 158 VAL   B O   1 
ATOM   2928 C CB  . VAL   B 2 65  ? 21.75671 -15.89048 -7.13757  1.000 87.90186  ? 158 VAL   B CB  1 
ATOM   2929 C CG1 . VAL   B 2 65  ? 21.37410 -15.86385 -5.66520  1.000 95.84663  ? 158 VAL   B CG1 1 
ATOM   2930 C CG2 . VAL   B 2 65  ? 21.92989 -17.32425 -7.61618  1.000 86.53817  ? 158 VAL   B CG2 1 
ATOM   2931 N N   . TYR   B 2 66  ? 21.21763 -12.82303 -7.60022  1.000 83.72797  ? 159 TYR   B N   1 
ATOM   2932 C CA  . TYR   B 2 66  ? 20.97706 -11.46399 -7.13775  1.000 79.01120  ? 159 TYR   B CA  1 
ATOM   2933 C C   . TYR   B 2 66  ? 20.28833 -10.60058 -8.18663  1.000 78.31574  ? 159 TYR   B C   1 
ATOM   2934 O O   . TYR   B 2 66  ? 20.18414 -9.38372  -7.99777  1.000 74.86495  ? 159 TYR   B O   1 
ATOM   2935 C CB  . TYR   B 2 66  ? 22.29302 -10.81901 -6.69738  1.000 84.27024  ? 159 TYR   B CB  1 
ATOM   2936 C CG  . TYR   B 2 66  ? 22.88172 -11.46188 -5.46218  1.000 83.21122  ? 159 TYR   B CG  1 
ATOM   2937 C CD1 . TYR   B 2 66  ? 23.72768 -12.55843 -5.56202  1.000 89.73940  ? 159 TYR   B CD1 1 
ATOM   2938 C CD2 . TYR   B 2 66  ? 22.58071 -10.98040 -4.19490  1.000 84.43344  ? 159 TYR   B CD2 1 
ATOM   2939 C CE1 . TYR   B 2 66  ? 24.26265 -13.15410 -4.43445  1.000 89.53832  ? 159 TYR   B CE1 1 
ATOM   2940 C CE2 . TYR   B 2 66  ? 23.11138 -11.56946 -3.06156  1.000 94.08256  ? 159 TYR   B CE2 1 
ATOM   2941 C CZ  . TYR   B 2 66  ? 23.95212 -12.65574 -3.18691  1.000 94.03378  ? 159 TYR   B CZ  1 
ATOM   2942 O OH  . TYR   B 2 66  ? 24.48285 -13.24488 -2.06070  1.000 100.31685 ? 159 TYR   B OH  1 
ATOM   2943 N N   . LYS   B 2 67  ? 19.81899 -11.20616 -9.28052  1.000 82.01691  ? 160 LYS   B N   1 
ATOM   2944 C CA  . LYS   B 2 67  ? 19.03553 -10.51418 -10.30535 1.000 80.93508  ? 160 LYS   B CA  1 
ATOM   2945 C C   . LYS   B 2 67  ? 19.80201 -9.33340  -10.89892 1.000 72.18877  ? 160 LYS   B C   1 
ATOM   2946 O O   . LYS   B 2 67  ? 19.24090 -8.26387  -11.14789 1.000 65.84207  ? 160 LYS   B O   1 
ATOM   2947 C CB  . LYS   B 2 67  ? 17.67996 -10.07053 -9.74982  1.000 84.31445  ? 160 LYS   B CB  1 
ATOM   2948 C CG  . LYS   B 2 67  ? 16.79991 -11.23064 -9.30734  1.000 90.55872  ? 160 LYS   B CG  1 
ATOM   2949 C CD  . LYS   B 2 67  ? 15.49874 -10.75112 -8.68760  1.000 102.68414 ? 160 LYS   B CD  1 
ATOM   2950 C CE  . LYS   B 2 67  ? 14.56699 -11.91947 -8.40461  1.000 101.19329 ? 160 LYS   B CE  1 
ATOM   2951 N NZ  . LYS   B 2 67  ? 15.21646 -12.95299 -7.55473  1.000 99.78410  ? 160 LYS   B NZ  1 
ATOM   2952 N N   . LEU   B 2 68  ? 21.09599 -9.53046  -11.13268 1.000 70.39005  ? 161 LEU   B N   1 
ATOM   2953 C CA  . LEU   B 2 68  ? 21.91711 -8.49876  -11.74582 1.000 65.33136  ? 161 LEU   B CA  1 
ATOM   2954 C C   . LEU   B 2 68  ? 21.67245 -8.44774  -13.24895 1.000 59.67144  ? 161 LEU   B C   1 
ATOM   2955 O O   . LEU   B 2 68  ? 21.28841 -9.44116  -13.87257 1.000 68.84059  ? 161 LEU   B O   1 
ATOM   2956 C CB  . LEU   B 2 68  ? 23.39821 -8.75044  -11.46225 1.000 65.45799  ? 161 LEU   B CB  1 
ATOM   2957 C CG  . LEU   B 2 68  ? 23.79301 -8.78392  -9.98503  1.000 71.72372  ? 161 LEU   B CG  1 
ATOM   2958 C CD1 . LEU   B 2 68  ? 25.29862 -8.93656  -9.83134  1.000 66.92344  ? 161 LEU   B CD1 1 
ATOM   2959 C CD2 . LEU   B 2 68  ? 23.29681 -7.53545  -9.27250  1.000 60.59533  ? 161 LEU   B CD2 1 
ATOM   2960 N N   . HIS   B 2 69  ? 21.90058 -7.27249  -13.82828 1.000 59.18215  ? 162 HIS   B N   1 
ATOM   2961 C CA  . HIS   B 2 69  ? 21.64165 -7.07197  -15.24453 1.000 69.58631  ? 162 HIS   B CA  1 
ATOM   2962 C C   . HIS   B 2 69  ? 22.69515 -7.77271  -16.09982 1.000 62.82259  ? 162 HIS   B C   1 
ATOM   2963 O O   . HIS   B 2 69  ? 23.81039 -8.06195  -15.65538 1.000 62.77726  ? 162 HIS   B O   1 
ATOM   2964 C CB  . HIS   B 2 69  ? 21.60213 -5.57963  -15.57696 1.000 61.19117  ? 162 HIS   B CB  1 
ATOM   2965 C CG  . HIS   B 2 69  ? 20.36633 -4.88619  -15.09471 1.000 66.67604  ? 162 HIS   B CG  1 
ATOM   2966 N ND1 . HIS   B 2 69  ? 20.18750 -4.51117  -13.78089 1.000 77.54948  ? 162 HIS   B ND1 1 
ATOM   2967 C CD2 . HIS   B 2 69  ? 19.24398 -4.50616  -15.75034 1.000 77.55310  ? 162 HIS   B CD2 1 
ATOM   2968 C CE1 . HIS   B 2 69  ? 19.01002 -3.92703  -13.64819 1.000 82.14032  ? 162 HIS   B CE1 1 
ATOM   2969 N NE2 . HIS   B 2 69  ? 18.41736 -3.91136  -14.82851 1.000 80.11874  ? 162 HIS   B NE2 1 
ATOM   2970 N N   . ARG   B 2 70  ? 22.31563 -8.05572  -17.34915 1.000 68.31069  ? 163 ARG   B N   1 
ATOM   2971 C CA  . ARG   B 2 70  ? 23.25848 -8.64588  -18.29388 1.000 68.05978  ? 163 ARG   B CA  1 
ATOM   2972 C C   . ARG   B 2 70  ? 24.44920 -7.72567  -18.52388 1.000 58.13531  ? 163 ARG   B C   1 
ATOM   2973 O O   . ARG   B 2 70  ? 25.58161 -8.19342  -18.69137 1.000 62.42113  ? 163 ARG   B O   1 
ATOM   2974 C CB  . ARG   B 2 70  ? 22.55619 -8.94980  -19.61866 1.000 62.73690  ? 163 ARG   B CB  1 
ATOM   2975 C CG  . ARG   B 2 70  ? 21.35283 -9.86377  -19.49112 1.000 64.57934  ? 163 ARG   B CG  1 
ATOM   2976 C CD  . ARG   B 2 70  ? 20.72718 -10.14354 -20.84665 1.000 69.67516  ? 163 ARG   B CD  1 
ATOM   2977 N NE  . ARG   B 2 70  ? 19.60352 -11.06678 -20.74586 1.000 64.42793  ? 163 ARG   B NE  1 
ATOM   2978 C CZ  . ARG   B 2 70  ? 19.72187 -12.38705 -20.72247 1.000 66.91935  ? 163 ARG   B CZ  1 
ATOM   2979 N NH1 . ARG   B 2 70  ? 20.90476 -12.97559 -20.78929 1.000 68.80364  ? 163 ARG   B NH1 1 
ATOM   2980 N NH2 . ARG   B 2 70  ? 18.62639 -13.13543 -20.62743 1.000 73.76321  ? 163 ARG   B NH2 1 
ATOM   2981 N N   . GLU   B 2 71  ? 24.20876 -6.41109  -18.53554 1.000 56.15868  ? 164 GLU   B N   1 
ATOM   2982 C CA  . GLU   B 2 71  ? 25.29682 -5.45117  -18.68754 1.000 56.21171  ? 164 GLU   B CA  1 
ATOM   2983 C C   . GLU   B 2 71  ? 26.31805 -5.59559  -17.56644 1.000 60.29485  ? 164 GLU   B C   1 
ATOM   2984 O O   . GLU   B 2 71  ? 27.52449 -5.43760  -17.78932 1.000 58.69495  ? 164 GLU   B O   1 
ATOM   2985 C CB  . GLU   B 2 71  ? 24.72795 -4.03137  -18.72857 1.000 60.49613  ? 164 GLU   B CB  1 
ATOM   2986 C CG  . GLU   B 2 71  ? 25.77243 -2.92184  -18.70660 1.000 75.29699  ? 164 GLU   B CG  1 
ATOM   2987 C CD  . GLU   B 2 71  ? 26.54751 -2.81213  -20.00613 1.000 68.59750  ? 164 GLU   B CD  1 
ATOM   2988 O OE1 . GLU   B 2 71  ? 26.10868 -3.39827  -21.01803 1.000 70.16045  ? 164 GLU   B OE1 1 
ATOM   2989 O OE2 . GLU   B 2 71  ? 27.59664 -2.13439  -20.01435 1.000 72.05148  ? 164 GLU   B OE2 1 
ATOM   2990 N N   . THR   B 2 72  ? 25.85305 -5.91357  -16.35610 1.000 62.81292  ? 165 THR   B N   1 
ATOM   2991 C CA  . THR   B 2 72  ? 26.76362 -6.07260  -15.22793 1.000 61.44984  ? 165 THR   B CA  1 
ATOM   2992 C C   . THR   B 2 72  ? 27.69597 -7.26161  -15.42905 1.000 57.71555  ? 165 THR   B C   1 
ATOM   2993 O O   . THR   B 2 72  ? 28.89561 -7.17083  -15.14256 1.000 57.00161  ? 165 THR   B O   1 
ATOM   2994 C CB  . THR   B 2 72  ? 25.96715 -6.22458  -13.93205 1.000 64.10246  ? 165 THR   B CB  1 
ATOM   2995 O OG1 . THR   B 2 72  ? 25.12084 -5.08082  -13.75586 1.000 62.54745  ? 165 THR   B OG1 1 
ATOM   2996 C CG2 . THR   B 2 72  ? 26.90229 -6.34272  -12.74137 1.000 58.92731  ? 165 THR   B CG2 1 
ATOM   2997 N N   . PHE   B 2 73  ? 27.16995 -8.38468  -15.92143 1.000 60.39353  ? 166 PHE   B N   1 
ATOM   2998 C CA  . PHE   B 2 73  ? 28.02806 -9.53792  -16.17252 1.000 62.42055  ? 166 PHE   B CA  1 
ATOM   2999 C C   . PHE   B 2 73  ? 29.07445 -9.22248  -17.23415 1.000 61.02185  ? 166 PHE   B C   1 
ATOM   3000 O O   . PHE   B 2 73  ? 30.26673 -9.49029  -17.04579 1.000 64.45656  ? 166 PHE   B O   1 
ATOM   3001 C CB  . PHE   B 2 73  ? 27.19854 -10.74951 -16.59484 1.000 59.80627  ? 166 PHE   B CB  1 
ATOM   3002 C CG  . PHE   B 2 73  ? 28.01941 -11.83579 -17.22469 1.000 64.24997  ? 166 PHE   B CG  1 
ATOM   3003 C CD1 . PHE   B 2 73  ? 28.86108 -12.61819 -16.45190 1.000 67.95371  ? 166 PHE   B CD1 1 
ATOM   3004 C CD2 . PHE   B 2 73  ? 27.97318 -12.05666 -18.59116 1.000 69.56203  ? 166 PHE   B CD2 1 
ATOM   3005 C CE1 . PHE   B 2 73  ? 29.63178 -13.60759 -17.02603 1.000 70.92727  ? 166 PHE   B CE1 1 
ATOM   3006 C CE2 . PHE   B 2 73  ? 28.74153 -13.04694 -19.17133 1.000 72.88783  ? 166 PHE   B CE2 1 
ATOM   3007 C CZ  . PHE   B 2 73  ? 29.57299 -13.82197 -18.38664 1.000 75.71077  ? 166 PHE   B CZ  1 
ATOM   3008 N N   . TYR   B 2 74  ? 28.64535 -8.64580  -18.36049 1.000 52.29319  ? 167 TYR   B N   1 
ATOM   3009 C CA  . TYR   B 2 74  ? 29.57530 -8.39711  -19.45767 1.000 59.25366  ? 167 TYR   B CA  1 
ATOM   3010 C C   . TYR   B 2 74  ? 30.58943 -7.31436  -19.11250 1.000 60.15688  ? 167 TYR   B C   1 
ATOM   3011 O O   . TYR   B 2 74  ? 31.69326 -7.30701  -19.66953 1.000 58.46127  ? 167 TYR   B O   1 
ATOM   3012 C CB  . TYR   B 2 74  ? 28.80644 -8.04062  -20.72985 1.000 51.68769  ? 167 TYR   B CB  1 
ATOM   3013 C CG  . TYR   B 2 74  ? 28.33646 -9.25995  -21.48622 1.000 61.95419  ? 167 TYR   B CG  1 
ATOM   3014 C CD1 . TYR   B 2 74  ? 29.19485 -9.93926  -22.34204 1.000 68.06934  ? 167 TYR   B CD1 1 
ATOM   3015 C CD2 . TYR   B 2 74  ? 27.04427 -9.74423  -21.33347 1.000 56.81782  ? 167 TYR   B CD2 1 
ATOM   3016 C CE1 . TYR   B 2 74  ? 28.77915 -11.06020 -23.03094 1.000 60.69742  ? 167 TYR   B CE1 1 
ATOM   3017 C CE2 . TYR   B 2 74  ? 26.61764 -10.86832 -22.02096 1.000 59.44948  ? 167 TYR   B CE2 1 
ATOM   3018 C CZ  . TYR   B 2 74  ? 27.49046 -11.52160 -22.86788 1.000 68.50185  ? 167 TYR   B CZ  1 
ATOM   3019 O OH  . TYR   B 2 74  ? 27.07602 -12.63899 -23.55753 1.000 63.48524  ? 167 TYR   B OH  1 
ATOM   3020 N N   . LEU   B 2 75  ? 30.24344 -6.39664  -18.20604 1.000 57.50858  ? 168 LEU   B N   1 
ATOM   3021 C CA  . LEU   B 2 75  ? 31.25426 -5.49397  -17.66452 1.000 55.99350  ? 168 LEU   B CA  1 
ATOM   3022 C C   . LEU   B 2 75  ? 32.31225 -6.26836  -16.89169 1.000 59.89561  ? 168 LEU   B C   1 
ATOM   3023 O O   . LEU   B 2 75  ? 33.51303 -6.01310  -17.04017 1.000 64.04033  ? 168 LEU   B O   1 
ATOM   3024 C CB  . LEU   B 2 75  ? 30.60587 -4.44248  -16.76419 1.000 55.99017  ? 168 LEU   B CB  1 
ATOM   3025 C CG  . LEU   B 2 75  ? 29.90727 -3.25705  -17.42720 1.000 60.05294  ? 168 LEU   B CG  1 
ATOM   3026 C CD1 . LEU   B 2 75  ? 29.26627 -2.36694  -16.37353 1.000 57.09966  ? 168 LEU   B CD1 1 
ATOM   3027 C CD2 . LEU   B 2 75  ? 30.89277 -2.46855  -18.26953 1.000 59.44199  ? 168 LEU   B CD2 1 
ATOM   3028 N N   . ALA   B 2 76  ? 31.88304 -7.22347  -16.06209 1.000 58.81878  ? 169 ALA   B N   1 
ATOM   3029 C CA  . ALA   B 2 76  ? 32.83328 -8.03428  -15.30850 1.000 67.11474  ? 169 ALA   B CA  1 
ATOM   3030 C C   . ALA   B 2 76  ? 33.68069 -8.89591  -16.23488 1.000 60.41004  ? 169 ALA   B C   1 
ATOM   3031 O O   . ALA   B 2 76  ? 34.87271 -9.10406  -15.98031 1.000 71.91304  ? 169 ALA   B O   1 
ATOM   3032 C CB  . ALA   B 2 76  ? 32.09288 -8.90442  -14.29403 1.000 64.81434  ? 169 ALA   B CB  1 
ATOM   3033 N N   . GLN   B 2 77  ? 33.08272 -9.40935  -17.31084 1.000 62.20929  ? 170 GLN   B N   1 
ATOM   3034 C CA  . GLN   B 2 77  ? 33.84662 -10.18178 -18.28480 1.000 67.43880  ? 170 GLN   B CA  1 
ATOM   3035 C C   . GLN   B 2 77  ? 34.92010 -9.32195  -18.93961 1.000 69.58307  ? 170 GLN   B C   1 
ATOM   3036 O O   . GLN   B 2 77  ? 36.07943 -9.73621  -19.05707 1.000 70.59486  ? 170 GLN   B O   1 
ATOM   3037 C CB  . GLN   B 2 77  ? 32.90395 -10.77388 -19.33511 1.000 66.27972  ? 170 GLN   B CB  1 
ATOM   3038 C CG  . GLN   B 2 77  ? 33.60307 -11.41444 -20.52772 1.000 72.78775  ? 170 GLN   B CG  1 
ATOM   3039 C CD  . GLN   B 2 77  ? 33.78086 -10.45562 -21.69279 1.000 72.67777  ? 170 GLN   B CD  1 
ATOM   3040 O OE1 . GLN   B 2 77  ? 32.90565 -9.63849  -21.98047 1.000 67.96281  ? 170 GLN   B OE1 1 
ATOM   3041 N NE2 . GLN   B 2 77  ? 34.92108 -10.54896 -22.36607 1.000 80.02690  ? 170 GLN   B NE2 1 
ATOM   3042 N N   . ASP   B 2 78  ? 34.55117 -8.11043  -19.36353 1.000 66.58453  ? 171 ASP   B N   1 
ATOM   3043 C CA  . ASP   B 2 78  ? 35.51186 -7.23284  -20.02415 1.000 68.87822  ? 171 ASP   B CA  1 
ATOM   3044 C C   . ASP   B 2 78  ? 36.60006 -6.77302  -19.06091 1.000 70.47546  ? 171 ASP   B C   1 
ATOM   3045 O O   . ASP   B 2 78  ? 37.77144 -6.67001  -19.44438 1.000 67.40452  ? 171 ASP   B O   1 
ATOM   3046 C CB  . ASP   B 2 78  ? 34.79133 -6.03196  -20.63504 1.000 69.01518  ? 171 ASP   B CB  1 
ATOM   3047 C CG  . ASP   B 2 78  ? 35.73571 -5.09525  -21.35786 1.000 70.71383  ? 171 ASP   B CG  1 
ATOM   3048 O OD1 . ASP   B 2 78  ? 36.23440 -5.46934  -22.44096 1.000 76.06009  ? 171 ASP   B OD1 1 
ATOM   3049 O OD2 . ASP   B 2 78  ? 35.98353 -3.98670  -20.84054 1.000 72.05187  ? 171 ASP   B OD2 1 
ATOM   3050 N N   . PHE   B 2 79  ? 36.23433 -6.48701  -17.80843 1.000 64.96918  ? 172 PHE   B N   1 
ATOM   3051 C CA  . PHE   B 2 79  ? 37.23946 -6.11523  -16.81723 1.000 69.88308  ? 172 PHE   B CA  1 
ATOM   3052 C C   . PHE   B 2 79  ? 38.19153 -7.27270  -16.54834 1.000 68.68550  ? 172 PHE   B C   1 
ATOM   3053 O O   . PHE   B 2 79  ? 39.39246 -7.06581  -16.34310 1.000 74.91538  ? 172 PHE   B O   1 
ATOM   3054 C CB  . PHE   B 2 79  ? 36.56688 -5.66598  -15.51806 1.000 57.97826  ? 172 PHE   B CB  1 
ATOM   3055 C CG  . PHE   B 2 79  ? 35.74850 -4.40955  -15.65320 1.000 59.85164  ? 172 PHE   B CG  1 
ATOM   3056 C CD1 . PHE   B 2 79  ? 35.88677 -3.58601  -16.75802 1.000 58.33637  ? 172 PHE   B CD1 1 
ATOM   3057 C CD2 . PHE   B 2 79  ? 34.84566 -4.04886  -14.66513 1.000 65.87699  ? 172 PHE   B CD2 1 
ATOM   3058 C CE1 . PHE   B 2 79  ? 35.13432 -2.43119  -16.87983 1.000 61.08399  ? 172 PHE   B CE1 1 
ATOM   3059 C CE2 . PHE   B 2 79  ? 34.09173 -2.89429  -14.78011 1.000 58.99906  ? 172 PHE   B CE2 1 
ATOM   3060 C CZ  . PHE   B 2 79  ? 34.23619 -2.08511  -15.88926 1.000 62.36423  ? 172 PHE   B CZ  1 
ATOM   3061 N N   . PHE   B 2 80  ? 37.67111 -8.50080  -16.55571 1.000 67.27664  ? 173 PHE   B N   1 
ATOM   3062 C CA  . PHE   B 2 80  ? 38.50441 -9.67203  -16.30771 1.000 75.97170  ? 173 PHE   B CA  1 
ATOM   3063 C C   . PHE   B 2 80  ? 39.49034 -9.90189  -17.44799 1.000 81.39795  ? 173 PHE   B C   1 
ATOM   3064 O O   . PHE   B 2 80  ? 40.68312 -10.12774 -17.21366 1.000 80.82426  ? 173 PHE   B O   1 
ATOM   3065 C CB  . PHE   B 2 80  ? 37.61623 -10.89974 -16.10085 1.000 76.08020  ? 173 PHE   B CB  1 
ATOM   3066 C CG  . PHE   B 2 80  ? 38.37696 -12.18259 -15.94889 1.000 78.41114  ? 173 PHE   B CG  1 
ATOM   3067 C CD1 . PHE   B 2 80  ? 38.98427 -12.50347 -14.74698 1.000 89.26585  ? 173 PHE   B CD1 1 
ATOM   3068 C CD2 . PHE   B 2 80  ? 38.47465 -13.07485 -17.00367 1.000 85.48170  ? 173 PHE   B CD2 1 
ATOM   3069 C CE1 . PHE   B 2 80  ? 39.68221 -13.68521 -14.60185 1.000 87.23478  ? 173 PHE   B CE1 1 
ATOM   3070 C CE2 . PHE   B 2 80  ? 39.17182 -14.25935 -16.86414 1.000 87.90730  ? 173 PHE   B CE2 1 
ATOM   3071 C CZ  . PHE   B 2 80  ? 39.77643 -14.56473 -15.66166 1.000 86.69704  ? 173 PHE   B CZ  1 
ATOM   3072 N N   . ASP   B 2 81  ? 39.01077 -9.84298  -18.69339 1.000 73.87440  ? 174 ASP   B N   1 
ATOM   3073 C CA  . ASP   B 2 81  ? 39.87875 -10.13017 -19.83183 1.000 77.09637  ? 174 ASP   B CA  1 
ATOM   3074 C C   . ASP   B 2 81  ? 40.93093 -9.04432  -20.02425 1.000 84.03497  ? 174 ASP   B C   1 
ATOM   3075 O O   . ASP   B 2 81  ? 42.07690 -9.34233  -20.38050 1.000 92.52577  ? 174 ASP   B O   1 
ATOM   3076 C CB  . ASP   B 2 81  ? 39.04517 -10.29835 -21.10185 1.000 75.72468  ? 174 ASP   B CB  1 
ATOM   3077 C CG  . ASP   B 2 81  ? 38.16395 -11.53255 -21.06233 1.000 81.58614  ? 174 ASP   B CG  1 
ATOM   3078 O OD1 . ASP   B 2 81  ? 38.52401 -12.49974 -20.35970 1.000 87.69425  ? 174 ASP   B OD1 1 
ATOM   3079 O OD2 . ASP   B 2 81  ? 37.11210 -11.53737 -21.73611 1.000 83.53945  ? 174 ASP   B OD2 1 
ATOM   3080 N N   . ARG   B 2 82  ? 40.56707 -7.78033  -19.79689 1.000 71.99463  ? 175 ARG   B N   1 
ATOM   3081 C CA  . ARG   B 2 82  ? 41.52985 -6.70160  -19.98808 1.000 74.97782  ? 175 ARG   B CA  1 
ATOM   3082 C C   . ARG   B 2 82  ? 42.53068 -6.61258  -18.84383 1.000 89.00331  ? 175 ARG   B C   1 
ATOM   3083 O O   . ARG   B 2 82  ? 43.68305 -6.22443  -19.06717 1.000 93.43391  ? 175 ARG   B O   1 
ATOM   3084 C CB  . ARG   B 2 82  ? 40.80588 -5.36635  -20.16281 1.000 69.20719  ? 175 ARG   B CB  1 
ATOM   3085 C CG  . ARG   B 2 82  ? 40.13673 -5.21488  -21.51707 1.000 75.48784  ? 175 ARG   B CG  1 
ATOM   3086 C CD  . ARG   B 2 82  ? 39.78168 -3.76822  -21.81788 1.000 69.95499  ? 175 ARG   B CD  1 
ATOM   3087 N NE  . ARG   B 2 82  ? 38.73720 -3.25604  -20.93963 1.000 71.53854  ? 175 ARG   B NE  1 
ATOM   3088 C CZ  . ARG   B 2 82  ? 38.90393 -2.27585  -20.06259 1.000 64.57446  ? 175 ARG   B CZ  1 
ATOM   3089 N NH1 . ARG   B 2 82  ? 40.07034 -1.66898  -19.91642 1.000 78.23822  ? 175 ARG   B NH1 1 
ATOM   3090 N NH2 . ARG   B 2 82  ? 37.87033 -1.88608  -19.32271 1.000 65.00567  ? 175 ARG   B NH2 1 
ATOM   3091 N N   . TYR   B 2 83  ? 42.11860 -6.96093  -17.62244 1.000 81.09638  ? 176 TYR   B N   1 
ATOM   3092 C CA  . TYR   B 2 83  ? 43.05867 -6.96605  -16.50674 1.000 79.07511  ? 176 TYR   B CA  1 
ATOM   3093 C C   . TYR   B 2 83  ? 44.08308 -8.08220  -16.65872 1.000 83.23434  ? 176 TYR   B C   1 
ATOM   3094 O O   . TYR   B 2 83  ? 45.25847 -7.90533  -16.31820 1.000 91.99180  ? 176 TYR   B O   1 
ATOM   3095 C CB  . TYR   B 2 83  ? 42.30630 -7.10120  -15.18309 1.000 80.11964  ? 176 TYR   B CB  1 
ATOM   3096 C CG  . TYR   B 2 83  ? 43.20559 -7.28175  -13.98032 1.000 81.43296  ? 176 TYR   B CG  1 
ATOM   3097 C CD1 . TYR   B 2 83  ? 43.90609 -6.20891  -13.44547 1.000 79.31171  ? 176 TYR   B CD1 1 
ATOM   3098 C CD2 . TYR   B 2 83  ? 43.34836 -8.52417  -13.37607 1.000 86.78001  ? 176 TYR   B CD2 1 
ATOM   3099 C CE1 . TYR   B 2 83  ? 44.72857 -6.36872  -12.34493 1.000 83.43970  ? 176 TYR   B CE1 1 
ATOM   3100 C CE2 . TYR   B 2 83  ? 44.16803 -8.69459  -12.27513 1.000 83.29685  ? 176 TYR   B CE2 1 
ATOM   3101 C CZ  . TYR   B 2 83  ? 44.85560 -7.61368  -11.76369 1.000 91.54667  ? 176 TYR   B CZ  1 
ATOM   3102 O OH  . TYR   B 2 83  ? 45.67356 -7.77883  -10.66842 1.000 91.48829  ? 176 TYR   B OH  1 
ATOM   3103 N N   . MET   B 2 84  ? 43.65605 -9.23786  -17.17172 1.000 89.96439  ? 177 MET   B N   1 
ATOM   3104 C CA  . MET   B 2 84  ? 44.58459 -10.34116 -17.38727 1.000 85.03481  ? 177 MET   B CA  1 
ATOM   3105 C C   . MET   B 2 84  ? 45.61034 -10.01484 -18.46401 1.000 92.55476  ? 177 MET   B C   1 
ATOM   3106 O O   . MET   B 2 84  ? 46.75469 -10.47620 -18.38638 1.000 90.02635  ? 177 MET   B O   1 
ATOM   3107 C CB  . MET   B 2 84  ? 43.81405 -11.60601 -17.75611 1.000 90.76097  ? 177 MET   B CB  1 
ATOM   3108 C CG  . MET   B 2 84  ? 43.05677 -12.22060 -16.60033 1.000 84.05484  ? 177 MET   B CG  1 
ATOM   3109 S SD  . MET   B 2 84  ? 44.16404 -12.55344 -15.22555 1.000 98.25234  ? 177 MET   B SD  1 
ATOM   3110 C CE  . MET   B 2 84  ? 43.15359 -13.64387 -14.23419 1.000 106.33978 ? 177 MET   B CE  1 
ATOM   3111 N N   . ALA   B 2 85  ? 45.22462 -9.22643  -19.47075 1.000 91.87118  ? 178 ALA   B N   1 
ATOM   3112 C CA  . ALA   B 2 85  ? 46.16346 -8.83503  -20.51497 1.000 85.67447  ? 178 ALA   B CA  1 
ATOM   3113 C C   . ALA   B 2 85  ? 47.28022 -7.94577  -19.98535 1.000 95.82217  ? 178 ALA   B C   1 
ATOM   3114 O O   . ALA   B 2 85  ? 48.31416 -7.81132  -20.64888 1.000 91.04120  ? 178 ALA   B O   1 
ATOM   3115 C CB  . ALA   B 2 85  ? 45.42342 -8.12535  -21.64910 1.000 91.73522  ? 178 ALA   B CB  1 
ATOM   3116 N N   . THR   B 2 86  ? 47.09623 -7.33903  -18.81123 1.000 89.53262  ? 179 THR   B N   1 
ATOM   3117 C CA  . THR   B 2 86  ? 48.12241 -6.51854  -18.18439 1.000 86.76813  ? 179 THR   B CA  1 
ATOM   3118 C C   . THR   B 2 86  ? 48.95895 -7.28228  -17.16621 1.000 91.48631  ? 179 THR   B C   1 
ATOM   3119 O O   . THR   B 2 86  ? 50.02231 -6.79190  -16.77215 1.000 93.16115  ? 179 THR   B O   1 
ATOM   3120 C CB  . THR   B 2 86  ? 47.48903 -5.29903  -17.49669 1.000 86.56165  ? 179 THR   B CB  1 
ATOM   3121 O OG1 . THR   B 2 86  ? 46.68318 -5.72970  -16.39201 1.000 82.65853  ? 179 THR   B OG1 1 
ATOM   3122 C CG2 . THR   B 2 86  ? 46.62240 -4.52082  -18.47576 1.000 87.74302  ? 179 THR   B CG2 1 
ATOM   3123 N N   . GLN   B 2 87  ? 48.51314 -8.45785  -16.73489 1.000 88.53942  ? 180 GLN   B N   1 
ATOM   3124 C CA  . GLN   B 2 87  ? 49.20515 -9.23435  -15.71744 1.000 89.68484  ? 180 GLN   B CA  1 
ATOM   3125 C C   . GLN   B 2 87  ? 49.95947 -10.40153 -16.34673 1.000 94.84905  ? 180 GLN   B C   1 
ATOM   3126 O O   . GLN   B 2 87  ? 49.81878 -10.70509 -17.53366 1.000 103.94221 ? 180 GLN   B O   1 
ATOM   3127 C CB  . GLN   B 2 87  ? 48.21511 -9.74469  -14.66587 1.000 85.26154  ? 180 GLN   B CB  1 
ATOM   3128 C CG  . GLN   B 2 87  ? 47.41076 -8.64565  -13.99278 1.000 88.81551  ? 180 GLN   B CG  1 
ATOM   3129 C CD  . GLN   B 2 87  ? 48.28845 -7.62327  -13.30203 1.000 87.49733  ? 180 GLN   B CD  1 
ATOM   3130 O OE1 . GLN   B 2 87  ? 49.19769 -7.97531  -12.55071 1.000 96.35011  ? 180 GLN   B OE1 1 
ATOM   3131 N NE2 . GLN   B 2 87  ? 48.02492 -6.34716  -13.55890 1.000 89.03446  ? 180 GLN   B NE2 1 
ATOM   3132 N N   . GLU   B 2 88  ? 50.77654 -11.05724 -15.52328 1.000 104.71397 ? 181 GLU   B N   1 
ATOM   3133 C CA  . GLU   B 2 88  ? 51.56315 -12.21041 -15.94229 1.000 112.96087 ? 181 GLU   B CA  1 
ATOM   3134 C C   . GLU   B 2 88  ? 51.59150 -13.22725 -14.81212 1.000 111.06139 ? 181 GLU   B C   1 
ATOM   3135 O O   . GLU   B 2 88  ? 51.79875 -12.85731 -13.65271 1.000 132.04696 ? 181 GLU   B O   1 
ATOM   3136 C CB  . GLU   B 2 88  ? 52.99480 -11.80546 -16.32130 1.000 115.69092 ? 181 GLU   B CB  1 
ATOM   3137 C CG  . GLU   B 2 88  ? 53.09212 -10.85545 -17.50619 1.000 120.23498 ? 181 GLU   B CG  1 
ATOM   3138 C CD  . GLU   B 2 88  ? 54.52035 -10.45539 -17.81783 1.000 121.10524 ? 181 GLU   B CD  1 
ATOM   3139 O OE1 . GLU   B 2 88  ? 55.44530 -11.01014 -17.18861 1.000 124.69027 ? 181 GLU   B OE1 1 
ATOM   3140 O OE2 . GLU   B 2 88  ? 54.71762 -9.58454  -18.69112 1.000 123.42301 ? 181 GLU   B OE2 1 
ATOM   3141 N N   . ASN   B 2 89  ? 51.37622 -14.49986 -15.15736 1.000 106.43711 ? 182 ASN   B N   1 
ATOM   3142 C CA  . ASN   B 2 89  ? 51.44482 -15.61862 -14.21952 1.000 111.35091 ? 182 ASN   B CA  1 
ATOM   3143 C C   . ASN   B 2 89  ? 50.40901 -15.50356 -13.10442 1.000 110.52440 ? 182 ASN   B C   1 
ATOM   3144 O O   . ASN   B 2 89  ? 50.61200 -14.77055 -12.13114 1.000 124.30869 ? 182 ASN   B O   1 
ATOM   3145 C CB  . ASN   B 2 89  ? 52.85215 -15.73226 -13.62330 1.000 103.58778 ? 182 ASN   B CB  1 
ATOM   3146 C CG  . ASN   B 2 89  ? 53.93906 -15.72740 -14.68440 1.000 122.42259 ? 182 ASN   B CG  1 
ATOM   3147 O OD1 . ASN   B 2 89  ? 54.20099 -16.74458 -15.32822 1.000 104.62918 ? 182 ASN   B OD1 1 
ATOM   3148 N ND2 . ASN   B 2 89  ? 54.58251 -14.57909 -14.86669 1.000 120.00516 ? 182 ASN   B ND2 1 
ATOM   3149 N N   . VAL   B 2 90  ? 49.30299 -16.23638 -13.22905 1.000 110.96714 ? 183 VAL   B N   1 
ATOM   3150 C CA  . VAL   B 2 90  ? 48.22822 -16.22997 -12.24288 1.000 107.48591 ? 183 VAL   B CA  1 
ATOM   3151 C C   . VAL   B 2 90  ? 47.84209 -17.66975 -11.92953 1.000 93.04720  ? 183 VAL   B C   1 
ATOM   3152 O O   . VAL   B 2 90  ? 47.74391 -18.50770 -12.83278 1.000 115.06900 ? 183 VAL   B O   1 
ATOM   3153 C CB  . VAL   B 2 90  ? 47.00632 -15.42387 -12.73879 1.000 110.82194 ? 183 VAL   B CB  1 
ATOM   3154 C CG1 . VAL   B 2 90  ? 45.79758 -15.66055 -11.84613 1.000 102.69544 ? 183 VAL   B CG1 1 
ATOM   3155 C CG2 . VAL   B 2 90  ? 47.33687 -13.94058 -12.78574 1.000 95.60880  ? 183 VAL   B CG2 1 
ATOM   3156 N N   . VAL   B 2 91  ? 47.63074 -17.95633 -10.64472 1.000 123.87557 ? 184 VAL   B N   1 
ATOM   3157 C CA  . VAL   B 2 91  ? 47.27519 -19.29557 -10.18708 1.000 132.19929 ? 184 VAL   B CA  1 
ATOM   3158 C C   . VAL   B 2 91  ? 45.76153 -19.46672 -10.25898 1.000 127.37306 ? 184 VAL   B C   1 
ATOM   3159 O O   . VAL   B 2 91  ? 45.02141 -18.48727 -10.40420 1.000 125.35757 ? 184 VAL   B O   1 
ATOM   3160 C CB  . VAL   B 2 91  ? 47.80450 -19.54534 -8.76096  1.000 130.33231 ? 184 VAL   B CB  1 
ATOM   3161 C CG1 . VAL   B 2 91  ? 46.92256 -18.85234 -7.73178  1.000 125.52863 ? 184 VAL   B CG1 1 
ATOM   3162 C CG2 . VAL   B 2 91  ? 47.93107 -21.03945 -8.47281  1.000 125.55305 ? 184 VAL   B CG2 1 
ATOM   3163 N N   . LYS   B 2 92  ? 45.29307 -20.71455 -10.16112 1.000 118.27335 ? 185 LYS   B N   1 
ATOM   3164 C CA  . LYS   B 2 92  ? 43.86236 -20.98906 -10.26144 1.000 117.81668 ? 185 LYS   B CA  1 
ATOM   3165 C C   . LYS   B 2 92  ? 43.08845 -20.38050 -9.09771  1.000 113.55640 ? 185 LYS   B C   1 
ATOM   3166 O O   . LYS   B 2 92  ? 42.00103 -19.82506 -9.29375  1.000 106.45015 ? 185 LYS   B O   1 
ATOM   3167 C CB  . LYS   B 2 92  ? 43.62174 -22.49724 -10.32345 1.000 126.59989 ? 185 LYS   B CB  1 
ATOM   3168 C CG  . LYS   B 2 92  ? 44.17896 -23.17569 -11.56131 1.000 119.14000 ? 185 LYS   B CG  1 
ATOM   3169 C CD  . LYS   B 2 92  ? 44.06830 -24.68788 -11.44688 1.000 137.43075 ? 185 LYS   B CD  1 
ATOM   3170 C CE  . LYS   B 2 92  ? 42.63835 -25.11898 -11.16059 1.000 141.95548 ? 185 LYS   B CE  1 
ATOM   3171 N NZ  . LYS   B 2 92  ? 42.53113 -26.59244 -10.96862 1.000 136.44046 ? 185 LYS   B NZ  1 
ATOM   3172 N N   . THR   B 2 93  ? 43.62601 -20.48075 -7.87860  1.000 109.89884 ? 186 THR   B N   1 
ATOM   3173 C CA  . THR   B 2 93  ? 42.91205 -19.98948 -6.70447  1.000 113.30848 ? 186 THR   B CA  1 
ATOM   3174 C C   . THR   B 2 93  ? 42.73832 -18.47603 -6.71668  1.000 112.09102 ? 186 THR   B C   1 
ATOM   3175 O O   . THR   B 2 93  ? 41.86682 -17.95976 -6.00885  1.000 106.87705 ? 186 THR   B O   1 
ATOM   3176 C CB  . THR   B 2 93  ? 43.63594 -20.41470 -5.42486  1.000 122.80943 ? 186 THR   B CB  1 
ATOM   3177 O OG1 . THR   B 2 93  ? 44.93076 -19.80278 -5.37721  1.000 123.85703 ? 186 THR   B OG1 1 
ATOM   3178 C CG2 . THR   B 2 93  ? 43.79332 -21.92829 -5.37979  1.000 118.99434 ? 186 THR   B CG2 1 
ATOM   3179 N N   . LEU   B 2 94  ? 43.54291 -17.75650 -7.49860  1.000 113.18463 ? 187 LEU   B N   1 
ATOM   3180 C CA  . LEU   B 2 94  ? 43.39878 -16.31222 -7.62149  1.000 110.14464 ? 187 LEU   B CA  1 
ATOM   3181 C C   . LEU   B 2 94  ? 42.33369 -15.91208 -8.63584  1.000 109.04126 ? 187 LEU   B C   1 
ATOM   3182 O O   . LEU   B 2 94  ? 41.93452 -14.74240 -8.66359  1.000 102.47879 ? 187 LEU   B O   1 
ATOM   3183 C CB  . LEU   B 2 94  ? 44.74668 -15.68778 -8.00107  1.000 110.91960 ? 187 LEU   B CB  1 
ATOM   3184 C CG  . LEU   B 2 94  ? 44.91227 -14.17128 -7.87047  1.000 108.37631 ? 187 LEU   B CG  1 
ATOM   3185 C CD1 . LEU   B 2 94  ? 44.59178 -13.71468 -6.45658  1.000 106.65046 ? 187 LEU   B CD1 1 
ATOM   3186 C CD2 . LEU   B 2 94  ? 46.31884 -13.74898 -8.26593  1.000 106.74980 ? 187 LEU   B CD2 1 
ATOM   3187 N N   . LEU   B 2 95  ? 41.85575 -16.85292 -9.45512  1.000 106.13452 ? 188 LEU   B N   1 
ATOM   3188 C CA  . LEU   B 2 95  ? 40.85932 -16.51962 -10.46882 1.000 95.95997  ? 188 LEU   B CA  1 
ATOM   3189 C C   . LEU   B 2 95  ? 39.53200 -16.11723 -9.83729  1.000 90.02383  ? 188 LEU   B C   1 
ATOM   3190 O O   . LEU   B 2 95  ? 38.87268 -15.18445 -10.31105 1.000 92.99561  ? 188 LEU   B O   1 
ATOM   3191 C CB  . LEU   B 2 95  ? 40.66260 -17.70065 -11.42014 1.000 102.39250 ? 188 LEU   B CB  1 
ATOM   3192 C CG  . LEU   B 2 95  ? 41.86260 -18.10571 -12.27981 1.000 111.02270 ? 188 LEU   B CG  1 
ATOM   3193 C CD1 . LEU   B 2 95  ? 41.55708 -19.36080 -13.08339 1.000 95.63441  ? 188 LEU   B CD1 1 
ATOM   3194 C CD2 . LEU   B 2 95  ? 42.26409 -16.96865 -13.20152 1.000 96.40013  ? 188 LEU   B CD2 1 
ATOM   3195 N N   . GLN   B 2 96  ? 39.12360 -16.80497 -8.76756  1.000 90.40565  ? 189 GLN   B N   1 
ATOM   3196 C CA  . GLN   B 2 96  ? 37.83355 -16.50910 -8.15168  1.000 89.47398  ? 189 GLN   B CA  1 
ATOM   3197 C C   . GLN   B 2 96  ? 37.81278 -15.10802 -7.55184  1.000 94.59490  ? 189 GLN   B C   1 
ATOM   3198 O O   . GLN   B 2 96  ? 36.78795 -14.41777 -7.60976  1.000 85.73554  ? 189 GLN   B O   1 
ATOM   3199 C CB  . GLN   B 2 96  ? 37.50591 -17.55643 -7.08765  1.000 92.74231  ? 189 GLN   B CB  1 
ATOM   3200 C CG  . GLN   B 2 96  ? 36.10681 -17.42795 -6.50617  1.000 98.81261  ? 189 GLN   B CG  1 
ATOM   3201 C CD  . GLN   B 2 96  ? 35.78720 -18.51867 -5.50353  1.000 112.61157 ? 189 GLN   B CD  1 
ATOM   3202 O OE1 . GLN   B 2 96  ? 36.68520 -19.16503 -4.96315  1.000 128.06578 ? 189 GLN   B OE1 1 
ATOM   3203 N NE2 . GLN   B 2 96  ? 34.50043 -18.73201 -5.25250  1.000 104.45841 ? 189 GLN   B NE2 1 
ATOM   3204 N N   . LEU   B 2 97  ? 38.93626 -14.66756 -6.97927  1.000 92.67971  ? 190 LEU   B N   1 
ATOM   3205 C CA  . LEU   B 2 97  ? 38.99677 -13.32679 -6.40443  1.000 91.63487  ? 190 LEU   B CA  1 
ATOM   3206 C C   . LEU   B 2 97  ? 38.92941 -12.25567 -7.48629  1.000 87.64459  ? 190 LEU   B C   1 
ATOM   3207 O O   . LEU   B 2 97  ? 38.22984 -11.24841 -7.32726  1.000 83.37120  ? 190 LEU   B O   1 
ATOM   3208 C CB  . LEU   B 2 97  ? 40.26980 -13.16826 -5.57301  1.000 83.34207  ? 190 LEU   B CB  1 
ATOM   3209 C CG  . LEU   B 2 97  ? 40.54541 -11.77036 -5.01361  1.000 78.38426  ? 190 LEU   B CG  1 
ATOM   3210 C CD1 . LEU   B 2 97  ? 39.44265 -11.33998 -4.05646  1.000 88.66582  ? 190 LEU   B CD1 1 
ATOM   3211 C CD2 . LEU   B 2 97  ? 41.90271 -11.72219 -4.33140  1.000 97.49849  ? 190 LEU   B CD2 1 
ATOM   3212 N N   . ILE   B 2 98  ? 39.65218 -12.45327 -8.59046  1.000 76.45475  ? 191 ILE   B N   1 
ATOM   3213 C CA  . ILE   B 2 98  ? 39.63857 -11.47619 -9.67430  1.000 89.41979  ? 191 ILE   B CA  1 
ATOM   3214 C C   . ILE   B 2 98  ? 38.25934 -11.41205 -10.31863 1.000 85.85436  ? 191 ILE   B C   1 
ATOM   3215 O O   . ILE   B 2 98  ? 37.78006 -10.33252 -10.68862 1.000 76.93787  ? 191 ILE   B O   1 
ATOM   3216 C CB  . ILE   B 2 98  ? 40.73534 -11.81255 -10.70173 1.000 91.22466  ? 191 ILE   B CB  1 
ATOM   3217 C CG1 . ILE   B 2 98  ? 42.11047 -11.78014 -10.03266 1.000 87.95025  ? 191 ILE   B CG1 1 
ATOM   3218 C CG2 . ILE   B 2 98  ? 40.68731 -10.85214 -11.88344 1.000 82.20881  ? 191 ILE   B CG2 1 
ATOM   3219 C CD1 . ILE   B 2 98  ? 43.25649 -12.08292 -10.96727 1.000 84.83913  ? 191 ILE   B CD1 1 
ATOM   3220 N N   . GLY   B 2 99  ? 37.59299 -12.56050 -10.44688 1.000 85.32306  ? 192 GLY   B N   1 
ATOM   3221 C CA  . GLY   B 2 99  ? 36.28036 -12.57564 -11.07225 1.000 79.19672  ? 192 GLY   B CA  1 
ATOM   3222 C C   . GLY   B 2 99  ? 35.21671 -11.90777 -10.22035 1.000 80.21340  ? 192 GLY   B C   1 
ATOM   3223 O O   . GLY   B 2 99  ? 34.44287 -11.07944 -10.70944 1.000 78.06963  ? 192 GLY   B O   1 
ATOM   3224 N N   . ILE   B 2 100 ? 35.16272 -12.25714 -8.93249  1.000 80.25971  ? 193 ILE   B N   1 
ATOM   3225 C CA  . ILE   B 2 100 ? 34.12948 -11.69462 -8.06874  1.000 86.30433  ? 193 ILE   B CA  1 
ATOM   3226 C C   . ILE   B 2 100 ? 34.37158 -10.20735 -7.83229  1.000 79.02456  ? 193 ILE   B C   1 
ATOM   3227 O O   . ILE   B 2 100 ? 33.41946 -9.43995  -7.64398  1.000 74.67653  ? 193 ILE   B O   1 
ATOM   3228 C CB  . ILE   B 2 100 ? 34.04689 -12.48279 -6.74540  1.000 85.22087  ? 193 ILE   B CB  1 
ATOM   3229 C CG1 . ILE   B 2 100 ? 32.72552 -12.19249 -6.03136  1.000 75.82882  ? 193 ILE   B CG1 1 
ATOM   3230 C CG2 . ILE   B 2 100 ? 35.22855 -12.16340 -5.83669  1.000 77.65075  ? 193 ILE   B CG2 1 
ATOM   3231 C CD1 . ILE   B 2 100 ? 31.50390 -12.60023 -6.82725  1.000 78.27837  ? 193 ILE   B CD1 1 
ATOM   3232 N N   . SER   B 2 101 ? 35.63331 -9.76848  -7.85476  1.000 81.82909  ? 194 SER   B N   1 
ATOM   3233 C CA  . SER   B 2 101 ? 35.92507 -8.35099  -7.67403  1.000 69.61239  ? 194 SER   B CA  1 
ATOM   3234 C C   . SER   B 2 101 ? 35.60029 -7.55252  -8.92913  1.000 69.39778  ? 194 SER   B C   1 
ATOM   3235 O O   . SER   B 2 101 ? 35.16806 -6.39803  -8.83573  1.000 67.66788  ? 194 SER   B O   1 
ATOM   3236 C CB  . SER   B 2 101 ? 37.38954 -8.15781  -7.28272  1.000 72.75646  ? 194 SER   B CB  1 
ATOM   3237 O OG  . SER   B 2 101 ? 37.68783 -8.85664  -6.08617  1.000 80.67409  ? 194 SER   B OG  1 
ATOM   3238 N N   . SER   B 2 102 ? 35.81294 -8.14536  -10.10799 1.000 69.75341  ? 195 SER   B N   1 
ATOM   3239 C CA  . SER   B 2 102 ? 35.37486 -7.50750  -11.34521 1.000 63.97244  ? 195 SER   B CA  1 
ATOM   3240 C C   . SER   B 2 102 ? 33.86086 -7.34459  -11.36455 1.000 66.10166  ? 195 SER   B C   1 
ATOM   3241 O O   . SER   B 2 102 ? 33.34168 -6.32380  -11.83149 1.000 60.94449  ? 195 SER   B O   1 
ATOM   3242 C CB  . SER   B 2 102 ? 35.84246 -8.32288  -12.55191 1.000 63.96469  ? 195 SER   B CB  1 
ATOM   3243 O OG  . SER   B 2 102 ? 37.25339 -8.44270  -12.57602 1.000 71.95591  ? 195 SER   B OG  1 
ATOM   3244 N N   . LEU   B 2 103 ? 33.13603 -8.34494  -10.85944 1.000 68.29305  ? 196 LEU   B N   1 
ATOM   3245 C CA  . LEU   B 2 103 ? 31.68761 -8.22922  -10.74371 1.000 62.08252  ? 196 LEU   B CA  1 
ATOM   3246 C C   . LEU   B 2 103 ? 31.29335 -7.21238  -9.68150  1.000 60.02380  ? 196 LEU   B C   1 
ATOM   3247 O O   . LEU   B 2 103 ? 30.26108 -6.54558  -9.81619  1.000 64.29336  ? 196 LEU   B O   1 
ATOM   3248 C CB  . LEU   B 2 103 ? 31.08117 -9.59640  -10.42861 1.000 69.16190  ? 196 LEU   B CB  1 
ATOM   3249 C CG  . LEU   B 2 103 ? 29.55747 -9.67929  -10.34238 1.000 67.86428  ? 196 LEU   B CG  1 
ATOM   3250 C CD1 . LEU   B 2 103 ? 28.92695 -9.24147  -11.65215 1.000 73.16040  ? 196 LEU   B CD1 1 
ATOM   3251 C CD2 . LEU   B 2 103 ? 29.12773 -11.09129 -9.98180  1.000 69.71598  ? 196 LEU   B CD2 1 
ATOM   3252 N N   . PHE   B 2 104 ? 32.09894 -7.07875  -8.62475  1.000 70.44113  ? 197 PHE   B N   1 
ATOM   3253 C CA  . PHE   B 2 104 ? 31.81379 -6.08381  -7.59575  1.000 63.64108  ? 197 PHE   B CA  1 
ATOM   3254 C C   . PHE   B 2 104 ? 31.93908 -4.67091  -8.15042  1.000 62.75018  ? 197 PHE   B C   1 
ATOM   3255 O O   . PHE   B 2 104 ? 31.08450 -3.81610  -7.88772  1.000 62.86746  ? 197 PHE   B O   1 
ATOM   3256 C CB  . PHE   B 2 104 ? 32.74887 -6.28683  -6.40275  1.000 71.50752  ? 197 PHE   B CB  1 
ATOM   3257 C CG  . PHE   B 2 104 ? 32.49653 -5.34257  -5.26101  1.000 74.22222  ? 197 PHE   B CG  1 
ATOM   3258 C CD1 . PHE   B 2 104 ? 31.24583 -5.26541  -4.66987  1.000 69.54670  ? 197 PHE   B CD1 1 
ATOM   3259 C CD2 . PHE   B 2 104 ? 33.51736 -4.54731  -4.76448  1.000 80.34398  ? 197 PHE   B CD2 1 
ATOM   3260 C CE1 . PHE   B 2 104 ? 31.01419 -4.40165  -3.61321  1.000 84.58472  ? 197 PHE   B CE1 1 
ATOM   3261 C CE2 . PHE   B 2 104 ? 33.29313 -3.68395  -3.70716  1.000 76.69702  ? 197 PHE   B CE2 1 
ATOM   3262 C CZ  . PHE   B 2 104 ? 32.03978 -3.61110  -3.13065  1.000 71.32061  ? 197 PHE   B CZ  1 
ATOM   3263 N N   . ILE   B 2 105 ? 32.99668 -4.40930  -8.92188  1.000 68.08284  ? 198 ILE   B N   1 
ATOM   3264 C CA  . ILE   B 2 105 ? 33.13196 -3.11885  -9.59114  1.000 60.21439  ? 198 ILE   B CA  1 
ATOM   3265 C C   . ILE   B 2 105 ? 31.98207 -2.90611  -10.56537 1.000 60.66241  ? 198 ILE   B C   1 
ATOM   3266 O O   . ILE   B 2 105 ? 31.40015 -1.81638  -10.63630 1.000 55.16063  ? 198 ILE   B O   1 
ATOM   3267 C CB  . ILE   B 2 105 ? 34.49489 -3.02782  -10.30276 1.000 66.11356  ? 198 ILE   B CB  1 
ATOM   3268 C CG1 . ILE   B 2 105 ? 35.63708 -3.25239  -9.31072  1.000 61.77602  ? 198 ILE   B CG1 1 
ATOM   3269 C CG2 . ILE   B 2 105 ? 34.64671 -1.68402  -11.00418 1.000 50.09346  ? 198 ILE   B CG2 1 
ATOM   3270 C CD1 . ILE   B 2 105 ? 36.97638 -3.47161  -9.97642  1.000 57.39914  ? 198 ILE   B CD1 1 
ATOM   3271 N N   . ALA   B 2 106 ? 31.63141 -3.94658  -11.32589 1.000 56.29157  ? 199 ALA   B N   1 
ATOM   3272 C CA  . ALA   B 2 106 ? 30.57967 -3.81238  -12.32817 1.000 61.33019  ? 199 ALA   B CA  1 
ATOM   3273 C C   . ALA   B 2 106 ? 29.22582 -3.54624  -11.68339 1.000 53.31883  ? 199 ALA   B C   1 
ATOM   3274 O O   . ALA   B 2 106 ? 28.46062 -2.70345  -12.16530 1.000 51.58312  ? 199 ALA   B O   1 
ATOM   3275 C CB  . ALA   B 2 106 ? 30.52252 -5.06662  -13.20030 1.000 60.13048  ? 199 ALA   B CB  1 
ATOM   3276 N N   . ALA   B 2 107 ? 28.91331 -4.25207  -10.59361 1.000 55.79443  ? 200 ALA   B N   1 
ATOM   3277 C CA  . ALA   B 2 107 ? 27.62336 -4.06380  -9.93825  1.000 59.33288  ? 200 ALA   B CA  1 
ATOM   3278 C C   . ALA   B 2 107 ? 27.48614 -2.65445  -9.37600  1.000 56.93812  ? 200 ALA   B C   1 
ATOM   3279 O O   . ALA   B 2 107 ? 26.41059 -2.05016  -9.45677  1.000 59.80229  ? 200 ALA   B O   1 
ATOM   3280 C CB  . ALA   B 2 107 ? 27.43728 -5.10320  -8.83442  1.000 61.05557  ? 200 ALA   B CB  1 
ATOM   3281 N N   . LYS   B 2 108 ? 28.56401 -2.11134  -8.80187  1.000 66.61436  ? 201 LYS   B N   1 
ATOM   3282 C CA  . LYS   B 2 108 ? 28.50121 -0.75397  -8.26930  1.000 56.92384  ? 201 LYS   B CA  1 
ATOM   3283 C C   . LYS   B 2 108 ? 28.35155 0.27886   -9.37884  1.000 63.27028  ? 201 LYS   B C   1 
ATOM   3284 O O   . LYS   B 2 108 ? 27.82807 1.37289   -9.13788  1.000 57.61654  ? 201 LYS   B O   1 
ATOM   3285 C CB  . LYS   B 2 108 ? 29.74371 -0.45175  -7.42616  1.000 61.53215  ? 201 LYS   B CB  1 
ATOM   3286 C CG  . LYS   B 2 108 ? 29.73985 -1.11519  -6.05884  1.000 64.10710  ? 201 LYS   B CG  1 
ATOM   3287 C CD  . LYS   B 2 108 ? 30.85989 -0.58989  -5.17032  1.000 65.41679  ? 201 LYS   B CD  1 
ATOM   3288 C CE  . LYS   B 2 108 ? 32.22845 -0.93235  -5.73529  1.000 69.93312  ? 201 LYS   B CE  1 
ATOM   3289 N NZ  . LYS   B 2 108 ? 33.33281 -0.47065  -4.84951  1.000 58.89221  ? 201 LYS   B NZ  1 
ATOM   3290 N N   . LEU   B 2 109 ? 28.79573 -0.04761  -10.59500 1.000 63.17005  ? 202 LEU   B N   1 
ATOM   3291 C CA  . LEU   B 2 109 ? 28.69360 0.89303   -11.70493 1.000 60.50370  ? 202 LEU   B CA  1 
ATOM   3292 C C   . LEU   B 2 109 ? 27.30046 0.89758   -12.32331 1.000 62.50136  ? 202 LEU   B C   1 
ATOM   3293 O O   . LEU   B 2 109 ? 26.77867 1.96275   -12.67183 1.000 61.40705  ? 202 LEU   B O   1 
ATOM   3294 C CB  . LEU   B 2 109 ? 29.73970 0.56072   -12.76954 1.000 54.97279  ? 202 LEU   B CB  1 
ATOM   3295 C CG  . LEU   B 2 109 ? 31.16013 1.06220   -12.51485 1.000 68.91775  ? 202 LEU   B CG  1 
ATOM   3296 C CD1 . LEU   B 2 109 ? 32.12626 0.43335   -13.50149 1.000 55.13591  ? 202 LEU   B CD1 1 
ATOM   3297 C CD2 . LEU   B 2 109 ? 31.20144 2.57947   -12.61742 1.000 67.74372  ? 202 LEU   B CD2 1 
ATOM   3298 N N   . GLU   B 2 110 ? 26.68259 -0.27431  -12.46318 1.000 64.66192  ? 203 GLU   B N   1 
ATOM   3299 C CA  . GLU   B 2 110 ? 25.46295 -0.41924  -13.24966 1.000 62.67293  ? 203 GLU   B CA  1 
ATOM   3300 C C   . GLU   B 2 110 ? 24.19120 -0.45354  -12.41026 1.000 73.75160  ? 203 GLU   B C   1 
ATOM   3301 O O   . GLU   B 2 110 ? 23.20029 0.18486   -12.77839 1.000 68.23234  ? 203 GLU   B O   1 
ATOM   3302 C CB  . GLU   B 2 110 ? 25.54194 -1.68998  -14.10310 1.000 60.70833  ? 203 GLU   B CB  1 
ATOM   3303 C CG  . GLU   B 2 110 ? 24.44002 -1.81115  -15.14682 1.000 73.09863  ? 203 GLU   B CG  1 
ATOM   3304 C CD  . GLU   B 2 110 ? 24.53081 -0.74457  -16.22506 1.000 84.86672  ? 203 GLU   B CD  1 
ATOM   3305 O OE1 . GLU   B 2 110 ? 25.64482 -0.23763  -16.47870 1.000 79.91614  ? 203 GLU   B OE1 1 
ATOM   3306 O OE2 . GLU   B 2 110 ? 23.48455 -0.41178  -16.81992 1.000 97.41976  ? 203 GLU   B OE2 1 
ATOM   3307 N N   . GLU   B 2 111 ? 24.18688 -1.18219  -11.29660 1.000 64.26907  ? 204 GLU   B N   1 
ATOM   3308 C CA  . GLU   B 2 111 ? 22.96412 -1.35678  -10.52523 1.000 68.27011  ? 204 GLU   B CA  1 
ATOM   3309 C C   . GLU   B 2 111 ? 22.61405 -0.09152  -9.74908  1.000 74.16547  ? 204 GLU   B C   1 
ATOM   3310 O O   . GLU   B 2 111 ? 23.48764 0.66680   -9.31907  1.000 71.67881  ? 204 GLU   B O   1 
ATOM   3311 C CB  . GLU   B 2 111 ? 23.10447 -2.53283  -9.55858  1.000 57.21071  ? 204 GLU   B CB  1 
ATOM   3312 C CG  . GLU   B 2 111 ? 23.50562 -3.84035  -10.21864 1.000 64.34958  ? 204 GLU   B CG  1 
ATOM   3313 C CD  . GLU   B 2 111 ? 22.45470 -4.35868  -11.18272 1.000 76.79609  ? 204 GLU   B CD  1 
ATOM   3314 O OE1 . GLU   B 2 111 ? 21.27331 -3.97218  -11.05038 1.000 74.80901  ? 204 GLU   B OE1 1 
ATOM   3315 O OE2 . GLU   B 2 111 ? 22.81245 -5.15426  -12.07619 1.000 69.40059  ? 204 GLU   B OE2 1 
ATOM   3316 N N   . ILE   B 2 112 ? 21.31023 0.13020   -9.57256  1.000 65.70525  ? 205 ILE   B N   1 
ATOM   3317 C CA  . ILE   B 2 112 ? 20.85160 1.24527   -8.74994  1.000 76.96876  ? 205 ILE   B CA  1 
ATOM   3318 C C   . ILE   B 2 112 ? 21.08248 0.94278   -7.27357  1.000 75.98097  ? 205 ILE   B C   1 
ATOM   3319 O O   . ILE   B 2 112 ? 21.63835 1.76362   -6.53414  1.000 75.22503  ? 205 ILE   B O   1 
ATOM   3320 C CB  . ILE   B 2 112 ? 19.37239 1.55591   -9.04128  1.000 72.40562  ? 205 ILE   B CB  1 
ATOM   3321 C CG1 . ILE   B 2 112 ? 19.19833 2.00045   -10.49464 1.000 69.31096  ? 205 ILE   B CG1 1 
ATOM   3322 C CG2 . ILE   B 2 112 ? 18.85007 2.62016   -8.08582  1.000 69.68170  ? 205 ILE   B CG2 1 
ATOM   3323 C CD1 . ILE   B 2 112 ? 17.76887 2.33657   -10.86559 1.000 62.07227  ? 205 ILE   B CD1 1 
ATOM   3324 N N   . TYR   B 2 113 ? 20.66218 -0.24366  -6.82301  1.000 66.88846  ? 206 TYR   B N   1 
ATOM   3325 C CA  . TYR   B 2 113 ? 20.88439 -0.71443  -5.45635  1.000 75.49266  ? 206 TYR   B CA  1 
ATOM   3326 C C   . TYR   B 2 113 ? 21.70190 -1.99943  -5.53112  1.000 69.58085  ? 206 TYR   B C   1 
ATOM   3327 O O   . TYR   B 2 113 ? 21.14613 -3.10726  -5.47268  1.000 74.22048  ? 206 TYR   B O   1 
ATOM   3328 C CB  . TYR   B 2 113 ? 19.56807 -0.94039  -4.71293  1.000 70.87936  ? 206 TYR   B CB  1 
ATOM   3329 C CG  . TYR   B 2 113 ? 18.67249 0.27721   -4.65731  1.000 77.27899  ? 206 TYR   B CG  1 
ATOM   3330 C CD1 . TYR   B 2 113 ? 18.95732 1.33624   -3.80359  1.000 68.27807  ? 206 TYR   B CD1 1 
ATOM   3331 C CD2 . TYR   B 2 113 ? 17.53752 0.36443   -5.45403  1.000 77.82871  ? 206 TYR   B CD2 1 
ATOM   3332 C CE1 . TYR   B 2 113 ? 18.13908 2.45152   -3.74925  1.000 81.32800  ? 206 TYR   B CE1 1 
ATOM   3333 C CE2 . TYR   B 2 113 ? 16.71299 1.47453   -5.40630  1.000 85.24230  ? 206 TYR   B CE2 1 
ATOM   3334 C CZ  . TYR   B 2 113 ? 17.01820 2.51467   -4.55309  1.000 93.17345  ? 206 TYR   B CZ  1 
ATOM   3335 O OH  . TYR   B 2 113 ? 16.19878 3.61970   -4.50532  1.000 91.28145  ? 206 TYR   B OH  1 
ATOM   3336 N N   . PRO   B 2 114 ? 23.02170 -1.89150  -5.65180  1.000 73.41060  ? 207 PRO   B N   1 
ATOM   3337 C CA  . PRO   B 2 114 ? 23.85977 -3.08483  -5.81078  1.000 71.87502  ? 207 PRO   B CA  1 
ATOM   3338 C C   . PRO   B 2 114 ? 23.93402 -3.87991  -4.52110  1.000 69.77193  ? 207 PRO   B C   1 
ATOM   3339 O O   . PRO   B 2 114 ? 23.63166 -3.35504  -3.43906  1.000 83.06142  ? 207 PRO   B O   1 
ATOM   3340 C CB  . PRO   B 2 114 ? 25.23020 -2.50097  -6.18259  1.000 69.47552  ? 207 PRO   B CB  1 
ATOM   3341 C CG  . PRO   B 2 114 ? 25.23518 -1.15580  -5.54653  1.000 70.43258  ? 207 PRO   B CG  1 
ATOM   3342 C CD  . PRO   B 2 114 ? 23.81835 -0.65215  -5.64466  1.000 69.83544  ? 207 PRO   B CD  1 
ATOM   3343 N N   . PRO   B 2 115 ? 24.32299 -5.15066  -4.59326  1.000 79.92456  ? 208 PRO   B N   1 
ATOM   3344 C CA  . PRO   B 2 115 ? 24.52750 -5.92927  -3.36843  1.000 74.98498  ? 208 PRO   B CA  1 
ATOM   3345 C C   . PRO   B 2 115 ? 25.70226 -5.39279  -2.56501  1.000 84.80647  ? 208 PRO   B C   1 
ATOM   3346 O O   . PRO   B 2 115 ? 26.60753 -4.73944  -3.08884  1.000 69.14294  ? 208 PRO   B O   1 
ATOM   3347 C CB  . PRO   B 2 115 ? 24.81046 -7.34563  -3.88365  1.000 74.31336  ? 208 PRO   B CB  1 
ATOM   3348 C CG  . PRO   B 2 115 ? 24.28938 -7.36164  -5.28816  1.000 72.77521  ? 208 PRO   B CG  1 
ATOM   3349 C CD  . PRO   B 2 115 ? 24.48937 -5.97179  -5.80354  1.000 77.56597  ? 208 PRO   B CD  1 
ATOM   3350 N N   . LYS   B 2 116 ? 25.67415 -5.68250  -1.26628  1.000 83.51037  ? 209 LYS   B N   1 
ATOM   3351 C CA  . LYS   B 2 116 ? 26.71681 -5.22106  -0.36494  1.000 80.21479  ? 209 LYS   B CA  1 
ATOM   3352 C C   . LYS   B 2 116 ? 27.98928 -6.04710  -0.54596  1.000 82.38712  ? 209 LYS   B C   1 
ATOM   3353 O O   . LYS   B 2 116 ? 28.00211 -7.08894  -1.20686  1.000 86.95726  ? 209 LYS   B O   1 
ATOM   3354 C CB  . LYS   B 2 116 ? 26.23841 -5.28225  1.08549   1.000 86.42705  ? 209 LYS   B CB  1 
ATOM   3355 C CG  . LYS   B 2 116 ? 25.15758 -4.26726  1.42707   1.000 77.21353  ? 209 LYS   B CG  1 
ATOM   3356 C CD  . LYS   B 2 116 ? 25.65168 -2.84477  1.21124   1.000 85.52278  ? 209 LYS   B CD  1 
ATOM   3357 C CE  . LYS   B 2 116 ? 24.59952 -1.81884  1.60679   1.000 85.84627  ? 209 LYS   B CE  1 
ATOM   3358 N NZ  . LYS   B 2 116 ? 23.36874 -1.92149  0.77529   1.000 76.58257  ? 209 LYS   B NZ  1 
ATOM   3359 N N   . LEU   B 2 117 ? 29.07428 -5.56395  0.06554   1.000 84.63823  ? 210 LEU   B N   1 
ATOM   3360 C CA  . LEU   B 2 117 ? 30.37500 -6.20377  -0.10749  1.000 81.30464  ? 210 LEU   B CA  1 
ATOM   3361 C C   . LEU   B 2 117 ? 30.38070 -7.62376  0.44273   1.000 88.02993  ? 210 LEU   B C   1 
ATOM   3362 O O   . LEU   B 2 117 ? 30.89749 -8.54359  -0.20274  1.000 93.65645  ? 210 LEU   B O   1 
ATOM   3363 C CB  . LEU   B 2 117 ? 31.46415 -5.37074  0.56735   1.000 83.23612  ? 210 LEU   B CB  1 
ATOM   3364 C CG  . LEU   B 2 117 ? 32.82044 -6.06015  0.73575   1.000 83.79805  ? 210 LEU   B CG  1 
ATOM   3365 C CD1 . LEU   B 2 117 ? 33.46591 -6.33732  -0.61480  1.000 76.54560  ? 210 LEU   B CD1 1 
ATOM   3366 C CD2 . LEU   B 2 117 ? 33.73986 -5.23182  1.61851   1.000 80.92726  ? 210 LEU   B CD2 1 
ATOM   3367 N N   . HIS   B 2 118 ? 29.81352 -7.82459  1.63472   1.000 90.10437  ? 211 HIS   B N   1 
ATOM   3368 C CA  . HIS   B 2 118 ? 29.88074 -9.14149  2.25941   1.000 103.33438 ? 211 HIS   B CA  1 
ATOM   3369 C C   . HIS   B 2 118 ? 29.10107 -10.18297 1.46530   1.000 92.92957  ? 211 HIS   B C   1 
ATOM   3370 O O   . HIS   B 2 118 ? 29.43181 -11.37266 1.51962   1.000 94.09179  ? 211 HIS   B O   1 
ATOM   3371 C CB  . HIS   B 2 118 ? 29.37310 -9.07182  3.70104   1.000 102.47905 ? 211 HIS   B CB  1 
ATOM   3372 C CG  . HIS   B 2 118 ? 27.89002 -9.22322  3.82920   1.000 103.64971 ? 211 HIS   B CG  1 
ATOM   3373 N ND1 . HIS   B 2 118 ? 27.00852 -8.20597  3.53284   1.000 97.55368  ? 211 HIS   B ND1 1 
ATOM   3374 C CD2 . HIS   B 2 118 ? 27.13315 -10.27409 4.22463   1.000 104.10294 ? 211 HIS   B CD2 1 
ATOM   3375 C CE1 . HIS   B 2 118 ? 25.77233 -8.62424  3.73811   1.000 104.93232 ? 211 HIS   B CE1 1 
ATOM   3376 N NE2 . HIS   B 2 118 ? 25.82021 -9.87575  4.15827   1.000 112.62280 ? 211 HIS   B NE2 1 
ATOM   3377 N N   . GLN   B 2 119 ? 28.07556 -9.76178  0.71968   1.000 93.30068  ? 212 GLN   B N   1 
ATOM   3378 C CA  . GLN   B 2 119 ? 27.35052 -10.70336 -0.12915  1.000 103.06208 ? 212 GLN   B CA  1 
ATOM   3379 C C   . GLN   B 2 119 ? 28.22731 -11.20604 -1.26883  1.000 89.78135  ? 212 GLN   B C   1 
ATOM   3380 O O   . GLN   B 2 119 ? 28.13872 -12.37665 -1.65734  1.000 90.24220  ? 212 GLN   B O   1 
ATOM   3381 C CB  . GLN   B 2 119 ? 26.07918 -10.05566 -0.67542  1.000 89.95949  ? 212 GLN   B CB  1 
ATOM   3382 C CG  . GLN   B 2 119 ? 24.97108 -9.91505  0.35204   1.000 102.31825 ? 212 GLN   B CG  1 
ATOM   3383 C CD  . GLN   B 2 119 ? 23.72003 -9.28659  -0.22571  1.000 97.05588  ? 212 GLN   B CD  1 
ATOM   3384 O OE1 . GLN   B 2 119 ? 23.74750 -8.15651  -0.71382  1.000 93.25525  ? 212 GLN   B OE1 1 
ATOM   3385 N NE2 . GLN   B 2 119 ? 22.61305 -10.01951 -0.17664  1.000 106.45458 ? 212 GLN   B NE2 1 
ATOM   3386 N N   . PHE   B 2 120 ? 29.07667 -10.33569 -1.82071  1.000 89.85200  ? 213 PHE   B N   1 
ATOM   3387 C CA  . PHE   B 2 120 ? 30.04227 -10.78707 -2.81571  1.000 82.67514  ? 213 PHE   B CA  1 
ATOM   3388 C C   . PHE   B 2 120 ? 31.07235 -11.72676 -2.20364  1.000 83.32883  ? 213 PHE   B C   1 
ATOM   3389 O O   . PHE   B 2 120 ? 31.52825 -12.66288 -2.86856  1.000 82.55473  ? 213 PHE   B O   1 
ATOM   3390 C CB  . PHE   B 2 120 ? 30.72618 -9.58784  -3.47080  1.000 82.87639  ? 213 PHE   B CB  1 
ATOM   3391 C CG  . PHE   B 2 120 ? 29.87766 -8.90012  -4.50254  1.000 79.14373  ? 213 PHE   B CG  1 
ATOM   3392 C CD1 . PHE   B 2 120 ? 28.97703 -7.91458  -4.13528  1.000 81.67322  ? 213 PHE   B CD1 1 
ATOM   3393 C CD2 . PHE   B 2 120 ? 29.97657 -9.24568  -5.84008  1.000 77.98799  ? 213 PHE   B CD2 1 
ATOM   3394 C CE1 . PHE   B 2 120 ? 28.19322 -7.28397  -5.08273  1.000 78.29355  ? 213 PHE   B CE1 1 
ATOM   3395 C CE2 . PHE   B 2 120 ? 29.19635 -8.61945  -6.79286  1.000 74.69498  ? 213 PHE   B CE2 1 
ATOM   3396 C CZ  . PHE   B 2 120 ? 28.30327 -7.63628  -6.41370  1.000 76.92787  ? 213 PHE   B CZ  1 
ATOM   3397 N N   . ALA   B 2 121 ? 31.44868 -11.50117 -0.94410  1.000 93.48666  ? 214 ALA   B N   1 
ATOM   3398 C CA  . ALA   B 2 121 ? 32.30174 -12.45764 -0.25252  1.000 92.78495  ? 214 ALA   B CA  1 
ATOM   3399 C C   . ALA   B 2 121 ? 31.53162 -13.70130 0.17179   1.000 88.37116  ? 214 ALA   B C   1 
ATOM   3400 O O   . ALA   B 2 121 ? 32.14012 -14.76021 0.35822   1.000 90.61537  ? 214 ALA   B O   1 
ATOM   3401 C CB  . ALA   B 2 121 ? 32.95475 -11.79866 0.96483   1.000 82.07532  ? 214 ALA   B CB  1 
ATOM   3402 N N   . TYR   B 2 122 ? 30.20667 -13.59805 0.30616   1.000 88.32172  ? 215 TYR   B N   1 
ATOM   3403 C CA  . TYR   B 2 122 ? 29.40619 -14.72319 0.78067   1.000 82.56447  ? 215 TYR   B CA  1 
ATOM   3404 C C   . TYR   B 2 122 ? 29.26581 -15.80542 -0.28493  1.000 93.92190  ? 215 TYR   B C   1 
ATOM   3405 O O   . TYR   B 2 122 ? 29.27454 -17.00005 0.03442   1.000 90.99873  ? 215 TYR   B O   1 
ATOM   3406 C CB  . TYR   B 2 122 ? 28.03364 -14.22005 1.23238   1.000 90.41737  ? 215 TYR   B CB  1 
ATOM   3407 C CG  . TYR   B 2 122 ? 27.00630 -15.30317 1.46924   1.000 92.94027  ? 215 TYR   B CG  1 
ATOM   3408 C CD1 . TYR   B 2 122 ? 27.10679 -16.15999 2.55811   1.000 97.46792  ? 215 TYR   B CD1 1 
ATOM   3409 C CD2 . TYR   B 2 122 ? 25.92368 -15.45608 0.61272   1.000 96.82020  ? 215 TYR   B CD2 1 
ATOM   3410 C CE1 . TYR   B 2 122 ? 26.16442 -17.14893 2.77924   1.000 88.68816  ? 215 TYR   B CE1 1 
ATOM   3411 C CE2 . TYR   B 2 122 ? 24.97596 -16.43838 0.82621   1.000 105.39459 ? 215 TYR   B CE2 1 
ATOM   3412 C CZ  . TYR   B 2 122 ? 25.10082 -17.28304 1.91020   1.000 102.94914 ? 215 TYR   B CZ  1 
ATOM   3413 O OH  . TYR   B 2 122 ? 24.15867 -18.26407 2.12363   1.000 101.09254 ? 215 TYR   B OH  1 
ATOM   3414 N N   . VAL   B 2 123 ? 29.13650 -15.41283 -1.55604  1.000 93.25790  ? 216 VAL   B N   1 
ATOM   3415 C CA  . VAL   B 2 123 ? 28.95190 -16.39855 -2.61610  1.000 87.98618  ? 216 VAL   B CA  1 
ATOM   3416 C C   . VAL   B 2 123 ? 30.23141 -17.17000 -2.90784  1.000 94.02667  ? 216 VAL   B C   1 
ATOM   3417 O O   . VAL   B 2 123 ? 30.17636 -18.24291 -3.51997  1.000 110.24127 ? 216 VAL   B O   1 
ATOM   3418 C CB  . VAL   B 2 123 ? 28.42742 -15.72884 -3.89990  1.000 96.90860  ? 216 VAL   B CB  1 
ATOM   3419 C CG1 . VAL   B 2 123 ? 27.07269 -15.09069 -3.64688  1.000 94.66174  ? 216 VAL   B CG1 1 
ATOM   3420 C CG2 . VAL   B 2 123 ? 29.42387 -14.70015 -4.41215  1.000 96.10108  ? 216 VAL   B CG2 1 
ATOM   3421 N N   . THR   B 2 124 ? 31.38514 -16.65822 -2.48446  1.000 91.19482  ? 217 THR   B N   1 
ATOM   3422 C CA  . THR   B 2 124 ? 32.65295 -17.34368 -2.70003  1.000 101.52049 ? 217 THR   B CA  1 
ATOM   3423 C C   . THR   B 2 124 ? 32.86532 -18.51771 -1.75285  1.000 103.96249 ? 217 THR   B C   1 
ATOM   3424 O O   . THR   B 2 124 ? 33.92268 -19.15473 -1.81825  1.000 105.20299 ? 217 THR   B O   1 
ATOM   3425 C CB  . THR   B 2 124 ? 33.81660 -16.35942 -2.55516  1.000 103.74911 ? 217 THR   B CB  1 
ATOM   3426 O OG1 . THR   B 2 124 ? 33.83190 -15.82804 -1.22403  1.000 104.22623 ? 217 THR   B OG1 1 
ATOM   3427 C CG2 . THR   B 2 124 ? 33.67359 -15.21821 -3.54797  1.000 94.31304  ? 217 THR   B CG2 1 
ATOM   3428 N N   . ASP   B 2 125 ? 31.89576 -18.81284 -0.88281  1.000 120.83005 ? 218 ASP   B N   1 
ATOM   3429 C CA  . ASP   B 2 125 ? 31.99785 -19.90541 0.08799   1.000 125.75432 ? 218 ASP   B CA  1 
ATOM   3430 C C   . ASP   B 2 125 ? 33.22456 -19.73464 0.98289   1.000 126.81381 ? 218 ASP   B C   1 
ATOM   3431 O O   . ASP   B 2 125 ? 33.91475 -20.69982 1.31777   1.000 132.20992 ? 218 ASP   B O   1 
ATOM   3432 C CB  . ASP   B 2 125 ? 32.01029 -21.26962 -0.60923  1.000 145.28831 ? 218 ASP   B CB  1 
ATOM   3433 C CG  . ASP   B 2 125 ? 31.66094 -22.41229 0.32957   1.000 147.27770 ? 218 ASP   B CG  1 
ATOM   3434 O OD1 . ASP   B 2 125 ? 31.40712 -22.15024 1.52423   1.000 156.34499 ? 218 ASP   B OD1 1 
ATOM   3435 O OD2 . ASP   B 2 125 ? 31.63849 -23.57402 -0.12944  1.000 143.96499 ? 218 ASP   B OD2 1 
ATOM   3436 N N   . GLY   B 2 126 ? 33.50208 -18.48920 1.36913   1.000 107.17151 ? 219 GLY   B N   1 
ATOM   3437 C CA  . GLY   B 2 126 ? 34.59585 -18.18770 2.26685   1.000 123.11195 ? 219 GLY   B CA  1 
ATOM   3438 C C   . GLY   B 2 126 ? 35.96369 -18.09957 1.62772   1.000 119.88647 ? 219 GLY   B C   1 
ATOM   3439 O O   . GLY   B 2 126 ? 36.92043 -17.70838 2.30923   1.000 125.23025 ? 219 GLY   B O   1 
ATOM   3440 N N   . ALA   B 2 127 ? 36.09752 -18.44631 0.34604   1.000 114.18281 ? 220 ALA   B N   1 
ATOM   3441 C CA  . ALA   B 2 127 ? 37.39339 -18.37828 -0.31817  1.000 114.78731 ? 220 ALA   B CA  1 
ATOM   3442 C C   . ALA   B 2 127 ? 37.86848 -16.94919 -0.54568  1.000 114.92683 ? 220 ALA   B C   1 
ATOM   3443 O O   . ALA   B 2 127 ? 39.04786 -16.75118 -0.85688  1.000 118.78819 ? 220 ALA   B O   1 
ATOM   3444 C CB  . ALA   B 2 127 ? 37.33995 -19.12353 -1.65315  1.000 115.12682 ? 220 ALA   B CB  1 
ATOM   3445 N N   . CYS   B 2 128 ? 36.99123 -15.95770 -0.40028  1.000 109.51248 ? 221 CYS   B N   1 
ATOM   3446 C CA  . CYS   B 2 128 ? 37.35512 -14.55862 -0.58084  1.000 112.81652 ? 221 CYS   B CA  1 
ATOM   3447 C C   . CYS   B 2 128 ? 36.70920 -13.73047 0.51776   1.000 110.25354 ? 221 CYS   B C   1 
ATOM   3448 O O   . CYS   B 2 128 ? 35.48930 -13.78145 0.69891   1.000 105.22359 ? 221 CYS   B O   1 
ATOM   3449 C CB  . CYS   B 2 128 ? 36.91763 -14.04088 -1.95634  1.000 103.26329 ? 221 CYS   B CB  1 
ATOM   3450 S SG  . CYS   B 2 128 ? 37.61095 -14.94870 -3.35604  1.000 105.93234 ? 221 CYS   B SG  1 
ATOM   3451 N N   . SER   B 2 129 ? 37.52404 -12.97333 1.24436   1.000 102.88012 ? 222 SER   B N   1 
ATOM   3452 C CA  . SER   B 2 129 ? 37.02571 -12.10812 2.30023   1.000 95.80010  ? 222 SER   B CA  1 
ATOM   3453 C C   . SER   B 2 129 ? 36.63852 -10.74570 1.73183   1.000 97.07719  ? 222 SER   B C   1 
ATOM   3454 O O   . SER   B 2 129 ? 36.92226 -10.41840 0.57772   1.000 97.21745  ? 222 SER   B O   1 
ATOM   3455 C CB  . SER   B 2 129 ? 38.07260 -11.94629 3.40147   1.000 107.02841 ? 222 SER   B CB  1 
ATOM   3456 O OG  . SER   B 2 129 ? 39.18955 -11.20963 2.93582   1.000 107.70829 ? 222 SER   B OG  1 
ATOM   3457 N N   . GLY   B 2 130 ? 35.97427 -9.94431  2.56611   1.000 96.34442  ? 223 GLY   B N   1 
ATOM   3458 C CA  . GLY   B 2 130 ? 35.60300 -8.60471  2.14254   1.000 82.70321  ? 223 GLY   B CA  1 
ATOM   3459 C C   . GLY   B 2 130 ? 36.80941 -7.72663  1.87365   1.000 92.66653  ? 223 GLY   B C   1 
ATOM   3460 O O   . GLY   B 2 130 ? 36.82493 -6.95370  0.91246   1.000 85.77641  ? 223 GLY   B O   1 
ATOM   3461 N N   . ASP   B 2 131 ? 37.84162 -7.84043  2.71478   1.000 88.61558  ? 224 ASP   B N   1 
ATOM   3462 C CA  . ASP   B 2 131 ? 39.05159 -7.04875  2.51819   1.000 96.50739  ? 224 ASP   B CA  1 
ATOM   3463 C C   . ASP   B 2 131 ? 39.84141 -7.51421  1.30220   1.000 87.12019  ? 224 ASP   B C   1 
ATOM   3464 O O   . ASP   B 2 131 ? 40.50477 -6.70007  0.64944   1.000 88.13442  ? 224 ASP   B O   1 
ATOM   3465 C CB  . ASP   B 2 131 ? 39.92607 -7.10202  3.77138   1.000 98.81135  ? 224 ASP   B CB  1 
ATOM   3466 C CG  . ASP   B 2 131 ? 39.40487 -6.21273  4.88256   1.000 107.07064 ? 224 ASP   B CG  1 
ATOM   3467 O OD1 . ASP   B 2 131 ? 38.44522 -5.45232  4.63372   1.000 107.28360 ? 224 ASP   B OD1 1 
ATOM   3468 O OD2 . ASP   B 2 131 ? 39.95452 -6.27299  6.00341   1.000 122.08877 ? 224 ASP   B OD2 1 
ATOM   3469 N N   . GLU   B 2 132 ? 39.79430 -8.81107  0.98768   1.000 84.10311  ? 225 GLU   B N   1 
ATOM   3470 C CA  . GLU   B 2 132 ? 40.45256 -9.29594  -0.22112  1.000 95.40993  ? 225 GLU   B CA  1 
ATOM   3471 C C   . GLU   B 2 132 ? 39.80033 -8.71683  -1.47042  1.000 83.64616  ? 225 GLU   B C   1 
ATOM   3472 O O   . GLU   B 2 132 ? 40.48668 -8.40010  -2.44901  1.000 86.87302  ? 225 GLU   B O   1 
ATOM   3473 C CB  . GLU   B 2 132 ? 40.42519 -10.82413 -0.26115  1.000 93.21235  ? 225 GLU   B CB  1 
ATOM   3474 C CG  . GLU   B 2 132 ? 41.45317 -11.49589 0.63604   1.000 104.15450 ? 225 GLU   B CG  1 
ATOM   3475 C CD  . GLU   B 2 132 ? 41.33137 -13.00906 0.62871   1.000 116.28134 ? 225 GLU   B CD  1 
ATOM   3476 O OE1 . GLU   B 2 132 ? 40.19062 -13.51495 0.67599   1.000 115.18980 ? 225 GLU   B OE1 1 
ATOM   3477 O OE2 . GLU   B 2 132 ? 42.37494 -13.69317 0.56740   1.000 117.81641 ? 225 GLU   B OE2 1 
ATOM   3478 N N   . ILE   B 2 133 ? 38.47433 -8.56766  -1.45384  1.000 82.12369  ? 226 ILE   B N   1 
ATOM   3479 C CA  . ILE   B 2 133 ? 37.77394 -8.01515  -2.60861  1.000 80.08557  ? 226 ILE   B CA  1 
ATOM   3480 C C   . ILE   B 2 133 ? 38.10893 -6.53917  -2.78113  1.000 82.80377  ? 226 ILE   B C   1 
ATOM   3481 O O   . ILE   B 2 133 ? 38.34127 -6.06962  -3.90144  1.000 76.75239  ? 226 ILE   B O   1 
ATOM   3482 C CB  . ILE   B 2 133 ? 36.25795 -8.24478  -2.46955  1.000 76.02161  ? 226 ILE   B CB  1 
ATOM   3483 C CG1 . ILE   B 2 133 ? 35.94187 -9.74179  -2.51048  1.000 81.27469  ? 226 ILE   B CG1 1 
ATOM   3484 C CG2 . ILE   B 2 133 ? 35.49857 -7.50303  -3.55613  1.000 70.66171  ? 226 ILE   B CG2 1 
ATOM   3485 C CD1 . ILE   B 2 133 ? 34.46451 -10.05652 -2.41698  1.000 86.83025  ? 226 ILE   B CD1 1 
ATOM   3486 N N   . LEU   B 2 134 ? 38.14898 -5.78587  -1.67739  1.000 83.16851  ? 227 LEU   B N   1 
ATOM   3487 C CA  . LEU   B 2 134 ? 38.48154 -4.36727  -1.76116  1.000 74.10032  ? 227 LEU   B CA  1 
ATOM   3488 C C   . LEU   B 2 134 ? 39.91903 -4.15103  -2.21524  1.000 76.56715  ? 227 LEU   B C   1 
ATOM   3489 O O   . LEU   B 2 134 ? 40.20400 -3.17989  -2.92497  1.000 81.88861  ? 227 LEU   B O   1 
ATOM   3490 C CB  . LEU   B 2 134 ? 38.24418 -3.68976  -0.41268  1.000 76.78248  ? 227 LEU   B CB  1 
ATOM   3491 C CG  . LEU   B 2 134 ? 36.82572 -3.79803  0.14702   1.000 85.00127  ? 227 LEU   B CG  1 
ATOM   3492 C CD1 . LEU   B 2 134 ? 36.66750 -2.93324  1.39026   1.000 86.50049  ? 227 LEU   B CD1 1 
ATOM   3493 C CD2 . LEU   B 2 134 ? 35.80001 -3.42628  -0.91216  1.000 72.79748  ? 227 LEU   B CD2 1 
ATOM   3494 N N   . THR   B 2 135 ? 40.83597 -5.03206  -1.81379  1.000 73.98445  ? 228 THR   B N   1 
ATOM   3495 C CA  . THR   B 2 135 ? 42.20128 -4.94816  -2.31942  1.000 80.85929  ? 228 THR   B CA  1 
ATOM   3496 C C   . THR   B 2 135 ? 42.25194 -5.28585  -3.80377  1.000 86.33397  ? 228 THR   B C   1 
ATOM   3497 O O   . THR   B 2 135 ? 43.00291 -4.66446  -4.56527  1.000 90.49272  ? 228 THR   B O   1 
ATOM   3498 C CB  . THR   B 2 135 ? 43.11458 -5.88135  -1.52187  1.000 85.76880  ? 228 THR   B CB  1 
ATOM   3499 O OG1 . THR   B 2 135 ? 43.05391 -5.53639  -0.13263  1.000 92.48561  ? 228 THR   B OG1 1 
ATOM   3500 C CG2 . THR   B 2 135 ? 44.55588 -5.76963  -2.00162  1.000 68.99164  ? 228 THR   B CG2 1 
ATOM   3501 N N   . MET   B 2 136 ? 41.44098 -6.25368  -4.23588  1.000 87.75822  ? 229 MET   B N   1 
ATOM   3502 C CA  . MET   B 2 136 ? 41.47215 -6.67909  -5.63045  1.000 71.38725  ? 229 MET   B CA  1 
ATOM   3503 C C   . MET   B 2 136 ? 40.80752 -5.65402  -6.54129  1.000 80.23915  ? 229 MET   B C   1 
ATOM   3504 O O   . MET   B 2 136 ? 41.27085 -5.42651  -7.66497  1.000 72.35514  ? 229 MET   B O   1 
ATOM   3505 C CB  . MET   B 2 136 ? 40.79996 -8.04382  -5.77399  1.000 83.36464  ? 229 MET   B CB  1 
ATOM   3506 C CG  . MET   B 2 136 ? 40.95685 -8.68823  -7.14506  1.000 83.28521  ? 229 MET   B CG  1 
ATOM   3507 S SD  . MET   B 2 136 ? 42.63888 -9.24533  -7.48280  1.000 99.73412  ? 229 MET   B SD  1 
ATOM   3508 C CE  . MET   B 2 136 ? 43.20988 -7.96073  -8.58906  1.000 69.56371  ? 229 MET   B CE  1 
ATOM   3509 N N   . GLU   B 2 137 ? 39.72235 -5.02305  -6.07883  1.000 70.99166  ? 230 GLU   B N   1 
ATOM   3510 C CA  . GLU   B 2 137 ? 39.03391 -4.04960  -6.92121  1.000 73.30904  ? 230 GLU   B CA  1 
ATOM   3511 C C   . GLU   B 2 137 ? 39.90862 -2.83483  -7.20247  1.000 75.74290  ? 230 GLU   B C   1 
ATOM   3512 O O   . GLU   B 2 137 ? 39.80848 -2.23941  -8.28090  1.000 68.72869  ? 230 GLU   B O   1 
ATOM   3513 C CB  . GLU   B 2 137 ? 37.71169 -3.61696  -6.28006  1.000 74.77925  ? 230 GLU   B CB  1 
ATOM   3514 C CG  . GLU   B 2 137 ? 37.85342 -2.72995  -5.04921  1.000 80.21482  ? 230 GLU   B CG  1 
ATOM   3515 C CD  . GLU   B 2 137 ? 36.66960 -1.79641  -4.85709  1.000 81.07663  ? 230 GLU   B CD  1 
ATOM   3516 O OE1 . GLU   B 2 137 ? 35.73679 -1.83355  -5.68783  1.000 78.83713  ? 230 GLU   B OE1 1 
ATOM   3517 O OE2 . GLU   B 2 137 ? 36.67449 -1.02020  -3.87790  1.000 81.31373  ? 230 GLU   B OE2 1 
ATOM   3518 N N   . LEU   B 2 138 ? 40.77357 -2.45833  -6.25744  1.000 73.00192  ? 231 LEU   B N   1 
ATOM   3519 C CA  . LEU   B 2 138 ? 41.67865 -1.33921  -6.49376  1.000 73.71150  ? 231 LEU   B CA  1 
ATOM   3520 C C   . LEU   B 2 138 ? 42.78694 -1.72410  -7.46451  1.000 74.74655  ? 231 LEU   B C   1 
ATOM   3521 O O   . LEU   B 2 138 ? 43.17254 -0.92282  -8.32320  1.000 74.44632  ? 231 LEU   B O   1 
ATOM   3522 C CB  . LEU   B 2 138 ? 42.26472 -0.84772  -5.17086  1.000 70.22806  ? 231 LEU   B CB  1 
ATOM   3523 C CG  . LEU   B 2 138 ? 41.39994 0.13648   -4.38221  1.000 80.99101  ? 231 LEU   B CG  1 
ATOM   3524 C CD1 . LEU   B 2 138 ? 41.96490 0.35327   -2.98958  1.000 78.41886  ? 231 LEU   B CD1 1 
ATOM   3525 C CD2 . LEU   B 2 138 ? 41.30054 1.45629   -5.13008  1.000 76.75603  ? 231 LEU   B CD2 1 
ATOM   3526 N N   . MET   B 2 139 ? 43.30973 -2.94643  -7.34741  1.000 79.06959  ? 232 MET   B N   1 
ATOM   3527 C CA  . MET   B 2 139 ? 44.33481 -3.39768  -8.28222  1.000 76.07319  ? 232 MET   B CA  1 
ATOM   3528 C C   . MET   B 2 139 ? 43.77862 -3.52836  -9.69446  1.000 70.39418  ? 232 MET   B C   1 
ATOM   3529 O O   . MET   B 2 139 ? 44.48192 -3.24432  -10.67090 1.000 70.70106  ? 232 MET   B O   1 
ATOM   3530 C CB  . MET   B 2 139 ? 44.92846 -4.72432  -7.81178  1.000 78.24262  ? 232 MET   B CB  1 
ATOM   3531 C CG  . MET   B 2 139 ? 45.78955 -4.60490  -6.56539  1.000 77.01971  ? 232 MET   B CG  1 
ATOM   3532 S SD  . MET   B 2 139 ? 46.54208 -6.17160  -6.09759  1.000 110.75431 ? 232 MET   B SD  1 
ATOM   3533 C CE  . MET   B 2 139 ? 45.09609 -7.10273  -5.60659  1.000 80.02071  ? 232 MET   B CE  1 
ATOM   3534 N N   . ILE   B 2 140 ? 42.51999 -3.95258  -9.82449  1.000 74.46288  ? 233 ILE   B N   1 
ATOM   3535 C CA  . ILE   B 2 140 ? 41.91174 -4.07442  -11.14638 1.000 65.61425  ? 233 ILE   B CA  1 
ATOM   3536 C C   . ILE   B 2 140 ? 41.72715 -2.69936  -11.77578 1.000 65.76294  ? 233 ILE   B C   1 
ATOM   3537 O O   . ILE   B 2 140 ? 42.11502 -2.46791  -12.92649 1.000 69.16937  ? 233 ILE   B O   1 
ATOM   3538 C CB  . ILE   B 2 140 ? 40.57771 -4.83826  -11.05939 1.000 70.72137  ? 233 ILE   B CB  1 
ATOM   3539 C CG1 . ILE   B 2 140 ? 40.82025 -6.30286  -10.69189 1.000 77.08195  ? 233 ILE   B CG1 1 
ATOM   3540 C CG2 . ILE   B 2 140 ? 39.81815 -4.74552  -12.37673 1.000 67.89529  ? 233 ILE   B CG2 1 
ATOM   3541 C CD1 . ILE   B 2 140 ? 39.55273 -7.12010  -10.57100 1.000 78.29526  ? 233 ILE   B CD1 1 
ATOM   3542 N N   . MET   B 2 141 ? 41.14155 -1.76287  -11.02707 1.000 72.84718  ? 234 MET   B N   1 
ATOM   3543 C CA  . MET   B 2 141 ? 40.85287 -0.44620  -11.58658 1.000 65.89437  ? 234 MET   B CA  1 
ATOM   3544 C C   . MET   B 2 141 ? 42.13268 0.31830   -11.90623 1.000 68.82573  ? 234 MET   B C   1 
ATOM   3545 O O   . MET   B 2 141 ? 42.19834 1.03215   -12.91437 1.000 67.42735  ? 234 MET   B O   1 
ATOM   3546 C CB  . MET   B 2 141 ? 39.96692 0.34640   -10.62428 1.000 65.79503  ? 234 MET   B CB  1 
ATOM   3547 C CG  . MET   B 2 141 ? 38.57709 -0.25400  -10.44768 1.000 71.00286  ? 234 MET   B CG  1 
ATOM   3548 S SD  . MET   B 2 141 ? 37.46453 0.73237   -9.42414  1.000 75.79206  ? 234 MET   B SD  1 
ATOM   3549 C CE  . MET   B 2 141 ? 38.30663 0.66612   -7.84692  1.000 67.71960  ? 234 MET   B CE  1 
ATOM   3550 N N   . LYS   B 2 142 ? 43.16373 0.17227   -11.07002 1.000 59.91569  ? 235 LYS   B N   1 
ATOM   3551 C CA  . LYS   B 2 142 ? 44.42548 0.86282   -11.32318 1.000 65.69439  ? 235 LYS   B CA  1 
ATOM   3552 C C   . LYS   B 2 142 ? 45.15581 0.26957   -12.52300 1.000 69.36246  ? 235 LYS   B C   1 
ATOM   3553 O O   . LYS   B 2 142 ? 45.75805 1.00549   -13.31383 1.000 75.79956  ? 235 LYS   B O   1 
ATOM   3554 C CB  . LYS   B 2 142 ? 45.30985 0.81598   -10.07615 1.000 71.80598  ? 235 LYS   B CB  1 
ATOM   3555 C CG  . LYS   B 2 142 ? 44.83599 1.71958   -8.94679  1.000 72.15841  ? 235 LYS   B CG  1 
ATOM   3556 C CD  . LYS   B 2 142 ? 45.51077 1.37257   -7.62506  1.000 75.61895  ? 235 LYS   B CD  1 
ATOM   3557 C CE  . LYS   B 2 142 ? 47.01947 1.53564   -7.70104  1.000 87.43702  ? 235 LYS   B CE  1 
ATOM   3558 N NZ  . LYS   B 2 142 ? 47.66774 1.26518   -6.38600  1.000 81.44590  ? 235 LYS   B NZ  1 
ATOM   3559 N N   . ALA   B 2 143 ? 45.11806 -1.05734  -12.67673 1.000 69.93882  ? 236 ALA   B N   1 
ATOM   3560 C CA  . ALA   B 2 143 ? 45.78264 -1.68275  -13.81676 1.000 75.16577  ? 236 ALA   B CA  1 
ATOM   3561 C C   . ALA   B 2 143 ? 45.07812 -1.35741  -15.12684 1.000 72.87262  ? 236 ALA   B C   1 
ATOM   3562 O O   . ALA   B 2 143 ? 45.73144 -1.24968  -16.17047 1.000 81.20991  ? 236 ALA   B O   1 
ATOM   3563 C CB  . ALA   B 2 143 ? 45.86135 -3.19673  -13.62265 1.000 69.63185  ? 236 ALA   B CB  1 
ATOM   3564 N N   . LEU   B 2 144 ? 43.75821 -1.19866  -15.09547 1.000 73.54164  ? 237 LEU   B N   1 
ATOM   3565 C CA  . LEU   B 2 144 ? 42.98807 -0.83516  -16.27651 1.000 71.07053  ? 237 LEU   B CA  1 
ATOM   3566 C C   . LEU   B 2 144 ? 43.00279 0.66194   -16.55551 1.000 72.84181  ? 237 LEU   B C   1 
ATOM   3567 O O   . LEU   B 2 144 ? 42.23054 1.12022   -17.40528 1.000 72.69133  ? 237 LEU   B O   1 
ATOM   3568 C CB  . LEU   B 2 144 ? 41.54246 -1.31641  -16.12836 1.000 63.54428  ? 237 LEU   B CB  1 
ATOM   3569 C CG  . LEU   B 2 144 ? 41.35023 -2.82971  -16.03287 1.000 70.67488  ? 237 LEU   B CG  1 
ATOM   3570 C CD1 . LEU   B 2 144 ? 39.87609 -3.17460  -15.89631 1.000 59.26999  ? 237 LEU   B CD1 1 
ATOM   3571 C CD2 . LEU   B 2 144 ? 41.96057 -3.51811  -17.24006 1.000 70.73939  ? 237 LEU   B CD2 1 
ATOM   3572 N N   . LYS   B 2 145 ? 43.85290 1.42343   -15.86071 1.000 70.86715  ? 238 LYS   B N   1 
ATOM   3573 C CA  . LYS   B 2 145 ? 43.92601 2.87870   -16.00605 1.000 67.41176  ? 238 LYS   B CA  1 
ATOM   3574 C C   . LYS   B 2 145 ? 42.56577 3.53868   -15.78858 1.000 68.99543  ? 238 LYS   B C   1 
ATOM   3575 O O   . LYS   B 2 145 ? 42.27560 4.58892   -16.36822 1.000 75.03645  ? 238 LYS   B O   1 
ATOM   3576 C CB  . LYS   B 2 145 ? 44.50059 3.27506   -17.37056 1.000 77.94125  ? 238 LYS   B CB  1 
ATOM   3577 C CG  . LYS   B 2 145 ? 45.93030 2.81237   -17.61294 1.000 80.75349  ? 238 LYS   B CG  1 
ATOM   3578 C CD  . LYS   B 2 145 ? 46.91394 3.56180   -16.73126 1.000 91.20574  ? 238 LYS   B CD  1 
ATOM   3579 C CE  . LYS   B 2 145 ? 48.34776 3.15920   -17.04381 1.000 105.31861 ? 238 LYS   B CE  1 
ATOM   3580 N NZ  . LYS   B 2 145 ? 49.33292 3.90219   -16.20822 1.000 101.38649 ? 238 LYS   B NZ  1 
ATOM   3581 N N   . TRP   B 2 146 ? 41.72462 2.91654   -14.95804 1.000 63.14054  ? 239 TRP   B N   1 
ATOM   3582 C CA  . TRP   B 2 146 ? 40.37651 3.40508   -14.65733 1.000 65.78705  ? 239 TRP   B CA  1 
ATOM   3583 C C   . TRP   B 2 146 ? 39.51720 3.53281   -15.91524 1.000 70.78841  ? 239 TRP   B C   1 
ATOM   3584 O O   . TRP   B 2 146 ? 38.57313 4.32576   -15.95899 1.000 62.08359  ? 239 TRP   B O   1 
ATOM   3585 C CB  . TRP   B 2 146 ? 40.42296 4.73338   -13.89336 1.000 62.34841  ? 239 TRP   B CB  1 
ATOM   3586 C CG  . TRP   B 2 146 ? 41.15076 4.63700   -12.57944 1.000 61.29134  ? 239 TRP   B CG  1 
ATOM   3587 C CD1 . TRP   B 2 146 ? 42.49013 4.79642   -12.37153 1.000 58.91290  ? 239 TRP   B CD1 1 
ATOM   3588 C CD2 . TRP   B 2 146 ? 40.57742 4.35308   -11.29521 1.000 68.29041  ? 239 TRP   B CD2 1 
ATOM   3589 N NE1 . TRP   B 2 146 ? 42.78680 4.63029   -11.04022 1.000 60.29574  ? 239 TRP   B NE1 1 
ATOM   3590 C CE2 . TRP   B 2 146 ? 41.63060 4.35776   -10.35770 1.000 61.16758  ? 239 TRP   B CE2 1 
ATOM   3591 C CE3 . TRP   B 2 146 ? 39.27686 4.09737   -10.84761 1.000 54.64324  ? 239 TRP   B CE3 1 
ATOM   3592 C CZ2 . TRP   B 2 146 ? 41.42427 4.11598   -9.00007  1.000 62.04737  ? 239 TRP   B CZ2 1 
ATOM   3593 C CZ3 . TRP   B 2 146 ? 39.07425 3.85788   -9.49981  1.000 63.79484  ? 239 TRP   B CZ3 1 
ATOM   3594 C CH2 . TRP   B 2 146 ? 40.14277 3.86831   -8.59193  1.000 67.08663  ? 239 TRP   B CH2 1 
ATOM   3595 N N   . ARG   B 2 147 ? 39.83357 2.74936   -16.94839 1.000 66.99309  ? 240 ARG   B N   1 
ATOM   3596 C CA  . ARG   B 2 147 ? 39.00686 2.67493   -18.15308 1.000 68.13427  ? 240 ARG   B CA  1 
ATOM   3597 C C   . ARG   B 2 147 ? 37.92567 1.62649   -17.91230 1.000 57.77396  ? 240 ARG   B C   1 
ATOM   3598 O O   . ARG   B 2 147 ? 38.04799 0.45619   -18.27861 1.000 65.27978  ? 240 ARG   B O   1 
ATOM   3599 C CB  . ARG   B 2 147 ? 39.85550 2.34496   -19.37531 1.000 72.07734  ? 240 ARG   B CB  1 
ATOM   3600 C CG  . ARG   B 2 147 ? 40.75721 3.47537   -19.84455 1.000 71.16367  ? 240 ARG   B CG  1 
ATOM   3601 C CD  . ARG   B 2 147 ? 39.95231 4.72065   -20.18706 1.000 86.76534  ? 240 ARG   B CD  1 
ATOM   3602 N NE  . ARG   B 2 147 ? 40.72129 5.66926   -20.98428 1.000 99.12838  ? 240 ARG   B NE  1 
ATOM   3603 C CZ  . ARG   B 2 147 ? 41.60466 6.52437   -20.48723 1.000 102.60304 ? 240 ARG   B CZ  1 
ATOM   3604 N NH1 . ARG   B 2 147 ? 41.86978 6.56956   -19.19204 1.000 99.65618  ? 240 ARG   B NH1 1 
ATOM   3605 N NH2 . ARG   B 2 147 ? 42.24112 7.35244   -21.31101 1.000 101.29033 ? 240 ARG   B NH2 1 
ATOM   3606 N N   . LEU   B 2 148 ? 36.83969 2.06569   -17.27590 1.000 63.21373  ? 241 LEU   B N   1 
ATOM   3607 C CA  . LEU   B 2 148 ? 35.78946 1.15883   -16.82852 1.000 61.37347  ? 241 LEU   B CA  1 
ATOM   3608 C C   . LEU   B 2 148 ? 34.45940 1.41272   -17.52801 1.000 65.74208  ? 241 LEU   B C   1 
ATOM   3609 O O   . LEU   B 2 148 ? 33.41061 1.01598   -17.01129 1.000 62.90368  ? 241 LEU   B O   1 
ATOM   3610 C CB  . LEU   B 2 148 ? 35.61516 1.25913   -15.31225 1.000 63.84259  ? 241 LEU   B CB  1 
ATOM   3611 C CG  . LEU   B 2 148 ? 36.88294 1.06291   -14.47789 1.000 65.90898  ? 241 LEU   B CG  1 
ATOM   3612 C CD1 . LEU   B 2 148 ? 36.58312 1.27209   -13.00803 1.000 57.25710  ? 241 LEU   B CD1 1 
ATOM   3613 C CD2 . LEU   B 2 148 ? 37.48236 -0.31462  -14.70796 1.000 61.24848  ? 241 LEU   B CD2 1 
ATOM   3614 N N   . SER   B 2 149 ? 34.47372 2.04551   -18.70004 1.000 61.94947  ? 242 SER   B N   1 
ATOM   3615 C CA  . SER   B 2 149 ? 33.25191 2.36182   -19.44119 1.000 58.43034  ? 242 SER   B CA  1 
ATOM   3616 C C   . SER   B 2 149 ? 33.33070 1.81003   -20.86111 1.000 65.64870  ? 242 SER   B C   1 
ATOM   3617 O O   . SER   B 2 149 ? 33.33235 2.57175   -21.83491 1.000 70.23532  ? 242 SER   B O   1 
ATOM   3618 C CB  . SER   B 2 149 ? 33.01071 3.87197   -19.46313 1.000 65.88179  ? 242 SER   B CB  1 
ATOM   3619 O OG  . SER   B 2 149 ? 32.95831 4.40381   -18.15005 1.000 80.73973  ? 242 SER   B OG  1 
ATOM   3620 N N   . PRO   B 2 150 ? 33.37613 0.48996   -21.01926 1.000 72.18533  ? 243 PRO   B N   1 
ATOM   3621 C CA  . PRO   B 2 150 ? 33.43163 -0.09723  -22.35747 1.000 57.33080  ? 243 PRO   B CA  1 
ATOM   3622 C C   . PRO   B 2 150 ? 32.03378 -0.33629  -22.91836 1.000 72.69399  ? 243 PRO   B C   1 
ATOM   3623 O O   . PRO   B 2 150 ? 31.02485 -0.23616  -22.21805 1.000 73.91393  ? 243 PRO   B O   1 
ATOM   3624 C CB  . PRO   B 2 150 ? 34.14985 -1.42605  -22.10817 1.000 67.44625  ? 243 PRO   B CB  1 
ATOM   3625 C CG  . PRO   B 2 150 ? 33.63913 -1.83351  -20.76720 1.000 55.71329  ? 243 PRO   B CG  1 
ATOM   3626 C CD  . PRO   B 2 150 ? 33.42158 -0.55526  -19.97948 1.000 65.27798  ? 243 PRO   B CD  1 
ATOM   3627 N N   . LEU   B 2 151 ? 31.99776 -0.65835  -24.20912 1.000 66.83018  ? 244 LEU   B N   1 
ATOM   3628 C CA  . LEU   B 2 151 ? 30.77284 -1.07641  -24.88666 1.000 70.72392  ? 244 LEU   B CA  1 
ATOM   3629 C C   . LEU   B 2 151 ? 30.75558 -2.60050  -24.88632 1.000 71.08383  ? 244 LEU   B C   1 
ATOM   3630 O O   . LEU   B 2 151 ? 31.47149 -3.24264  -25.65873 1.000 78.02959  ? 244 LEU   B O   1 
ATOM   3631 C CB  . LEU   B 2 151 ? 30.70286 -0.50895  -26.30030 1.000 56.17676  ? 244 LEU   B CB  1 
ATOM   3632 C CG  . LEU   B 2 151 ? 30.70243 1.01840   -26.39092 1.000 69.20559  ? 244 LEU   B CG  1 
ATOM   3633 C CD1 . LEU   B 2 151 ? 30.57047 1.47541   -27.83456 1.000 64.23038  ? 244 LEU   B CD1 1 
ATOM   3634 C CD2 . LEU   B 2 151 ? 29.59697 1.61273   -25.52828 1.000 61.86482  ? 244 LEU   B CD2 1 
ATOM   3635 N N   . THR   B 2 152 ? 29.93473 -3.17551  -24.01355 1.000 61.21950  ? 245 THR   B N   1 
ATOM   3636 C CA  . THR   B 2 152 ? 29.90403 -4.61629  -23.83473 1.000 67.91130  ? 245 THR   B CA  1 
ATOM   3637 C C   . THR   B 2 152 ? 29.27961 -5.30297  -25.04803 1.000 66.46747  ? 245 THR   B C   1 
ATOM   3638 O O   . THR   B 2 152 ? 28.71725 -4.66775  -25.94585 1.000 64.37387  ? 245 THR   B O   1 
ATOM   3639 C CB  . THR   B 2 152 ? 29.12160 -4.97916  -22.57559 1.000 64.18742  ? 245 THR   B CB  1 
ATOM   3640 O OG1 . THR   B 2 152 ? 27.77978 -4.49103  -22.69668 1.000 64.63387  ? 245 THR   B OG1 1 
ATOM   3641 C CG2 . THR   B 2 152 ? 29.77215 -4.36162  -21.34906 1.000 61.51487  ? 245 THR   B CG2 1 
ATOM   3642 N N   . ILE   B 2 153 ? 29.38678 -6.63310  -25.05990 1.000 59.08622  ? 246 ILE   B N   1 
ATOM   3643 C CA  . ILE   B 2 153 ? 28.76193 -7.42295  -26.11590 1.000 61.84056  ? 246 ILE   B CA  1 
ATOM   3644 C C   . ILE   B 2 153 ? 27.24710 -7.27436  -26.06351 1.000 63.34645  ? 246 ILE   B C   1 
ATOM   3645 O O   . ILE   B 2 153 ? 26.57827 -7.19741  -27.10136 1.000 67.52122  ? 246 ILE   B O   1 
ATOM   3646 C CB  . ILE   B 2 153 ? 29.19066 -8.89773  -26.00017 1.000 61.32322  ? 246 ILE   B CB  1 
ATOM   3647 C CG1 . ILE   B 2 153 ? 30.71507 -9.01235  -26.01278 1.000 62.98010  ? 246 ILE   B CG1 1 
ATOM   3648 C CG2 . ILE   B 2 153 ? 28.58761 -9.72378  -27.12341 1.000 62.79164  ? 246 ILE   B CG2 1 
ATOM   3649 C CD1 . ILE   B 2 153 ? 31.21921 -10.43123 -25.88740 1.000 67.94786  ? 246 ILE   B CD1 1 
ATOM   3650 N N   . VAL   B 2 154 ? 26.68245 -7.22099  -24.85646 1.000 60.11855  ? 247 VAL   B N   1 
ATOM   3651 C CA  . VAL   B 2 154 ? 25.23163 -7.14839  -24.73031 1.000 58.28654  ? 247 VAL   B CA  1 
ATOM   3652 C C   . VAL   B 2 154 ? 24.72283 -5.74196  -25.02864 1.000 52.74296  ? 247 VAL   B C   1 
ATOM   3653 O O   . VAL   B 2 154 ? 23.57902 -5.57412  -25.46944 1.000 66.14592  ? 247 VAL   B O   1 
ATOM   3654 C CB  . VAL   B 2 154 ? 24.79378 -7.62871  -23.33446 1.000 62.45007  ? 247 VAL   B CB  1 
ATOM   3655 C CG1 . VAL   B 2 154 ? 25.26235 -6.66079  -22.25508 1.000 63.18588  ? 247 VAL   B CG1 1 
ATOM   3656 C CG2 . VAL   B 2 154 ? 23.28279 -7.82346  -23.28073 1.000 62.61888  ? 247 VAL   B CG2 1 
ATOM   3657 N N   . SER   B 2 155 ? 25.55021 -4.71581  -24.81349 1.000 52.83491  ? 248 SER   B N   1 
ATOM   3658 C CA  . SER   B 2 155 ? 25.12272 -3.35536  -25.12356 1.000 59.23439  ? 248 SER   B CA  1 
ATOM   3659 C C   . SER   B 2 155 ? 24.92021 -3.17084  -26.62181 1.000 60.80890  ? 248 SER   B C   1 
ATOM   3660 O O   . SER   B 2 155 ? 23.98920 -2.47673  -27.04559 1.000 62.21703  ? 248 SER   B O   1 
ATOM   3661 C CB  . SER   B 2 155 ? 26.13742 -2.34541  -24.58943 1.000 59.53337  ? 248 SER   B CB  1 
ATOM   3662 O OG  . SER   B 2 155 ? 27.35786 -2.41997  -25.30284 1.000 65.69480  ? 248 SER   B OG  1 
ATOM   3663 N N   . TRP   B 2 156 ? 25.77627 -3.78817  -27.44046 1.000 60.95393  ? 249 TRP   B N   1 
ATOM   3664 C CA  . TRP   B 2 156 ? 25.59010 -3.70987  -28.88595 1.000 61.43417  ? 249 TRP   B CA  1 
ATOM   3665 C C   . TRP   B 2 156 ? 24.29072 -4.38138  -29.30989 1.000 60.31150  ? 249 TRP   B C   1 
ATOM   3666 O O   . TRP   B 2 156 ? 23.58768 -3.88318  -30.19667 1.000 62.33689  ? 249 TRP   B O   1 
ATOM   3667 C CB  . TRP   B 2 156 ? 26.77950 -4.33785  -29.61330 1.000 60.64523  ? 249 TRP   B CB  1 
ATOM   3668 C CG  . TRP   B 2 156 ? 28.00189 -3.47301  -29.63552 1.000 62.83675  ? 249 TRP   B CG  1 
ATOM   3669 C CD1 . TRP   B 2 156 ? 29.16059 -3.67365  -28.94532 1.000 60.72004  ? 249 TRP   B CD1 1 
ATOM   3670 C CD2 . TRP   B 2 156 ? 28.18578 -2.26649  -30.38616 1.000 58.31850  ? 249 TRP   B CD2 1 
ATOM   3671 N NE1 . TRP   B 2 156 ? 30.05578 -2.66821  -29.21969 1.000 63.17226  ? 249 TRP   B NE1 1 
ATOM   3672 C CE2 . TRP   B 2 156 ? 29.48121 -1.79096  -30.10106 1.000 61.53948  ? 249 TRP   B CE2 1 
ATOM   3673 C CE3 . TRP   B 2 156 ? 27.38115 -1.54271  -31.27135 1.000 66.16812  ? 249 TRP   B CE3 1 
ATOM   3674 C CZ2 . TRP   B 2 156 ? 29.99068 -0.62524  -30.66891 1.000 67.41111  ? 249 TRP   B CZ2 1 
ATOM   3675 C CZ3 . TRP   B 2 156 ? 27.88892 -0.38480  -31.83450 1.000 69.60552  ? 249 TRP   B CZ3 1 
ATOM   3676 C CH2 . TRP   B 2 156 ? 29.18143 0.06174   -31.53140 1.000 71.59542  ? 249 TRP   B CH2 1 
ATOM   3677 N N   . LEU   B 2 157 ? 23.95210 -5.51307  -28.68565 1.000 62.44564  ? 250 LEU   B N   1 
ATOM   3678 C CA  . LEU   B 2 157 ? 22.69669 -6.18263  -29.01047 1.000 62.13783  ? 250 LEU   B CA  1 
ATOM   3679 C C   . LEU   B 2 157 ? 21.49585 -5.30515  -28.68288 1.000 63.47331  ? 250 LEU   B C   1 
ATOM   3680 O O   . LEU   B 2 157 ? 20.48800 -5.34081  -29.39761 1.000 61.99173  ? 250 LEU   B O   1 
ATOM   3681 C CB  . LEU   B 2 157 ? 22.60165 -7.51628  -28.26754 1.000 61.73444  ? 250 LEU   B CB  1 
ATOM   3682 C CG  . LEU   B 2 157 ? 21.32928 -8.32474  -28.51994 1.000 61.89404  ? 250 LEU   B CG  1 
ATOM   3683 C CD1 . LEU   B 2 157 ? 21.15830 -8.59469  -30.00871 1.000 58.72309  ? 250 LEU   B CD1 1 
ATOM   3684 C CD2 . LEU   B 2 157 ? 21.34792 -9.62285  -27.73063 1.000 70.72963  ? 250 LEU   B CD2 1 
ATOM   3685 N N   . ASN   B 2 158 ? 21.58440 -4.50813  -27.61514 1.000 64.30276  ? 251 ASN   B N   1 
ATOM   3686 C CA  . ASN   B 2 158 ? 20.49786 -3.58977  -27.29308 1.000 69.34455  ? 251 ASN   B CA  1 
ATOM   3687 C C   . ASN   B 2 158 ? 20.33937 -2.52661  -28.37335 1.000 71.96847  ? 251 ASN   B C   1 
ATOM   3688 O O   . ASN   B 2 158 ? 19.21368 -2.15343  -28.72459 1.000 73.02792  ? 251 ASN   B O   1 
ATOM   3689 C CB  . ASN   B 2 158 ? 20.74261 -2.94432  -25.93043 1.000 65.89401  ? 251 ASN   B CB  1 
ATOM   3690 C CG  . ASN   B 2 158 ? 19.54373 -3.05644  -25.01183 1.000 82.03860  ? 251 ASN   B CG  1 
ATOM   3691 O OD1 . ASN   B 2 158 ? 19.45059 -3.98223  -24.20537 1.000 95.08786  ? 251 ASN   B OD1 1 
ATOM   3692 N ND2 . ASN   B 2 158 ? 18.61514 -2.11465  -25.13150 1.000 75.55231  ? 251 ASN   B ND2 1 
ATOM   3693 N N   . VAL   B 2 159 ? 21.45450 -2.03305  -28.91605 1.000 73.51831  ? 252 VAL   B N   1 
ATOM   3694 C CA  . VAL   B 2 159 ? 21.38664 -1.07468  -30.01578 1.000 61.20815  ? 252 VAL   B CA  1 
ATOM   3695 C C   . VAL   B 2 159 ? 20.77905 -1.72804  -31.24991 1.000 72.18627  ? 252 VAL   B C   1 
ATOM   3696 O O   . VAL   B 2 159 ? 19.89469 -1.16217  -31.90300 1.000 75.45037  ? 252 VAL   B O   1 
ATOM   3697 C CB  . VAL   B 2 159 ? 22.78321 -0.50040  -30.31764 1.000 65.52474  ? 252 VAL   B CB  1 
ATOM   3698 C CG1 . VAL   B 2 159 ? 22.68797 0.60837   -31.35375 1.000 80.84132  ? 252 VAL   B CG1 1 
ATOM   3699 C CG2 . VAL   B 2 159 ? 23.44436 0.00589   -29.04953 1.000 61.06716  ? 252 VAL   B CG2 1 
ATOM   3700 N N   . TYR   B 2 160 ? 21.24115 -2.93531  -31.58203 1.000 67.73362  ? 253 TYR   B N   1 
ATOM   3701 C CA  . TYR   B 2 160 ? 20.77217 -3.60414  -32.78980 1.000 64.22106  ? 253 TYR   B CA  1 
ATOM   3702 C C   . TYR   B 2 160 ? 19.29065 -3.94498  -32.70468 1.000 75.39207  ? 253 TYR   B C   1 
ATOM   3703 O O   . TYR   B 2 160 ? 18.59631 -3.95298  -33.72767 1.000 70.68945  ? 253 TYR   B O   1 
ATOM   3704 C CB  . TYR   B 2 160 ? 21.59199 -4.87104  -33.04182 1.000 70.13500  ? 253 TYR   B CB  1 
ATOM   3705 C CG  . TYR   B 2 160 ? 23.07941 -4.64042  -33.21954 1.000 65.25318  ? 253 TYR   B CG  1 
ATOM   3706 C CD1 . TYR   B 2 160 ? 23.58234 -3.38071  -33.52208 1.000 62.58107  ? 253 TYR   B CD1 1 
ATOM   3707 C CD2 . TYR   B 2 160 ? 23.97996 -5.68939  -33.09083 1.000 60.80097  ? 253 TYR   B CD2 1 
ATOM   3708 C CE1 . TYR   B 2 160 ? 24.94138 -3.17310  -33.68430 1.000 72.92714  ? 253 TYR   B CE1 1 
ATOM   3709 C CE2 . TYR   B 2 160 ? 25.33699 -5.49219  -33.25217 1.000 56.62773  ? 253 TYR   B CE2 1 
ATOM   3710 C CZ  . TYR   B 2 160 ? 25.81346 -4.23361  -33.54875 1.000 67.48089  ? 253 TYR   B CZ  1 
ATOM   3711 O OH  . TYR   B 2 160 ? 27.16677 -4.03784  -33.71064 1.000 67.93252  ? 253 TYR   B OH  1 
ATOM   3712 N N   . MET   B 2 161 ? 18.78800 -4.22617  -31.50100 1.000 73.31529  ? 254 MET   B N   1 
ATOM   3713 C CA  . MET   B 2 161 ? 17.37918 -4.57265  -31.35196 1.000 76.58678  ? 254 MET   B CA  1 
ATOM   3714 C C   . MET   B 2 161 ? 16.48244 -3.34771  -31.47807 1.000 82.25182  ? 254 MET   B C   1 
ATOM   3715 O O   . MET   B 2 161 ? 15.38139 -3.43663  -32.03338 1.000 82.12414  ? 254 MET   B O   1 
ATOM   3716 C CB  . MET   B 2 161 ? 17.15005 -5.27187  -30.01295 1.000 68.20818  ? 254 MET   B CB  1 
ATOM   3717 C CG  . MET   B 2 161 ? 17.63012 -6.71233  -29.98831 1.000 58.11320  ? 254 MET   B CG  1 
ATOM   3718 S SD  . MET   B 2 161 ? 16.81726 -7.70807  -31.24992 1.000 77.00129  ? 254 MET   B SD  1 
ATOM   3719 C CE  . MET   B 2 161 ? 15.09892 -7.46793  -30.80448 1.000 79.35896  ? 254 MET   B CE  1 
ATOM   3720 N N   . GLN   B 2 162 ? 16.93557 -2.19796  -30.97567 1.000 75.32913  ? 255 GLN   B N   1 
ATOM   3721 C CA  . GLN   B 2 162 ? 16.14100 -0.98115  -31.10144 1.000 80.29938  ? 255 GLN   B CA  1 
ATOM   3722 C C   . GLN   B 2 162 ? 16.04255 -0.53199  -32.55403 1.000 91.81503  ? 255 GLN   B C   1 
ATOM   3723 O O   . GLN   B 2 162 ? 14.96973 -0.11916  -33.01072 1.000 87.36633  ? 255 GLN   B O   1 
ATOM   3724 C CB  . GLN   B 2 162 ? 16.73779 0.12855   -30.23854 1.000 79.50817  ? 255 GLN   B CB  1 
ATOM   3725 C CG  . GLN   B 2 162 ? 15.91787 1.40590   -30.22556 1.000 84.01157  ? 255 GLN   B CG  1 
ATOM   3726 C CD  . GLN   B 2 162 ? 14.54503 1.20832   -29.61545 1.000 84.98346  ? 255 GLN   B CD  1 
ATOM   3727 O OE1 . GLN   B 2 162 ? 14.34216 0.31746   -28.79057 1.000 82.20710  ? 255 GLN   B OE1 1 
ATOM   3728 N NE2 . GLN   B 2 162 ? 13.59113 2.03703   -30.02341 1.000 96.64328  ? 255 GLN   B NE2 1 
ATOM   3729 N N   . VAL   B 2 163 ? 17.14980 -0.60684  -33.29613 1.000 78.79115  ? 256 VAL   B N   1 
ATOM   3730 C CA  . VAL   B 2 163 ? 17.12932 -0.18405  -34.69229 1.000 92.08387  ? 256 VAL   B CA  1 
ATOM   3731 C C   . VAL   B 2 163 ? 16.29864 -1.14301  -35.53621 1.000 85.25108  ? 256 VAL   B C   1 
ATOM   3732 O O   . VAL   B 2 163 ? 15.63833 -0.72353  -36.49495 1.000 86.89045  ? 256 VAL   B O   1 
ATOM   3733 C CB  . VAL   B 2 163 ? 18.56667 -0.04846  -35.22869 1.000 82.15874  ? 256 VAL   B CB  1 
ATOM   3734 C CG1 . VAL   B 2 163 ? 18.55815 0.45583   -36.66379 1.000 84.13040  ? 256 VAL   B CG1 1 
ATOM   3735 C CG2 . VAL   B 2 163 ? 19.37287 0.88579   -34.33980 1.000 75.90491  ? 256 VAL   B CG2 1 
ATOM   3736 N N   . ALA   B 2 164 ? 16.30148 -2.43452  -35.19383 1.000 78.65076  ? 257 ALA   B N   1 
ATOM   3737 C CA  . ALA   B 2 164 ? 15.49873 -3.39836  -35.93985 1.000 90.68463  ? 257 ALA   B CA  1 
ATOM   3738 C C   . ALA   B 2 164 ? 14.01074 -3.10373  -35.81775 1.000 99.59079  ? 257 ALA   B C   1 
ATOM   3739 O O   . ALA   B 2 164 ? 13.25246 -3.32808  -36.76930 1.000 92.04162  ? 257 ALA   B O   1 
ATOM   3740 C CB  . ALA   B 2 164 ? 15.80132 -4.81846  -35.46070 1.000 79.72046  ? 257 ALA   B CB  1 
ATOM   3741 N N   . TYR   B 2 165 ? 13.57638 -2.60027  -34.66552 1.000 91.84758  ? 258 TYR   B N   1 
ATOM   3742 C CA  . TYR   B 2 165 ? 12.18087 -2.25627  -34.42383 1.000 90.86098  ? 258 TYR   B CA  1 
ATOM   3743 C C   . TYR   B 2 165 ? 11.99612 -0.74691  -34.30457 1.000 100.17318 ? 258 TYR   B C   1 
ATOM   3744 O O   . TYR   B 2 165 ? 11.25401 -0.25675  -33.45186 1.000 114.03735 ? 258 TYR   B O   1 
ATOM   3745 C CB  . TYR   B 2 165 ? 11.65732 -2.97449  -33.18345 1.000 89.50636  ? 258 TYR   B CB  1 
ATOM   3746 C CG  . TYR   B 2 165 ? 11.37906 -4.44037  -33.42849 1.000 98.18752  ? 258 TYR   B CG  1 
ATOM   3747 C CD1 . TYR   B 2 165 ? 12.39842 -5.38226  -33.36504 1.000 91.33905  ? 258 TYR   B CD1 1 
ATOM   3748 C CD2 . TYR   B 2 165 ? 10.09874 -4.88042  -33.74052 1.000 98.11848  ? 258 TYR   B CD2 1 
ATOM   3749 C CE1 . TYR   B 2 165 ? 12.14851 -6.72342  -33.59966 1.000 96.34076  ? 258 TYR   B CE1 1 
ATOM   3750 C CE2 . TYR   B 2 165 ? 9.83879  -6.21836  -33.97330 1.000 97.78484  ? 258 TYR   B CE2 1 
ATOM   3751 C CZ  . TYR   B 2 165 ? 10.86636 -7.13529  -33.90189 1.000 87.57715  ? 258 TYR   B CZ  1 
ATOM   3752 O OH  . TYR   B 2 165 ? 10.60915 -8.46759  -34.13282 1.000 101.42130 ? 258 TYR   B OH  1 
ATOM   3753 N N   . LEU   B 2 166 ? 12.67958 0.00428   -35.16342 1.000 97.24535  ? 259 LEU   B N   1 
ATOM   3754 C CA  . LEU   B 2 166 ? 12.48117 1.44347   -35.23868 1.000 105.61716 ? 259 LEU   B CA  1 
ATOM   3755 C C   . LEU   B 2 166 ? 11.22823 1.74862   -36.04550 1.000 114.94744 ? 259 LEU   B C   1 
ATOM   3756 O O   . LEU   B 2 166 ? 11.07952 1.28268   -37.17973 1.000 104.01028 ? 259 LEU   B O   1 
ATOM   3757 C CB  . LEU   B 2 166 ? 13.69151 2.12421   -35.87486 1.000 102.77407 ? 259 LEU   B CB  1 
ATOM   3758 C CG  . LEU   B 2 166 ? 14.80879 2.58142   -34.93917 1.000 100.12714 ? 259 LEU   B CG  1 
ATOM   3759 C CD1 . LEU   B 2 166 ? 15.96176 3.14389   -35.75032 1.000 101.62152 ? 259 LEU   B CD1 1 
ATOM   3760 C CD2 . LEU   B 2 166 ? 14.29382 3.60978   -33.94289 1.000 98.31058  ? 259 LEU   B CD2 1 
ATOM   3761 N N   . ASN   B 2 167 ? 10.32646 2.52703   -35.45668 1.000 134.22376 ? 260 ASN   B N   1 
ATOM   3762 C CA  . ASN   B 2 167 ? 9.13950  2.95898   -36.17143 1.000 157.38583 ? 260 ASN   B CA  1 
ATOM   3763 C C   . ASN   B 2 167 ? 9.50675  4.03608   -37.19047 1.000 174.43406 ? 260 ASN   B C   1 
ATOM   3764 O O   . ASN   B 2 167 ? 10.65019 4.49589   -37.26900 1.000 167.66730 ? 260 ASN   B O   1 
ATOM   3765 C CB  . ASN   B 2 167 ? 8.08900  3.48340   -35.19334 1.000 159.14681 ? 260 ASN   B CB  1 
ATOM   3766 C CG  . ASN   B 2 167 ? 7.91624  2.58227   -33.98565 1.000 150.01832 ? 260 ASN   B CG  1 
ATOM   3767 O OD1 . ASN   B 2 167 ? 7.16571  1.60747   -34.02571 1.000 142.00789 ? 260 ASN   B OD1 1 
ATOM   3768 N ND2 . ASN   B 2 167 ? 8.61232  2.90626   -32.90118 1.000 144.08837 ? 260 ASN   B ND2 1 
ATOM   3769 N N   . ASP   B 2 168 ? 8.51386  4.43728   -37.98821 1.000 222.54607 ? 261 ASP   B N   1 
ATOM   3770 C CA  . ASP   B 2 168 ? 8.72871  5.54274   -38.91573 1.000 231.75916 ? 261 ASP   B CA  1 
ATOM   3771 C C   . ASP   B 2 168 ? 9.03928  6.83485   -38.17190 1.000 222.13284 ? 261 ASP   B C   1 
ATOM   3772 O O   . ASP   B 2 168 ? 9.76772  7.68991   -38.68891 1.000 205.34183 ? 261 ASP   B O   1 
ATOM   3773 C CB  . ASP   B 2 168 ? 7.50986  5.71662   -39.82264 1.000 240.22168 ? 261 ASP   B CB  1 
ATOM   3774 C CG  . ASP   B 2 168 ? 6.20051  5.58731   -39.07178 1.000 238.81279 ? 261 ASP   B CG  1 
ATOM   3775 O OD1 . ASP   B 2 168 ? 6.23687  5.34193   -37.84827 1.000 238.35479 ? 261 ASP   B OD1 1 
ATOM   3776 O OD2 . ASP   B 2 168 ? 5.13409  5.72634   -39.70687 1.000 241.37509 ? 261 ASP   B OD2 1 
ATOM   3777 N N   . LEU   B 2 169 ? 8.50331  6.99264   -36.96327 1.000 188.80873 ? 262 LEU   B N   1 
ATOM   3778 C CA  . LEU   B 2 169 ? 8.89208  8.08418   -36.07321 1.000 171.85610 ? 262 LEU   B CA  1 
ATOM   3779 C C   . LEU   B 2 169 ? 10.16005 7.65793   -35.34308 1.000 165.67971 ? 262 LEU   B C   1 
ATOM   3780 O O   . LEU   B 2 169 ? 10.11841 6.84288   -34.41860 1.000 164.01831 ? 262 LEU   B O   1 
ATOM   3781 C CB  . LEU   B 2 169 ? 7.76578  8.42228   -35.10161 1.000 158.81111 ? 262 LEU   B CB  1 
ATOM   3782 C CG  . LEU   B 2 169 ? 6.95928  7.27204   -34.49153 1.000 149.72960 ? 262 LEU   B CG  1 
ATOM   3783 C CD1 . LEU   B 2 169 ? 6.72268  7.51107   -33.00911 1.000 124.98732 ? 262 LEU   B CD1 1 
ATOM   3784 C CD2 . LEU   B 2 169 ? 5.63381  7.10320   -35.21746 1.000 150.46696 ? 262 LEU   B CD2 1 
ATOM   3785 N N   . HIS   B 2 170 ? 11.29632 8.20784   -35.76242 1.000 164.12413 ? 263 HIS   B N   1 
ATOM   3786 C CA  . HIS   B 2 170 ? 12.60150 7.77851   -35.26347 1.000 155.93952 ? 263 HIS   B CA  1 
ATOM   3787 C C   . HIS   B 2 170 ? 12.81068 8.30332   -33.84835 1.000 158.06328 ? 263 HIS   B C   1 
ATOM   3788 O O   . HIS   B 2 170 ? 13.11663 9.48008   -33.64483 1.000 158.92505 ? 263 HIS   B O   1 
ATOM   3789 C CB  . HIS   B 2 170 ? 13.70684 8.25815   -36.19798 1.000 145.96602 ? 263 HIS   B CB  1 
ATOM   3790 C CG  . HIS   B 2 170 ? 13.66150 7.63408   -37.55856 1.000 148.16535 ? 263 HIS   B CG  1 
ATOM   3791 N ND1 . HIS   B 2 170 ? 13.00156 6.45112   -37.81313 1.000 152.64630 ? 263 HIS   B ND1 1 
ATOM   3792 C CD2 . HIS   B 2 170 ? 14.19171 8.03040   -38.74005 1.000 136.45067 ? 263 HIS   B CD2 1 
ATOM   3793 C CE1 . HIS   B 2 170 ? 13.12854 6.14457   -39.09190 1.000 148.75080 ? 263 HIS   B CE1 1 
ATOM   3794 N NE2 . HIS   B 2 170 ? 13.84615 7.08668   -39.67681 1.000 137.63701 ? 263 HIS   B NE2 1 
ATOM   3795 N N   . GLU   B 2 171 ? 12.64441 7.42366   -32.86132 1.000 159.81303 ? 264 GLU   B N   1 
ATOM   3796 C CA  . GLU   B 2 171 ? 12.96253 7.71475   -31.46333 1.000 152.25427 ? 264 GLU   B CA  1 
ATOM   3797 C C   . GLU   B 2 171 ? 13.77621 6.53588   -30.93838 1.000 141.33921 ? 264 GLU   B C   1 
ATOM   3798 O O   . GLU   B 2 171 ? 13.21718 5.48987   -30.59528 1.000 135.49982 ? 264 GLU   B O   1 
ATOM   3799 C CB  . GLU   B 2 171 ? 11.70277 7.94248   -30.63322 1.000 151.03036 ? 264 GLU   B CB  1 
ATOM   3800 C CG  . GLU   B 2 171 ? 11.97660 8.20018   -29.15835 1.000 147.26005 ? 264 GLU   B CG  1 
ATOM   3801 C CD  . GLU   B 2 171 ? 12.88429 9.39528   -28.93108 1.000 155.63273 ? 264 GLU   B CD  1 
ATOM   3802 O OE1 . GLU   B 2 171 ? 12.73867 10.40312  -29.65488 1.000 152.39330 ? 264 GLU   B OE1 1 
ATOM   3803 O OE2 . GLU   B 2 171 ? 13.74888 9.32394   -28.03196 1.000 150.74502 ? 264 GLU   B OE2 1 
ATOM   3804 N N   . VAL   B 2 172 ? 15.09967 6.70927   -30.87358 1.000 120.08216 ? 265 VAL   B N   1 
ATOM   3805 C CA  . VAL   B 2 172 ? 15.99883 5.59430   -30.58740 1.000 108.78713 ? 265 VAL   B CA  1 
ATOM   3806 C C   . VAL   B 2 172 ? 16.31121 5.43700   -29.10449 1.000 96.58000  ? 265 VAL   B C   1 
ATOM   3807 O O   . VAL   B 2 172 ? 16.92024 4.42836   -28.71455 1.000 91.49695  ? 265 VAL   B O   1 
ATOM   3808 C CB  . VAL   B 2 172 ? 17.30753 5.75620   -31.38945 1.000 105.98876 ? 265 VAL   B CB  1 
ATOM   3809 C CG1 . VAL   B 2 172 ? 18.27775 6.67608   -30.65831 1.000 98.92228  ? 265 VAL   B CG1 1 
ATOM   3810 C CG2 . VAL   B 2 172 ? 17.93752 4.39914   -31.68750 1.000 99.40982  ? 265 VAL   B CG2 1 
ATOM   3811 N N   . LEU   B 2 173 ? 15.90637 6.38558   -28.26044 1.000 91.81843  ? 266 LEU   B N   1 
ATOM   3812 C CA  . LEU   B 2 173 ? 16.24380 6.31144   -26.84383 1.000 93.67649  ? 266 LEU   B CA  1 
ATOM   3813 C C   . LEU   B 2 173 ? 15.20014 5.57320   -26.01427 1.000 84.89722  ? 266 LEU   B C   1 
ATOM   3814 O O   . LEU   B 2 173 ? 15.54033 5.01895   -24.96272 1.000 78.56767  ? 266 LEU   B O   1 
ATOM   3815 C CB  . LEU   B 2 173 ? 16.45426 7.71785   -26.27548 1.000 90.08569  ? 266 LEU   B CB  1 
ATOM   3816 C CG  . LEU   B 2 173 ? 17.73195 8.42132   -26.73947 1.000 83.46170  ? 266 LEU   B CG  1 
ATOM   3817 C CD1 . LEU   B 2 173 ? 17.94818 9.71904   -25.97486 1.000 80.32137  ? 266 LEU   B CD1 1 
ATOM   3818 C CD2 . LEU   B 2 173 ? 18.93475 7.49909   -26.59370 1.000 81.92857  ? 266 LEU   B CD2 1 
ATOM   3819 N N   . LEU   B 2 174 ? 13.94337 5.54393   -26.45547 1.000 86.60925  ? 267 LEU   B N   1 
ATOM   3820 C CA  . LEU   B 2 174 ? 12.90305 4.82123   -25.73397 1.000 86.83696  ? 267 LEU   B CA  1 
ATOM   3821 C C   . LEU   B 2 174 ? 12.85848 3.37764   -26.21804 1.000 93.74333  ? 267 LEU   B C   1 
ATOM   3822 O O   . LEU   B 2 174 ? 12.67492 3.14478   -27.42196 1.000 92.75923  ? 267 LEU   B O   1 
ATOM   3823 C CB  . LEU   B 2 174 ? 11.55086 5.49079   -25.92521 1.000 82.63785  ? 267 LEU   B CB  1 
ATOM   3824 C CG  . LEU   B 2 174 ? 10.55411 5.40052   -24.76389 1.000 88.85107  ? 267 LEU   B CG  1 
ATOM   3825 C CD1 . LEU   B 2 174 ? 9.51345  6.50610   -24.86395 1.000 99.69372  ? 267 LEU   B CD1 1 
ATOM   3826 C CD2 . LEU   B 2 174 ? 9.87672  4.03941   -24.72465 1.000 86.80342  ? 267 LEU   B CD2 1 
ATOM   3827 N N   . PRO   B 2 175 ? 13.01121 2.39323   -25.33262 1.000 86.73068  ? 268 PRO   B N   1 
ATOM   3828 C CA  . PRO   B 2 175 ? 13.14397 1.00162   -25.78298 1.000 82.06586  ? 268 PRO   B CA  1 
ATOM   3829 C C   . PRO   B 2 175 ? 11.82910 0.44405   -26.30893 1.000 84.64391  ? 268 PRO   B C   1 
ATOM   3830 O O   . PRO   B 2 175 ? 10.75272 0.73252   -25.78005 1.000 88.13372  ? 268 PRO   B O   1 
ATOM   3831 C CB  . PRO   B 2 175 ? 13.58872 0.26177   -24.51615 1.000 84.59464  ? 268 PRO   B CB  1 
ATOM   3832 C CG  . PRO   B 2 175 ? 13.04493 1.09839   -23.39166 1.000 81.52332  ? 268 PRO   B CG  1 
ATOM   3833 C CD  . PRO   B 2 175 ? 13.11955 2.52039   -23.87155 1.000 81.94591  ? 268 PRO   B CD  1 
ATOM   3834 N N   . GLN   B 2 176 ? 11.92954 -0.37065  -27.36198 1.000 78.08563  ? 269 GLN   B N   1 
ATOM   3835 C CA  . GLN   B 2 176 ? 10.75130 -1.00092  -27.95233 1.000 87.32098  ? 269 GLN   B CA  1 
ATOM   3836 C C   . GLN   B 2 176 ? 11.23976 -2.12561  -28.86610 1.000 86.51715  ? 269 GLN   B C   1 
ATOM   3837 O O   . GLN   B 2 176 ? 11.63874 -1.86984  -30.00747 1.000 93.32064  ? 269 GLN   B O   1 
ATOM   3838 C CB  . GLN   B 2 176 ? 9.90076  0.01043   -28.71329 1.000 78.14592  ? 269 GLN   B CB  1 
ATOM   3839 C CG  . GLN   B 2 176 ? 8.54780  -0.51453  -29.19048 1.000 98.01146  ? 269 GLN   B CG  1 
ATOM   3840 C CD  . GLN   B 2 176 ? 8.62120  -1.21817  -30.54124 1.000 113.76424 ? 269 GLN   B CD  1 
ATOM   3841 O OE1 . GLN   B 2 176 ? 9.35207  -0.79152  -31.43504 1.000 113.91888 ? 269 GLN   B OE1 1 
ATOM   3842 N NE2 . GLN   B 2 176 ? 7.86080  -2.29973  -30.69289 1.000 97.73434  ? 269 GLN   B NE2 1 
ATOM   3843 N N   . TYR   B 2 177 ? 11.20453 -3.35438  -28.35131 1.000 81.82011  ? 270 TYR   B N   1 
ATOM   3844 C CA  . TYR   B 2 177 ? 11.53934 -4.54348  -29.12335 1.000 86.45261  ? 270 TYR   B CA  1 
ATOM   3845 C C   . TYR   B 2 177 ? 11.08986 -5.76549  -28.33872 1.000 78.41801  ? 270 TYR   B C   1 
ATOM   3846 O O   . TYR   B 2 177 ? 10.96905 -5.69526  -27.11061 1.000 89.43354  ? 270 TYR   B O   1 
ATOM   3847 C CB  . TYR   B 2 177 ? 13.04475 -4.61869  -29.42841 1.000 85.71473  ? 270 TYR   B CB  1 
ATOM   3848 C CG  . TYR   B 2 177 ? 13.95351 -4.46217  -28.22921 1.000 83.27041  ? 270 TYR   B CG  1 
ATOM   3849 C CD1 . TYR   B 2 177 ? 14.25351 -5.54453  -27.41009 1.000 72.60212  ? 270 TYR   B CD1 1 
ATOM   3850 C CD2 . TYR   B 2 177 ? 14.53351 -3.23621  -27.93445 1.000 71.63276  ? 270 TYR   B CD2 1 
ATOM   3851 C CE1 . TYR   B 2 177 ? 15.09529 -5.40521  -26.32185 1.000 67.91618  ? 270 TYR   B CE1 1 
ATOM   3852 C CE2 . TYR   B 2 177 ? 15.37640 -3.08743  -26.85109 1.000 81.65726  ? 270 TYR   B CE2 1 
ATOM   3853 C CZ  . TYR   B 2 177 ? 15.65426 -4.17362  -26.04838 1.000 76.98196  ? 270 TYR   B CZ  1 
ATOM   3854 O OH  . TYR   B 2 177 ? 16.49469 -4.01874  -24.97062 1.000 79.64871  ? 270 TYR   B OH  1 
ATOM   3855 N N   . PRO   B 2 178 ? 10.81578 -6.88227  -29.00972 1.000 79.83481  ? 271 PRO   B N   1 
ATOM   3856 C CA  . PRO   B 2 178 ? 10.36865 -8.08416  -28.29445 1.000 77.23864  ? 271 PRO   B CA  1 
ATOM   3857 C C   . PRO   B 2 178 ? 11.42824 -8.59306  -27.32946 1.000 75.99587  ? 271 PRO   B C   1 
ATOM   3858 O O   . PRO   B 2 178 ? 12.58740 -8.79713  -27.69723 1.000 70.84706  ? 271 PRO   B O   1 
ATOM   3859 C CB  . PRO   B 2 178 ? 10.10611 -9.08761  -29.42096 1.000 59.91344  ? 271 PRO   B CB  1 
ATOM   3860 C CG  . PRO   B 2 178 ? 9.85814  -8.23784  -30.62363 1.000 85.87301  ? 271 PRO   B CG  1 
ATOM   3861 C CD  . PRO   B 2 178 ? 10.72908 -7.04085  -30.46874 1.000 82.68314  ? 271 PRO   B CD  1 
ATOM   3862 N N   . GLN   B 2 179 ? 11.00979 -8.80801  -26.08204 1.000 73.49134  ? 272 GLN   B N   1 
ATOM   3863 C CA  . GLN   B 2 179 ? 11.90706 -9.36728  -25.07968 1.000 70.51151  ? 272 GLN   B CA  1 
ATOM   3864 C C   . GLN   B 2 179 ? 12.21394 -10.83396 -25.35284 1.000 69.46170  ? 272 GLN   B C   1 
ATOM   3865 O O   . GLN   B 2 179 ? 13.30389 -11.31088 -25.01488 1.000 68.08260  ? 272 GLN   B O   1 
ATOM   3866 C CB  . GLN   B 2 179 ? 11.28902 -9.20467  -23.69367 1.000 73.41412  ? 272 GLN   B CB  1 
ATOM   3867 C CG  . GLN   B 2 179 ? 10.86508 -7.78319  -23.37678 1.000 78.84124  ? 272 GLN   B CG  1 
ATOM   3868 C CD  . GLN   B 2 179 ? 9.98462  -7.70312  -22.14879 1.000 93.06039  ? 272 GLN   B CD  1 
ATOM   3869 O OE1 . GLN   B 2 179 ? 8.99163  -8.42238  -22.03606 1.000 95.52455  ? 272 GLN   B OE1 1 
ATOM   3870 N NE2 . GLN   B 2 179 ? 10.34811 -6.83104  -21.21517 1.000 92.00773  ? 272 GLN   B NE2 1 
ATOM   3871 N N   . GLN   B 2 180 ? 11.27142 -11.55806 -25.96183 1.000 66.88555  ? 273 GLN   B N   1 
ATOM   3872 C CA  . GLN   B 2 180 ? 11.45188 -12.98870 -26.19076 1.000 77.36893  ? 273 GLN   B CA  1 
ATOM   3873 C C   . GLN   B 2 180 ? 12.63118 -13.25602 -27.11855 1.000 73.86604  ? 273 GLN   B C   1 
ATOM   3874 O O   . GLN   B 2 180 ? 13.48074 -14.10687 -26.83260 1.000 79.77463  ? 273 GLN   B O   1 
ATOM   3875 C CB  . GLN   B 2 180 ? 10.16705 -13.58784 -26.76513 1.000 89.94329  ? 273 GLN   B CB  1 
ATOM   3876 C CG  . GLN   B 2 180 ? 10.20245 -15.09558 -26.96690 1.000 100.84302 ? 273 GLN   B CG  1 
ATOM   3877 C CD  . GLN   B 2 180 ? 9.56277  -15.85352 -25.81991 1.000 105.51856 ? 273 GLN   B CD  1 
ATOM   3878 O OE1 . GLN   B 2 180 ? 9.95751  -15.70414 -24.66363 1.000 95.61662  ? 273 GLN   B OE1 1 
ATOM   3879 N NE2 . GLN   B 2 180 ? 8.56121  -16.66774 -26.13551 1.000 102.63444 ? 273 GLN   B NE2 1 
ATOM   3880 N N   . ILE   B 2 181 ? 12.70209 -12.53675 -28.24006 1.000 76.64801  ? 274 ILE   B N   1 
ATOM   3881 C CA  . ILE   B 2 181 ? 13.78379 -12.77642 -29.18869 1.000 76.15096  ? 274 ILE   B CA  1 
ATOM   3882 C C   . ILE   B 2 181 ? 15.09352 -12.14690 -28.72745 1.000 73.74248  ? 274 ILE   B C   1 
ATOM   3883 O O   . ILE   B 2 181 ? 16.16780 -12.57168 -29.17242 1.000 71.56706  ? 274 ILE   B O   1 
ATOM   3884 C CB  . ILE   B 2 181 ? 13.39031 -12.27851 -30.59160 1.000 77.48003  ? 274 ILE   B CB  1 
ATOM   3885 C CG1 . ILE   B 2 181 ? 14.01238 -10.91537 -30.89204 1.000 70.76166  ? 274 ILE   B CG1 1 
ATOM   3886 C CG2 . ILE   B 2 181 ? 11.87333 -12.21187 -30.73053 1.000 82.99433  ? 274 ILE   B CG2 1 
ATOM   3887 C CD1 . ILE   B 2 181 ? 15.06821 -10.96104 -31.97457 1.000 76.06645  ? 274 ILE   B CD1 1 
ATOM   3888 N N   . PHE   B 2 182 ? 15.03872 -11.15576 -27.83541 1.000 64.89989  ? 275 PHE   B N   1 
ATOM   3889 C CA  . PHE   B 2 182 ? 16.26575 -10.56200 -27.31545 1.000 66.06131  ? 275 PHE   B CA  1 
ATOM   3890 C C   . PHE   B 2 182 ? 17.03047 -11.55544 -26.44923 1.000 68.22617  ? 275 PHE   B C   1 
ATOM   3891 O O   . PHE   B 2 182 ? 18.25337 -11.69109 -26.57381 1.000 63.33487  ? 275 PHE   B O   1 
ATOM   3892 C CB  . PHE   B 2 182 ? 15.94185 -9.29381  -26.52384 1.000 63.28913  ? 275 PHE   B CB  1 
ATOM   3893 C CG  . PHE   B 2 182 ? 17.12651 -8.70460  -25.80999 1.000 63.30074  ? 275 PHE   B CG  1 
ATOM   3894 C CD1 . PHE   B 2 182 ? 17.99469 -7.85022  -26.46948 1.000 66.25611  ? 275 PHE   B CD1 1 
ATOM   3895 C CD2 . PHE   B 2 182 ? 17.36886 -8.99992  -24.47679 1.000 66.24940  ? 275 PHE   B CD2 1 
ATOM   3896 C CE1 . PHE   B 2 182 ? 19.08372 -7.30435  -25.81531 1.000 61.48643  ? 275 PHE   B CE1 1 
ATOM   3897 C CE2 . PHE   B 2 182 ? 18.45724 -8.45892  -23.81754 1.000 68.56336  ? 275 PHE   B CE2 1 
ATOM   3898 C CZ  . PHE   B 2 182 ? 19.31536 -7.60938  -24.48781 1.000 69.03255  ? 275 PHE   B CZ  1 
ATOM   3899 N N   . ILE   B 2 183 ? 16.32586 -12.25866 -25.55836 1.000 65.30579  ? 276 ILE   B N   1 
ATOM   3900 C CA  . ILE   B 2 183 ? 16.99487 -13.20595 -24.67581 1.000 66.93724  ? 276 ILE   B CA  1 
ATOM   3901 C C   . ILE   B 2 183 ? 17.47142 -14.43709 -25.43447 1.000 71.81419  ? 276 ILE   B C   1 
ATOM   3902 O O   . ILE   B 2 183 ? 18.39106 -15.12394 -24.97579 1.000 74.61084  ? 276 ILE   B O   1 
ATOM   3903 C CB  . ILE   B 2 183 ? 16.07400 -13.59681 -23.50197 1.000 69.38757  ? 276 ILE   B CB  1 
ATOM   3904 C CG1 . ILE   B 2 183 ? 14.87981 -14.42052 -23.98740 1.000 74.50959  ? 276 ILE   B CG1 1 
ATOM   3905 C CG2 . ILE   B 2 183 ? 15.58878 -12.35410 -22.77143 1.000 63.41802  ? 276 ILE   B CG2 1 
ATOM   3906 C CD1 . ILE   B 2 183 ? 14.93499 -15.87972 -23.58328 1.000 78.51079  ? 276 ILE   B CD1 1 
ATOM   3907 N N   . GLN   B 2 184 ? 16.87797 -14.73276 -26.59378 1.000 71.00565  ? 277 GLN   B N   1 
ATOM   3908 C CA  . GLN   B 2 184 ? 17.35657 -15.85452 -27.39451 1.000 77.78968  ? 277 GLN   B CA  1 
ATOM   3909 C C   . GLN   B 2 184 ? 18.70766 -15.54116 -28.02546 1.000 68.50887  ? 277 GLN   B C   1 
ATOM   3910 O O   . GLN   B 2 184 ? 19.60338 -16.39357 -28.04279 1.000 75.57751  ? 277 GLN   B O   1 
ATOM   3911 C CB  . GLN   B 2 184 ? 16.32598 -16.21491 -28.46560 1.000 82.92881  ? 277 GLN   B CB  1 
ATOM   3912 C CG  . GLN   B 2 184 ? 15.00667 -16.72657 -27.90385 1.000 88.12762  ? 277 GLN   B CG  1 
ATOM   3913 C CD  . GLN   B 2 184 ? 13.96683 -16.98018 -28.97950 1.000 103.67987 ? 277 GLN   B CD  1 
ATOM   3914 O OE1 . GLN   B 2 184 ? 14.24865 -16.86828 -30.17329 1.000 107.63434 ? 277 GLN   B OE1 1 
ATOM   3915 N NE2 . GLN   B 2 184 ? 12.75468 -17.32516 -28.55922 1.000 98.26724  ? 277 GLN   B NE2 1 
ATOM   3916 N N   . ILE   B 2 185 ? 18.87606 -14.32271 -28.54399 1.000 64.23956  ? 278 ILE   B N   1 
ATOM   3917 C CA  . ILE   B 2 185 ? 20.16499 -13.93218 -29.10616 1.000 67.73747  ? 278 ILE   B CA  1 
ATOM   3918 C C   . ILE   B 2 185 ? 21.20503 -13.79151 -28.00211 1.000 67.11137  ? 278 ILE   B C   1 
ATOM   3919 O O   . ILE   B 2 185 ? 22.37858 -14.13806 -28.18560 1.000 66.27313  ? 278 ILE   B O   1 
ATOM   3920 C CB  . ILE   B 2 185 ? 20.02133 -12.63430 -29.92097 1.000 66.97510  ? 278 ILE   B CB  1 
ATOM   3921 C CG1 . ILE   B 2 185 ? 18.92557 -12.78884 -30.97681 1.000 74.41676  ? 278 ILE   B CG1 1 
ATOM   3922 C CG2 . ILE   B 2 185 ? 21.34381 -12.26741 -30.57891 1.000 65.20245  ? 278 ILE   B CG2 1 
ATOM   3923 C CD1 . ILE   B 2 185 ? 18.67751 -11.53670 -31.78119 1.000 66.55098  ? 278 ILE   B CD1 1 
ATOM   3924 N N   . ALA   B 2 186 ? 20.79437 -13.28111 -26.83862 1.000 68.89366  ? 279 ALA   B N   1 
ATOM   3925 C CA  . ALA   B 2 186 ? 21.70936 -13.20137 -25.70634 1.000 64.34696  ? 279 ALA   B CA  1 
ATOM   3926 C C   . ALA   B 2 186 ? 22.18007 -14.58264 -25.27439 1.000 70.44190  ? 279 ALA   B C   1 
ATOM   3927 O O   . ALA   B 2 186 ? 23.32758 -14.73951 -24.84052 1.000 67.71720  ? 279 ALA   B O   1 
ATOM   3928 C CB  . ALA   B 2 186 ? 21.03936 -12.47682 -24.53895 1.000 61.54495  ? 279 ALA   B CB  1 
ATOM   3929 N N   . GLU   B 2 187 ? 21.31283 -15.59256 -25.39084 1.000 65.35679  ? 280 GLU   B N   1 
ATOM   3930 C CA  . GLU   B 2 187 ? 21.70504 -16.95666 -25.05034 1.000 72.95875  ? 280 GLU   B CA  1 
ATOM   3931 C C   . GLU   B 2 187 ? 22.86500 -17.42949 -25.91752 1.000 75.83525  ? 280 GLU   B C   1 
ATOM   3932 O O   . GLU   B 2 187 ? 23.79805 -18.07312 -25.42253 1.000 72.88277  ? 280 GLU   B O   1 
ATOM   3933 C CB  . GLU   B 2 187 ? 20.50514 -17.89327 -25.19551 1.000 86.14721  ? 280 GLU   B CB  1 
ATOM   3934 C CG  . GLU   B 2 187 ? 20.83650 -19.37167 -25.07542 1.000 92.31876  ? 280 GLU   B CG  1 
ATOM   3935 C CD  . GLU   B 2 187 ? 19.64465 -20.25937 -25.38620 1.000 121.13468 ? 280 GLU   B CD  1 
ATOM   3936 O OE1 . GLU   B 2 187 ? 18.50925 -19.73925 -25.42883 1.000 123.15974 ? 280 GLU   B OE1 1 
ATOM   3937 O OE2 . GLU   B 2 187 ? 19.84271 -21.47556 -25.59374 1.000 134.70663 ? 280 GLU   B OE2 1 
ATOM   3938 N N   . LEU   B 2 188 ? 22.82609 -17.11812 -27.21605 1.000 73.87451  ? 281 LEU   B N   1 
ATOM   3939 C CA  . LEU   B 2 188 ? 23.93307 -17.48525 -28.09339 1.000 72.84346  ? 281 LEU   B CA  1 
ATOM   3940 C C   . LEU   B 2 188 ? 25.20261 -16.73018 -27.72230 1.000 73.09828  ? 281 LEU   B C   1 
ATOM   3941 O O   . LEU   B 2 188 ? 26.30100 -17.29743 -27.75209 1.000 72.18970  ? 281 LEU   B O   1 
ATOM   3942 C CB  . LEU   B 2 188 ? 23.55989 -17.22314 -29.55215 1.000 65.88942  ? 281 LEU   B CB  1 
ATOM   3943 C CG  . LEU   B 2 188 ? 24.67195 -17.43947 -30.58184 1.000 72.59699  ? 281 LEU   B CG  1 
ATOM   3944 C CD1 . LEU   B 2 188 ? 25.21526 -18.85873 -30.49990 1.000 78.20866  ? 281 LEU   B CD1 1 
ATOM   3945 C CD2 . LEU   B 2 188 ? 24.17681 -17.13197 -31.98853 1.000 72.93314  ? 281 LEU   B CD2 1 
ATOM   3946 N N   . LEU   B 2 189 ? 25.07241 -15.45178 -27.36352 1.000 66.94129  ? 282 LEU   B N   1 
ATOM   3947 C CA  . LEU   B 2 189 ? 26.24663 -14.67120 -26.99095 1.000 69.80037  ? 282 LEU   B CA  1 
ATOM   3948 C C   . LEU   B 2 189 ? 26.82096 -15.13433 -25.65740 1.000 70.74502  ? 282 LEU   B C   1 
ATOM   3949 O O   . LEU   B 2 189 ? 28.04352 -15.13639 -25.47169 1.000 69.42652  ? 282 LEU   B O   1 
ATOM   3950 C CB  . LEU   B 2 189 ? 25.89354 -13.18521 -26.94539 1.000 64.58677  ? 282 LEU   B CB  1 
ATOM   3951 C CG  . LEU   B 2 189 ? 25.67749 -12.53242 -28.31118 1.000 69.15212  ? 282 LEU   B CG  1 
ATOM   3952 C CD1 . LEU   B 2 189 ? 25.12043 -11.12841 -28.15926 1.000 65.54734  ? 282 LEU   B CD1 1 
ATOM   3953 C CD2 . LEU   B 2 189 ? 26.98338 -12.51371 -29.09460 1.000 69.21301  ? 282 LEU   B CD2 1 
ATOM   3954 N N   . ASP   B 2 190 ? 25.95839 -15.53479 -24.71798 1.000 69.95932  ? 283 ASP   B N   1 
ATOM   3955 C CA  . ASP   B 2 190 ? 26.44875 -16.02882 -23.43426 1.000 73.70387  ? 283 ASP   B CA  1 
ATOM   3956 C C   . ASP   B 2 190 ? 27.26433 -17.30370 -23.60020 1.000 77.96509  ? 283 ASP   B C   1 
ATOM   3957 O O   . ASP   B 2 190 ? 28.15188 -17.58340 -22.78655 1.000 83.88059  ? 283 ASP   B O   1 
ATOM   3958 C CB  . ASP   B 2 190 ? 25.28247 -16.26822 -22.47353 1.000 67.96556  ? 283 ASP   B CB  1 
ATOM   3959 C CG  . ASP   B 2 190 ? 24.62449 -14.97844 -22.01785 1.000 79.43887  ? 283 ASP   B CG  1 
ATOM   3960 O OD1 . ASP   B 2 190 ? 25.28183 -13.91702 -22.07422 1.000 73.71311  ? 283 ASP   B OD1 1 
ATOM   3961 O OD2 . ASP   B 2 190 ? 23.44846 -15.02774 -21.59796 1.000 83.14058  ? 283 ASP   B OD2 1 
ATOM   3962 N N   . LEU   B 2 191 ? 26.98145 -18.08840 -24.63986 1.000 73.87928  ? 284 LEU   B N   1 
ATOM   3963 C CA  . LEU   B 2 191 ? 27.77807 -19.28053 -24.90143 1.000 80.27445  ? 284 LEU   B CA  1 
ATOM   3964 C C   . LEU   B 2 191 ? 29.10195 -18.91584 -25.56293 1.000 85.18447  ? 284 LEU   B C   1 
ATOM   3965 O O   . LEU   B 2 191 ? 30.16096 -19.41472 -25.16585 1.000 90.73291  ? 284 LEU   B O   1 
ATOM   3966 C CB  . LEU   B 2 191 ? 26.98480 -20.25795 -25.77443 1.000 94.14793  ? 284 LEU   B CB  1 
ATOM   3967 C CG  . LEU   B 2 191 ? 27.28209 -21.75945 -25.67366 1.000 107.12053 ? 284 LEU   B CG  1 
ATOM   3968 C CD1 . LEU   B 2 191 ? 26.18710 -22.55445 -26.36741 1.000 98.62955  ? 284 LEU   B CD1 1 
ATOM   3969 C CD2 . LEU   B 2 191 ? 28.64128 -22.11871 -26.25770 1.000 109.54216 ? 284 LEU   B CD2 1 
ATOM   3970 N N   . CYS   B 2 192 ? 29.05682 -18.04191 -26.57308 1.000 79.03545  ? 285 CYS   B N   1 
ATOM   3971 C CA  . CYS   B 2 192 ? 30.26579 -17.69042 -27.31132 1.000 83.64570  ? 285 CYS   B CA  1 
ATOM   3972 C C   . CYS   B 2 192 ? 31.27880 -16.97008 -26.43328 1.000 84.84245  ? 285 CYS   B C   1 
ATOM   3973 O O   . CYS   B 2 192 ? 32.48747 -17.06899 -26.67428 1.000 87.36150  ? 285 CYS   B O   1 
ATOM   3974 C CB  . CYS   B 2 192 ? 29.91145 -16.82215 -28.51926 1.000 91.10201  ? 285 CYS   B CB  1 
ATOM   3975 S SG  . CYS   B 2 192 ? 28.81880 -17.61111 -29.72047 1.000 92.32846  ? 285 CYS   B SG  1 
ATOM   3976 N N   . VAL   B 2 193 ? 30.81236 -16.23777 -25.41841 1.000 85.02319  ? 286 VAL   B N   1 
ATOM   3977 C CA  . VAL   B 2 193 ? 31.73105 -15.49600 -24.56575 1.000 82.80127  ? 286 VAL   B CA  1 
ATOM   3978 C C   . VAL   B 2 193 ? 32.53479 -16.42980 -23.67037 1.000 74.88344  ? 286 VAL   B C   1 
ATOM   3979 O O   . VAL   B 2 193 ? 33.60417 -16.04626 -23.18321 1.000 84.91727  ? 286 VAL   B O   1 
ATOM   3980 C CB  . VAL   B 2 193 ? 30.96371 -14.44353 -23.73934 1.000 72.84441  ? 286 VAL   B CB  1 
ATOM   3981 C CG1 . VAL   B 2 193 ? 30.22263 -15.09346 -22.58004 1.000 74.27663  ? 286 VAL   B CG1 1 
ATOM   3982 C CG2 . VAL   B 2 193 ? 31.90635 -13.35269 -23.24894 1.000 66.04033  ? 286 VAL   B CG2 1 
ATOM   3983 N N   . LEU   B 2 194 ? 32.05799 -17.65836 -23.45314 1.000 77.75175  ? 287 LEU   B N   1 
ATOM   3984 C CA  . LEU   B 2 194 ? 32.82164 -18.62478 -22.67325 1.000 83.23779  ? 287 LEU   B CA  1 
ATOM   3985 C C   . LEU   B 2 194 ? 34.06691 -19.10088 -23.40914 1.000 91.87657  ? 287 LEU   B C   1 
ATOM   3986 O O   . LEU   B 2 194 ? 35.02583 -19.53746 -22.76372 1.000 98.21923  ? 287 LEU   B O   1 
ATOM   3987 C CB  . LEU   B 2 194 ? 31.93949 -19.81877 -22.30690 1.000 79.56332  ? 287 LEU   B CB  1 
ATOM   3988 C CG  . LEU   B 2 194 ? 30.65677 -19.48154 -21.54399 1.000 81.79613  ? 287 LEU   B CG  1 
ATOM   3989 C CD1 . LEU   B 2 194 ? 29.89678 -20.74665 -21.17333 1.000 90.55332  ? 287 LEU   B CD1 1 
ATOM   3990 C CD2 . LEU   B 2 194 ? 30.97048 -18.65778 -20.30670 1.000 77.76296  ? 287 LEU   B CD2 1 
ATOM   3991 N N   . ASP   B 2 195 ? 34.07462 -19.02770 -24.73712 1.000 87.28282  ? 288 ASP   B N   1 
ATOM   3992 C CA  . ASP   B 2 195 ? 35.24610 -19.37904 -25.52701 1.000 97.17799  ? 288 ASP   B CA  1 
ATOM   3993 C C   . ASP   B 2 195 ? 36.13666 -18.15138 -25.66628 1.000 91.37858  ? 288 ASP   B C   1 
ATOM   3994 O O   . ASP   B 2 195 ? 35.67038 -17.08220 -26.07159 1.000 93.75791  ? 288 ASP   B O   1 
ATOM   3995 C CB  . ASP   B 2 195 ? 34.83152 -19.90508 -26.90281 1.000 95.33647  ? 288 ASP   B CB  1 
ATOM   3996 C CG  . ASP   B 2 195 ? 35.96809 -20.59828 -27.63621 1.000 100.43866 ? 288 ASP   B CG  1 
ATOM   3997 O OD1 . ASP   B 2 195 ? 37.11243 -20.10020 -27.59118 1.000 102.68968 ? 288 ASP   B OD1 1 
ATOM   3998 O OD2 . ASP   B 2 195 ? 35.71512 -21.64910 -28.26220 1.000 111.47313 ? 288 ASP   B OD2 1 
ATOM   3999 N N   . VAL   B 2 196 ? 37.42068 -18.31217 -25.33601 1.000 90.95005  ? 289 VAL   B N   1 
ATOM   4000 C CA  . VAL   B 2 196 ? 38.33715 -17.17766 -25.32000 1.000 96.81159  ? 289 VAL   B CA  1 
ATOM   4001 C C   . VAL   B 2 196 ? 38.62740 -16.65115 -26.72072 1.000 91.95514  ? 289 VAL   B C   1 
ATOM   4002 O O   . VAL   B 2 196 ? 39.01753 -15.48713 -26.87228 1.000 93.72560  ? 289 VAL   B O   1 
ATOM   4003 C CB  . VAL   B 2 196 ? 39.64575 -17.56527 -24.60623 1.000 96.48970  ? 289 VAL   B CB  1 
ATOM   4004 C CG1 . VAL   B 2 196 ? 40.39123 -16.32044 -24.13945 1.000 86.86210  ? 289 VAL   B CG1 1 
ATOM   4005 C CG2 . VAL   B 2 196 ? 39.35559 -18.49779 -23.43894 1.000 101.72426 ? 289 VAL   B CG2 1 
ATOM   4006 N N   . ASP   B 2 197 ? 38.44176 -17.47202 -27.75497 1.000 95.76367  ? 290 ASP   B N   1 
ATOM   4007 C CA  . ASP   B 2 197 ? 38.72835 -17.04192 -29.11931 1.000 97.41741  ? 290 ASP   B CA  1 
ATOM   4008 C C   . ASP   B 2 197 ? 37.75124 -15.99266 -29.64030 1.000 95.75184  ? 290 ASP   B C   1 
ATOM   4009 O O   . ASP   B 2 197 ? 37.96518 -15.47860 -30.74402 1.000 93.38281  ? 290 ASP   B O   1 
ATOM   4010 C CB  . ASP   B 2 197 ? 38.74267 -18.25232 -30.05581 1.000 99.56845  ? 290 ASP   B CB  1 
ATOM   4011 C CG  . ASP   B 2 197 ? 39.96435 -19.13064 -29.85389 1.000 106.67034 ? 290 ASP   B CG  1 
ATOM   4012 O OD1 . ASP   B 2 197 ? 41.06852 -18.57932 -29.65555 1.000 106.95465 ? 290 ASP   B OD1 1 
ATOM   4013 O OD2 . ASP   B 2 197 ? 39.81992 -20.37155 -29.88814 1.000 107.31159 ? 290 ASP   B OD2 1 
ATOM   4014 N N   . CYS   B 2 198 ? 36.69997 -15.65577 -28.88803 1.000 95.87723  ? 291 CYS   B N   1 
ATOM   4015 C CA  . CYS   B 2 198 ? 35.78346 -14.60722 -29.32216 1.000 88.24623  ? 291 CYS   B CA  1 
ATOM   4016 C C   . CYS   B 2 198 ? 36.43425 -13.23052 -29.31933 1.000 90.95267  ? 291 CYS   B C   1 
ATOM   4017 O O   . CYS   B 2 198 ? 36.00364 -12.35644 -30.07906 1.000 86.09526  ? 291 CYS   B O   1 
ATOM   4018 C CB  . CYS   B 2 198 ? 34.53867 -14.58969 -28.43394 1.000 80.36467  ? 291 CYS   B CB  1 
ATOM   4019 S SG  . CYS   B 2 198 ? 34.83086 -14.03572 -26.73572 1.000 92.59643  ? 291 CYS   B SG  1 
ATOM   4020 N N   . LEU   B 2 199 ? 37.46720 -13.02350 -28.49641 1.000 91.56095  ? 292 LEU   B N   1 
ATOM   4021 C CA  . LEU   B 2 199 ? 38.12821 -11.72488 -28.42748 1.000 90.11370  ? 292 LEU   B CA  1 
ATOM   4022 C C   . LEU   B 2 199 ? 38.84446 -11.36589 -29.72077 1.000 96.71228  ? 292 LEU   B C   1 
ATOM   4023 O O   . LEU   B 2 199 ? 39.20919 -10.19978 -29.90543 1.000 94.52308  ? 292 LEU   B O   1 
ATOM   4024 C CB  . LEU   B 2 199 ? 39.11905 -11.69614 -27.26312 1.000 91.13364  ? 292 LEU   B CB  1 
ATOM   4025 C CG  . LEU   B 2 199 ? 38.50788 -11.86111 -25.87093 1.000 91.68181  ? 292 LEU   B CG  1 
ATOM   4026 C CD1 . LEU   B 2 199 ? 39.57720 -11.77872 -24.79077 1.000 88.83404  ? 292 LEU   B CD1 1 
ATOM   4027 C CD2 . LEU   B 2 199 ? 37.42280 -10.81993 -25.64006 1.000 84.08064  ? 292 LEU   B CD2 1 
ATOM   4028 N N   . GLU   B 2 200 ? 39.06681 -12.33966 -30.60769 1.000 88.36188  ? 293 GLU   B N   1 
ATOM   4029 C CA  . GLU   B 2 200 ? 39.60350 -12.02960 -31.92836 1.000 95.07887  ? 293 GLU   B CA  1 
ATOM   4030 C C   . GLU   B 2 200 ? 38.71134 -11.03578 -32.66063 1.000 90.15685  ? 293 GLU   B C   1 
ATOM   4031 O O   . GLU   B 2 200 ? 39.20371 -10.13654 -33.35275 1.000 95.29784  ? 293 GLU   B O   1 
ATOM   4032 C CB  . GLU   B 2 200 ? 39.75716 -13.31417 -32.74358 1.000 91.72451  ? 293 GLU   B CB  1 
ATOM   4033 C CG  . GLU   B 2 200 ? 40.08073 -13.09050 -34.21139 1.000 104.99215 ? 293 GLU   B CG  1 
ATOM   4034 C CD  . GLU   B 2 200 ? 39.97981 -14.36355 -35.03001 1.000 94.50989  ? 293 GLU   B CD  1 
ATOM   4035 O OE1 . GLU   B 2 200 ? 39.92109 -15.45531 -34.42598 1.000 97.37579  ? 293 GLU   B OE1 1 
ATOM   4036 O OE2 . GLU   B 2 200 ? 39.95297 -14.27232 -36.27587 1.000 96.40720  ? 293 GLU   B OE2 1 
ATOM   4037 N N   . PHE   B 2 201 ? 37.39702 -11.17453 -32.50878 1.000 81.20492  ? 294 PHE   B N   1 
ATOM   4038 C CA  . PHE   B 2 201 ? 36.42700 -10.30570 -33.15570 1.000 87.12870  ? 294 PHE   B CA  1 
ATOM   4039 C C   . PHE   B 2 201 ? 35.95283 -9.22333  -32.19567 1.000 79.20326  ? 294 PHE   B C   1 
ATOM   4040 O O   . PHE   B 2 201 ? 35.78103 -9.48581  -30.99957 1.000 74.67479  ? 294 PHE   B O   1 
ATOM   4041 C CB  . PHE   B 2 201 ? 35.22207 -11.11070 -33.64367 1.000 84.59836  ? 294 PHE   B CB  1 
ATOM   4042 C CG  . PHE   B 2 201 ? 35.58669 -12.42960 -34.26184 1.000 78.01332  ? 294 PHE   B CG  1 
ATOM   4043 C CD1 . PHE   B 2 201 ? 36.10863 -12.48932 -35.54226 1.000 84.52567  ? 294 PHE   B CD1 1 
ATOM   4044 C CD2 . PHE   B 2 201 ? 35.40666 -13.61063 -33.56051 1.000 82.83295  ? 294 PHE   B CD2 1 
ATOM   4045 C CE1 . PHE   B 2 201 ? 36.44565 -13.70263 -36.11188 1.000 92.62512  ? 294 PHE   B CE1 1 
ATOM   4046 C CE2 . PHE   B 2 201 ? 35.74149 -14.82705 -34.12480 1.000 83.92501  ? 294 PHE   B CE2 1 
ATOM   4047 C CZ  . PHE   B 2 201 ? 36.26136 -14.87279 -35.40138 1.000 89.45154  ? 294 PHE   B CZ  1 
ATOM   4048 N N   . PRO   B 2 202 ? 35.74273 -8.00592  -32.69387 1.000 77.69694  ? 295 PRO   B N   1 
ATOM   4049 C CA  . PRO   B 2 202 ? 35.23759 -6.93185  -31.83223 1.000 68.80621  ? 295 PRO   B CA  1 
ATOM   4050 C C   . PRO   B 2 202 ? 33.86675 -7.27002  -31.26414 1.000 80.96814  ? 295 PRO   B C   1 
ATOM   4051 O O   . PRO   B 2 202 ? 33.12461 -8.09618  -31.80187 1.000 68.35730  ? 295 PRO   B O   1 
ATOM   4052 C CB  . PRO   B 2 202 ? 35.16712 -5.72168  -32.77236 1.000 71.38984  ? 295 PRO   B CB  1 
ATOM   4053 C CG  . PRO   B 2 202 ? 36.11304 -6.04716  -33.88668 1.000 71.66727  ? 295 PRO   B CG  1 
ATOM   4054 C CD  . PRO   B 2 202 ? 36.03774 -7.53415  -34.05678 1.000 66.68971  ? 295 PRO   B CD  1 
ATOM   4055 N N   . TYR   B 2 203 ? 33.53629 -6.60820  -30.15040 1.000 70.16631  ? 296 TYR   B N   1 
ATOM   4056 C CA  . TYR   B 2 203 ? 32.26653 -6.87295  -29.47973 1.000 69.55447  ? 296 TYR   B CA  1 
ATOM   4057 C C   . TYR   B 2 203 ? 31.08305 -6.55324  -30.38515 1.000 60.52143  ? 296 TYR   B C   1 
ATOM   4058 O O   . TYR   B 2 203 ? 30.08198 -7.27952  -30.38948 1.000 64.07892  ? 296 TYR   B O   1 
ATOM   4059 C CB  . TYR   B 2 203 ? 32.17820 -6.07243  -28.17926 1.000 66.29600  ? 296 TYR   B CB  1 
ATOM   4060 C CG  . TYR   B 2 203 ? 33.08610 -6.56818  -27.07414 1.000 72.11871  ? 296 TYR   B CG  1 
ATOM   4061 C CD1 . TYR   B 2 203 ? 33.76411 -7.77508  -27.18925 1.000 66.39740  ? 296 TYR   B CD1 1 
ATOM   4062 C CD2 . TYR   B 2 203 ? 33.25693 -5.83096  -25.90996 1.000 62.04548  ? 296 TYR   B CD2 1 
ATOM   4063 C CE1 . TYR   B 2 203 ? 34.59034 -8.22991  -26.17721 1.000 69.33919  ? 296 TYR   B CE1 1 
ATOM   4064 C CE2 . TYR   B 2 203 ? 34.07914 -6.27769  -24.89507 1.000 74.31064  ? 296 TYR   B CE2 1 
ATOM   4065 C CZ  . TYR   B 2 203 ? 34.74412 -7.47653  -25.03290 1.000 73.01819  ? 296 TYR   B CZ  1 
ATOM   4066 O OH  . TYR   B 2 203 ? 35.56451 -7.92118  -24.01980 1.000 77.33468  ? 296 TYR   B OH  1 
ATOM   4067 N N   . GLY   B 2 204 ? 31.17806 -5.47024  -31.16016 1.000 60.12639  ? 297 GLY   B N   1 
ATOM   4068 C CA  . GLY   B 2 204 ? 30.11285 -5.14277  -32.09192 1.000 65.24070  ? 297 GLY   B CA  1 
ATOM   4069 C C   . GLY   B 2 204 ? 29.94801 -6.16777  -33.19585 1.000 70.16056  ? 297 GLY   B C   1 
ATOM   4070 O O   . GLY   B 2 204 ? 28.83988 -6.36438  -33.70362 1.000 65.31009  ? 297 GLY   B O   1 
ATOM   4071 N N   . ILE   B 2 205 ? 31.03856 -6.83376  -33.58160 1.000 71.90995  ? 298 ILE   B N   1 
ATOM   4072 C CA  . ILE   B 2 205 ? 30.95621 -7.87592  -34.59981 1.000 65.94575  ? 298 ILE   B CA  1 
ATOM   4073 C C   . ILE   B 2 205 ? 30.29520 -9.12590  -34.03211 1.000 69.90007  ? 298 ILE   B C   1 
ATOM   4074 O O   . ILE   B 2 205 ? 29.46632 -9.76186  -34.69524 1.000 68.44803  ? 298 ILE   B O   1 
ATOM   4075 C CB  . ILE   B 2 205 ? 32.35798 -8.17914  -35.16130 1.000 71.82896  ? 298 ILE   B CB  1 
ATOM   4076 C CG1 . ILE   B 2 205 ? 32.92789 -6.95139  -35.87228 1.000 76.46529  ? 298 ILE   B CG1 1 
ATOM   4077 C CG2 . ILE   B 2 205 ? 32.31374 -9.35682  -36.11190 1.000 68.08143  ? 298 ILE   B CG2 1 
ATOM   4078 C CD1 . ILE   B 2 205 ? 32.20405 -6.59597  -37.14546 1.000 81.89420  ? 298 ILE   B CD1 1 
ATOM   4079 N N   . LEU   B 2 206 ? 30.64687 -9.49492  -32.79606 1.000 66.69958  ? 299 LEU   B N   1 
ATOM   4080 C CA  . LEU   B 2 206 ? 30.07133 -10.68658 -32.17810 1.000 71.31852  ? 299 LEU   B CA  1 
ATOM   4081 C C   . LEU   B 2 206 ? 28.56138 -10.55755 -32.01817 1.000 70.46288  ? 299 LEU   B C   1 
ATOM   4082 O O   . LEU   B 2 206 ? 27.81707 -11.50462 -32.29917 1.000 69.28655  ? 299 LEU   B O   1 
ATOM   4083 C CB  . LEU   B 2 206 ? 30.73197 -10.94329 -30.82275 1.000 62.79588  ? 299 LEU   B CB  1 
ATOM   4084 C CG  . LEU   B 2 206 ? 32.15655 -11.49833 -30.83961 1.000 67.86321  ? 299 LEU   B CG  1 
ATOM   4085 C CD1 . LEU   B 2 206 ? 32.80222 -11.36148 -29.46912 1.000 78.82801  ? 299 LEU   B CD1 1 
ATOM   4086 C CD2 . LEU   B 2 206 ? 32.14643 -12.95147 -31.27740 1.000 74.06887  ? 299 LEU   B CD2 1 
ATOM   4087 N N   . ALA   B 2 207 ? 28.09054 -9.39215  -31.56667 1.000 58.96942  ? 300 ALA   B N   1 
ATOM   4088 C CA  . ALA   B 2 207 ? 26.65604 -9.19358  -31.38496 1.000 66.63234  ? 300 ALA   B CA  1 
ATOM   4089 C C   . ALA   B 2 207 ? 25.92188 -9.19939  -32.72008 1.000 61.61207  ? 300 ALA   B C   1 
ATOM   4090 O O   . ALA   B 2 207 ? 24.82562 -9.76143  -32.82933 1.000 62.92663  ? 300 ALA   B O   1 
ATOM   4091 C CB  . ALA   B 2 207 ? 26.39755 -7.88731  -30.63397 1.000 53.49776  ? 300 ALA   B CB  1 
ATOM   4092 N N   . ALA   B 2 208 ? 26.50808 -8.57863  -33.74665 1.000 60.59546  ? 301 ALA   B N   1 
ATOM   4093 C CA  . ALA   B 2 208 ? 25.88329 -8.58750  -35.06520 1.000 72.36693  ? 301 ALA   B CA  1 
ATOM   4094 C C   . ALA   B 2 208 ? 25.85812 -9.99161  -35.65367 1.000 66.43339  ? 301 ALA   B C   1 
ATOM   4095 O O   . ALA   B 2 208 ? 24.89932 -10.36643 -36.33951 1.000 65.47836  ? 301 ALA   B O   1 
ATOM   4096 C CB  . ALA   B 2 208 ? 26.61454 -7.62589  -36.00076 1.000 67.58604  ? 301 ALA   B CB  1 
ATOM   4097 N N   . SER   B 2 209 ? 26.90056 -10.78414 -35.39108 1.000 65.77035  ? 302 SER   B N   1 
ATOM   4098 C CA  . SER   B 2 209 ? 26.94965 -12.14233 -35.92159 1.000 64.89474  ? 302 SER   B CA  1 
ATOM   4099 C C   . SER   B 2 209 ? 25.91493 -13.03599 -35.25021 1.000 70.85421  ? 302 SER   B C   1 
ATOM   4100 O O   . SER   B 2 209 ? 25.32648 -13.90887 -35.89950 1.000 72.77503  ? 302 SER   B O   1 
ATOM   4101 C CB  . SER   B 2 209 ? 28.35300 -12.72022 -35.74946 1.000 77.03319  ? 302 SER   B CB  1 
ATOM   4102 O OG  . SER   B 2 209 ? 29.31851 -11.91112 -36.39848 1.000 74.86983  ? 302 SER   B OG  1 
ATOM   4103 N N   . ALA   B 2 210 ? 25.68346 -12.83909 -33.94946 1.000 70.30617  ? 303 ALA   B N   1 
ATOM   4104 C CA  . ALA   B 2 210 ? 24.63892 -13.59623 -33.26755 1.000 70.98147  ? 303 ALA   B CA  1 
ATOM   4105 C C   . ALA   B 2 210 ? 23.25679 -13.19181 -33.76162 1.000 63.69922  ? 303 ALA   B C   1 
ATOM   4106 O O   . ALA   B 2 210 ? 22.37171 -14.04202 -33.91512 1.000 68.60483  ? 303 ALA   B O   1 
ATOM   4107 C CB  . ALA   B 2 210 ? 24.74571 -13.40053 -31.75743 1.000 63.66812  ? 303 ALA   B CB  1 
ATOM   4108 N N   . LEU   B 2 211 ? 23.05273 -11.89672 -34.01166 1.000 65.49815  ? 304 LEU   B N   1 
ATOM   4109 C CA  . LEU   B 2 211 ? 21.78318 -11.44274 -34.56869 1.000 75.66742  ? 304 LEU   B CA  1 
ATOM   4110 C C   . LEU   B 2 211 ? 21.54279 -12.03989 -35.94960 1.000 61.88606  ? 304 LEU   B C   1 
ATOM   4111 O O   . LEU   B 2 211 ? 20.40700 -12.38873 -36.29473 1.000 71.22128  ? 304 LEU   B O   1 
ATOM   4112 C CB  . LEU   B 2 211 ? 21.75861 -9.91684  -34.63278 1.000 76.01957  ? 304 LEU   B CB  1 
ATOM   4113 C CG  . LEU   B 2 211 ? 20.58615 -9.29524  -35.39225 1.000 77.91019  ? 304 LEU   B CG  1 
ATOM   4114 C CD1 . LEU   B 2 211 ? 19.33619 -9.23701  -34.52916 1.000 64.55864  ? 304 LEU   B CD1 1 
ATOM   4115 C CD2 . LEU   B 2 211 ? 20.96350 -7.91956  -35.89404 1.000 89.65252  ? 304 LEU   B CD2 1 
ATOM   4116 N N   . TYR   B 2 212 ? 22.60355 -12.17283 -36.75124 1.000 72.42950  ? 305 TYR   B N   1 
ATOM   4117 C CA  . TYR   B 2 212 ? 22.45464 -12.73187 -38.09197 1.000 73.21809  ? 305 TYR   B CA  1 
ATOM   4118 C C   . TYR   B 2 212 ? 21.93499 -14.16295 -38.04527 1.000 70.98723  ? 305 TYR   B C   1 
ATOM   4119 O O   . TYR   B 2 212 ? 21.08786 -14.54919 -38.85913 1.000 74.96104  ? 305 TYR   B O   1 
ATOM   4120 C CB  . TYR   B 2 212 ? 23.78701 -12.67510 -38.84103 1.000 69.71043  ? 305 TYR   B CB  1 
ATOM   4121 C CG  . TYR   B 2 212 ? 23.82216 -13.54831 -40.07806 1.000 73.27108  ? 305 TYR   B CG  1 
ATOM   4122 C CD1 . TYR   B 2 212 ? 23.21098 -13.14168 -41.25662 1.000 74.85995  ? 305 TYR   B CD1 1 
ATOM   4123 C CD2 . TYR   B 2 212 ? 24.46366 -14.78101 -40.06549 1.000 71.59145  ? 305 TYR   B CD2 1 
ATOM   4124 C CE1 . TYR   B 2 212 ? 23.23674 -13.93723 -42.38848 1.000 77.12876  ? 305 TYR   B CE1 1 
ATOM   4125 C CE2 . TYR   B 2 212 ? 24.49465 -15.58335 -41.19216 1.000 86.72940  ? 305 TYR   B CE2 1 
ATOM   4126 C CZ  . TYR   B 2 212 ? 23.87985 -15.15660 -42.35042 1.000 76.93540  ? 305 TYR   B CZ  1 
ATOM   4127 O OH  . TYR   B 2 212 ? 23.90999 -15.95127 -43.47328 1.000 92.36416  ? 305 TYR   B OH  1 
ATOM   4128 N N   . HIS   B 2 213 ? 22.42961 -14.96684 -37.10083 1.000 71.09124  ? 306 HIS   B N   1 
ATOM   4129 C CA  . HIS   B 2 213 ? 22.01220 -16.36257 -37.02849 1.000 75.08696  ? 306 HIS   B CA  1 
ATOM   4130 C C   . HIS   B 2 213 ? 20.54731 -16.51492 -36.64394 1.000 65.78709  ? 306 HIS   B C   1 
ATOM   4131 O O   . HIS   B 2 213 ? 19.96386 -17.57586 -36.89017 1.000 73.52347  ? 306 HIS   B O   1 
ATOM   4132 C CB  . HIS   B 2 213 ? 22.89827 -17.12841 -36.04532 1.000 72.29790  ? 306 HIS   B CB  1 
ATOM   4133 C CG  . HIS   B 2 213 ? 24.25489 -17.45196 -36.58869 1.000 81.22307  ? 306 HIS   B CG  1 
ATOM   4134 N ND1 . HIS   B 2 213 ? 25.37340 -16.70167 -36.29641 1.000 71.19467  ? 306 HIS   B ND1 1 
ATOM   4135 C CD2 . HIS   B 2 213 ? 24.66918 -18.43686 -37.42098 1.000 77.57399  ? 306 HIS   B CD2 1 
ATOM   4136 C CE1 . HIS   B 2 213 ? 26.42002 -17.21600 -36.91736 1.000 87.64813  ? 306 HIS   B CE1 1 
ATOM   4137 N NE2 . HIS   B 2 213 ? 26.01972 -18.26924 -37.60711 1.000 85.60291  ? 306 HIS   B NE2 1 
ATOM   4138 N N   . PHE   B 2 214 ? 19.94164 -15.48626 -36.05557 1.000 68.83301  ? 307 PHE   B N   1 
ATOM   4139 C CA  . PHE   B 2 214 ? 18.52276 -15.49654 -35.73136 1.000 76.49832  ? 307 PHE   B CA  1 
ATOM   4140 C C   . PHE   B 2 214 ? 17.68803 -14.67162 -36.70128 1.000 76.45400  ? 307 PHE   B C   1 
ATOM   4141 O O   . PHE   B 2 214 ? 16.45972 -14.65284 -36.57807 1.000 86.31408  ? 307 PHE   B O   1 
ATOM   4142 C CB  . PHE   B 2 214 ? 18.30511 -14.99507 -34.29983 1.000 69.81389  ? 307 PHE   B CB  1 
ATOM   4143 C CG  . PHE   B 2 214 ? 18.78523 -15.95221 -33.24775 1.000 69.53540  ? 307 PHE   B CG  1 
ATOM   4144 C CD1 . PHE   B 2 214 ? 20.09096 -15.90196 -32.78989 1.000 67.92401  ? 307 PHE   B CD1 1 
ATOM   4145 C CD2 . PHE   B 2 214 ? 17.93250 -16.90992 -32.72373 1.000 72.30541  ? 307 PHE   B CD2 1 
ATOM   4146 C CE1 . PHE   B 2 214 ? 20.53733 -16.78631 -31.82462 1.000 74.41092  ? 307 PHE   B CE1 1 
ATOM   4147 C CE2 . PHE   B 2 214 ? 18.37207 -17.79681 -31.75861 1.000 74.91829  ? 307 PHE   B CE2 1 
ATOM   4148 C CZ  . PHE   B 2 214 ? 19.67623 -17.73487 -31.30852 1.000 73.62457  ? 307 PHE   B CZ  1 
ATOM   4149 N N   . SER   B 2 215 ? 18.31926 -13.99678 -37.66209 1.000 81.04843  ? 308 SER   B N   1 
ATOM   4150 C CA  . SER   B 2 215 ? 17.59064 -13.20221 -38.64347 1.000 65.20053  ? 308 SER   B CA  1 
ATOM   4151 C C   . SER   B 2 215 ? 18.15942 -13.40800 -40.04174 1.000 71.76696  ? 308 SER   B C   1 
ATOM   4152 O O   . SER   B 2 215 ? 18.01400 -14.48689 -40.62575 1.000 65.14517  ? 308 SER   B O   1 
ATOM   4153 C CB  . SER   B 2 215 ? 17.62867 -11.71949 -38.26802 1.000 69.09646  ? 308 SER   B CB  1 
ATOM   4154 O OG  . SER   B 2 215 ? 18.96116 -11.24252 -38.20924 1.000 73.65484  ? 308 SER   B OG  1 
ATOM   4155 N N   . SER   B 2 216 ? 18.80867 -12.38123 -40.58425 1.000 68.61121  ? 309 SER   B N   1 
ATOM   4156 C CA  . SER   B 2 216 ? 19.34808 -12.44232 -41.93577 1.000 77.56108  ? 309 SER   B CA  1 
ATOM   4157 C C   . SER   B 2 216 ? 20.44121 -11.39307 -42.07404 1.000 73.98580  ? 309 SER   B C   1 
ATOM   4158 O O   . SER   B 2 216 ? 20.61263 -10.52615 -41.21390 1.000 70.70384  ? 309 SER   B O   1 
ATOM   4159 C CB  . SER   B 2 216 ? 18.25326 -12.22551 -42.98391 1.000 73.52997  ? 309 SER   B CB  1 
ATOM   4160 O OG  . SER   B 2 216 ? 17.68657 -10.93369 -42.85123 1.000 76.06888  ? 309 SER   B OG  1 
ATOM   4161 N N   . SER   B 2 217 ? 21.17932 -11.48119 -43.18335 1.000 78.59454  ? 310 SER   B N   1 
ATOM   4162 C CA  . SER   B 2 217 ? 22.24006 -10.51385 -43.44297 1.000 77.20265  ? 310 SER   B CA  1 
ATOM   4163 C C   . SER   B 2 217 ? 21.67824 -9.13633  -43.77029 1.000 78.60434  ? 310 SER   B C   1 
ATOM   4164 O O   . SER   B 2 217 ? 22.33300 -8.12258  -43.50170 1.000 72.95646  ? 310 SER   B O   1 
ATOM   4165 C CB  . SER   B 2 217 ? 23.13644 -11.00917 -44.57888 1.000 95.64402  ? 310 SER   B CB  1 
ATOM   4166 O OG  . SER   B 2 217 ? 22.38389 -11.26542 -45.75217 1.000 91.64917  ? 310 SER   B OG  1 
ATOM   4167 N N   . GLU   B 2 218 ? 20.47485 -9.07638  -44.34605 1.000 77.67710  ? 311 GLU   B N   1 
ATOM   4168 C CA  . GLU   B 2 218 ? 19.86100 -7.78430  -44.63578 1.000 76.56038  ? 311 GLU   B CA  1 
ATOM   4169 C C   . GLU   B 2 218 ? 19.43494 -7.07895  -43.35497 1.000 69.87012  ? 311 GLU   B C   1 
ATOM   4170 O O   . GLU   B 2 218 ? 19.67569 -5.87695  -43.19144 1.000 76.93841  ? 311 GLU   B O   1 
ATOM   4171 C CB  . GLU   B 2 218 ? 18.66574 -7.96314  -45.57410 1.000 84.55593  ? 311 GLU   B CB  1 
ATOM   4172 C CG  . GLU   B 2 218 ? 19.02440 -8.44734  -46.97422 1.000 79.41397  ? 311 GLU   B CG  1 
ATOM   4173 C CD  . GLU   B 2 218 ? 19.29942 -9.93887  -47.03315 1.000 95.22083  ? 311 GLU   B CD  1 
ATOM   4174 O OE1 . GLU   B 2 218 ? 19.03436 -10.63540 -46.03013 1.000 94.53461  ? 311 GLU   B OE1 1 
ATOM   4175 O OE2 . GLU   B 2 218 ? 19.78137 -10.41433 -48.08314 1.000 104.97971 ? 311 GLU   B OE2 1 
ATOM   4176 N N   . LEU   B 2 219 ? 18.79863 -7.80936  -42.43615 1.000 76.13216  ? 312 LEU   B N   1 
ATOM   4177 C CA  . LEU   B 2 219 ? 18.42058 -7.22059  -41.15569 1.000 64.18667  ? 312 LEU   B CA  1 
ATOM   4178 C C   . LEU   B 2 219 ? 19.65221 -6.84297  -40.34388 1.000 67.24994  ? 312 LEU   B C   1 
ATOM   4179 O O   . LEU   B 2 219 ? 19.67865 -5.78795  -39.69944 1.000 66.11717  ? 312 LEU   B O   1 
ATOM   4180 C CB  . LEU   B 2 219 ? 17.53144 -8.19375  -40.37808 1.000 76.73339  ? 312 LEU   B CB  1 
ATOM   4181 C CG  . LEU   B 2 219 ? 16.83695 -7.72576  -39.09441 1.000 65.70577  ? 312 LEU   B CG  1 
ATOM   4182 C CD1 . LEU   B 2 219 ? 17.70554 -7.95468  -37.86457 1.000 69.40510  ? 312 LEU   B CD1 1 
ATOM   4183 C CD2 . LEU   B 2 219 ? 16.42877 -6.26244  -39.20459 1.000 75.56094  ? 312 LEU   B CD2 1 
ATOM   4184 N N   . MET   B 2 220 ? 20.67946 -7.69473  -40.36285 1.000 70.59064  ? 313 MET   B N   1 
ATOM   4185 C CA  . MET   B 2 220 ? 21.91473 -7.39371  -39.64637 1.000 73.59250  ? 313 MET   B CA  1 
ATOM   4186 C C   . MET   B 2 220 ? 22.53549 -6.09860  -40.15110 1.000 73.61108  ? 313 MET   B C   1 
ATOM   4187 O O   . MET   B 2 220 ? 22.94784 -5.24282  -39.36046 1.000 71.70589  ? 313 MET   B O   1 
ATOM   4188 C CB  . MET   B 2 220 ? 22.89446 -8.56112  -39.79284 1.000 75.63799  ? 313 MET   B CB  1 
ATOM   4189 C CG  . MET   B 2 220 ? 24.26507 -8.35434  -39.15023 1.000 79.67152  ? 313 MET   B CG  1 
ATOM   4190 S SD  . MET   B 2 220 ? 25.44891 -7.44781  -40.17392 1.000 78.94861  ? 313 MET   B SD  1 
ATOM   4191 C CE  . MET   B 2 220 ? 25.20290 -8.23572  -41.76346 1.000 88.40883  ? 313 MET   B CE  1 
ATOM   4192 N N   . GLN   B 2 221 ? 22.60283 -5.93602  -41.47337 1.000 76.76341  ? 314 GLN   B N   1 
ATOM   4193 C CA  . GLN   B 2 221 ? 23.26925 -4.77275  -42.04641 1.000 81.00094  ? 314 GLN   B CA  1 
ATOM   4194 C C   . GLN   B 2 221 ? 22.48462 -3.49085  -41.80023 1.000 70.56103  ? 314 GLN   B C   1 
ATOM   4195 O O   . GLN   B 2 221 ? 23.08472 -2.42288  -41.63338 1.000 76.31789  ? 314 GLN   B O   1 
ATOM   4196 C CB  . GLN   B 2 221 ? 23.48748 -4.98961  -43.54393 1.000 76.04637  ? 314 GLN   B CB  1 
ATOM   4197 C CG  . GLN   B 2 221 ? 24.41458 -3.98427  -44.19900 1.000 74.69654  ? 314 GLN   B CG  1 
ATOM   4198 C CD  . GLN   B 2 221 ? 24.78384 -4.38254  -45.61207 1.000 82.50018  ? 314 GLN   B CD  1 
ATOM   4199 O OE1 . GLN   B 2 221 ? 24.18554 -5.29160  -46.18834 1.000 86.90036  ? 314 GLN   B OE1 1 
ATOM   4200 N NE2 . GLN   B 2 221 ? 25.77859 -3.70902  -46.17668 1.000 91.03204  ? 314 GLN   B NE2 1 
ATOM   4201 N N   . LYS   B 2 222 ? 21.15209 -3.57294  -41.76821 1.000 72.28979  ? 315 LYS   B N   1 
ATOM   4202 C CA  . LYS   B 2 222 ? 20.34609 -2.37381  -41.56381 1.000 73.76543  ? 315 LYS   B CA  1 
ATOM   4203 C C   . LYS   B 2 222 ? 20.48786 -1.83265  -40.14775 1.000 80.02073  ? 315 LYS   B C   1 
ATOM   4204 O O   . LYS   B 2 222 ? 20.38514 -0.61874  -39.93662 1.000 88.14787  ? 315 LYS   B O   1 
ATOM   4205 C CB  . LYS   B 2 222 ? 18.87621 -2.66595  -41.86922 1.000 80.27758  ? 315 LYS   B CB  1 
ATOM   4206 C CG  . LYS   B 2 222 ? 18.00586 -1.42095  -41.96322 1.000 91.85849  ? 315 LYS   B CG  1 
ATOM   4207 C CD  . LYS   B 2 222 ? 16.53111 -1.76909  -42.09973 1.000 99.36117  ? 315 LYS   B CD  1 
ATOM   4208 C CE  . LYS   B 2 222 ? 15.98478 -2.37794  -40.81728 1.000 103.67415 ? 315 LYS   B CE  1 
ATOM   4209 N NZ  . LYS   B 2 222 ? 14.51594 -2.61580  -40.89441 1.000 99.19008  ? 315 LYS   B NZ  1 
ATOM   4210 N N   . VAL   B 2 223 ? 20.72754 -2.70530  -39.17237 1.000 77.24713  ? 316 VAL   B N   1 
ATOM   4211 C CA  . VAL   B 2 223 ? 20.77029 -2.29819  -37.77539 1.000 83.62328  ? 316 VAL   B CA  1 
ATOM   4212 C C   . VAL   B 2 223 ? 22.18532 -2.24716  -37.21238 1.000 73.43686  ? 316 VAL   B C   1 
ATOM   4213 O O   . VAL   B 2 223 ? 22.38669 -1.63008  -36.15535 1.000 66.84918  ? 316 VAL   B O   1 
ATOM   4214 C CB  . VAL   B 2 223 ? 19.88545 -3.21243  -36.90397 1.000 83.11377  ? 316 VAL   B CB  1 
ATOM   4215 C CG1 . VAL   B 2 223 ? 18.59979 -3.54417  -37.63594 1.000 75.17637  ? 316 VAL   B CG1 1 
ATOM   4216 C CG2 . VAL   B 2 223 ? 20.63208 -4.47543  -36.53513 1.000 62.84430  ? 316 VAL   B CG2 1 
ATOM   4217 N N   . SER   B 2 224 ? 23.16700 -2.86901  -37.86962 1.000 75.48948  ? 317 SER   B N   1 
ATOM   4218 C CA  . SER   B 2 224 ? 24.54738 -2.82002  -37.41072 1.000 77.39879  ? 317 SER   B CA  1 
ATOM   4219 C C   . SER   B 2 224 ? 25.45160 -1.97296  -38.29066 1.000 85.39532  ? 317 SER   B C   1 
ATOM   4220 O O   . SER   B 2 224 ? 26.47563 -1.48488  -37.80297 1.000 80.44901  ? 317 SER   B O   1 
ATOM   4221 C CB  . SER   B 2 224 ? 25.13688 -4.23581  -37.32104 1.000 74.24415  ? 317 SER   B CB  1 
ATOM   4222 O OG  . SER   B 2 224 ? 25.23864 -4.83092  -38.60466 1.000 79.83968  ? 317 SER   B OG  1 
ATOM   4223 N N   . GLY   B 2 225 ? 25.10258 -1.78490  -39.56128 1.000 79.54452  ? 318 GLY   B N   1 
ATOM   4224 C CA  . GLY   B 2 225 ? 25.92676 -1.03162  -40.47890 1.000 87.48386  ? 318 GLY   B CA  1 
ATOM   4225 C C   . GLY   B 2 225 ? 27.12806 -1.77291  -41.01905 1.000 94.91499  ? 318 GLY   B C   1 
ATOM   4226 O O   . GLY   B 2 225 ? 27.84837 -1.21912  -41.85950 1.000 108.41196 ? 318 GLY   B O   1 
ATOM   4227 N N   . TYR   B 2 226 ? 27.36699 -3.00312  -40.57473 1.000 82.75916  ? 319 TYR   B N   1 
ATOM   4228 C CA  . TYR   B 2 226 ? 28.53138 -3.76423  -40.99979 1.000 83.04248  ? 319 TYR   B CA  1 
ATOM   4229 C C   . TYR   B 2 226 ? 28.18887 -4.62795  -42.20612 1.000 99.58896  ? 319 TYR   B C   1 
ATOM   4230 O O   . TYR   B 2 226 ? 27.14027 -5.27854  -42.24516 1.000 91.29930  ? 319 TYR   B O   1 
ATOM   4231 C CB  . TYR   B 2 226 ? 29.05061 -4.63728  -39.85568 1.000 88.83330  ? 319 TYR   B CB  1 
ATOM   4232 C CG  . TYR   B 2 226 ? 29.46881 -3.85334  -38.62868 1.000 93.09832  ? 319 TYR   B CG  1 
ATOM   4233 C CD1 . TYR   B 2 226 ? 29.85968 -2.52283  -38.72818 1.000 98.70414  ? 319 TYR   B CD1 1 
ATOM   4234 C CD2 . TYR   B 2 226 ? 29.46865 -4.44176  -37.37094 1.000 88.36089  ? 319 TYR   B CD2 1 
ATOM   4235 C CE1 . TYR   B 2 226 ? 30.23978 -1.80156  -37.60973 1.000 99.12756  ? 319 TYR   B CE1 1 
ATOM   4236 C CE2 . TYR   B 2 226 ? 29.85008 -3.72878  -36.24656 1.000 90.70335  ? 319 TYR   B CE2 1 
ATOM   4237 C CZ  . TYR   B 2 226 ? 30.23319 -2.40917  -36.37249 1.000 82.23227  ? 319 TYR   B CZ  1 
ATOM   4238 O OH  . TYR   B 2 226 ? 30.61118 -1.69469  -35.25896 1.000 89.54459  ? 319 TYR   B OH  1 
ATOM   4239 N N   . GLN   B 2 227 ? 29.08061 -4.62295  -43.19267 1.000 98.41967  ? 320 GLN   B N   1 
ATOM   4240 C CA  . GLN   B 2 227 ? 28.88600 -5.42465  -44.38840 1.000 97.18462  ? 320 GLN   B CA  1 
ATOM   4241 C C   . GLN   B 2 227 ? 29.04167 -6.90785  -44.05960 1.000 98.03264  ? 320 GLN   B C   1 
ATOM   4242 O O   . GLN   B 2 227 ? 29.59015 -7.28895  -43.02155 1.000 101.20948 ? 320 GLN   B O   1 
ATOM   4243 C CB  . GLN   B 2 227 ? 29.87994 -5.00727  -45.47500 1.000 105.37588 ? 320 GLN   B CB  1 
ATOM   4244 C CG  . GLN   B 2 227 ? 29.47763 -5.39670  -46.89093 1.000 122.19703 ? 320 GLN   B CG  1 
ATOM   4245 C CD  . GLN   B 2 227 ? 30.49706 -4.96476  -47.92793 1.000 129.10405 ? 320 GLN   B CD  1 
ATOM   4246 O OE1 . GLN   B 2 227 ? 30.34952 -5.24990  -49.11648 1.000 124.82844 ? 320 GLN   B OE1 1 
ATOM   4247 N NE2 . GLN   B 2 227 ? 31.53961 -4.27316  -47.48141 1.000 131.62078 ? 320 GLN   B NE2 1 
ATOM   4248 N N   . TRP   B 2 228 ? 28.53717 -7.75173  -44.96305 1.000 87.33272  ? 321 TRP   B N   1 
ATOM   4249 C CA  . TRP   B 2 228 ? 28.62415 -9.19362  -44.75822 1.000 94.12991  ? 321 TRP   B CA  1 
ATOM   4250 C C   . TRP   B 2 228 ? 30.06940 -9.67211  -44.69795 1.000 105.06310 ? 321 TRP   B C   1 
ATOM   4251 O O   . TRP   B 2 228 ? 30.37664 -10.62577 -43.97324 1.000 107.59855 ? 321 TRP   B O   1 
ATOM   4252 C CB  . TRP   B 2 228 ? 27.86890 -9.92726  -45.86601 1.000 84.35964  ? 321 TRP   B CB  1 
ATOM   4253 C CG  . TRP   B 2 228 ? 28.17277 -11.38864 -45.91385 1.000 91.31881  ? 321 TRP   B CG  1 
ATOM   4254 C CD1 . TRP   B 2 228 ? 28.90239 -12.04432 -46.86249 1.000 99.87286  ? 321 TRP   B CD1 1 
ATOM   4255 C CD2 . TRP   B 2 228 ? 27.77216 -12.37823 -44.96036 1.000 88.01870  ? 321 TRP   B CD2 1 
ATOM   4256 N NE1 . TRP   B 2 228 ? 28.97210 -13.38357 -46.56398 1.000 103.44744 ? 321 TRP   B NE1 1 
ATOM   4257 C CE2 . TRP   B 2 228 ? 28.28696 -13.61422 -45.40013 1.000 93.72859  ? 321 TRP   B CE2 1 
ATOM   4258 C CE3 . TRP   B 2 228 ? 27.02400 -12.34022 -43.78019 1.000 77.05703  ? 321 TRP   B CE3 1 
ATOM   4259 C CZ2 . TRP   B 2 228 ? 28.07781 -14.80049 -44.70149 1.000 93.46299  ? 321 TRP   B CZ2 1 
ATOM   4260 C CZ3 . TRP   B 2 228 ? 26.81783 -13.51826 -43.08830 1.000 85.98552  ? 321 TRP   B CZ3 1 
ATOM   4261 C CH2 . TRP   B 2 228 ? 27.34292 -14.73171 -43.55047 1.000 91.79152  ? 321 TRP   B CH2 1 
ATOM   4262 N N   . CYS   B 2 229 ? 30.96859 -9.02806  -45.44575 1.000 116.05117 ? 322 CYS   B N   1 
ATOM   4263 C CA  . CYS   B 2 229 ? 32.37364 -9.41781  -45.42381 1.000 117.17926 ? 322 CYS   B CA  1 
ATOM   4264 C C   . CYS   B 2 229 ? 33.03544 -9.12913  -44.08241 1.000 112.26145 ? 322 CYS   B C   1 
ATOM   4265 O O   . CYS   B 2 229 ? 34.03644 -9.77255  -43.74850 1.000 110.34363 ? 322 CYS   B O   1 
ATOM   4266 C CB  . CYS   B 2 229 ? 33.13255 -8.70451  -46.54382 1.000 121.72022 ? 322 CYS   B CB  1 
ATOM   4267 S SG  . CYS   B 2 229 ? 33.01363 -6.90012  -46.49113 1.000 128.90377 ? 322 CYS   B SG  1 
ATOM   4268 N N   . ASP   B 2 230 ? 32.50006 -8.18192  -43.30818 1.000 110.23784 ? 323 ASP   B N   1 
ATOM   4269 C CA  . ASP   B 2 230 ? 33.08697 -7.86859  -42.00919 1.000 112.24614 ? 323 ASP   B CA  1 
ATOM   4270 C C   . ASP   B 2 230 ? 32.80548 -8.96811  -40.99340 1.000 102.69414 ? 323 ASP   B C   1 
ATOM   4271 O O   . ASP   B 2 230 ? 33.67064 -9.30241  -40.17455 1.000 93.05069  ? 323 ASP   B O   1 
ATOM   4272 C CB  . ASP   B 2 230 ? 32.55370 -6.52972  -41.49802 1.000 93.50314  ? 323 ASP   B CB  1 
ATOM   4273 C CG  . ASP   B 2 230 ? 32.79315 -5.39412  -42.47138 1.000 105.52348 ? 323 ASP   B CG  1 
ATOM   4274 O OD1 . ASP   B 2 230 ? 33.68982 -5.52330  -43.33159 1.000 122.04163 ? 323 ASP   B OD1 1 
ATOM   4275 O OD2 . ASP   B 2 230 ? 32.08625 -4.36875  -42.37152 1.000 95.15751  ? 323 ASP   B OD2 1 
ATOM   4276 N N   . ILE   B 2 231 ? 31.60028 -9.54179  -41.02927 1.000 93.23064  ? 324 ILE   B N   1 
ATOM   4277 C CA  . ILE   B 2 231 ? 31.18035 -10.51451 -40.02926 1.000 93.14191  ? 324 ILE   B CA  1 
ATOM   4278 C C   . ILE   B 2 231 ? 31.28214 -11.94703 -40.52557 1.000 91.34685  ? 324 ILE   B C   1 
ATOM   4279 O O   . ILE   B 2 231 ? 31.03986 -12.87811 -39.74522 1.000 82.66498  ? 324 ILE   B O   1 
ATOM   4280 C CB  . ILE   B 2 231 ? 29.74365 -10.22693 -39.54834 1.000 87.74214  ? 324 ILE   B CB  1 
ATOM   4281 C CG1 . ILE   B 2 231 ? 28.72675 -10.69021 -40.59251 1.000 90.59156  ? 324 ILE   B CG1 1 
ATOM   4282 C CG2 . ILE   B 2 231 ? 29.56628 -8.74370  -39.26026 1.000 81.03303  ? 324 ILE   B CG2 1 
ATOM   4283 C CD1 . ILE   B 2 231 ? 27.29804 -10.66228 -40.10018 1.000 85.96293  ? 324 ILE   B CD1 1 
ATOM   4284 N N   . GLU   B 2 232 ? 31.63387 -12.15597 -41.79834 1.000 87.87934  ? 325 GLU   B N   1 
ATOM   4285 C CA  . GLU   B 2 232 ? 31.69219 -13.51254 -42.33561 1.000 89.85960  ? 325 GLU   B CA  1 
ATOM   4286 C C   . GLU   B 2 232 ? 32.68169 -14.37289 -41.56162 1.000 88.58934  ? 325 GLU   B C   1 
ATOM   4287 O O   . GLU   B 2 232 ? 32.40870 -15.54648 -41.28079 1.000 90.24151  ? 325 GLU   B O   1 
ATOM   4288 C CB  . GLU   B 2 232 ? 32.06082 -13.48142 -43.81915 1.000 95.63873  ? 325 GLU   B CB  1 
ATOM   4289 C CG  . GLU   B 2 232 ? 32.21770 -14.86365 -44.43613 1.000 94.24730  ? 325 GLU   B CG  1 
ATOM   4290 C CD  . GLU   B 2 232 ? 32.66053 -14.81374 -45.88378 1.000 104.23659 ? 325 GLU   B CD  1 
ATOM   4291 O OE1 . GLU   B 2 232 ? 32.89474 -13.69901 -46.39652 1.000 104.44020 ? 325 GLU   B OE1 1 
ATOM   4292 O OE2 . GLU   B 2 232 ? 32.77392 -15.88979 -46.50862 1.000 115.58941 ? 325 GLU   B OE2 1 
ATOM   4293 N N   . ASN   B 2 233 ? 33.83740 -13.80731 -41.20675 1.000 84.09242  ? 326 ASN   B N   1 
ATOM   4294 C CA  . ASN   B 2 233 ? 34.80438 -14.55637 -40.41264 1.000 86.32272  ? 326 ASN   B CA  1 
ATOM   4295 C C   . ASN   B 2 233 ? 34.23441 -14.89572 -39.04088 1.000 91.44850  ? 326 ASN   B C   1 
ATOM   4296 O O   . ASN   B 2 233 ? 34.39948 -16.01961 -38.55082 1.000 82.15160  ? 326 ASN   B O   1 
ATOM   4297 C CB  . ASN   B 2 233 ? 36.10252 -13.75928 -40.27981 1.000 104.11434 ? 326 ASN   B CB  1 
ATOM   4298 C CG  . ASN   B 2 233 ? 37.28187 -14.62680 -39.88489 1.000 108.27480 ? 326 ASN   B CG  1 
ATOM   4299 O OD1 . ASN   B 2 233 ? 37.32208 -15.81787 -40.19544 1.000 95.02442  ? 326 ASN   B OD1 1 
ATOM   4300 N ND2 . ASN   B 2 233 ? 38.25051 -14.03251 -39.19595 1.000 110.56929 ? 326 ASN   B ND2 1 
ATOM   4301 N N   . CYS   B 2 234 ? 33.54320 -13.93967 -38.41340 1.000 79.66532  ? 327 CYS   B N   1 
ATOM   4302 C CA  . CYS   B 2 234 ? 32.93479 -14.19939 -37.11265 1.000 79.97873  ? 327 CYS   B CA  1 
ATOM   4303 C C   . CYS   B 2 234 ? 31.75653 -15.15842 -37.23219 1.000 84.67870  ? 327 CYS   B C   1 
ATOM   4304 O O   . CYS   B 2 234 ? 31.58479 -16.04547 -36.38740 1.000 82.57078  ? 327 CYS   B O   1 
ATOM   4305 C CB  . CYS   B 2 234 ? 32.49361 -12.88624 -36.46843 1.000 81.12838  ? 327 CYS   B CB  1 
ATOM   4306 S SG  . CYS   B 2 234 ? 31.78135 -13.06178 -34.81396 1.000 79.29090  ? 327 CYS   B SG  1 
ATOM   4307 N N   . VAL   B 2 235 ? 30.93201 -14.99439 -38.27074 1.000 83.47676  ? 328 VAL   B N   1 
ATOM   4308 C CA  . VAL   B 2 235 ? 29.79540 -15.89125 -38.46498 1.000 69.41906  ? 328 VAL   B CA  1 
ATOM   4309 C C   . VAL   B 2 235 ? 30.27547 -17.32403 -38.65210 1.000 88.94707  ? 328 VAL   B C   1 
ATOM   4310 O O   . VAL   B 2 235 ? 29.73407 -18.25901 -38.04894 1.000 90.90321  ? 328 VAL   B O   1 
ATOM   4311 C CB  . VAL   B 2 235 ? 28.93428 -15.41892 -39.65192 1.000 90.42874  ? 328 VAL   B CB  1 
ATOM   4312 C CG1 . VAL   B 2 235 ? 27.98413 -16.52158 -40.09547 1.000 86.98632  ? 328 VAL   B CG1 1 
ATOM   4313 C CG2 . VAL   B 2 235 ? 28.15439 -14.16853 -39.27584 1.000 76.33417  ? 328 VAL   B CG2 1 
ATOM   4314 N N   . LYS   B 2 236 ? 31.31015 -17.51822 -39.47602 1.000 92.04811  ? 329 LYS   B N   1 
ATOM   4315 C CA  . LYS   B 2 236 ? 31.85033 -18.85870 -39.67797 1.000 93.37593  ? 329 LYS   B CA  1 
ATOM   4316 C C   . LYS   B 2 236 ? 32.44554 -19.42203 -38.39407 1.000 94.41741  ? 329 LYS   B C   1 
ATOM   4317 O O   . LYS   B 2 236 ? 32.39873 -20.63698 -38.17050 1.000 98.35272  ? 329 LYS   B O   1 
ATOM   4318 C CB  . LYS   B 2 236 ? 32.89939 -18.84585 -40.79080 1.000 108.77149 ? 329 LYS   B CB  1 
ATOM   4319 C CG  . LYS   B 2 236 ? 33.29830 -20.23353 -41.27594 1.000 116.58924 ? 329 LYS   B CG  1 
ATOM   4320 C CD  . LYS   B 2 236 ? 34.32719 -20.16870 -42.39457 1.000 119.12925 ? 329 LYS   B CD  1 
ATOM   4321 C CE  . LYS   B 2 236 ? 35.65191 -19.61020 -41.90075 1.000 124.12295 ? 329 LYS   B CE  1 
ATOM   4322 N NZ  . LYS   B 2 236 ? 36.69424 -19.63991 -42.96396 1.000 122.13476 ? 329 LYS   B NZ  1 
ATOM   4323 N N   . TRP   B 2 237 ? 33.00700 -18.56286 -37.53971 1.000 93.68097  ? 330 TRP   B N   1 
ATOM   4324 C CA  . TRP   B 2 237 ? 33.49740 -19.03299 -36.24809 1.000 95.64384  ? 330 TRP   B CA  1 
ATOM   4325 C C   . TRP   B 2 237 ? 32.34472 -19.32937 -35.29780 1.000 92.12201  ? 330 TRP   B C   1 
ATOM   4326 O O   . TRP   B 2 237 ? 32.39359 -20.30238 -34.53654 1.000 86.58036  ? 330 TRP   B O   1 
ATOM   4327 C CB  . TRP   B 2 237 ? 34.44623 -18.00481 -35.63274 1.000 92.50205  ? 330 TRP   B CB  1 
ATOM   4328 C CG  . TRP   B 2 237 ? 34.78049 -18.29968 -34.20182 1.000 98.18981  ? 330 TRP   B CG  1 
ATOM   4329 C CD1 . TRP   B 2 237 ? 35.75580 -19.13690 -33.74251 1.000 99.44173  ? 330 TRP   B CD1 1 
ATOM   4330 C CD2 . TRP   B 2 237 ? 34.13227 -17.76442 -33.04146 1.000 97.21244  ? 330 TRP   B CD2 1 
ATOM   4331 N NE1 . TRP   B 2 237 ? 35.75665 -19.15432 -32.36837 1.000 98.56254  ? 330 TRP   B NE1 1 
ATOM   4332 C CE2 . TRP   B 2 237 ? 34.76922 -18.32015 -31.91363 1.000 105.20016 ? 330 TRP   B CE2 1 
ATOM   4333 C CE3 . TRP   B 2 237 ? 33.07521 -16.86940 -32.84679 1.000 94.30314  ? 330 TRP   B CE3 1 
ATOM   4334 C CZ2 . TRP   B 2 237 ? 34.38539 -18.00842 -30.61052 1.000 102.80835 ? 330 TRP   B CZ2 1 
ATOM   4335 C CZ3 . TRP   B 2 237 ? 32.69575 -16.56134 -31.55232 1.000 83.79348  ? 330 TRP   B CZ3 1 
ATOM   4336 C CH2 . TRP   B 2 237 ? 33.34825 -17.13042 -30.45172 1.000 90.93590  ? 330 TRP   B CH2 1 
ATOM   4337 N N   . MET   B 2 238 ? 31.30152 -18.50056 -35.32589 1.000 86.67081  ? 331 MET   B N   1 
ATOM   4338 C CA  . MET   B 2 238 ? 30.11990 -18.70790 -34.49741 1.000 84.23001  ? 331 MET   B CA  1 
ATOM   4339 C C   . MET   B 2 238 ? 29.24542 -19.85167 -35.00063 1.000 94.25546  ? 331 MET   B C   1 
ATOM   4340 O O   . MET   B 2 238 ? 28.24687 -20.18038 -34.35015 1.000 94.58080  ? 331 MET   B O   1 
ATOM   4341 C CB  . MET   B 2 238 ? 29.31547 -17.40722 -34.43308 1.000 75.42645  ? 331 MET   B CB  1 
ATOM   4342 C CG  . MET   B 2 238 ? 28.32116 -17.31819 -33.29113 1.000 82.49256  ? 331 MET   B CG  1 
ATOM   4343 S SD  . MET   B 2 238 ? 27.56491 -15.68693 -33.19069 1.000 81.85888  ? 331 MET   B SD  1 
ATOM   4344 C CE  . MET   B 2 238 ? 28.96427 -14.69765 -32.66939 1.000 73.85342  ? 331 MET   B CE  1 
ATOM   4345 N N   . VAL   B 2 239 ? 29.61091 -20.46370 -36.13088 1.000 96.31103  ? 332 VAL   B N   1 
ATOM   4346 C CA  . VAL   B 2 239 ? 28.80283 -21.54310 -36.70241 1.000 103.69962 ? 332 VAL   B CA  1 
ATOM   4347 C C   . VAL   B 2 239 ? 28.53079 -22.66627 -35.70208 1.000 103.18268 ? 332 VAL   B C   1 
ATOM   4348 O O   . VAL   B 2 239 ? 27.35722 -23.00526 -35.49731 1.000 98.35153  ? 332 VAL   B O   1 
ATOM   4349 C CB  . VAL   B 2 239 ? 29.44117 -22.04506 -38.00714 1.000 94.30767  ? 332 VAL   B CB  1 
ATOM   4350 C CG1 . VAL   B 2 239 ? 29.04758 -23.48825 -38.28777 1.000 95.14910  ? 332 VAL   B CG1 1 
ATOM   4351 C CG2 . VAL   B 2 239 ? 29.04922 -21.14834 -39.16428 1.000 100.89178 ? 332 VAL   B CG2 1 
ATOM   4352 N N   . PRO   B 2 240 ? 29.53551 -23.27401 -35.05299 1.000 101.00265 ? 333 PRO   B N   1 
ATOM   4353 C CA  . PRO   B 2 240 ? 29.21722 -24.37861 -34.13069 1.000 104.78387 ? 333 PRO   B CA  1 
ATOM   4354 C C   . PRO   B 2 240 ? 28.35715 -23.95329 -32.95342 1.000 104.70809 ? 333 PRO   B C   1 
ATOM   4355 O O   . PRO   B 2 240 ? 27.44779 -24.69313 -32.55761 1.000 96.72094  ? 333 PRO   B O   1 
ATOM   4356 C CB  . PRO   B 2 240 ? 30.60177 -24.86515 -33.67768 1.000 111.98343 ? 333 PRO   B CB  1 
ATOM   4357 C CG  . PRO   B 2 240 ? 31.54652 -24.37576 -34.71516 1.000 110.93084 ? 333 PRO   B CG  1 
ATOM   4358 C CD  . PRO   B 2 240 ? 30.99094 -23.06151 -35.14889 1.000 104.33425 ? 333 PRO   B CD  1 
ATOM   4359 N N   . PHE   B 2 241 ? 28.61586 -22.77316 -32.38449 1.000 103.40492 ? 334 PHE   B N   1 
ATOM   4360 C CA  . PHE   B 2 241 ? 27.83384 -22.31429 -31.24137 1.000 102.70994 ? 334 PHE   B CA  1 
ATOM   4361 C C   . PHE   B 2 241 ? 26.37888 -22.06475 -31.61796 1.000 88.39945  ? 334 PHE   B C   1 
ATOM   4362 O O   . PHE   B 2 241 ? 25.48063 -22.28104 -30.79595 1.000 84.30896  ? 334 PHE   B O   1 
ATOM   4363 C CB  . PHE   B 2 241 ? 28.45105 -21.04238 -30.65759 1.000 88.74896  ? 334 PHE   B CB  1 
ATOM   4364 C CG  . PHE   B 2 241 ? 29.94481 -21.10661 -30.49794 1.000 90.99207  ? 334 PHE   B CG  1 
ATOM   4365 C CD1 . PHE   B 2 241 ? 30.51138 -21.62620 -29.34609 1.000 96.62630  ? 334 PHE   B CD1 1 
ATOM   4366 C CD2 . PHE   B 2 241 ? 30.78272 -20.63788 -31.49768 1.000 94.12532  ? 334 PHE   B CD2 1 
ATOM   4367 C CE1 . PHE   B 2 241 ? 31.88539 -21.68325 -29.19703 1.000 95.09270  ? 334 PHE   B CE1 1 
ATOM   4368 C CE2 . PHE   B 2 241 ? 32.15700 -20.69301 -31.35451 1.000 99.35923  ? 334 PHE   B CE2 1 
ATOM   4369 C CZ  . PHE   B 2 241 ? 32.70854 -21.21543 -30.20237 1.000 98.08260  ? 334 PHE   B CZ  1 
ATOM   4370 N N   . ALA   B 2 242 ? 26.12733 -21.61769 -32.84997 1.000 87.71993  ? 335 ALA   B N   1 
ATOM   4371 C CA  . ALA   B 2 242 ? 24.76179 -21.31016 -33.26220 1.000 92.83028  ? 335 ALA   B CA  1 
ATOM   4372 C C   . ALA   B 2 242 ? 23.90329 -22.56732 -33.34126 1.000 92.32477  ? 335 ALA   B C   1 
ATOM   4373 O O   . ALA   B 2 242 ? 22.73262 -22.55018 -32.94302 1.000 89.27599  ? 335 ALA   B O   1 
ATOM   4374 C CB  . ALA   B 2 242 ? 24.77195 -20.58099 -34.60565 1.000 91.81995  ? 335 ALA   B CB  1 
ATOM   4375 N N   . MET   B 2 243 ? 24.46441 -23.66952 -33.84567 1.000 78.19657  ? 336 MET   B N   1 
ATOM   4376 C CA  . MET   B 2 243 ? 23.66529 -24.87820 -34.02158 1.000 95.74439  ? 336 MET   B CA  1 
ATOM   4377 C C   . MET   B 2 243 ? 23.37386 -25.57380 -32.70015 1.000 95.86839  ? 336 MET   B C   1 
ATOM   4378 O O   . MET   B 2 243 ? 22.30111 -26.16754 -32.54371 1.000 94.19001  ? 336 MET   B O   1 
ATOM   4379 C CB  . MET   B 2 243 ? 24.36045 -25.84142 -34.97905 1.000 97.90403  ? 336 MET   B CB  1 
ATOM   4380 C CG  . MET   B 2 243 ? 24.02793 -25.59495 -36.43718 1.000 112.30887 ? 336 MET   B CG  1 
ATOM   4381 S SD  . MET   B 2 243 ? 22.27121 -25.74483 -36.83206 1.000 126.95154 ? 336 MET   B SD  1 
ATOM   4382 C CE  . MET   B 2 243 ? 21.77832 -24.02971 -36.96508 1.000 99.15437  ? 336 MET   B CE  1 
ATOM   4383 N N   . VAL   B 2 244 ? 24.30686 -25.52460 -31.74711 1.000 95.72887  ? 337 VAL   B N   1 
ATOM   4384 C CA  . VAL   B 2 244 ? 24.05721 -26.13332 -30.44374 1.000 87.03227  ? 337 VAL   B CA  1 
ATOM   4385 C C   . VAL   B 2 244 ? 22.85578 -25.47698 -29.77536 1.000 99.81917  ? 337 VAL   B C   1 
ATOM   4386 O O   . VAL   B 2 244 ? 22.06855 -26.13951 -29.08801 1.000 102.46749 ? 337 VAL   B O   1 
ATOM   4387 C CB  . VAL   B 2 244 ? 25.31813 -26.05062 -29.56418 1.000 110.48598 ? 337 VAL   B CB  1 
ATOM   4388 C CG1 . VAL   B 2 244 ? 25.07050 -26.71150 -28.22245 1.000 107.97104 ? 337 VAL   B CG1 1 
ATOM   4389 C CG2 . VAL   B 2 244 ? 26.49550 -26.70523 -30.26858 1.000 103.11450 ? 337 VAL   B CG2 1 
ATOM   4390 N N   . ILE   B 2 245 ? 22.68745 -24.16824 -29.97820 1.000 95.60711  ? 338 ILE   B N   1 
ATOM   4391 C CA  . ILE   B 2 245 ? 21.49704 -23.48569 -29.48176 1.000 98.94848  ? 338 ILE   B CA  1 
ATOM   4392 C C   . ILE   B 2 245 ? 20.26250 -23.93902 -30.25104 1.000 96.84625  ? 338 ILE   B C   1 
ATOM   4393 O O   . ILE   B 2 245 ? 19.18833 -24.13484 -29.66962 1.000 101.07969 ? 338 ILE   B O   1 
ATOM   4394 C CB  . ILE   B 2 245 ? 21.68551 -21.96038 -29.56375 1.000 91.26790  ? 338 ILE   B CB  1 
ATOM   4395 C CG1 . ILE   B 2 245 ? 22.88225 -21.52722 -28.71780 1.000 88.34208  ? 338 ILE   B CG1 1 
ATOM   4396 C CG2 . ILE   B 2 245 ? 20.42361 -21.24000 -29.11362 1.000 100.89465 ? 338 ILE   B CG2 1 
ATOM   4397 C CD1 . ILE   B 2 245 ? 22.72424 -21.83604 -27.24927 1.000 101.65577 ? 338 ILE   B CD1 1 
ATOM   4398 N N   . ARG   B 2 246 ? 20.39362 -24.11684 -31.56818 1.000 87.07849  ? 339 ARG   B N   1 
ATOM   4399 C CA  . ARG   B 2 246 ? 19.24955 -24.53135 -32.37347 1.000 91.37148  ? 339 ARG   B CA  1 
ATOM   4400 C C   . ARG   B 2 246 ? 18.84836 -25.97365 -32.09221 1.000 93.44884  ? 339 ARG   B C   1 
ATOM   4401 O O   . ARG   B 2 246 ? 17.66144 -26.30845 -32.17429 1.000 95.98780  ? 339 ARG   B O   1 
ATOM   4402 C CB  . ARG   B 2 246 ? 19.55584 -24.35283 -33.86043 1.000 94.71655  ? 339 ARG   B CB  1 
ATOM   4403 C CG  . ARG   B 2 246 ? 19.65742 -22.90747 -34.31695 1.000 93.48410  ? 339 ARG   B CG  1 
ATOM   4404 C CD  . ARG   B 2 246 ? 18.32602 -22.18890 -34.20060 1.000 89.06526  ? 339 ARG   B CD  1 
ATOM   4405 N NE  . ARG   B 2 246 ? 18.31046 -20.95377 -34.97487 1.000 81.11267  ? 339 ARG   B NE  1 
ATOM   4406 C CZ  . ARG   B 2 246 ? 17.35435 -20.03820 -34.90444 1.000 85.27293  ? 339 ARG   B CZ  1 
ATOM   4407 N NH1 . ARG   B 2 246 ? 16.32396 -20.17680 -34.08630 1.000 89.36090  ? 339 ARG   B NH1 1 
ATOM   4408 N NH2 . ARG   B 2 246 ? 17.43565 -18.95478 -35.67174 1.000 82.52262  ? 339 ARG   B NH2 1 
ATOM   4409 N N   . GLU   B 2 247 ? 19.81240 -26.83959 -31.76582 1.000 104.01427 ? 340 GLU   B N   1 
ATOM   4410 C CA  . GLU   B 2 247 ? 19.48601 -28.24024 -31.51196 1.000 94.64661  ? 340 GLU   B CA  1 
ATOM   4411 C C   . GLU   B 2 247 ? 18.66567 -28.39826 -30.23818 1.000 97.23294  ? 340 GLU   B C   1 
ATOM   4412 O O   . GLU   B 2 247 ? 17.75093 -29.22847 -30.18262 1.000 101.21381 ? 340 GLU   B O   1 
ATOM   4413 C CB  . GLU   B 2 247 ? 20.76219 -29.07740 -31.43052 1.000 100.37623 ? 340 GLU   B CB  1 
ATOM   4414 C CG  . GLU   B 2 247 ? 21.50637 -29.20811 -32.74584 1.000 109.30433 ? 340 GLU   B CG  1 
ATOM   4415 C CD  . GLU   B 2 247 ? 22.65419 -30.19590 -32.67364 1.000 126.37106 ? 340 GLU   B CD  1 
ATOM   4416 O OE1 . GLU   B 2 247 ? 22.63193 -31.07138 -31.78287 1.000 142.53058 ? 340 GLU   B OE1 1 
ATOM   4417 O OE2 . GLU   B 2 247 ? 23.57948 -30.09592 -33.50710 1.000 123.42958 ? 340 GLU   B OE2 1 
ATOM   4418 N N   . THR   B 2 248 ? 18.97565 -27.61460 -29.20572 1.000 95.60734  ? 341 THR   B N   1 
ATOM   4419 C CA  . THR   B 2 248 ? 18.25354 -27.70324 -27.94421 1.000 99.67544  ? 341 THR   B CA  1 
ATOM   4420 C C   . THR   B 2 248 ? 17.01703 -26.81736 -27.90044 1.000 112.46152 ? 341 THR   B C   1 
ATOM   4421 O O   . THR   B 2 248 ? 16.12755 -27.06130 -27.07703 1.000 115.05565 ? 341 THR   B O   1 
ATOM   4422 C CB  . THR   B 2 248 ? 19.17376 -27.33856 -26.77461 1.000 99.90654  ? 341 THR   B CB  1 
ATOM   4423 O OG1 . THR   B 2 248 ? 18.45695 -27.47701 -25.54172 1.000 123.87114 ? 341 THR   B OG1 1 
ATOM   4424 C CG2 . THR   B 2 248 ? 19.67058 -25.90515 -26.90684 1.000 106.55132 ? 341 THR   B CG2 1 
ATOM   4425 N N   . GLY   B 2 249 ? 16.93814 -25.80727 -28.75638 1.000 122.33249 ? 342 GLY   B N   1 
ATOM   4426 C CA  . GLY   B 2 249 ? 15.79775 -24.91472 -28.80875 1.000 114.51913 ? 342 GLY   B CA  1 
ATOM   4427 C C   . GLY   B 2 249 ? 16.10528 -23.56490 -28.18245 1.000 121.63909 ? 342 GLY   B C   1 
ATOM   4428 O O   . GLY   B 2 249 ? 17.18598 -23.31877 -27.64329 1.000 118.31282 ? 342 GLY   B O   1 
ATOM   4429 N N   . SER   B 2 250 ? 15.11119 -22.68720 -28.26954 1.000 132.70408 ? 343 SER   B N   1 
ATOM   4430 C CA  . SER   B 2 250 ? 15.19254 -21.34105 -27.72655 1.000 123.76463 ? 343 SER   B CA  1 
ATOM   4431 C C   . SER   B 2 250 ? 14.59619 -21.30063 -26.32461 1.000 128.28981 ? 343 SER   B C   1 
ATOM   4432 O O   . SER   B 2 250 ? 13.65359 -22.03135 -26.00892 1.000 136.50618 ? 343 SER   B O   1 
ATOM   4433 C CB  . SER   B 2 250 ? 14.46464 -20.34706 -28.63433 1.000 130.67661 ? 343 SER   B CB  1 
ATOM   4434 O OG  . SER   B 2 250 ? 14.92515 -20.44024 -29.97272 1.000 126.26936 ? 343 SER   B OG  1 
ATOM   4435 N N   . SER   B 2 251 ? 15.15487 -20.43343 -25.48688 1.000 127.19834 ? 344 SER   B N   1 
ATOM   4436 C CA  . SER   B 2 251 ? 14.72192 -20.30296 -24.10460 1.000 115.87953 ? 344 SER   B CA  1 
ATOM   4437 C C   . SER   B 2 251 ? 13.52850 -19.35880 -23.99236 1.000 106.61717 ? 344 SER   B C   1 
ATOM   4438 O O   . SER   B 2 251 ? 13.26867 -18.53324 -24.87078 1.000 101.93193 ? 344 SER   B O   1 
ATOM   4439 C CB  . SER   B 2 251 ? 15.86991 -19.80224 -23.22734 1.000 113.70025 ? 344 SER   B CB  1 
ATOM   4440 O OG  . SER   B 2 251 ? 16.95291 -20.71423 -23.23410 1.000 123.39176 ? 344 SER   B OG  1 
ATOM   4441 N N   . LYS   B 2 252 ? 12.80230 -19.49261 -22.88696 1.000 98.55651  ? 345 LYS   B N   1 
ATOM   4442 C CA  . LYS   B 2 252 ? 11.63749 -18.66871 -22.60444 1.000 96.26747  ? 345 LYS   B CA  1 
ATOM   4443 C C   . LYS   B 2 252 ? 12.02531 -17.47886 -21.73491 1.000 94.35670  ? 345 LYS   B C   1 
ATOM   4444 O O   . LYS   B 2 252 ? 12.99724 -17.52820 -20.97654 1.000 85.65652  ? 345 LYS   B O   1 
ATOM   4445 C CB  . LYS   B 2 252 ? 10.54556 -19.48505 -21.90822 1.000 96.60923  ? 345 LYS   B CB  1 
ATOM   4446 C CG  . LYS   B 2 252 ? 9.84488  -20.49760 -22.80370 1.000 104.67481 ? 345 LYS   B CG  1 
ATOM   4447 C CD  . LYS   B 2 252 ? 8.92853  -19.81211 -23.80577 1.000 90.08800  ? 345 LYS   B CD  1 
ATOM   4448 C CE  . LYS   B 2 252 ? 8.17143  -20.82630 -24.64938 1.000 108.34514 ? 345 LYS   B CE  1 
ATOM   4449 N NZ  . LYS   B 2 252 ? 7.23278  -20.16861 -25.60143 1.000 98.91339  ? 345 LYS   B NZ  1 
ATOM   4450 N N   . LEU   B 2 253 ? 11.25031 -16.40393 -21.85620 1.000 92.51456  ? 346 LEU   B N   1 
ATOM   4451 C CA  . LEU   B 2 253 ? 11.47907 -15.20708 -21.05671 1.000 83.30096  ? 346 LEU   B CA  1 
ATOM   4452 C C   . LEU   B 2 253 ? 11.01554 -15.44391 -19.62485 1.000 93.26387  ? 346 LEU   B C   1 
ATOM   4453 O O   . LEU   B 2 253 ? 9.82467  -15.66189 -19.37765 1.000 99.33676  ? 346 LEU   B O   1 
ATOM   4454 C CB  . LEU   B 2 253 ? 10.74401 -14.01732 -21.66763 1.000 80.85454  ? 346 LEU   B CB  1 
ATOM   4455 C CG  . LEU   B 2 253 ? 10.70670 -12.74298 -20.82288 1.000 86.41461  ? 346 LEU   B CG  1 
ATOM   4456 C CD1 . LEU   B 2 253 ? 12.10897 -12.18587 -20.61808 1.000 78.09436  ? 346 LEU   B CD1 1 
ATOM   4457 C CD2 . LEU   B 2 253 ? 9.79585  -11.70661 -21.46167 1.000 72.35786  ? 346 LEU   B CD2 1 
ATOM   4458 N N   . LYS   B 2 254 ? 11.95262 -15.40046 -18.68343 1.000 99.54188  ? 347 LYS   B N   1 
ATOM   4459 C CA  . LYS   B 2 254 ? 11.61957 -15.61766 -17.28630 1.000 92.01759  ? 347 LYS   B CA  1 
ATOM   4460 C C   . LYS   B 2 254 ? 11.01757 -14.35848 -16.66941 1.000 98.74641  ? 347 LYS   B C   1 
ATOM   4461 O O   . LYS   B 2 254 ? 11.18147 -13.24302 -17.17152 1.000 100.45165 ? 347 LYS   B O   1 
ATOM   4462 C CB  . LYS   B 2 254 ? 12.85686 -16.03753 -16.49092 1.000 85.72694  ? 347 LYS   B CB  1 
ATOM   4463 C CG  . LYS   B 2 254 ? 13.39049 -17.42178 -16.82032 1.000 85.00156  ? 347 LYS   B CG  1 
ATOM   4464 C CD  . LYS   B 2 254 ? 14.55132 -17.78149 -15.90293 1.000 93.36007  ? 347 LYS   B CD  1 
ATOM   4465 C CE  . LYS   B 2 254 ? 15.03623 -19.20319 -16.13766 1.000 108.93890 ? 347 LYS   B CE  1 
ATOM   4466 N NZ  . LYS   B 2 254 ? 16.11791 -19.58096 -15.18341 1.000 91.42196  ? 347 LYS   B NZ  1 
ATOM   4467 N N   . HIS   B 2 255 ? 10.30505 -14.55610 -15.56502 1.000 112.23014 ? 348 HIS   B N   1 
ATOM   4468 C CA  . HIS   B 2 255 ? 9.81784  -13.46931 -14.72837 1.000 110.16562 ? 348 HIS   B CA  1 
ATOM   4469 C C   . HIS   B 2 255 ? 10.55558 -13.51067 -13.39895 1.000 110.47164 ? 348 HIS   B C   1 
ATOM   4470 O O   . HIS   B 2 255 ? 10.65948 -14.57234 -12.77505 1.000 107.10115 ? 348 HIS   B O   1 
ATOM   4471 C CB  . HIS   B 2 255 ? 8.30896  -13.57055 -14.49821 1.000 118.36081 ? 348 HIS   B CB  1 
ATOM   4472 C CG  . HIS   B 2 255 ? 7.80998  -12.68778 -13.39649 1.000 128.94913 ? 348 HIS   B CG  1 
ATOM   4473 N ND1 . HIS   B 2 255 ? 7.89073  -11.31274 -13.44972 1.000 126.71308 ? 348 HIS   B ND1 1 
ATOM   4474 C CD2 . HIS   B 2 255 ? 7.23526  -12.98480 -12.20674 1.000 124.24094 ? 348 HIS   B CD2 1 
ATOM   4475 C CE1 . HIS   B 2 255 ? 7.38206  -10.80064 -12.34309 1.000 123.30151 ? 348 HIS   B CE1 1 
ATOM   4476 N NE2 . HIS   B 2 255 ? 6.97731  -11.79391 -11.57212 1.000 118.32795 ? 348 HIS   B NE2 1 
ATOM   4477 N N   . PHE   B 2 256 ? 11.06804 -12.36147 -12.97267 1.000 114.89868 ? 349 PHE   B N   1 
ATOM   4478 C CA  . PHE   B 2 256 ? 11.83530 -12.24961 -11.73960 1.000 112.72721 ? 349 PHE   B CA  1 
ATOM   4479 C C   . PHE   B 2 256 ? 11.05541 -11.39750 -10.74824 1.000 108.33006 ? 349 PHE   B C   1 
ATOM   4480 O O   . PHE   B 2 256 ? 10.71358 -10.24751 -11.04678 1.000 100.59602 ? 349 PHE   B O   1 
ATOM   4481 C CB  . PHE   B 2 256 ? 13.21630 -11.65318 -12.01099 1.000 100.31962 ? 349 PHE   B CB  1 
ATOM   4482 C CG  . PHE   B 2 256 ? 14.05893 -12.48323 -12.93897 1.000 94.15895  ? 349 PHE   B CG  1 
ATOM   4483 C CD1 . PHE   B 2 256 ? 14.80736 -13.54375 -12.45419 1.000 96.04226  ? 349 PHE   B CD1 1 
ATOM   4484 C CD2 . PHE   B 2 256 ? 14.09618 -12.20875 -14.29654 1.000 98.18441  ? 349 PHE   B CD2 1 
ATOM   4485 C CE1 . PHE   B 2 256 ? 15.58108 -14.31195 -13.30388 1.000 92.46799  ? 349 PHE   B CE1 1 
ATOM   4486 C CE2 . PHE   B 2 256 ? 14.86841 -12.97431 -15.15284 1.000 92.87320  ? 349 PHE   B CE2 1 
ATOM   4487 C CZ  . PHE   B 2 256 ? 15.61197 -14.02670 -14.65498 1.000 98.08063  ? 349 PHE   B CZ  1 
ATOM   4488 N N   . ARG   B 2 257 ? 10.77131 -11.96830 -9.57871  1.000 109.55546 ? 350 ARG   B N   1 
ATOM   4489 C CA  . ARG   B 2 257 ? 10.01496 -11.26027 -8.55464  1.000 105.03030 ? 350 ARG   B CA  1 
ATOM   4490 C C   . ARG   B 2 257 ? 10.76724 -10.01705 -8.09747  1.000 103.63733 ? 350 ARG   B C   1 
ATOM   4491 O O   . ARG   B 2 257 ? 11.96209 -10.07305 -7.79262  1.000 97.23570  ? 350 ARG   B O   1 
ATOM   4492 C CB  . ARG   B 2 257 ? 9.74191  -12.18942 -7.37216  1.000 117.99716 ? 350 ARG   B CB  1 
ATOM   4493 C CG  . ARG   B 2 257 ? 10.73919 -13.32988 -7.24525  1.000 121.18799 ? 350 ARG   B CG  1 
ATOM   4494 C CD  . ARG   B 2 257 ? 10.37699 -14.26192 -6.10165  1.000 138.07661 ? 350 ARG   B CD  1 
ATOM   4495 N NE  . ARG   B 2 257 ? 11.19005 -15.47218 -6.11008  1.000 150.78720 ? 350 ARG   B NE  1 
ATOM   4496 C CZ  . ARG   B 2 257 ? 12.39118 -15.57255 -5.55744  1.000 147.89949 ? 350 ARG   B CZ  1 
ATOM   4497 N NH1 . ARG   B 2 257 ? 12.95700 -14.54690 -4.94206  1.000 135.16740 ? 350 ARG   B NH1 1 
ATOM   4498 N NH2 . ARG   B 2 257 ? 13.04182 -16.73067 -5.62552  1.000 143.46978 ? 350 ARG   B NH2 1 
ATOM   4499 N N   . GLY   B 2 258 ? 10.05879 -8.88971  -8.05201  1.000 85.65971  ? 351 GLY   B N   1 
ATOM   4500 C CA  . GLY   B 2 258 ? 10.66254 -7.61198  -7.75306  1.000 90.38783  ? 351 GLY   B CA  1 
ATOM   4501 C C   . GLY   B 2 258 ? 11.13870 -6.83958  -8.96340  1.000 93.63545  ? 351 GLY   B C   1 
ATOM   4502 O O   . GLY   B 2 258 ? 11.41485 -5.63884  -8.84321  1.000 95.78261  ? 351 GLY   B O   1 
ATOM   4503 N N   . VAL   B 2 259 ? 11.24160 -7.48556  -10.12222 1.000 92.98627  ? 352 VAL   B N   1 
ATOM   4504 C CA  . VAL   B 2 259 ? 11.67181 -6.84313  -11.35805 1.000 91.91078  ? 352 VAL   B CA  1 
ATOM   4505 C C   . VAL   B 2 259 ? 10.44954 -6.62186  -12.23669 1.000 80.64552  ? 352 VAL   B C   1 
ATOM   4506 O O   . VAL   B 2 259 ? 9.65229  -7.54473  -12.44788 1.000 97.42625  ? 352 VAL   B O   1 
ATOM   4507 C CB  . VAL   B 2 259 ? 12.72712 -7.69139  -12.08878 1.000 89.78461  ? 352 VAL   B CB  1 
ATOM   4508 C CG1 . VAL   B 2 259 ? 13.23315 -6.96318  -13.32621 1.000 82.77780  ? 352 VAL   B CG1 1 
ATOM   4509 C CG2 . VAL   B 2 259 ? 13.87566 -8.03451  -11.15409 1.000 86.13659  ? 352 VAL   B CG2 1 
ATOM   4510 N N   . ALA   B 2 260 ? 10.29805 -5.40090  -12.74486 1.000 85.95648  ? 353 ALA   B N   1 
ATOM   4511 C CA  . ALA   B 2 260 ? 9.19112  -5.09906  -13.64065 1.000 99.48078  ? 353 ALA   B CA  1 
ATOM   4512 C C   . ALA   B 2 260 ? 9.30000  -5.92628  -14.91674 1.000 103.33428 ? 353 ALA   B C   1 
ATOM   4513 O O   . ALA   B 2 260 ? 10.39468 -6.27404  -15.36801 1.000 99.52074  ? 353 ALA   B O   1 
ATOM   4514 C CB  . ALA   B 2 260 ? 9.16781  -3.60769  -13.97744 1.000 89.98172  ? 353 ALA   B CB  1 
ATOM   4515 N N   . ASP   B 2 261 ? 8.14218  -6.24803  -15.49937 1.000 108.44656 ? 354 ASP   B N   1 
ATOM   4516 C CA  . ASP   B 2 261 ? 8.13140  -7.08564  -16.69422 1.000 109.81011 ? 354 ASP   B CA  1 
ATOM   4517 C C   . ASP   B 2 261 ? 8.72888  -6.36722  -17.89731 1.000 99.87575  ? 354 ASP   B C   1 
ATOM   4518 O O   . ASP   B 2 261 ? 9.27259  -7.01903  -18.79573 1.000 104.76038 ? 354 ASP   B O   1 
ATOM   4519 C CB  . ASP   B 2 261 ? 6.70804  -7.55114  -16.99931 1.000 121.04354 ? 354 ASP   B CB  1 
ATOM   4520 C CG  . ASP   B 2 261 ? 6.25823  -8.67795  -16.08953 1.000 123.98009 ? 354 ASP   B CG  1 
ATOM   4521 O OD1 . ASP   B 2 261 ? 7.12086  -9.47045  -15.65427 1.000 113.62449 ? 354 ASP   B OD1 1 
ATOM   4522 O OD2 . ASP   B 2 261 ? 5.04436  -8.77372  -15.81173 1.000 135.82516 ? 354 ASP   B OD2 1 
ATOM   4523 N N   . GLU   B 2 262 ? 8.64642  -5.03553  -17.93441 1.000 97.96928  ? 355 GLU   B N   1 
ATOM   4524 C CA  . GLU   B 2 262 ? 9.26858  -4.27676  -19.01307 1.000 100.22331 ? 355 GLU   B CA  1 
ATOM   4525 C C   . GLU   B 2 262 ? 10.78972 -4.27872  -18.93335 1.000 97.10914  ? 355 GLU   B C   1 
ATOM   4526 O O   . GLU   B 2 262 ? 11.44276 -3.84954  -19.89044 1.000 97.02285  ? 355 GLU   B O   1 
ATOM   4527 C CB  . GLU   B 2 262 ? 8.74664  -2.83837  -19.01131 1.000 106.25601 ? 355 GLU   B CB  1 
ATOM   4528 C CG  . GLU   B 2 262 ? 8.67245  -2.20662  -17.63298 1.000 109.91269 ? 355 GLU   B CG  1 
ATOM   4529 C CD  . GLU   B 2 262 ? 7.29723  -1.64544  -17.32628 1.000 114.42722 ? 355 GLU   B CD  1 
ATOM   4530 O OE1 . GLU   B 2 262 ? 6.52903  -1.39472  -18.27901 1.000 117.16775 ? 355 GLU   B OE1 1 
ATOM   4531 O OE2 . GLU   B 2 262 ? 6.98176  -1.46110  -16.13217 1.000 121.94042 ? 355 GLU   B OE2 1 
ATOM   4532 N N   . ASP   B 2 263 ? 11.36398 -4.74687  -17.82464 1.000 94.56582  ? 356 ASP   B N   1 
ATOM   4533 C CA  . ASP   B 2 263 ? 12.80802 -4.87713  -17.67504 1.000 77.64266  ? 356 ASP   B CA  1 
ATOM   4534 C C   . ASP   B 2 263 ? 13.22658 -6.32611  -17.44836 1.000 72.70764  ? 356 ASP   B C   1 
ATOM   4535 O O   . ASP   B 2 263 ? 14.38302 -6.58131  -17.09195 1.000 72.89902  ? 356 ASP   B O   1 
ATOM   4536 C CB  . ASP   B 2 263 ? 13.29903 -3.99058  -16.52312 1.000 80.31441  ? 356 ASP   B CB  1 
ATOM   4537 C CG  . ASP   B 2 263 ? 14.79555 -3.72414  -16.57875 1.000 92.90145  ? 356 ASP   B CG  1 
ATOM   4538 O OD1 . ASP   B 2 263 ? 15.24025 -2.99164  -17.48825 1.000 96.34203  ? 356 ASP   B OD1 1 
ATOM   4539 O OD2 . ASP   B 2 263 ? 15.52640 -4.24502  -15.70918 1.000 93.50670  ? 356 ASP   B OD2 1 
ATOM   4540 N N   . ALA   B 2 264 ? 12.31790 -7.28317  -17.65813 1.000 75.25997  ? 357 ALA   B N   1 
ATOM   4541 C CA  . ALA   B 2 264 ? 12.61101 -8.67707  -17.33896 1.000 71.79101  ? 357 ALA   B CA  1 
ATOM   4542 C C   . ALA   B 2 264 ? 13.67154 -9.26822  -18.25950 1.000 79.13919  ? 357 ALA   B C   1 
ATOM   4543 O O   . ALA   B 2 264 ? 14.39295 -10.18806 -17.85821 1.000 77.59667  ? 357 ALA   B O   1 
ATOM   4544 C CB  . ALA   B 2 264 ? 11.33140 -9.51030  -17.40894 1.000 77.89452  ? 357 ALA   B CB  1 
ATOM   4545 N N   . HIS   B 2 265 ? 13.78138 -8.76538  -19.48976 1.000 73.41886  ? 358 HIS   B N   1 
ATOM   4546 C CA  . HIS   B 2 265 ? 14.74669 -9.31737  -20.43259 1.000 74.69548  ? 358 HIS   B CA  1 
ATOM   4547 C C   . HIS   B 2 265 ? 16.17859 -8.90665  -20.11158 1.000 72.50284  ? 358 HIS   B C   1 
ATOM   4548 O O   . HIS   B 2 265 ? 17.11525 -9.60183  -20.52102 1.000 66.00920  ? 358 HIS   B O   1 
ATOM   4549 C CB  . HIS   B 2 265 ? 14.39115 -8.88431  -21.85399 1.000 67.98000  ? 358 HIS   B CB  1 
ATOM   4550 C CG  . HIS   B 2 265 ? 14.44980 -7.40427  -22.06100 1.000 69.49684  ? 358 HIS   B CG  1 
ATOM   4551 N ND1 . HIS   B 2 265 ? 13.55291 -6.53565  -21.47725 1.000 71.57952  ? 358 HIS   B ND1 1 
ATOM   4552 C CD2 . HIS   B 2 265 ? 15.30376 -6.63770  -22.77919 1.000 60.57637  ? 358 HIS   B CD2 1 
ATOM   4553 C CE1 . HIS   B 2 265 ? 13.84953 -5.29784  -21.83051 1.000 71.16850  ? 358 HIS   B CE1 1 
ATOM   4554 N NE2 . HIS   B 2 265 ? 14.90733 -5.33213  -22.62077 1.000 66.35369  ? 358 HIS   B NE2 1 
ATOM   4555 N N   . ASN   B 2 266 ? 16.36952 -7.80131  -19.39219 1.000 69.71489  ? 359 ASN   B N   1 
ATOM   4556 C CA  . ASN   B 2 266 ? 17.70114 -7.29678  -19.07835 1.000 69.32663  ? 359 ASN   B CA  1 
ATOM   4557 C C   . ASN   B 2 266 ? 18.35757 -8.01630  -17.90690 1.000 70.29299  ? 359 ASN   B C   1 
ATOM   4558 O O   . ASN   B 2 266 ? 19.50536 -7.70022  -17.57565 1.000 65.80338  ? 359 ASN   B O   1 
ATOM   4559 C CB  . ASN   B 2 266 ? 17.63629 -5.79520  -18.78378 1.000 60.38509  ? 359 ASN   B CB  1 
ATOM   4560 C CG  . ASN   B 2 266 ? 17.25417 -4.97794  -20.00256 1.000 69.27822  ? 359 ASN   B CG  1 
ATOM   4561 O OD1 . ASN   B 2 266 ? 17.68738 -5.26677  -21.11815 1.000 72.91970  ? 359 ASN   B OD1 1 
ATOM   4562 N ND2 . ASN   B 2 266 ? 16.43699 -3.95125  -19.79515 1.000 65.54440  ? 359 ASN   B ND2 1 
ATOM   4563 N N   . ILE   B 2 267 ? 17.67115 -8.96371  -17.27641 1.000 70.83361  ? 360 ILE   B N   1 
ATOM   4564 C CA  . ILE   B 2 267 ? 18.21366 -9.69080  -16.13464 1.000 67.34925  ? 360 ILE   B CA  1 
ATOM   4565 C C   . ILE   B 2 267 ? 19.02537 -10.87315 -16.64563 1.000 71.02145  ? 360 ILE   B C   1 
ATOM   4566 O O   . ILE   B 2 267 ? 18.56739 -11.62495 -17.51444 1.000 77.80351  ? 360 ILE   B O   1 
ATOM   4567 C CB  . ILE   B 2 267 ? 17.08959 -10.15555 -15.19359 1.000 73.66428  ? 360 ILE   B CB  1 
ATOM   4568 C CG1 . ILE   B 2 267 ? 16.23139 -8.96547  -14.75781 1.000 70.79932  ? 360 ILE   B CG1 1 
ATOM   4569 C CG2 . ILE   B 2 267 ? 17.66703 -10.87105 -13.98180 1.000 76.06315  ? 360 ILE   B CG2 1 
ATOM   4570 C CD1 . ILE   B 2 267 ? 17.01722 -7.85065  -14.10705 1.000 65.85512  ? 360 ILE   B CD1 1 
ATOM   4571 N N   . GLN   B 2 268 ? 20.23281 -11.03702 -16.10966 1.000 64.73794  ? 361 GLN   B N   1 
ATOM   4572 C CA  . GLN   B 2 268 ? 21.10290 -12.12318 -16.53923 1.000 65.15222  ? 361 GLN   B CA  1 
ATOM   4573 C C   . GLN   B 2 268 ? 20.55398 -13.46126 -16.06222 1.000 81.48484  ? 361 GLN   B C   1 
ATOM   4574 O O   . GLN   B 2 268 ? 20.15249 -13.60340 -14.90343 1.000 87.16132  ? 361 GLN   B O   1 
ATOM   4575 C CB  . GLN   B 2 268 ? 22.51855 -11.91396 -16.00352 1.000 67.04353  ? 361 GLN   B CB  1 
ATOM   4576 C CG  . GLN   B 2 268 ? 23.50817 -12.98262 -16.43855 1.000 70.59565  ? 361 GLN   B CG  1 
ATOM   4577 C CD  . GLN   B 2 268 ? 23.78370 -12.93972 -17.92669 1.000 76.79935  ? 361 GLN   B CD  1 
ATOM   4578 O OE1 . GLN   B 2 268 ? 23.91755 -11.86550 -18.51009 1.000 70.75658  ? 361 GLN   B OE1 1 
ATOM   4579 N NE2 . GLN   B 2 268 ? 23.86230 -14.10914 -18.55168 1.000 70.80790  ? 361 GLN   B NE2 1 
ATOM   4580 N N   . THR   B 2 269 ? 20.53398 -14.44068 -16.95782 1.000 82.35259  ? 362 THR   B N   1 
ATOM   4581 C CA  . THR   B 2 269 ? 20.11652 -15.79603 -16.63603 1.000 88.22820  ? 362 THR   B CA  1 
ATOM   4582 C C   . THR   B 2 269 ? 21.31049 -16.73744 -16.72403 1.000 84.33787  ? 362 THR   B C   1 
ATOM   4583 O O   . THR   B 2 269 ? 22.41464 -16.34969 -17.11461 1.000 80.89697  ? 362 THR   B O   1 
ATOM   4584 C CB  . THR   B 2 269 ? 18.99521 -16.26235 -17.57177 1.000 87.07697  ? 362 THR   B CB  1 
ATOM   4585 O OG1 . THR   B 2 269 ? 19.43734 -16.17517 -18.93201 1.000 91.43248  ? 362 THR   B OG1 1 
ATOM   4586 C CG2 . THR   B 2 269 ? 17.75524 -15.39930 -17.38702 1.000 87.09034  ? 362 THR   B CG2 1 
ATOM   4587 N N   . HIS   B 2 270 ? 21.07895 -17.99253 -16.34937 1.000 91.77540  ? 363 HIS   B N   1 
ATOM   4588 C CA  . HIS   B 2 270 ? 22.14257 -18.98982 -16.37041 1.000 98.92737  ? 363 HIS   B CA  1 
ATOM   4589 C C   . HIS   B 2 270 ? 21.55738 -20.35087 -16.70503 1.000 105.48503 ? 363 HIS   B C   1 
ATOM   4590 O O   . HIS   B 2 270 ? 20.66289 -20.83390 -16.00415 1.000 109.47018 ? 363 HIS   B O   1 
ATOM   4591 C CB  . HIS   B 2 270 ? 22.87825 -19.04518 -15.03025 1.000 92.96899  ? 363 HIS   B CB  1 
ATOM   4592 C CG  . HIS   B 2 270 ? 23.86616 -20.16584 -14.93438 1.000 97.80345  ? 363 HIS   B CG  1 
ATOM   4593 N ND1 . HIS   B 2 270 ? 23.53989 -21.40399 -14.42398 1.000 108.71092 ? 363 HIS   B ND1 1 
ATOM   4594 C CD2 . HIS   B 2 270 ? 25.16984 -20.23868 -15.29296 1.000 98.30712  ? 363 HIS   B CD2 1 
ATOM   4595 C CE1 . HIS   B 2 270 ? 24.60108 -22.18960 -14.46762 1.000 112.35490 ? 363 HIS   B CE1 1 
ATOM   4596 N NE2 . HIS   B 2 270 ? 25.60347 -21.50676 -14.99074 1.000 108.75531 ? 363 HIS   B NE2 1 
ATOM   4597 N N   . ARG   B 2 271 ? 22.06073 -20.95659 -17.77418 1.000 99.33554  ? 364 ARG   B N   1 
ATOM   4598 C CA  . ARG   B 2 271 ? 21.84286 -22.36174 -18.07053 1.000 114.70390 ? 364 ARG   B CA  1 
ATOM   4599 C C   . ARG   B 2 271 ? 23.14691 -23.10999 -17.83127 1.000 125.82145 ? 364 ARG   B C   1 
ATOM   4600 O O   . ARG   B 2 271 ? 24.22052 -22.50670 -17.74772 1.000 128.42584 ? 364 ARG   B O   1 
ATOM   4601 C CB  . ARG   B 2 271 ? 21.35569 -22.55767 -19.51269 1.000 123.97875 ? 364 ARG   B CB  1 
ATOM   4602 C CG  . ARG   B 2 271 ? 22.43678 -22.94981 -20.51111 1.000 126.57599 ? 364 ARG   B CG  1 
ATOM   4603 C CD  . ARG   B 2 271 ? 22.16321 -22.35902 -21.88831 1.000 124.36508 ? 364 ARG   B CD  1 
ATOM   4604 N NE  . ARG   B 2 271 ? 20.75548 -22.43428 -22.26398 1.000 124.28973 ? 364 ARG   B NE  1 
ATOM   4605 C CZ  . ARG   B 2 271 ? 20.24286 -23.32929 -23.09805 1.000 121.84591 ? 364 ARG   B CZ  1 
ATOM   4606 N NH1 . ARG   B 2 271 ? 20.99509 -24.25646 -23.66609 1.000 118.89772 ? 364 ARG   B NH1 1 
ATOM   4607 N NH2 . ARG   B 2 271 ? 18.94232 -23.28917 -23.37366 1.000 119.84499 ? 364 ARG   B NH2 1 
ATOM   4608 N N   . ASP   B 2 272 ? 23.04076 -24.43437 -17.69874 1.000 148.62183 ? 365 ASP   B N   1 
ATOM   4609 C CA  . ASP   B 2 272 ? 24.21882 -25.24887 -17.41360 1.000 172.80456 ? 365 ASP   B CA  1 
ATOM   4610 C C   . ASP   B 2 272 ? 25.32666 -24.98313 -18.42532 1.000 169.74671 ? 365 ASP   B C   1 
ATOM   4611 O O   . ASP   B 2 272 ? 26.45953 -24.65583 -18.05235 1.000 167.91761 ? 365 ASP   B O   1 
ATOM   4612 C CB  . ASP   B 2 272 ? 23.83849 -26.72894 -17.40435 1.000 170.30448 ? 365 ASP   B CB  1 
ATOM   4613 C CG  . ASP   B 2 272 ? 22.35287 -26.94276 -17.21196 1.000 166.81213 ? 365 ASP   B CG  1 
ATOM   4614 O OD1 . ASP   B 2 272 ? 21.59639 -26.74431 -18.18578 1.000 153.87594 ? 365 ASP   B OD1 1 
ATOM   4615 O OD2 . ASP   B 2 272 ? 21.94036 -27.30059 -16.08889 1.000 170.75313 ? 365 ASP   B OD2 1 
ATOM   4616 N N   . SER   B 2 273 ? 25.00506 -25.09961 -19.71222 1.000 138.86159 ? 366 SER   B N   1 
ATOM   4617 C CA  . SER   B 2 273 ? 25.92916 -24.80639 -20.81664 1.000 136.07655 ? 366 SER   B CA  1 
ATOM   4618 C C   . SER   B 2 273 ? 27.17716 -25.66371 -20.61447 1.000 144.20954 ? 366 SER   B C   1 
ATOM   4619 O O   . SER   B 2 273 ? 27.03712 -26.87490 -20.37780 1.000 148.18031 ? 366 SER   B O   1 
ATOM   4620 C CB  . SER   B 2 273 ? 26.16304 -23.30224 -20.88831 1.000 126.52860 ? 366 SER   B CB  1 
ATOM   4621 O OG  . SER   B 2 273 ? 27.04164 -22.97381 -21.95002 1.000 131.08029 ? 366 SER   B OG  1 
ATOM   4622 N N   . LEU   B 2 274 ? 28.38479 -25.09784 -20.69295 1.000 140.39419 ? 367 LEU   B N   1 
ATOM   4623 C CA  . LEU   B 2 274 ? 29.63415 -25.82721 -20.49027 1.000 139.60360 ? 367 LEU   B CA  1 
ATOM   4624 C C   . LEU   B 2 274 ? 29.74540 -27.01982 -21.43371 1.000 128.86181 ? 367 LEU   B C   1 
ATOM   4625 O O   . LEU   B 2 274 ? 30.62112 -27.04657 -22.30478 1.000 124.71411 ? 367 LEU   B O   1 
ATOM   4626 C CB  . LEU   B 2 274 ? 29.76268 -26.27726 -19.03246 1.000 134.60691 ? 367 LEU   B CB  1 
ATOM   4627 C CG  . LEU   B 2 274 ? 29.77447 -25.14901 -17.99701 1.000 133.01414 ? 367 LEU   B CG  1 
ATOM   4628 C CD1 . LEU   B 2 274 ? 29.94796 -25.70476 -16.59158 1.000 125.96539 ? 367 LEU   B CD1 1 
ATOM   4629 C CD2 . LEU   B 2 274 ? 30.86073 -24.12921 -18.31448 1.000 104.21655 ? 367 LEU   B CD2 1 
ATOM   4630 N N   . ASP   B 2 275 ? 28.86899 -28.01435 -21.26234 1.000 132.27120 ? 368 ASP   B N   1 
ATOM   4631 C CA  . ASP   B 2 275 ? 28.81516 -29.12236 -22.20981 1.000 136.88829 ? 368 ASP   B CA  1 
ATOM   4632 C C   . ASP   B 2 275 ? 28.47910 -28.63599 -23.61260 1.000 126.28182 ? 368 ASP   B C   1 
ATOM   4633 O O   . ASP   B 2 275 ? 28.91669 -29.23733 -24.59988 1.000 125.19805 ? 368 ASP   B O   1 
ATOM   4634 C CB  . ASP   B 2 275 ? 27.79131 -30.16113 -21.75015 1.000 136.32445 ? 368 ASP   B CB  1 
ATOM   4635 C CG  . ASP   B 2 275 ? 28.02637 -30.62160 -20.32422 1.000 150.00993 ? 368 ASP   B CG  1 
ATOM   4636 O OD1 . ASP   B 2 275 ? 28.89152 -30.03347 -19.64133 1.000 146.83073 ? 368 ASP   B OD1 1 
ATOM   4637 O OD2 . ASP   B 2 275 ? 27.34612 -31.57339 -19.88624 1.000 146.65219 ? 368 ASP   B OD2 1 
ATOM   4638 N N   . LEU   B 2 276 ? 27.70724 -27.55166 -23.72042 1.000 123.51319 ? 369 LEU   B N   1 
ATOM   4639 C CA  . LEU   B 2 276 ? 27.40432 -26.98490 -25.02992 1.000 127.24438 ? 369 LEU   B CA  1 
ATOM   4640 C C   . LEU   B 2 276 ? 28.64304 -26.35872 -25.65703 1.000 123.02882 ? 369 LEU   B C   1 
ATOM   4641 O O   . LEU   B 2 276 ? 28.82990 -26.42603 -26.87776 1.000 119.09465 ? 369 LEU   B O   1 
ATOM   4642 C CB  . LEU   B 2 276 ? 26.28660 -25.95161 -24.90610 1.000 124.18448 ? 369 LEU   B CB  1 
ATOM   4643 C CG  . LEU   B 2 276 ? 25.03389 -26.38634 -24.14529 1.000 123.73170 ? 369 LEU   B CG  1 
ATOM   4644 C CD1 . LEU   B 2 276 ? 24.02154 -25.25877 -24.12748 1.000 114.84614 ? 369 LEU   B CD1 1 
ATOM   4645 C CD2 . LEU   B 2 276 ? 24.43216 -27.64337 -24.75235 1.000 124.86427 ? 369 LEU   B CD2 1 
ATOM   4646 N N   . LEU   B 2 277 ? 29.49836 -25.74137 -24.83718 1.000 116.95103 ? 370 LEU   B N   1 
ATOM   4647 C CA  . LEU   B 2 277 ? 30.74576 -25.18430 -25.34850 1.000 114.77811 ? 370 LEU   B CA  1 
ATOM   4648 C C   . LEU   B 2 277 ? 31.68298 -26.27860 -25.84382 1.000 123.37533 ? 370 LEU   B C   1 
ATOM   4649 O O   . LEU   B 2 277 ? 32.52577 -26.02665 -26.71299 1.000 125.74353 ? 370 LEU   B O   1 
ATOM   4650 C CB  . LEU   B 2 277 ? 31.42570 -24.34504 -24.26545 1.000 102.62468 ? 370 LEU   B CB  1 
ATOM   4651 C CG  . LEU   B 2 277 ? 32.70518 -23.60020 -24.65332 1.000 105.94476 ? 370 LEU   B CG  1 
ATOM   4652 C CD1 . LEU   B 2 277 ? 32.41077 -22.52047 -25.68365 1.000 99.47121  ? 370 LEU   B CD1 1 
ATOM   4653 C CD2 . LEU   B 2 277 ? 33.38115 -23.00949 -23.42598 1.000 94.96081  ? 370 LEU   B CD2 1 
ATOM   4654 N N   . ASP   B 2 278 ? 31.54865 -27.49517 -25.31077 1.000 121.05080 ? 371 ASP   B N   1 
ATOM   4655 C CA  . ASP   B 2 278 ? 32.37045 -28.60877 -25.76921 1.000 134.78940 ? 371 ASP   B CA  1 
ATOM   4656 C C   . ASP   B 2 278 ? 31.84913 -29.20365 -27.07151 1.000 136.02603 ? 371 ASP   B C   1 
ATOM   4657 O O   . ASP   B 2 278 ? 32.64416 -29.66687 -27.89729 1.000 135.13920 ? 371 ASP   B O   1 
ATOM   4658 C CB  . ASP   B 2 278 ? 32.44117 -29.68919 -24.68870 1.000 135.99722 ? 371 ASP   B CB  1 
ATOM   4659 C CG  . ASP   B 2 278 ? 32.85321 -29.13622 -23.33715 1.000 140.34857 ? 371 ASP   B CG  1 
ATOM   4660 O OD1 . ASP   B 2 278 ? 33.53056 -28.08664 -23.30106 1.000 134.19574 ? 371 ASP   B OD1 1 
ATOM   4661 O OD2 . ASP   B 2 278 ? 32.49842 -29.75197 -22.30998 1.000 145.05675 ? 371 ASP   B OD2 1 
ATOM   4662 N N   . LYS   B 2 279 ? 30.52788 -29.20488 -27.27095 1.000 131.37430 ? 372 LYS   B N   1 
ATOM   4663 C CA  . LYS   B 2 279 ? 29.97003 -29.68318 -28.53160 1.000 127.40313 ? 372 LYS   B CA  1 
ATOM   4664 C C   . LYS   B 2 279 ? 30.37075 -28.78624 -29.69465 1.000 129.97614 ? 372 LYS   B C   1 
ATOM   4665 O O   . LYS   B 2 279 ? 30.48246 -29.25888 -30.83146 1.000 137.49253 ? 372 LYS   B O   1 
ATOM   4666 C CB  . LYS   B 2 279 ? 28.44669 -29.77203 -28.43374 1.000 112.20358 ? 372 LYS   B CB  1 
ATOM   4667 C CG  . LYS   B 2 279 ? 27.94580 -30.66835 -27.31386 1.000 118.46807 ? 372 LYS   B CG  1 
ATOM   4668 C CD  . LYS   B 2 279 ? 26.44444 -30.52827 -27.12123 1.000 112.16494 ? 372 LYS   B CD  1 
ATOM   4669 C CE  . LYS   B 2 279 ? 25.97254 -31.30247 -25.90053 1.000 122.08418 ? 372 LYS   B CE  1 
ATOM   4670 N NZ  . LYS   B 2 279 ? 24.52247 -31.09623 -25.63250 1.000 125.17153 ? 372 LYS   B NZ  1 
ATOM   4671 N N   . ALA   B 2 280 ? 30.59236 -27.49631 -29.43128 1.000 135.67811 ? 373 ALA   B N   1 
ATOM   4672 C CA  . ALA   B 2 280 ? 30.99933 -26.58233 -30.49184 1.000 143.57884 ? 373 ALA   B CA  1 
ATOM   4673 C C   . ALA   B 2 280 ? 32.44835 -26.80540 -30.90445 1.000 161.13181 ? 373 ALA   B C   1 
ATOM   4674 O O   . ALA   B 2 280 ? 32.81609 -26.51645 -32.04893 1.000 155.13838 ? 373 ALA   B O   1 
ATOM   4675 C CB  . ALA   B 2 280 ? 30.79082 -25.13547 -30.04586 1.000 125.18014 ? 373 ALA   B CB  1 
ATOM   4676 N N   . ARG   B 2 281 ? 33.28222 -27.31511 -29.99418 1.000 155.11634 ? 374 ARG   B N   1 
ATOM   4677 C CA  . ARG   B 2 281 ? 34.68105 -27.56029 -30.32872 1.000 146.25503 ? 374 ARG   B CA  1 
ATOM   4678 C C   . ARG   B 2 281 ? 34.82569 -28.67630 -31.35638 1.000 150.75871 ? 374 ARG   B C   1 
ATOM   4679 O O   . ARG   B 2 281 ? 35.80691 -28.70182 -32.10833 1.000 158.96463 ? 374 ARG   B O   1 
ATOM   4680 C CB  . ARG   B 2 281 ? 35.46998 -27.88990 -29.06055 1.000 160.36204 ? 374 ARG   B CB  1 
ATOM   4681 C CG  . ARG   B 2 281 ? 36.97233 -28.00798 -29.26402 1.000 170.31634 ? 374 ARG   B CG  1 
ATOM   4682 C CD  . ARG   B 2 281 ? 37.69179 -28.22931 -27.94385 1.000 174.95581 ? 374 ARG   B CD  1 
ATOM   4683 N NE  . ARG   B 2 281 ? 39.12545 -28.41909 -28.12833 1.000 177.74603 ? 374 ARG   B NE  1 
ATOM   4684 C CZ  . ARG   B 2 281 ? 39.99329 -28.57868 -27.13857 1.000 189.92329 ? 374 ARG   B CZ  1 
ATOM   4685 N NH1 . ARG   B 2 281 ? 39.60790 -28.56895 -25.87294 1.000 189.89915 ? 374 ARG   B NH1 1 
ATOM   4686 N NH2 . ARG   B 2 281 ? 41.28033 -28.75170 -27.42570 1.000 193.57197 ? 374 ARG   B NH2 1 
ATOM   4687 N N   . ALA   B 2 282 ? 33.86471 -29.59295 -31.41241 1.000 146.36915 ? 375 ALA   B N   1 
ATOM   4688 C CA  . ALA   B 2 282 ? 33.90215 -30.68855 -32.37418 1.000 147.67124 ? 375 ALA   B CA  1 
ATOM   4689 C C   . ALA   B 2 282 ? 33.68987 -30.18044 -33.79773 1.000 143.25395 ? 375 ALA   B C   1 
ATOM   4690 O O   . ALA   B 2 282 ? 32.99042 -29.19126 -34.01816 1.000 133.04565 ? 375 ALA   B O   1 
ATOM   4691 C CB  . ALA   B 2 282 ? 32.85636 -31.73546 -32.02365 1.000 144.82141 ? 375 ALA   B CB  1 
HETATM 4692 C C11 . A1CAE C 3 .   ? 37.25200 23.97125  -8.34279  1.000 48.08492  ? 301 A1CAE A C11 1 
HETATM 4693 C C14 . A1CAE C 3 .   ? 37.28680 21.69258  -8.82881  1.000 51.84378  ? 301 A1CAE A C14 1 
HETATM 4694 C C15 . A1CAE C 3 .   ? 37.11051 20.18113  -8.93639  1.000 52.84113  ? 301 A1CAE A C15 1 
HETATM 4695 C C16 . A1CAE C 3 .   ? 35.78911 19.70707  -9.63780  1.000 49.43424  ? 301 A1CAE A C16 1 
HETATM 4696 C C17 . A1CAE C 3 .   ? 34.90424 18.88019  -8.66898  1.000 51.16435  ? 301 A1CAE A C17 1 
HETATM 4697 C C19 . A1CAE C 3 .   ? 32.87442 19.20486  -7.27059  1.000 54.42528  ? 301 A1CAE A C19 1 
HETATM 4698 C C21 . A1CAE C 3 .   ? 32.34529 21.45715  -6.19939  1.000 61.42889  ? 301 A1CAE A C21 1 
HETATM 4699 C C22 . A1CAE C 3 .   ? 33.41707 21.90382  -5.21389  1.000 54.99759  ? 301 A1CAE A C22 1 
HETATM 4700 C C23 . A1CAE C 3 .   ? 31.16826 22.43415  -6.36596  1.000 71.59003  ? 301 A1CAE A C23 1 
HETATM 4701 C C24 . A1CAE C 3 .   ? 32.22257 22.41065  -7.42687  1.000 49.39797  ? 301 A1CAE A C24 1 
HETATM 4702 C C26 . A1CAE C 3 .   ? 36.00274 18.34135  -7.69536  1.000 48.42778  ? 301 A1CAE A C26 1 
HETATM 4703 C C27 . A1CAE C 3 .   ? 37.13480 19.40975  -7.61299  1.000 52.08780  ? 301 A1CAE A C27 1 
HETATM 4704 C C28 . A1CAE C 3 .   ? 36.67648 22.67192  -8.02022  1.000 43.37621  ? 301 A1CAE A C28 1 
HETATM 4705 C C30 . A1CAE C 3 .   ? 37.66616 27.79884  -5.30295  1.000 64.67463  ? 301 A1CAE A C30 1 
HETATM 4706 C C03 . A1CAE C 3 .   ? 38.91306 30.88440  -1.49934  1.000 80.75542  ? 301 A1CAE A C03 1 
HETATM 4707 C C04 . A1CAE C 3 .   ? 37.95946 28.54232  -2.92729  1.000 57.00926  ? 301 A1CAE A C04 1 
HETATM 4708 C C05 . A1CAE C 3 .   ? 36.57399 28.29328  -2.84307  1.000 61.04867  ? 301 A1CAE A C05 1 
HETATM 4709 C C06 . A1CAE C 3 .   ? 35.77076 27.82582  -3.91260  1.000 62.18093  ? 301 A1CAE A C06 1 
HETATM 4710 C C07 . A1CAE C 3 .   ? 36.27713 27.56500  -5.19854  1.000 62.37686  ? 301 A1CAE A C07 1 
HETATM 4711 C C08 . A1CAE C 3 .   ? 35.38291 27.03112  -6.37884  1.000 56.77007  ? 301 A1CAE A C08 1 
HETATM 4712 C C09 . A1CAE C 3 .   ? 35.74399 25.61560  -6.98547  1.000 50.82072  ? 301 A1CAE A C09 1 
HETATM 4713 C C31 . A1CAE C 3 .   ? 38.45338 28.26505  -4.21999  1.000 66.64134  ? 301 A1CAE A C31 1 
HETATM 4714 N N10 . A1CAE C 3 .   ? 36.90242 25.26925  -7.75820  1.000 50.23975  ? 301 A1CAE A N10 1 
HETATM 4715 N N12 . A1CAE C 3 .   ? 38.19118 23.75661  -9.33710  1.000 48.18297  ? 301 A1CAE A N12 1 
HETATM 4716 N N13 . A1CAE C 3 .   ? 38.19282 22.41227  -9.59835  1.000 49.57634  ? 301 A1CAE A N13 1 
HETATM 4717 N N20 . A1CAE C 3 .   ? 32.06712 20.01754  -6.43215  1.000 63.97710  ? 301 A1CAE A N20 1 
HETATM 4718 O O01 . A1CAE C 3 .   ? 38.45651 28.65381  -0.30539  1.000 85.01395  ? 301 A1CAE A O01 1 
HETATM 4719 O O18 . A1CAE C 3 .   ? 33.86671 19.74726  -8.10717  1.000 49.22744  ? 301 A1CAE A O18 1 
HETATM 4720 O O25 . A1CAE C 3 .   ? 32.73391 17.98532  -7.30334  1.000 65.07921  ? 301 A1CAE A O25 1 
HETATM 4721 O O29 . A1CAE C 3 .   ? 34.92984 24.72274  -6.72997  1.000 54.62808  ? 301 A1CAE A O29 1 
HETATM 4722 O O32 . A1CAE C 3 .   ? 40.33382 28.75589  -1.72981  1.000 79.78598  ? 301 A1CAE A O32 1 
HETATM 4723 S S02 . A1CAE C 3 .   ? 38.97349 29.13703  -1.54258  1.000 74.70711  ? 301 A1CAE A S02 1 
HETATM 4724 O O   . HOH   D 4 .   ? 18.26245 16.52052  -25.76782 1.000 48.13060  ? 401 HOH   A O   1 
HETATM 4725 O O   . HOH   D 4 .   ? 29.25022 6.16595   -26.26630 1.000 66.74860  ? 402 HOH   A O   1 
HETATM 4726 O O   . HOH   D 4 .   ? 34.85176 33.18930  -16.60728 1.000 61.07031  ? 403 HOH   A O   1 
HETATM 4727 O O   . HOH   D 4 .   ? 25.71813 5.02656   -4.62163  1.000 65.73387  ? 404 HOH   A O   1 
HETATM 4728 O O   . HOH   D 4 .   ? 28.39581 8.25947   -28.57016 1.000 52.62363  ? 405 HOH   A O   1 
HETATM 4729 O O   . HOH   D 4 .   ? 22.14312 35.73019  -7.33525  1.000 62.10918  ? 406 HOH   A O   1 
HETATM 4730 O O   . HOH   D 4 .   ? 15.94138 6.49534   -18.01478 1.000 65.69392  ? 407 HOH   A O   1 
HETATM 4731 O O   . HOH   D 4 .   ? 15.00489 13.01519  -21.62020 1.000 52.26643  ? 408 HOH   A O   1 
HETATM 4732 O O   . HOH   D 4 .   ? 13.36419 13.81072  -19.98322 1.000 49.33121  ? 409 HOH   A O   1 
HETATM 4733 O O   . HOH   D 4 .   ? 26.58466 14.91139  -12.01004 1.000 46.00784  ? 410 HOH   A O   1 
HETATM 4734 O O   . HOH   D 4 .   ? 25.84115 8.54067   -10.67137 1.000 59.99304  ? 411 HOH   A O   1 
HETATM 4735 O O   . HOH   D 4 .   ? 16.29640 18.49408  -14.66975 1.000 42.87492  ? 412 HOH   A O   1 
HETATM 4736 O O   . HOH   D 4 .   ? 44.51194 23.45529  -12.41036 1.000 64.88656  ? 413 HOH   A O   1 
HETATM 4737 O O   . HOH   D 4 .   ? 11.09819 14.18016  -8.13375  1.000 56.12612  ? 414 HOH   A O   1 
HETATM 4738 O O   . HOH   D 4 .   ? 14.87208 27.47326  -10.65827 1.000 53.24920  ? 415 HOH   A O   1 
HETATM 4739 O O   . HOH   D 4 .   ? 21.17522 17.64471  -25.97932 1.000 50.12330  ? 416 HOH   A O   1 
HETATM 4740 O O   . HOH   D 4 .   ? 38.82617 21.81062  -19.12134 1.000 54.46552  ? 417 HOH   A O   1 
HETATM 4741 O O   . HOH   D 4 .   ? 36.90232 35.90727  -16.68425 1.000 68.12335  ? 418 HOH   A O   1 
HETATM 4742 O O   . HOH   D 4 .   ? 37.63739 17.36343  -19.41610 1.000 58.53113  ? 419 HOH   A O   1 
HETATM 4743 O O   . HOH   D 4 .   ? 23.76997 30.15809  -33.50959 1.000 69.72230  ? 420 HOH   A O   1 
HETATM 4744 O O   . HOH   D 4 .   ? 16.76809 29.16331  -11.76191 1.000 52.72375  ? 421 HOH   A O   1 
HETATM 4745 O O   . HOH   D 4 .   ? 34.02564 17.13594  -11.58422 1.000 51.98448  ? 422 HOH   A O   1 
HETATM 4746 O O   . HOH   D 4 .   ? 30.39729 25.61628  -5.69764  1.000 51.88184  ? 423 HOH   A O   1 
HETATM 4747 O O   . HOH   D 4 .   ? 43.75750 25.66780  -13.50354 1.000 66.87444  ? 424 HOH   A O   1 
HETATM 4748 O O   . HOH   D 4 .   ? 38.64621 15.09622  -17.74799 1.000 53.03602  ? 425 HOH   A O   1 
HETATM 4749 O O   . HOH   D 4 .   ? 34.22633 17.72970  -14.36399 1.000 52.06718  ? 426 HOH   A O   1 
HETATM 4750 O O   . HOH   D 4 .   ? 20.84882 18.40255  -14.72513 1.000 48.80300  ? 427 HOH   A O   1 
HETATM 4751 O O   . HOH   D 4 .   ? 23.17992 4.27894   -7.95288  1.000 69.81977  ? 428 HOH   A O   1 
HETATM 4752 O O   . HOH   D 4 .   ? 12.82979 23.18220  -12.10114 1.000 44.80744  ? 429 HOH   A O   1 
HETATM 4753 O O   . HOH   D 4 .   ? 16.49755 18.32935  -24.67476 1.000 48.71926  ? 430 HOH   A O   1 
HETATM 4754 O O   . HOH   D 4 .   ? 16.24888 19.92219  -30.65771 1.000 54.92454  ? 431 HOH   A O   1 
HETATM 4755 O O   . HOH   D 4 .   ? 20.76350 33.59114  -7.98296  1.000 68.31977  ? 432 HOH   A O   1 
HETATM 4756 O O   . HOH   D 4 .   ? 32.89678 25.63735  -4.79958  1.000 58.10379  ? 433 HOH   A O   1 
HETATM 4757 O O   . HOH   D 4 .   ? 14.65402 33.82628  -32.47316 1.000 74.80031  ? 434 HOH   A O   1 
HETATM 4758 O O   . HOH   D 4 .   ? 14.50096 28.82140  -33.03847 1.000 72.59659  ? 435 HOH   A O   1 
HETATM 4759 O O   . HOH   D 4 .   ? 28.14538 15.10358  -5.76160  1.000 58.75284  ? 436 HOH   A O   1 
HETATM 4760 O O   . HOH   D 4 .   ? 11.62067 11.84363  -19.85177 1.000 50.10644  ? 437 HOH   A O   1 
HETATM 4761 O O   . HOH   D 4 .   ? 47.67506 25.96015  -12.28941 1.000 72.61994  ? 438 HOH   A O   1 
HETATM 4762 O O   . HOH   D 4 .   ? 5.58162  23.77659  -23.23938 1.000 55.02193  ? 439 HOH   A O   1 
HETATM 4763 O O   . HOH   D 4 .   ? 26.26049 1.93625   -4.45618  1.000 69.62712  ? 440 HOH   A O   1 
HETATM 4764 O O   . HOH   D 4 .   ? 13.72274 31.87344  -33.28774 1.000 74.93727  ? 441 HOH   A O   1 
HETATM 4765 O O   . HOH   D 4 .   ? 29.30326 23.82146  -3.78272  1.000 63.12480  ? 442 HOH   A O   1 
HETATM 4766 O O   . HOH   D 4 .   ? 14.65204 21.58913  -31.63643 1.000 63.24891  ? 443 HOH   A O   1 
HETATM 4767 O O   . HOH   E 4 .   ? 22.82504 17.97981  -27.96176 1.000 52.25358  ? 401 HOH   B O   1 
HETATM 4768 O O   . HOH   E 4 .   ? 16.11333 -11.86534 -18.74278 1.000 69.82623  ? 402 HOH   B O   1 
HETATM 4769 O O   . HOH   E 4 .   ? 20.15976 -6.14385  -21.26117 1.000 60.05308  ? 403 HOH   B O   1 
HETATM 4770 O O   . HOH   E 4 .   ? 25.31792 1.81620   -7.69635  1.000 64.53341  ? 404 HOH   B O   1 
HETATM 4771 O O   . HOH   E 4 .   ? 19.96628 -7.28262  -6.31089  1.000 83.35862  ? 405 HOH   B O   1 
HETATM 4772 O O   . HOH   E 4 .   ? 19.50226 -1.77555  -11.42655 1.000 65.83972  ? 406 HOH   B O   1 
HETATM 4773 O O   . HOH   E 4 .   ? 28.26904 -0.92273  -22.59760 1.000 67.93886  ? 407 HOH   B O   1 
HETATM 4774 O O   . HOH   E 4 .   ? 47.59948 -2.28864  -10.57295 1.000 77.16624  ? 408 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   ? 0.94674 1.56140 1.38151 0.15716  -0.19369 -0.28227 1   MET   A N   
2    C CA  . MET   A 4   ? 1.24484 1.83784 1.66560 0.13105  -0.18003 -0.26315 1   MET   A CA  
3    C C   . MET   A 4   ? 1.26784 1.89574 1.71467 0.12460  -0.18556 -0.27703 1   MET   A C   
4    O O   . MET   A 4   ? 1.24142 1.83993 1.66834 0.11614  -0.18993 -0.26639 1   MET   A O   
5    C CB  . MET   A 4   ? 1.27825 1.79953 1.64794 0.13452  -0.19049 -0.24120 1   MET   A CB  
6    C CG  . MET   A 4   ? 1.10843 1.59258 1.45126 0.12863  -0.17710 -0.22132 1   MET   A CG  
7    S SD  . MET   A 4   ? 1.18688 1.68870 1.54332 0.09538  -0.14123 -0.20702 1   MET   A SD  
8    C CE  . MET   A 4   ? 1.05998 1.55090 1.41077 0.07669  -0.13864 -0.19896 1   MET   A CE  
9    N N   . GLU   A 5   ? 1.30743 1.99771 1.79768 0.12764  -0.18429 -0.30116 2   GLU   A N   
10   C CA  . GLU   A 5   ? 1.32982 2.04428 1.83775 0.11963  -0.18607 -0.31279 2   GLU   A CA  
11   C C   . GLU   A 5   ? 1.30557 2.04707 1.83313 0.08526  -0.15812 -0.30731 2   GLU   A C   
12   O O   . GLU   A 5   ? 1.18405 1.92475 1.71410 0.07124  -0.15921 -0.30541 2   GLU   A O   
13   C CB  . GLU   A 5   ? 1.33043 2.07356 1.85563 0.13865  -0.19503 -0.33646 2   GLU   A CB  
14   C CG  . GLU   A 5   ? 1.33443 2.10676 1.88065 0.13124  -0.19727 -0.35065 2   GLU   A CG  
15   C CD  . GLU   A 5   ? 1.38455 2.19008 1.95064 0.14929  -0.20458 -0.37583 2   GLU   A CD  
16   O OE1 . GLU   A 5   ? 1.49043 2.29479 2.05284 0.16799  -0.20815 -0.38261 2   GLU   A OE1 
17   O OE2 . GLU   A 5   ? 1.26526 2.09849 1.85090 0.14485  -0.20710 -0.38983 2   GLU   A OE2 
18   N N   . ASN   A 6   ? 1.28462 2.04621 1.82273 0.07115  -0.13384 -0.30433 3   ASN   A N   
19   C CA  . ASN   A 6   ? 1.11478 1.89749 1.66681 0.03835  -0.10764 -0.29875 3   ASN   A CA  
20   C C   . ASN   A 6   ? 0.96539 1.72001 1.50296 0.01706  -0.09786 -0.27762 3   ASN   A C   
21   O O   . ASN   A 6   ? 0.97087 1.73445 1.51519 -0.01061 -0.07803 -0.27125 3   ASN   A O   
22   C CB  . ASN   A 6   ? 1.06211 1.86979 1.62350 0.03033  -0.08599 -0.30112 3   ASN   A CB  
23   C CG  . ASN   A 6   ? 1.19031 2.03679 1.77233 0.04227  -0.08946 -0.32483 3   ASN   A CG  
24   O OD1 . ASN   A 6   ? 1.18528 2.06206 1.78576 0.02607  -0.07992 -0.33392 3   ASN   A OD1 
25   N ND2 . ASN   A 6   ? 1.25198 2.09719 1.83052 0.07060  -0.10353 -0.33567 3   ASN   A ND2 
26   N N   . PHE   A 7   ? 0.88609 1.59284 1.39267 0.02835  -0.10932 -0.26317 4   PHE   A N   
27   C CA  . PHE   A 7   ? 0.85676 1.51563 1.33280 0.00977  -0.09689 -0.23814 4   PHE   A CA  
28   C C   . PHE   A 7   ? 0.75044 1.38385 1.21197 0.00921  -0.11069 -0.23571 4   PHE   A C   
29   O O   . PHE   A 7   ? 0.84048 1.46143 1.29170 0.03064  -0.13394 -0.24297 4   PHE   A O   
30   C CB  . PHE   A 7   ? 0.84850 1.45947 1.28927 0.01908  -0.09514 -0.21929 4   PHE   A CB  
31   C CG  . PHE   A 7   ? 0.87784 1.50533 1.32661 0.01357  -0.07726 -0.21659 4   PHE   A CG  
32   C CD1 . PHE   A 7   ? 0.79886 1.46726 1.27433 -0.00797 -0.05741 -0.22168 4   PHE   A CD1 
33   C CD2 . PHE   A 7   ? 0.79550 1.39633 1.22305 0.02877  -0.08044 -0.20897 4   PHE   A CD2 
34   C CE1 . PHE   A 7   ? 0.86391 1.54654 1.34340 -0.01355 -0.04093 -0.21906 4   PHE   A CE1 
35   C CE2 . PHE   A 7   ? 0.67705 1.29284 1.11061 0.02405  -0.06464 -0.20716 4   PHE   A CE2 
36   C CZ  . PHE   A 7   ? 0.87467 1.53156 1.33356 0.00324  -0.04479 -0.21215 4   PHE   A CZ  
37   N N   . GLN   A 8   ? 0.60570 1.22917 1.06422 -0.01512 -0.09698 -0.22560 5   GLN   A N   
38   C CA  . GLN   A 8   ? 0.67367 1.27320 1.11799 -0.01891 -0.10706 -0.22311 5   GLN   A CA  
39   C C   . GLN   A 8   ? 0.73354 1.28460 1.14621 -0.03309 -0.09358 -0.19964 5   GLN   A C   
40   O O   . GLN   A 8   ? 0.72662 1.28125 1.14545 -0.05389 -0.07367 -0.19147 5   GLN   A O   
41   C CB  . GLN   A 8   ? 0.62469 1.26688 1.10261 -0.03484 -0.10594 -0.23943 5   GLN   A CB  
42   C CG  . GLN   A 8   ? 0.81353 1.43180 1.27740 -0.04095 -0.11524 -0.23766 5   GLN   A CG  
43   C CD  . GLN   A 8   ? 1.00380 1.66477 1.50198 -0.05827 -0.11434 -0.25453 5   GLN   A CD  
44   O OE1 . GLN   A 8   ? 1.00594 1.65093 1.49621 -0.06856 -0.11821 -0.25357 5   GLN   A OE1 
45   N NE2 . GLN   A 8   ? 0.99482 1.71159 1.53149 -0.06228 -0.10892 -0.27101 5   GLN   A NE2 
46   N N   . LYS   A 9   ? 0.69584 1.20186 1.07393 -0.02184 -0.10467 -0.18938 6   LYS   A N   
47   C CA  . LYS   A 9   ? 0.69617 1.15869 1.04505 -0.03289 -0.09280 -0.16916 6   LYS   A CA  
48   C C   . LYS   A 9   ? 0.53903 1.00202 0.89416 -0.05357 -0.08486 -0.16892 6   LYS   A C   
49   O O   . LYS   A 9   ? 0.62202 1.09804 0.98665 -0.05412 -0.09630 -0.18131 6   LYS   A O   
50   C CB  . LYS   A 9   ? 0.75929 1.17777 1.07024 -0.01765 -0.10647 -0.16056 6   LYS   A CB  
51   C CG  . LYS   A 9   ? 0.70125 1.10790 0.99890 0.00062  -0.11352 -0.15725 6   LYS   A CG  
52   C CD  . LYS   A 9   ? 0.76065 1.12108 1.01737 0.01231  -0.12692 -0.14810 6   LYS   A CD  
53   C CE  . LYS   A 9   ? 0.80617 1.15020 1.04731 0.02869  -0.13435 -0.14413 6   LYS   A CE  
54   N NZ  . LYS   A 9   ? 0.98128 1.27795 1.17930 0.03779  -0.14766 -0.13473 6   LYS   A NZ  
55   N N   . VAL   A 10  ? 0.53627 0.98356 0.88533 -0.07007 -0.06644 -0.15530 7   VAL   A N   
56   C CA  . VAL   A 10  ? 0.69255 1.13439 1.04486 -0.09028 -0.05812 -0.15366 7   VAL   A CA  
57   C C   . VAL   A 10  ? 0.61092 1.00654 0.93097 -0.09064 -0.05667 -0.14029 7   VAL   A C   
58   O O   . VAL   A 10  ? 0.71446 1.09893 1.02837 -0.09594 -0.06176 -0.14396 7   VAL   A O   
59   C CB  . VAL   A 10  ? 0.60552 1.06440 0.97548 -0.11019 -0.03919 -0.14986 7   VAL   A CB  
60   C CG1 . VAL   A 10  ? 0.56699 1.01528 0.93779 -0.13139 -0.03255 -0.14830 7   VAL   A CG1 
61   C CG2 . VAL   A 10  ? 0.60120 1.11052 1.00378 -0.11085 -0.03887 -0.16476 7   VAL   A CG2 
62   N N   . GLU   A 11  ? 0.62895 0.99919 0.92888 -0.08509 -0.04970 -0.12597 8   GLU   A N   
63   C CA  . GLU   A 11  ? 0.64019 0.97137 0.91186 -0.08545 -0.04662 -0.11448 8   GLU   A CA  
64   C C   . GLU   A 11  ? 0.60331 0.91507 0.85556 -0.07442 -0.04413 -0.10277 8   GLU   A C   
65   O O   . GLU   A 11  ? 0.59690 0.92134 0.85859 -0.07204 -0.03902 -0.10008 8   GLU   A O   
66   C CB  . GLU   A 11  ? 0.63995 0.96050 0.91415 -0.10307 -0.03281 -0.10828 8   GLU   A CB  
67   C CG  . GLU   A 11  ? 0.89945 1.18440 1.14846 -0.10292 -0.03066 -0.10065 8   GLU   A CG  
68   C CD  . GLU   A 11  ? 1.01486 1.28780 1.26678 -0.11826 -0.02013 -0.09674 8   GLU   A CD  
69   O OE1 . GLU   A 11  ? 0.89204 1.18205 1.16316 -0.13113 -0.01460 -0.09891 8   GLU   A OE1 
70   O OE2 . GLU   A 11  ? 1.01658 1.26248 1.25057 -0.11759 -0.01758 -0.09194 8   GLU   A OE2 
71   N N   . LYS   A 12  ? 0.55598 0.83761 0.78048 -0.06870 -0.04751 -0.09650 9   LYS   A N   
72   C CA  . LYS   A 12  ? 0.61675 0.87750 0.82099 -0.06154 -0.04400 -0.08487 9   LYS   A CA  
73   C C   . LYS   A 12  ? 0.58648 0.83744 0.79130 -0.07134 -0.02760 -0.07420 9   LYS   A C   
74   O O   . LYS   A 12  ? 0.67516 0.91364 0.87527 -0.07917 -0.02205 -0.07263 9   LYS   A O   
75   C CB  . LYS   A 12  ? 0.65610 0.88976 0.82928 -0.05438 -0.05250 -0.08251 9   LYS   A CB  
76   C CG  . LYS   A 12  ? 0.68794 0.89897 0.83855 -0.05025 -0.04793 -0.07047 9   LYS   A CG  
77   C CD  . LYS   A 12  ? 0.66393 0.84885 0.78122 -0.04547 -0.05625 -0.06855 9   LYS   A CD  
78   C CE  . LYS   A 12  ? 0.73481 0.89798 0.82955 -0.04487 -0.05026 -0.05673 9   LYS   A CE  
79   N NZ  . LYS   A 12  ? 0.83736 0.97427 0.89610 -0.04217 -0.05822 -0.05442 9   LYS   A NZ  
80   N N   . ILE   A 13  ? 0.59184 0.84779 0.80191 -0.06982 -0.02106 -0.06777 10  ILE   A N   
81   C CA  . ILE   A 13  ? 0.62743 0.87384 0.83729 -0.07743 -0.00744 -0.05775 10  ILE   A CA  
82   C C   . ILE   A 13  ? 0.62113 0.84175 0.80802 -0.07385 -0.00483 -0.04940 10  ILE   A C   
83   O O   . ILE   A 13  ? 0.82668 1.03532 1.01014 -0.07956 0.00327  -0.04500 10  ILE   A O   
84   C CB  . ILE   A 13  ? 0.56502 0.82702 0.78777 -0.07740 -0.00182 -0.05467 10  ILE   A CB  
85   C CG1 . ILE   A 13  ? 0.54084 0.83102 0.78755 -0.08546 -0.00027 -0.06311 10  ILE   A CG1 
86   C CG2 . ILE   A 13  ? 0.54195 0.78999 0.75935 -0.08211 0.00957  -0.04332 10  ILE   A CG2 
87   C CD1 . ILE   A 13  ? 0.49706 0.80612 0.75581 -0.08584 0.00579  -0.06198 10  ILE   A CD1 
88   N N   A GLY   A 14  ? 0.72855 0.94030 0.89927 -0.06470 -0.01175 -0.04766 11  GLY   A N   
89   N N   B GLY   A 14  ? 0.73683 0.94837 0.90721 -0.06468 -0.01206 -0.04792 11  GLY   A N   
90   C CA  A GLY   A 14  ? 0.73451 0.92451 0.88331 -0.06363 -0.00814 -0.03997 11  GLY   A CA  
91   C CA  B GLY   A 14  ? 0.73171 0.92088 0.87911 -0.06366 -0.00916 -0.04099 11  GLY   A CA  
92   C C   A GLY   A 14  ? 0.76311 0.94299 0.89396 -0.05505 -0.01714 -0.03780 11  GLY   A C   
93   C C   B GLY   A 14  ? 0.76497 0.94287 0.89387 -0.05568 -0.01651 -0.03742 11  GLY   A C   
94   O O   A GLY   A 14  ? 0.67770 0.86695 0.81401 -0.04768 -0.02708 -0.04275 11  GLY   A O   
95   O O   B GLY   A 14  ? 0.68542 0.87243 0.82116 -0.04904 -0.02320 -0.03949 11  GLY   A O   
96   N N   A GLU   A 15  ? 0.84483 1.00514 0.95373 -0.05634 -0.01375 -0.03095 12  GLU   A N   
97   N N   B GLU   A 15  ? 0.80130 0.95880 0.90562 -0.05668 -0.01541 -0.03265 12  GLU   A N   
98   C CA  A GLU   A 15  ? 0.85216 0.99517 0.93725 -0.05087 -0.02217 -0.02726 12  GLU   A CA  
99   C CA  B GLU   A 15  ? 0.84394 0.98434 0.92541 -0.05215 -0.02147 -0.02735 12  GLU   A CA  
100  C C   A GLU   A 15  ? 0.94040 1.07414 1.01812 -0.05455 -0.01339 -0.01798 12  GLU   A C   
101  C C   B GLU   A 15  ? 0.89179 1.02200 0.96370 -0.05875 -0.00961 -0.01881 12  GLU   A C   
102  O O   A GLU   A 15  ? 0.92660 1.06042 1.00624 -0.06162 -0.00163 -0.01478 12  GLU   A O   
103  O O   B GLU   A 15  ? 0.86767 0.99397 0.93333 -0.06491 -0.00156 -0.01864 12  GLU   A O   
104  C CB  A GLU   A 15  ? 0.81062 0.93509 0.86811 -0.05124 -0.02879 -0.02872 12  GLU   A CB  
105  C CB  B GLU   A 15  ? 0.81845 0.94161 0.87326 -0.04866 -0.03362 -0.03018 12  GLU   A CB  
106  C CG  A GLU   A 15  ? 0.86449 0.96449 0.89100 -0.04748 -0.03820 -0.02349 12  GLU   A CG  
107  C CG  B GLU   A 15  ? 0.88113 0.98165 0.90890 -0.04399 -0.04272 -0.02443 12  GLU   A CG  
108  C CD  A GLU   A 15  ? 0.91606 0.99649 0.91214 -0.04773 -0.04663 -0.02513 12  GLU   A CD  
109  C CD  B GLU   A 15  ? 0.94097 1.01636 0.93283 -0.04462 -0.05114 -0.02357 12  GLU   A CD  
110  O OE1 A GLU   A 15  ? 0.91292 1.00059 0.91335 -0.05065 -0.04428 -0.03101 12  GLU   A OE1 
111  O OE1 B GLU   A 15  ? 0.94677 1.02464 0.93585 -0.04795 -0.04962 -0.02835 12  GLU   A OE1 
112  O OE2 A GLU   A 15  ? 1.01021 1.06569 0.97573 -0.04529 -0.05624 -0.02047 12  GLU   A OE2 
113  O OE2 B GLU   A 15  ? 0.96375 1.01466 0.92780 -0.04224 -0.05967 -0.01799 12  GLU   A OE2 
114  N N   A GLY   A 16  ? 0.88077 1.00700 0.95083 -0.04911 -0.02009 -0.01487 13  GLY   A N   
115  N N   B GLY   A 16  ? 0.92212 1.04981 0.99397 -0.05718 -0.00881 -0.01316 13  GLY   A N   
116  C CA  A GLY   A 16  ? 0.87846 0.99379 0.93896 -0.05309 -0.01399 -0.00659 13  GLY   A CA  
117  C CA  B GLY   A 16  ? 0.79349 0.91516 0.85981 -0.06364 0.00167  -0.00600 13  GLY   A CA  
118  C C   A GLY   A 16  ? 0.88808 0.97568 0.91520 -0.05285 -0.02264 -0.00215 13  GLY   A C   
119  C C   B GLY   A 16  ? 0.81423 0.92314 0.86745 -0.06131 -0.00373 -0.00054 13  GLY   A C   
120  O O   A GLY   A 16  ? 0.89160 0.96591 0.89907 -0.05099 -0.03149 -0.00442 13  GLY   A O   
121  O O   B GLY   A 16  ? 0.90183 0.99812 0.94004 -0.05493 -0.01661 -0.00166 13  GLY   A O   
122  N N   A THR   A 17  ? 0.87013 0.94663 0.88846 -0.05539 -0.02095 0.00437  14  THR   A N   
123  N N   B THR   A 17  ? 0.72048 0.83145 0.77892 -0.06588 0.00485  0.00475  14  THR   A N   
124  C CA  A THR   A 17  ? 0.84152 0.88707 0.82496 -0.05758 -0.02907 0.00992  14  THR   A CA  
125  C CA  B THR   A 17  ? 0.76936 0.86811 0.81710 -0.06450 -0.00005 0.00957  14  THR   A CA  
126  C C   A THR   A 17  ? 0.87531 0.90705 0.84694 -0.04434 -0.04857 0.00596  14  THR   A C   
127  C C   B THR   A 17  ? 0.80548 0.91152 0.86541 -0.05363 -0.00946 0.00584  14  THR   A C   
128  O O   A THR   A 17  ? 0.84809 0.86099 0.79499 -0.04241 -0.05887 0.00522  14  THR   A O   
129  O O   B THR   A 17  ? 0.85250 0.94352 0.89847 -0.04848 -0.01934 0.00702  14  THR   A O   
130  C CB  A THR   A 17  ? 0.92527 0.96324 0.90482 -0.06419 -0.02320 0.01693  14  THR   A CB  
131  C CB  B THR   A 17  ? 0.81156 0.91602 0.86751 -0.07148 0.01101  0.01430  14  THR   A CB  
132  O OG1 A THR   A 17  ? 0.92656 0.97876 0.91730 -0.07541 -0.00642 0.01913  14  THR   A OG1 
133  O OG1 B THR   A 17  ? 0.80873 0.93430 0.89233 -0.06863 0.01671  0.01223  14  THR   A OG1 
134  C CG2 A THR   A 17  ? 0.89510 0.89688 0.83550 -0.06873 -0.03208 0.02338  14  THR   A CG2 
135  C CG2 B THR   A 17  ? 0.80284 0.90529 0.84959 -0.08182 0.02105  0.01565  14  THR   A CG2 
136  N N   A TYR   A 18  ? 0.99086 1.03179 0.97910 -0.03434 -0.05446 0.00255  15  TYR   A N   
137  N N   B TYR   A 18  ? 0.80013 0.92879 0.88523 -0.05051 -0.00648 0.00073  15  TYR   A N   
138  C CA  A TYR   A 18  ? 0.92392 0.95545 0.90502 -0.01908 -0.07382 -0.00371 15  TYR   A CA  
139  C CA  B TYR   A 18  ? 0.80916 0.95076 0.90816 -0.04123 -0.01353 -0.00480 15  TYR   A CA  
140  C C   A TYR   A 18  ? 0.90864 0.97081 0.91859 -0.00913 -0.07787 -0.01547 15  TYR   A C   
141  C C   B TYR   A 18  ? 0.83203 0.96728 0.92102 -0.03196 -0.02851 -0.01135 15  TYR   A C   
142  O O   A TYR   A 18  ? 0.90208 0.95918 0.90576 0.00349  -0.09491 -0.02284 15  TYR   A O   
143  O O   B TYR   A 18  ? 0.85533 0.99280 0.94653 -0.02183 -0.03815 -0.01597 15  TYR   A O   
144  C CB  A TYR   A 18  ? 0.85469 0.87876 0.83611 -0.01236 -0.07937 -0.00302 15  TYR   A CB  
145  C CB  B TYR   A 18  ? 0.78838 0.95540 0.91428 -0.04359 -0.00532 -0.00839 15  TYR   A CB  
146  C CG  A TYR   A 18  ? 0.93034 0.92181 0.88217 -0.02243 -0.07802 0.00776  15  TYR   A CG  
147  C CG  B TYR   A 18  ? 0.73455 0.90389 0.86405 -0.05081 0.00121  -0.00886 15  TYR   A CG  
148  C CD1 A TYR   A 18  ? 0.87859 0.82981 0.78998 -0.02295 -0.09139 0.01258  15  TYR   A CD1 
149  C CD1 B TYR   A 18  ? 0.63408 0.80639 0.76357 -0.04933 -0.00484 -0.01549 15  TYR   A CD1 
150  C CD2 A TYR   A 18  ? 0.89213 0.89211 0.85523 -0.03215 -0.06412 0.01299  15  TYR   A CD2 
151  C CD2 B TYR   A 18  ? 0.69130 0.85974 0.82438 -0.05804 0.01223  -0.00387 15  TYR   A CD2 
152  C CE1 A TYR   A 18  ? 0.92367 0.84421 0.80663 -0.03506 -0.08956 0.02264  15  TYR   A CE1 
153  C CE1 B TYR   A 18  ? 0.73788 0.91062 0.86956 -0.05562 0.00047  -0.01685 15  TYR   A CE1 
154  C CE2 A TYR   A 18  ? 0.87994 0.85269 0.81794 -0.04307 -0.06271 0.02184  15  TYR   A CE2 
155  C CE2 B TYR   A 18  ? 0.64900 0.81799 0.78485 -0.06299 0.01717  -0.00571 15  TYR   A CE2 
156  C CZ  A TYR   A 18  ? 0.82993 0.76312 0.72792 -0.04552 -0.07480 0.02677  15  TYR   A CZ  
157  C CZ  B TYR   A 18  ? 0.78257 0.95292 0.91707 -0.06214 0.01154  -0.01206 15  TYR   A CZ  
158  O OH  A TYR   A 18  ? 0.89248 0.79774 0.76413 -0.05927 -0.07273 0.03583  15  TYR   A OH  
159  O OH  B TYR   A 18  ? 0.81372 0.98303 0.94994 -0.06681 0.01583  -0.01477 15  TYR   A OH  
160  N N   A GLY   A 19  ? 1.05032 1.14328 1.09083 -0.01477 -0.06355 -0.01777 16  GLY   A N   
161  N N   B GLY   A 19  ? 1.00085 1.12830 1.07846 -0.03407 -0.03163 -0.01287 16  GLY   A N   
162  C CA  A GLY   A 19  ? 0.87482 0.99947 0.94508 -0.00839 -0.06531 -0.02881 16  GLY   A CA  
163  C CA  B GLY   A 19  ? 0.94410 1.06640 1.01275 -0.02447 -0.04738 -0.01995 16  GLY   A CA  
164  C C   A GLY   A 19  ? 0.84112 0.97866 0.92133 -0.01672 -0.05767 -0.03094 16  GLY   A C   
165  C C   B GLY   A 19  ? 0.83561 0.97424 0.91746 -0.02611 -0.04698 -0.02716 16  GLY   A C   
166  O O   A GLY   A 19  ? 0.85043 0.98627 0.93044 -0.02812 -0.04393 -0.02449 16  GLY   A O   
167  O O   B GLY   A 19  ? 0.80265 0.94476 0.88867 -0.03586 -0.03556 -0.02470 16  GLY   A O   
168  N N   A VAL   A 20  ? 0.84686 0.99778 0.93651 -0.01026 -0.06761 -0.04126 17  VAL   A N   
169  N N   B VAL   A 20  ? 0.85376 1.00296 0.94301 -0.01622 -0.06012 -0.03719 17  VAL   A N   
170  C CA  A VAL   A 20  ? 0.72628 0.89359 0.83050 -0.01740 -0.06199 -0.04602 17  VAL   A CA  
171  C CA  B VAL   A 20  ? 0.69964 0.86641 0.80337 -0.01797 -0.06147 -0.04570 17  VAL   A CA  
172  C C   A VAL   A 20  ? 0.72014 0.92323 0.85994 -0.01690 -0.05830 -0.05491 17  VAL   A C   
173  C C   B VAL   A 20  ? 0.71891 0.92080 0.85791 -0.01715 -0.05749 -0.05394 17  VAL   A C   
174  O O   A VAL   A 20  ? 0.70886 0.92696 0.85988 -0.00599 -0.06871 -0.06399 17  VAL   A O   
175  O O   B VAL   A 20  ? 0.70328 0.91842 0.85239 -0.00632 -0.06681 -0.06163 17  VAL   A O   
176  C CB  A VAL   A 20  ? 0.78165 0.93765 0.86875 -0.01248 -0.07637 -0.05174 17  VAL   A CB  
177  C CB  B VAL   A 20  ? 0.78806 0.94277 0.87399 -0.00848 -0.08011 -0.05226 17  VAL   A CB  
178  C CG1 A VAL   A 20  ? 0.71453 0.88964 0.81961 -0.01953 -0.07178 -0.05864 17  VAL   A CG1 
179  C CG1 B VAL   A 20  ? 0.73117 0.89623 0.82420 -0.01392 -0.07967 -0.05863 17  VAL   A CG1 
180  C CG2 A VAL   A 20  ? 0.81298 0.93283 0.86117 -0.01599 -0.07790 -0.04217 17  VAL   A CG2 
181  C CG2 B VAL   A 20  ? 0.86893 0.98472 0.91435 -0.00785 -0.08627 -0.04297 17  VAL   A CG2 
182  N N   . VAL   A 21  ? 0.54227 0.75866 0.69882 -0.02879 -0.04377 -0.05287 18  VAL   A N   
183  C CA  . VAL   A 21  ? 0.60959 0.85713 0.79632 -0.03266 -0.03706 -0.05884 18  VAL   A CA  
184  C C   . VAL   A 21  ? 0.58676 0.85093 0.78821 -0.03810 -0.03911 -0.06817 18  VAL   A C   
185  O O   . VAL   A 21  ? 0.55114 0.80351 0.74542 -0.04617 -0.03495 -0.06536 18  VAL   A O   
186  C CB  . VAL   A 21  ? 0.55736 0.80483 0.75009 -0.04292 -0.02069 -0.04946 18  VAL   A CB  
187  C CG1 . VAL   A 21  ? 0.46197 0.73890 0.68115 -0.04908 -0.01338 -0.05469 18  VAL   A CG1 
188  C CG2 . VAL   A 21  ? 0.62334 0.85530 0.80213 -0.03798 -0.01960 -0.04120 18  VAL   A CG2 
189  N N   . TYR   A 22  ? 0.41116 0.70407 0.63402 -0.03365 -0.04568 -0.08050 19  TYR   A N   
190  C CA  . TYR   A 22  ? 0.47283 0.78749 0.71452 -0.04030 -0.04756 -0.09116 19  TYR   A CA  
191  C C   . TYR   A 22  ? 0.57244 0.91849 0.84237 -0.05130 -0.03558 -0.09507 19  TYR   A C   
192  O O   . TYR   A 22  ? 0.59908 0.95796 0.87699 -0.04829 -0.03083 -0.09455 19  TYR   A O   
193  C CB  . TYR   A 22  ? 0.57052 0.89732 0.81586 -0.02694 -0.06649 -0.10499 19  TYR   A CB  
194  C CG  . TYR   A 22  ? 0.62924 0.92317 0.84266 -0.01632 -0.08055 -0.10163 19  TYR   A CG  
195  C CD1 . TYR   A 22  ? 0.74682 1.02684 0.94722 -0.02071 -0.08481 -0.10239 19  TYR   A CD1 
196  C CD2 . TYR   A 22  ? 0.72355 0.99862 0.91749 -0.00260 -0.08997 -0.09793 19  TYR   A CD2 
197  C CE1 . TYR   A 22  ? 0.88891 1.13803 1.05642 -0.01244 -0.09703 -0.09897 19  TYR   A CE1 
198  C CE2 . TYR   A 22  ? 0.81847 1.06010 0.97894 0.00495  -0.10278 -0.09380 19  TYR   A CE2 
199  C CZ  . TYR   A 22  ? 0.83477 1.06412 0.98156 -0.00034 -0.10580 -0.09411 19  TYR   A CZ  
200  O OH  . TYR   A 22  ? 0.93983 1.13498 1.04968 0.00574  -0.11783 -0.08956 19  TYR   A OH  
201  N N   . LYS   A 23  ? 0.60790 0.96486 0.89086 -0.06507 -0.03070 -0.09907 20  LYS   A N   
202  C CA  . LYS   A 23  ? 0.46211 0.85082 0.77128 -0.07816 -0.02080 -0.10482 20  LYS   A CA  
203  C C   . LYS   A 23  ? 0.47220 0.89766 0.80500 -0.07333 -0.03152 -0.12321 20  LYS   A C   
204  O O   . LYS   A 23  ? 0.56121 0.98762 0.89573 -0.07332 -0.04143 -0.13102 20  LYS   A O   
205  C CB  . LYS   A 23  ? 0.48115 0.85918 0.79037 -0.09730 -0.01041 -0.09933 20  LYS   A CB  
206  C CG  . LYS   A 23  ? 0.47499 0.88262 0.80785 -0.11469 -0.00037 -0.10488 20  LYS   A CG  
207  C CD  . LYS   A 23  ? 0.57504 0.96461 0.90357 -0.13328 0.00697  -0.09936 20  LYS   A CD  
208  C CE  . LYS   A 23  ? 0.60963 1.02546 0.95821 -0.15381 0.01702  -0.10410 20  LYS   A CE  
209  N NZ  . LYS   A 23  ? 0.78127 1.17264 1.12166 -0.17230 0.02298  -0.09760 20  LYS   A NZ  
210  N N   . ALA   A 24  ? 0.46026 0.91722 0.81159 -0.06839 -0.03014 -0.13135 21  ALA   A N   
211  C CA  . ALA   A 24  ? 0.45969 0.95781 0.83756 -0.06182 -0.04029 -0.15124 21  ALA   A CA  
212  C C   . ALA   A 24  ? 0.58095 1.12029 0.98813 -0.08029 -0.02604 -0.15914 21  ALA   A C   
213  O O   . ALA   A 24  ? 0.57900 1.11341 0.98277 -0.09479 -0.00926 -0.14843 21  ALA   A O   
214  C CB  . ALA   A 24  ? 0.56987 1.07471 0.94667 -0.03813 -0.05275 -0.15828 21  ALA   A CB  
215  N N   . ARG   A 25  ? 0.61508 1.19569 1.05044 -0.08018 -0.03326 -0.17847 22  ARG   A N   
216  C CA  . ARG   A 25  ? 0.52234 1.14728 0.98760 -0.10026 -0.01985 -0.18849 22  ARG   A CA  
217  C C   . ARG   A 25  ? 0.58583 1.26374 1.08264 -0.08692 -0.02865 -0.21176 22  ARG   A C   
218  O O   . ARG   A 25  ? 0.67401 1.36253 1.17968 -0.07222 -0.04749 -0.22545 22  ARG   A O   
219  C CB  . ARG   A 25  ? 0.60232 1.22648 1.07380 -0.12184 -0.01732 -0.18974 22  ARG   A CB  
220  C CG  . ARG   A 25  ? 0.66392 1.32968 1.16287 -0.14746 -0.00206 -0.19830 22  ARG   A CG  
221  C CD  . ARG   A 25  ? 0.80313 1.46498 1.30712 -0.16837 -0.00223 -0.20059 22  ARG   A CD  
222  N NE  . ARG   A 25  ? 1.01441 1.69486 1.52814 -0.19093 0.01266  -0.20236 22  ARG   A NE  
223  C CZ  . ARG   A 25  ? 1.08942 1.80598 1.62338 -0.18997 0.01048  -0.21813 22  ARG   A CZ  
224  N NH1 . ARG   A 25  ? 1.08080 1.82089 1.62974 -0.16701 -0.00684 -0.23470 22  ARG   A NH1 
225  N NH2 . ARG   A 25  ? 0.92814 1.65669 1.46633 -0.21253 0.02547  -0.21755 22  ARG   A NH2 
226  N N   . ASN   A 26  ? 0.71055 1.42198 1.22370 -0.09123 -0.01567 -0.21712 23  ASN   A N   
227  C CA  . ASN   A 26  ? 0.68731 1.43663 1.22011 -0.07729 -0.02124 -0.23651 23  ASN   A CA  
228  C C   . ASN   A 26  ? 0.73542 1.50831 1.28508 -0.09220 -0.01900 -0.24748 23  ASN   A C   
229  O O   . ASN   A 26  ? 0.79793 1.56903 1.34613 -0.11906 -0.00210 -0.23960 23  ASN   A O   
230  C CB  . ASN   A 26  ? 0.77206 1.53472 1.30385 -0.07797 -0.00572 -0.23519 23  ASN   A CB  
231  C CG  . ASN   A 26  ? 0.82080 1.61912 1.36981 -0.05941 -0.01271 -0.25629 23  ASN   A CG  
232  O OD1 . ASN   A 26  ? 0.73949 1.56779 1.30477 -0.06919 -0.00691 -0.26835 23  ASN   A OD1 
233  N ND2 . ASN   A 26  ? 0.77693 1.57158 1.32202 -0.03242 -0.02566 -0.26155 23  ASN   A ND2 
234  N N   . LYS   A 27  ? 0.81870 1.61178 1.38302 -0.07451 -0.03714 -0.26571 24  LYS   A N   
235  C CA  . LYS   A 27  ? 0.84868 1.66401 1.42996 -0.08746 -0.03766 -0.27716 24  LYS   A CA  
236  C C   . LYS   A 27  ? 0.88327 1.73565 1.48083 -0.09967 -0.02133 -0.28688 24  LYS   A C   
237  O O   . LYS   A 27  ? 0.87211 1.73678 1.47845 -0.12303 -0.01153 -0.28849 24  LYS   A O   
238  C CB  . LYS   A 27  ? 0.98520 1.80845 1.57515 -0.06361 -0.06373 -0.29361 24  LYS   A CB  
239  C CG  . LYS   A 27  ? 1.03306 1.82101 1.60620 -0.05771 -0.08004 -0.28527 24  LYS   A CG  
240  C CD  . LYS   A 27  ? 1.10560 1.89346 1.67854 -0.02746 -0.10850 -0.29926 24  LYS   A CD  
241  C CE  . LYS   A 27  ? 1.05974 1.84104 1.62385 -0.00034 -0.11765 -0.30052 24  LYS   A CE  
242  N NZ  . LYS   A 27  ? 1.11661 1.88629 1.67243 0.02980  -0.14772 -0.31115 24  LYS   A NZ  
243  N N   . LEU   A 28  ? 1.02669 1.89682 1.62755 -0.08491 -0.01843 -0.29398 25  LEU   A N   
244  C CA  . LEU   A 28  ? 1.09654 2.00518 1.71276 -0.09539 -0.00358 -0.30574 25  LEU   A CA  
245  C C   . LEU   A 28  ? 1.02120 1.92032 1.62396 -0.12244 0.02151  -0.28907 25  LEU   A C   
246  O O   . LEU   A 28  ? 0.96360 1.88216 1.57377 -0.14605 0.03615  -0.29157 25  LEU   A O   
247  C CB  . LEU   A 28  ? 0.99895 1.93188 1.62423 -0.06742 -0.01206 -0.32313 25  LEU   A CB  
248  C CG  . LEU   A 28  ? 0.98759 1.93737 1.62845 -0.04060 -0.03649 -0.34441 25  LEU   A CG  
249  C CD1 . LEU   A 28  ? 0.87291 1.84506 1.52091 -0.01490 -0.04265 -0.36174 25  LEU   A CD1 
250  C CD2 . LEU   A 28  ? 0.86372 1.84322 1.52594 -0.05495 -0.03604 -0.35772 25  LEU   A CD2 
251  N N   . THR   A 29  ? 0.83178 1.70017 1.41354 -0.11960 0.02613  -0.27203 26  THR   A N   
252  C CA  . THR   A 29  ? 0.80596 1.66293 1.37183 -0.14161 0.04811  -0.25635 26  THR   A CA  
253  C C   . THR   A 29  ? 0.73482 1.55377 1.28279 -0.16543 0.05571  -0.23518 26  THR   A C   
254  O O   . THR   A 29  ? 0.75509 1.56367 1.28949 -0.18787 0.07349  -0.22272 26  THR   A O   
255  C CB  . THR   A 29  ? 0.68426 1.53071 1.23699 -0.12511 0.04961  -0.25065 26  THR   A CB  
256  O OG1 . THR   A 29  ? 0.72548 1.53527 1.26394 -0.11396 0.03877  -0.23760 26  THR   A OG1 
257  C CG2 . THR   A 29  ? 0.80788 1.68718 1.37654 -0.09853 0.03929  -0.27249 26  THR   A CG2 
258  N N   . GLY   A 30  ? 0.72332 1.52008 1.26932 -0.16089 0.04206  -0.23141 27  GLY   A N   
259  C CA  . GLY   A 30  ? 0.76479 1.52304 1.29286 -0.18053 0.04759  -0.21260 27  GLY   A CA  
260  C C   . GLY   A 30  ? 0.66224 1.38594 1.16800 -0.17629 0.05111  -0.19465 27  GLY   A C   
261  O O   . GLY   A 30  ? 0.67234 1.36202 1.16188 -0.19138 0.05557  -0.17915 27  GLY   A O   
262  N N   . GLU   A 31  ? 0.59766 1.32864 1.10207 -0.15614 0.04881  -0.19702 28  GLU   A N   
263  C CA  . GLU   A 31  ? 0.63574 1.33647 1.12034 -0.15116 0.05154  -0.18107 28  GLU   A CA  
264  C C   . GLU   A 31  ? 0.61025 1.28514 1.08933 -0.14214 0.03737  -0.17608 28  GLU   A C   
265  O O   . GLU   A 31  ? 0.56892 1.25031 1.05709 -0.12594 0.02008  -0.18752 28  GLU   A O   
266  C CB  . GLU   A 31  ? 0.62423 1.34051 1.11056 -0.12962 0.04952  -0.18753 28  GLU   A CB  
267  C CG  . GLU   A 31  ? 0.86941 1.60787 1.35632 -0.13850 0.06536  -0.19084 28  GLU   A CG  
268  C CD  . GLU   A 31  ? 0.95792 1.71701 1.45086 -0.11399 0.05987  -0.20299 28  GLU   A CD  
269  O OE1 . GLU   A 31  ? 0.77361 1.55335 1.28326 -0.09330 0.04429  -0.22052 28  GLU   A OE1 
270  O OE2 . GLU   A 31  ? 0.93958 1.69234 1.41930 -0.11465 0.06996  -0.19538 28  GLU   A OE2 
271  N N   . VAL   A 32  ? 0.54703 1.17284 0.99605 -0.14818 0.04309  -0.15453 29  VAL   A N   
272  C CA  . VAL   A 32  ? 0.53954 1.11787 0.96419 -0.13423 0.03086  -0.14308 29  VAL   A CA  
273  C C   . VAL   A 32  ? 0.51264 1.06607 0.91637 -0.11827 0.03075  -0.13184 29  VAL   A C   
274  O O   . VAL   A 32  ? 0.47296 1.02683 0.87091 -0.12588 0.04377  -0.12433 29  VAL   A O   
275  C CB  . VAL   A 32  ? 0.48573 1.02757 0.89388 -0.15224 0.03571  -0.12939 29  VAL   A CB  
276  C CG1 . VAL   A 32  ? 0.51588 1.07952 0.94370 -0.16770 0.03368  -0.14137 29  VAL   A CG1 
277  C CG2 . VAL   A 32  ? 0.61412 1.13826 1.00760 -0.16933 0.05236  -0.11401 29  VAL   A CG2 
278  N N   . VAL   A 33  ? 0.45324 0.98459 0.84429 -0.09690 0.01560  -0.13099 30  VAL   A N   
279  C CA  . VAL   A 33  ? 0.41074 0.91648 0.78136 -0.08169 0.01330  -0.12120 30  VAL   A CA  
280  C C   . VAL   A 33  ? 0.47175 0.93309 0.81738 -0.07422 0.00407  -0.10992 30  VAL   A C   
281  O O   . VAL   A 33  ? 0.43965 0.89430 0.78497 -0.07555 -0.00363 -0.11308 30  VAL   A O   
282  C CB  . VAL   A 33  ? 0.40449 0.93411 0.78552 -0.06053 0.00305  -0.13518 30  VAL   A CB  
283  C CG1 . VAL   A 33  ? 0.48496 1.06233 0.89108 -0.06758 0.01410  -0.14774 30  VAL   A CG1 
284  C CG2 . VAL   A 33  ? 0.38440 0.91972 0.77205 -0.04530 -0.01635 -0.14814 30  VAL   A CG2 
285  N N   . ALA   A 34  ? 0.45757 0.88980 0.78197 -0.06722 0.00539  -0.09733 31  ALA   A N   
286  C CA  . ALA   A 34  ? 0.42813 0.82166 0.72828 -0.05900 -0.00278 -0.08781 31  ALA   A CA  
287  C C   . ALA   A 34  ? 0.53728 0.92643 0.82977 -0.03830 -0.01741 -0.09333 31  ALA   A C   
288  O O   . ALA   A 34  ? 0.57275 0.96731 0.86523 -0.03055 -0.01647 -0.09393 31  ALA   A O   
289  C CB  . ALA   A 34  ? 0.48348 0.84795 0.76559 -0.06581 0.00761  -0.07104 31  ALA   A CB  
290  N N   . LEU   A 35  ? 0.41903 0.79593 0.70272 -0.02939 -0.03171 -0.09743 32  LEU   A N   
291  C CA  . LEU   A 35  ? 0.39436 0.76517 0.66934 -0.00941 -0.04906 -0.10434 32  LEU   A CA  
292  C C   . LEU   A 35  ? 0.60455 0.93041 0.84584 -0.00508 -0.05469 -0.09130 32  LEU   A C   
293  O O   . LEU   A 35  ? 0.63000 0.93779 0.85810 -0.00919 -0.05782 -0.08768 32  LEU   A O   
294  C CB  . LEU   A 35  ? 0.44306 0.83588 0.73286 -0.00211 -0.06323 -0.12061 32  LEU   A CB  
295  C CG  . LEU   A 35  ? 0.62225 1.01657 0.90908 0.02068  -0.08400 -0.13240 32  LEU   A CG  
296  C CD1 . LEU   A 35  ? 0.62072 1.03959 0.92332 0.02984  -0.08202 -0.14060 32  LEU   A CD1 
297  C CD2 . LEU   A 35  ? 0.53150 0.94929 0.83491 0.02562  -0.09741 -0.14847 32  LEU   A CD2 
298  N N   . LYS   A 36  ? 0.55336 0.86188 0.78024 0.00215  -0.05555 -0.08489 33  LYS   A N   
299  C CA  . LYS   A 36  ? 0.67861 0.94598 0.87313 0.00498  -0.06084 -0.07329 33  LYS   A CA  
300  C C   . LYS   A 36  ? 0.68861 0.94119 0.86750 0.02235  -0.08208 -0.08017 33  LYS   A C   
301  O O   . LYS   A 36  ? 0.69908 0.96152 0.88466 0.03591  -0.09095 -0.08880 33  LYS   A O   
302  C CB  . LYS   A 36  ? 0.54941 0.80313 0.73493 0.00194  -0.05142 -0.06249 33  LYS   A CB  
303  C CG  . LYS   A 36  ? 0.68819 0.90194 0.84151 0.00166  -0.05510 -0.05074 33  LYS   A CG  
304  C CD  . LYS   A 36  ? 0.74402 0.94716 0.89100 -0.00152 -0.04687 -0.04166 33  LYS   A CD  
305  C CE  . LYS   A 36  ? 0.71864 0.93401 0.87923 -0.01528 -0.02900 -0.03516 33  LYS   A CE  
306  N NZ  . LYS   A 36  ? 0.76793 0.97334 0.92218 -0.01777 -0.02245 -0.02691 33  LYS   A NZ  
307  N N   . LYS   A 37  ? 0.65889 0.88632 0.81514 0.02243  -0.09084 -0.07672 34  LYS   A N   
308  C CA  . LYS   A 37  ? 0.71555 0.92307 0.85142 0.03812  -0.11295 -0.08215 34  LYS   A CA  
309  C C   . LYS   A 37  ? 0.82496 0.98705 0.92239 0.03860  -0.11708 -0.06890 34  LYS   A C   
310  O O   . LYS   A 37  ? 0.90008 1.04294 0.98073 0.02482  -0.10572 -0.05648 34  LYS   A O   
311  C CB  . LYS   A 37  ? 0.71510 0.92285 0.84722 0.03716  -0.12122 -0.08730 34  LYS   A CB  
312  C CG  . LYS   A 37  ? 0.98062 1.16837 1.09120 0.05437  -0.14651 -0.09406 34  LYS   A CG  
313  C CD  . LYS   A 37  ? 1.03805 1.21671 1.13545 0.05008  -0.15257 -0.09500 34  LYS   A CD  
314  C CE  . LYS   A 37  ? 1.13863 1.30198 1.21777 0.06848  -0.17992 -0.10401 34  LYS   A CE  
315  N NZ  . LYS   A 37  ? 1.10151 1.30720 1.21767 0.08217  -0.19110 -0.12400 34  LYS   A NZ  
316  N N   . ILE   A 38  ? 0.80511 0.95052 0.88886 0.05411  -0.13345 -0.07243 35  ILE   A N   
317  C CA  . ILE   A 38  ? 0.88250 0.98148 0.92714 0.05425  -0.13989 -0.06057 35  ILE   A CA  
318  C C   . ILE   A 38  ? 1.00228 1.07303 1.01983 0.07028  -0.16592 -0.06568 35  ILE   A C   
319  O O   . ILE   A 38  ? 0.98053 1.06185 1.00924 0.08922  -0.18205 -0.07885 35  ILE   A O   
320  C CB  . ILE   A 38  ? 0.87305 0.96974 0.92124 0.05698  -0.13574 -0.05818 35  ILE   A CB  
321  C CG1 . ILE   A 38  ? 0.75888 0.88125 0.83117 0.04169  -0.11151 -0.05273 35  ILE   A CG1 
322  C CG2 . ILE   A 38  ? 0.80765 0.85410 0.81400 0.05554  -0.14373 -0.04638 35  ILE   A CG2 
323  C CD1 . ILE   A 38  ? 0.70152 0.82376 0.77774 0.04384  -0.10708 -0.05092 35  ILE   A CD1 
324  N N   . ARG   A 39  ? 0.92925 0.96423 0.91034 0.06324  -0.17048 -0.05601 36  ARG   A N   
325  C CA  . ARG   A 39  ? 0.99384 0.99418 0.94105 0.07681  -0.19610 -0.05842 36  ARG   A CA  
326  C C   . ARG   A 39  ? 1.01988 0.97422 0.93118 0.08072  -0.20650 -0.04969 36  ARG   A C   
327  O O   . ARG   A 39  ? 1.15486 1.07932 1.03794 0.06418  -0.19619 -0.03448 36  ARG   A O   
328  C CB  . ARG   A 39  ? 1.17481 1.15638 1.09550 0.06591  -0.19559 -0.05177 36  ARG   A CB  
329  C CG  . ARG   A 39  ? 1.22523 1.24704 1.17839 0.05517  -0.17882 -0.05635 36  ARG   A CG  
330  C CD  . ARG   A 39  ? 1.30786 1.33865 1.26270 0.06433  -0.19469 -0.06777 36  ARG   A CD  
331  N NE  . ARG   A 39  ? 1.45748 1.44658 1.36507 0.06028  -0.20400 -0.05963 36  ARG   A NE  
332  C CZ  . ARG   A 39  ? 1.47565 1.42825 1.34712 0.07386  -0.22908 -0.06014 36  ARG   A CZ  
333  N NH1 . ARG   A 39  ? 1.45706 1.40962 1.33563 0.09456  -0.24896 -0.06965 36  ARG   A NH1 
334  N NH2 . ARG   A 39  ? 1.47764 1.39195 1.30325 0.06696  -0.23490 -0.05142 36  ARG   A NH2 
335  N N   . LEU   A 40  ? 1.05463 1.00382 0.96743 0.10241  -0.22717 -0.06032 37  LEU   A N   
336  C CA  . LEU   A 40  ? 1.13503 1.03944 1.01521 0.10730  -0.23848 -0.05349 37  LEU   A CA  
337  C C   . LEU   A 40  ? 1.17866 1.02202 1.00117 0.10707  -0.25749 -0.04343 37  LEU   A C   
338  O O   . LEU   A 40  ? 1.17264 0.97074 0.95858 0.09960  -0.25994 -0.03113 37  LEU   A O   
339  C CB  . LEU   A 40  ? 1.07529 0.99471 0.97683 0.13222  -0.25473 -0.06998 37  LEU   A CB  
340  C CG  . LEU   A 40  ? 0.93205 0.90903 0.88608 0.13266  -0.23668 -0.08028 37  LEU   A CG  
341  C CD1 . LEU   A 40  ? 0.99352 0.98496 0.96532 0.15903  -0.25463 -0.09885 37  LEU   A CD1 
342  C CD2 . LEU   A 40  ? 0.84265 0.81602 0.79632 0.11300  -0.21368 -0.06653 37  LEU   A CD2 
343  N N   . ASP   A 41  ? 1.19414 1.03397 1.00583 0.11399  -0.27131 -0.04827 38  ASP   A N   
344  C CA  . ASP   A 41  ? 1.25482 1.03456 1.00727 0.11291  -0.28971 -0.03808 38  ASP   A CA  
345  C C   . ASP   A 41  ? 1.25378 1.00749 0.97380 0.08379  -0.26946 -0.01851 38  ASP   A C   
346  O O   . ASP   A 41  ? 1.22173 0.91886 0.88676 0.07740  -0.28045 -0.00637 38  ASP   A O   
347  C CB  . ASP   A 41  ? 1.35357 1.13992 1.10397 0.12649  -0.30822 -0.04858 38  ASP   A CB  
348  C CG  . ASP   A 41  ? 1.38041 1.22755 1.17931 0.12011  -0.28988 -0.05761 38  ASP   A CG  
349  O OD1 . ASP   A 41  ? 1.34036 1.23490 1.18756 0.11916  -0.27341 -0.06486 38  ASP   A OD1 
350  O OD2 . ASP   A 41  ? 1.43870 1.28415 1.22523 0.11544  -0.29232 -0.05738 38  ASP   A OD2 
351  N N   . THR   A 42  ? 1.22889 1.02228 0.98087 0.06590  -0.24047 -0.01572 39  THR   A N   
352  C CA  . THR   A 42  ? 1.30576 1.08207 1.03324 0.03918  -0.21973 0.00021  39  THR   A CA  
353  C C   . THR   A 42  ? 1.34813 1.10854 1.06897 0.02775  -0.20911 0.01002  39  THR   A C   
354  O O   . THR   A 42  ? 1.47543 1.20555 1.16174 0.00739  -0.19967 0.02385  39  THR   A O   
355  C CB  . THR   A 42  ? 1.34518 1.16931 1.10912 0.02689  -0.19540 -0.00247 39  THR   A CB  
356  O OG1 . THR   A 42  ? 1.41533 1.25811 1.19090 0.03845  -0.20628 -0.01376 39  THR   A OG1 
357  C CG2 . THR   A 42  ? 1.46237 1.27022 1.19900 0.00185  -0.17651 0.01103  39  THR   A CG2 
358  N N   . GLU   A 43  ? 1.21415 0.99515 0.96676 0.03982  -0.21051 0.00239  40  GLU   A N   
359  C CA  . GLU   A 43  ? 1.17361 0.94612 0.92634 0.02956  -0.19966 0.00981  40  GLU   A CA  
360  C C   . GLU   A 43  ? 1.28954 1.00328 0.99646 0.03570  -0.22201 0.01509  40  GLU   A C   
361  O O   . GLU   A 43  ? 1.26943 0.97475 0.97820 0.05924  -0.24429 0.00471  40  GLU   A O   
362  C CB  . GLU   A 43  ? 1.11695 0.93772 0.92221 0.03917  -0.19065 -0.00102 40  GLU   A CB  
363  C CG  . GLU   A 43  ? 1.13886 1.01442 0.98821 0.03582  -0.17278 -0.00764 40  GLU   A CG  
364  C CD  . GLU   A 43  ? 1.23936 1.12375 1.08966 0.01176  -0.14810 0.00312  40  GLU   A CD  
365  O OE1 . GLU   A 43  ? 1.24029 1.10199 1.07063 -0.00259 -0.14029 0.01396  40  GLU   A OE1 
366  O OE2 . GLU   A 43  ? 1.23501 1.14963 1.10672 0.00739  -0.13701 -0.00028 40  GLU   A OE2 
367  N N   . THR   A 44  ? 1.18897 0.86206 0.85466 0.01416  -0.21616 0.03051  41  THR   A N   
368  C CA  . THR   A 44  ? 1.36291 0.97397 0.98024 0.01610  -0.23668 0.03744  41  THR   A CA  
369  C C   . THR   A 44  ? 1.42811 1.04150 1.06380 0.02372  -0.23879 0.03317  41  THR   A C   
370  O O   . THR   A 44  ? 1.30734 0.87951 0.91737 0.03855  -0.26285 0.03089  41  THR   A O   
371  C CB  . THR   A 44  ? 1.39468 0.96411 0.96310 -0.01308 -0.22727 0.05522  41  THR   A CB  
372  O OG1 . THR   A 44  ? 1.48041 1.08312 1.07500 -0.03522 -0.19778 0.06013  41  THR   A OG1 
373  C CG2 . THR   A 44  ? 1.54856 1.10672 1.08910 -0.01869 -0.22923 0.05905  41  THR   A CG2 
374  N N   . GLU   A 45  ? 1.16451 0.82329 0.84235 0.01462  -0.21522 0.03161  42  GLU   A N   
375  C CA  . GLU   A 45  ? 1.17582 0.83971 0.87142 0.01994  -0.21498 0.02764  42  GLU   A CA  
376  C C   . GLU   A 45  ? 1.16817 0.87651 0.91005 0.04551  -0.21993 0.00995  42  GLU   A C   
377  O O   . GLU   A 45  ? 1.09908 0.83149 0.86882 0.04741  -0.21125 0.00533  42  GLU   A O   
378  C CB  . GLU   A 45  ? 1.16521 0.85090 0.87738 -0.00465 -0.18790 0.03595  42  GLU   A CB  
379  C CG  . GLU   A 45  ? 1.39779 1.05031 1.07039 -0.03273 -0.17862 0.05171  42  GLU   A CG  
380  C CD  . GLU   A 45  ? 1.53976 1.12453 1.15796 -0.03715 -0.19794 0.06009  42  GLU   A CD  
381  O OE1 . GLU   A 45  ? 1.39449 0.96319 1.01304 -0.02603 -0.21030 0.05575  42  GLU   A OE1 
382  O OE2 . GLU   A 45  ? 1.52217 1.06791 1.09515 -0.05215 -0.20105 0.07092  42  GLU   A OE2 
383  N N   . GLY   A 46  ? 1.06804 0.78911 0.81840 0.06439  -0.23348 -0.00062 43  GLY   A N   
384  C CA  . GLY   A 46  ? 1.13520 0.90308 0.93090 0.08674  -0.23678 -0.01870 43  GLY   A CA  
385  C C   . GLY   A 46  ? 0.98155 0.81051 0.82535 0.07641  -0.20956 -0.02115 43  GLY   A C   
386  O O   . GLY   A 46  ? 1.00768 0.84747 0.85287 0.05794  -0.19255 -0.01238 43  GLY   A O   
387  N N   . VAL   A 47  ? 0.84348 0.71148 0.72547 0.08870  -0.20584 -0.03370 44  VAL   A N   
388  C CA  . VAL   A 47  ? 0.85037 0.77298 0.77545 0.07900  -0.18118 -0.03577 44  VAL   A CA  
389  C C   . VAL   A 47  ? 0.87271 0.78839 0.79130 0.05483  -0.16077 -0.02062 44  VAL   A C   
390  O O   . VAL   A 47  ? 0.81437 0.70402 0.71609 0.05094  -0.16273 -0.01528 44  VAL   A O   
391  C CB  . VAL   A 47  ? 0.78246 0.74363 0.74359 0.09485  -0.18080 -0.05118 44  VAL   A CB  
392  C CG1 . VAL   A 47  ? 0.74980 0.76404 0.75131 0.08424  -0.15687 -0.05288 44  VAL   A CG1 
393  C CG2 . VAL   A 47  ? 0.85544 0.82292 0.82249 0.12052  -0.20319 -0.06834 44  VAL   A CG2 
394  N N   . PRO   A 48  ? 0.83668 0.77427 0.76801 0.03865  -0.14203 -0.01435 45  PRO   A N   
395  C CA  . PRO   A 48  ? 0.75692 0.69018 0.68355 0.01706  -0.12371 -0.00170 45  PRO   A CA  
396  C C   . PRO   A 48  ? 0.81120 0.76358 0.75981 0.01666  -0.11445 -0.00346 45  PRO   A C   
397  O O   . PRO   A 48  ? 0.77760 0.76217 0.75524 0.02851  -0.11339 -0.01394 45  PRO   A O   
398  C CB  . PRO   A 48  ? 0.76819 0.73005 0.71277 0.00615  -0.10747 0.00024  45  PRO   A CB  
399  C CG  . PRO   A 48  ? 0.91135 0.87339 0.85218 0.01790  -0.12086 -0.00711 45  PRO   A CG  
400  C CD  . PRO   A 48  ? 0.84491 0.80951 0.79334 0.03970  -0.13853 -0.01931 45  PRO   A CD  
401  N N   . SER   A 49  ? 0.79490 0.72784 0.72852 0.00188  -0.10754 0.00654  46  SER   A N   
402  C CA  . SER   A 49  ? 0.73490 0.68292 0.68609 0.00041  -0.09958 0.00554  46  SER   A CA  
403  C C   . SER   A 49  ? 0.75546 0.75047 0.74438 -0.00217 -0.08197 0.00261  46  SER   A C   
404  O O   . SER   A 49  ? 0.75459 0.77160 0.76401 0.00490  -0.07906 -0.00354 46  SER   A O   
405  C CB  . SER   A 49  ? 0.79522 0.71715 0.72539 -0.01763 -0.09442 0.01663  46  SER   A CB  
406  O OG  . SER   A 49  ? 1.08341 1.01338 1.01400 -0.03536 -0.07935 0.02464  46  SER   A OG  
407  N N   . THR   A 50  ? 0.67262 0.68150 0.66883 -0.01234 -0.07054 0.00675  47  THR   A N   
408  C CA  . THR   A 50  ? 0.74370 0.79171 0.77228 -0.01495 -0.05551 0.00443  47  THR   A CA  
409  C C   . THR   A 50  ? 0.62156 0.69597 0.67173 -0.00056 -0.05982 -0.00708 47  THR   A C   
410  O O   . THR   A 50  ? 0.68317 0.78726 0.75807 -0.00069 -0.04980 -0.01029 47  THR   A O   
411  C CB  . THR   A 50  ? 0.75330 0.80696 0.78295 -0.02737 -0.04447 0.00987  47  THR   A CB  
412  O OG1 . THR   A 50  ? 0.74754 0.78853 0.76234 -0.02329 -0.05393 0.00777  47  THR   A OG1 
413  C CG2 . THR   A 50  ? 0.77655 0.81422 0.79148 -0.04296 -0.03667 0.01933  47  THR   A CG2 
414  N N   . ALA   A 51  ? 0.61061 0.67518 0.65132 0.01140  -0.07484 -0.01379 48  ALA   A N   
415  C CA  . ALA   A 51  ? 0.59330 0.68723 0.65706 0.02517  -0.07942 -0.02699 48  ALA   A CA  
416  C C   . ALA   A 51  ? 0.69455 0.79529 0.76534 0.03778  -0.08530 -0.03546 48  ALA   A C   
417  O O   . ALA   A 51  ? 0.57782 0.71391 0.67496 0.04190  -0.07847 -0.04400 48  ALA   A O   
418  C CB  . ALA   A 51  ? 0.63988 0.72323 0.69277 0.03524  -0.09514 -0.03300 48  ALA   A CB  
419  N N   . ILE   A 52  ? 0.68167 0.74812 0.72766 0.04318  -0.09774 -0.03356 49  ILE   A N   
420  C CA  . ILE   A 52  ? 0.71828 0.78813 0.76866 0.05593  -0.10416 -0.04244 49  ILE   A CA  
421  C C   . ILE   A 52  ? 0.55283 0.64529 0.62028 0.04650  -0.08705 -0.03928 49  ILE   A C   
422  O O   . ILE   A 52  ? 0.63225 0.75221 0.71854 0.05489  -0.08421 -0.04937 49  ILE   A O   
423  C CB  . ILE   A 52  ? 0.67526 0.69697 0.69159 0.06147  -0.12153 -0.03962 49  ILE   A CB  
424  C CG1 . ILE   A 52  ? 0.76219 0.75591 0.75601 0.06934  -0.13923 -0.04053 49  ILE   A CG1 
425  C CG2 . ILE   A 52  ? 0.73516 0.75969 0.75585 0.07804  -0.13083 -0.05168 49  ILE   A CG2 
426  C CD1 . ILE   A 52  ? 0.78287 0.72308 0.73829 0.07466  -0.15852 -0.03726 49  ILE   A CD1 
427  N N   . ARG   A 53  ? 0.61379 0.69612 0.67452 0.02916  -0.07563 -0.02601 50  ARG   A N   
428  C CA  . ARG   A 53  ? 0.64627 0.74826 0.72180 0.02061  -0.06092 -0.02252 50  ARG   A CA  
429  C C   . ARG   A 53  ? 0.55841 0.70047 0.66161 0.01934  -0.04854 -0.02695 50  ARG   A C   
430  O O   . ARG   A 53  ? 0.59904 0.76363 0.71609 0.02253  -0.04286 -0.03242 50  ARG   A O   
431  C CB  . ARG   A 53  ? 0.76303 0.84933 0.82849 0.00331  -0.05225 -0.00909 50  ARG   A CB  
432  C CG  . ARG   A 53  ? 0.94331 0.99370 0.98336 -0.00042 -0.06070 -0.00390 50  ARG   A CG  
433  C CD  . ARG   A 53  ? 1.00249 1.04721 1.03870 -0.01881 -0.04968 0.00731  50  ARG   A CD  
434  N NE  . ARG   A 53  ? 0.92239 0.93396 0.93436 -0.02617 -0.05645 0.01250  50  ARG   A NE  
435  C CZ  . ARG   A 53  ? 0.99034 0.99631 0.99772 -0.04271 -0.04831 0.02057  50  ARG   A CZ  
436  N NH1 . ARG   A 53  ? 0.72435 0.75459 0.74954 -0.05148 -0.03411 0.02391  50  ARG   A NH1 
437  N NH2 . ARG   A 53  ? 0.87132 0.84678 0.85591 -0.05075 -0.05500 0.02453  50  ARG   A NH2 
438  N N   . GLU   A 54  ? 0.49369 0.64366 0.60321 0.01361  -0.04418 -0.02468 51  GLU   A N   
439  C CA  . GLU   A 54  ? 0.57962 0.76321 0.71296 0.00888  -0.03194 -0.02727 51  GLU   A CA  
440  C C   . GLU   A 54  ? 0.48894 0.70076 0.63915 0.02056  -0.03493 -0.04152 51  GLU   A C   
441  O O   . GLU   A 54  ? 0.53651 0.77533 0.70305 0.01668  -0.02390 -0.04420 51  GLU   A O   
442  C CB  . GLU   A 54  ? 0.57719 0.76064 0.71218 0.00158  -0.02911 -0.02372 51  GLU   A CB  
443  C CG  . GLU   A 54  ? 0.63741 0.85091 0.79475 -0.00513 -0.01733 -0.02588 51  GLU   A CG  
444  C CD  . GLU   A 54  ? 0.74583 0.95664 0.90360 -0.01239 -0.01510 -0.02286 51  GLU   A CD  
445  O OE1 . GLU   A 54  ? 0.85186 1.04208 0.99375 -0.00974 -0.02411 -0.02172 51  GLU   A OE1 
446  O OE2 . GLU   A 54  ? 0.74056 0.96772 0.91229 -0.02110 -0.00473 -0.02162 51  GLU   A OE2 
447  N N   . ILE   A 55  ? 0.47776 0.68404 0.62349 0.03486  -0.05003 -0.05136 52  ILE   A N   
448  C CA  . ILE   A 55  ? 0.55129 0.78887 0.71597 0.04764  -0.05372 -0.06781 52  ILE   A CA  
449  C C   . ILE   A 55  ? 0.52175 0.76947 0.68946 0.05273  -0.05040 -0.07291 52  ILE   A C   
450  O O   . ILE   A 55  ? 0.55449 0.83738 0.74164 0.05100  -0.03982 -0.08020 52  ILE   A O   
451  C CB  . ILE   A 55  ? 0.59589 0.82166 0.75321 0.06473  -0.07382 -0.07810 52  ILE   A CB  
452  C CG1 . ILE   A 55  ? 0.47245 0.69698 0.63055 0.06001  -0.07621 -0.07585 52  ILE   A CG1 
453  C CG2 . ILE   A 55  ? 0.60263 0.86126 0.77994 0.08118  -0.07942 -0.09772 52  ILE   A CG2 
454  C CD1 . ILE   A 55  ? 0.50808 0.71470 0.65364 0.07657  -0.09806 -0.08410 52  ILE   A CD1 
455  N N   . SER   A 56  ? 0.56411 0.78042 0.71098 0.05779  -0.05912 -0.06923 53  SER   A N   
456  C CA  . SER   A 56  ? 0.54876 0.77175 0.69603 0.06414  -0.05803 -0.07532 53  SER   A CA  
457  C C   . SER   A 56  ? 0.61597 0.85532 0.77073 0.04924  -0.03973 -0.06716 53  SER   A C   
458  O O   . SER   A 56  ? 0.58461 0.84894 0.74930 0.05207  -0.03311 -0.07512 53  SER   A O   
459  C CB  . SER   A 56  ? 0.66034 0.84146 0.78147 0.07052  -0.07203 -0.07203 53  SER   A CB  
460  O OG  . SER   A 56  ? 0.82172 0.97597 0.92755 0.05466  -0.06730 -0.05517 53  SER   A OG  
461  N N   . LEU   A 57  ? 0.49825 0.72364 0.64720 0.03383  -0.03187 -0.05196 54  LEU   A N   
462  C CA  . LEU   A 57  ? 0.63292 0.87031 0.78713 0.02118  -0.01693 -0.04410 54  LEU   A CA  
463  C C   . LEU   A 57  ? 0.54907 0.82191 0.72299 0.01567  -0.00488 -0.04853 54  LEU   A C   
464  O O   . LEU   A 57  ? 0.54747 0.83785 0.72579 0.01131  0.00493  -0.04926 54  LEU   A O   
465  C CB  . LEU   A 57  ? 0.49715 0.71274 0.64235 0.00804  -0.01285 -0.02891 54  LEU   A CB  
466  C CG  . LEU   A 57  ? 0.59452 0.77758 0.72042 0.00784  -0.02106 -0.02285 54  LEU   A CG  
467  C CD1 . LEU   A 57  ? 0.53617 0.70606 0.65787 -0.00577 -0.01518 -0.01024 54  LEU   A CD1 
468  C CD2 . LEU   A 57  ? 0.58731 0.76961 0.70839 0.01130  -0.02175 -0.02529 54  LEU   A CD2 
469  N N   . LEU   A 58  ? 0.55167 0.83461 0.73593 0.01473  -0.00564 -0.05163 55  LEU   A N   
470  C CA  . LEU   A 58  ? 0.51355 0.82822 0.71597 0.00604  0.00623  -0.05494 55  LEU   A CA  
471  C C   . LEU   A 58  ? 0.54998 0.89898 0.76700 0.01451  0.00729  -0.07153 55  LEU   A C   
472  O O   . LEU   A 58  ? 0.62779 1.00465 0.85662 0.00475  0.02021  -0.07393 55  LEU   A O   
473  C CB  . LEU   A 58  ? 0.45238 0.76690 0.66147 0.00137  0.00472  -0.05361 55  LEU   A CB  
474  C CG  . LEU   A 58  ? 0.56531 0.85583 0.76467 -0.01054 0.00896  -0.03844 55  LEU   A CG  
475  C CD1 . LEU   A 58  ? 0.46325 0.75634 0.66941 -0.01471 0.00778  -0.03927 55  LEU   A CD1 
476  C CD2 . LEU   A 58  ? 0.61251 0.90686 0.81223 -0.02298 0.02217  -0.02959 55  LEU   A CD2 
477  N N   . LYS   A 59  ? 0.51572 0.86323 0.73143 0.03224  -0.00614 -0.08370 56  LYS   A N   
478  C CA  . LYS   A 59  ? 0.59817 0.98131 0.82922 0.04240  -0.00536 -0.10198 56  LYS   A CA  
479  C C   . LYS   A 59  ? 0.68296 1.07449 0.90867 0.03994  0.00412  -0.10223 56  LYS   A C   
480  O O   . LYS   A 59  ? 0.69724 1.12324 0.93577 0.04508  0.00902  -0.11722 56  LYS   A O   
481  C CB  . LYS   A 59  ? 0.65356 1.02973 0.88338 0.06477  -0.02476 -0.11612 56  LYS   A CB  
482  C CG  . LYS   A 59  ? 0.65435 1.03101 0.89194 0.06950  -0.03505 -0.12038 56  LYS   A CG  
483  C CD  . LYS   A 59  ? 0.75714 1.13235 0.99546 0.09379  -0.05520 -0.13748 56  LYS   A CD  
484  C CE  . LYS   A 59  ? 0.92634 1.35395 1.19517 0.10204  -0.05359 -0.15935 56  LYS   A CE  
485  N NZ  . LYS   A 59  ? 0.73622 1.18401 1.02205 0.09165  -0.04945 -0.15931 56  LYS   A NZ  
486  N N   . GLU   A 60  ? 0.61957 0.98243 0.82700 0.03226  0.00675  -0.08708 57  GLU   A N   
487  C CA  . GLU   A 60  ? 0.65893 1.02670 0.85847 0.02853  0.01532  -0.08552 57  GLU   A CA  
488  C C   . GLU   A 60  ? 0.56862 0.93053 0.76226 0.00924  0.02858  -0.06900 57  GLU   A C   
489  O O   . GLU   A 60  ? 0.65776 1.01664 0.84038 0.00511  0.03422  -0.06456 57  GLU   A O   
490  C CB  . GLU   A 60  ? 0.80991 1.14794 0.99145 0.03995  0.00318  -0.08520 57  GLU   A CB  
491  C CG  . GLU   A 60  ? 0.85981 1.19953 1.04352 0.06094  -0.01163 -0.10255 57  GLU   A CG  
492  C CD  . GLU   A 60  ? 1.00977 1.31896 1.17382 0.07080  -0.02316 -0.10293 57  GLU   A CD  
493  O OE1 . GLU   A 60  ? 1.09035 1.37602 1.24016 0.06053  -0.02058 -0.08883 57  GLU   A OE1 
494  O OE2 . GLU   A 60  ? 1.00415 1.31291 1.16739 0.08915  -0.03563 -0.11826 57  GLU   A OE2 
495  N N   . LEU   A 61  ? 0.49847 0.85706 0.69785 -0.00167 0.03239  -0.06039 58  LEU   A N   
496  C CA  . LEU   A 61  ? 0.57587 0.92729 0.76975 -0.01852 0.04331  -0.04588 58  LEU   A CA  
497  C C   . LEU   A 61  ? 0.63367 1.01112 0.84101 -0.03095 0.05466  -0.04814 58  LEU   A C   
498  O O   . LEU   A 61  ? 0.67137 1.04029 0.88186 -0.04005 0.05638  -0.04051 58  LEU   A O   
499  C CB  . LEU   A 61  ? 0.55695 0.87661 0.74313 -0.02183 0.03786  -0.03270 58  LEU   A CB  
500  C CG  . LEU   A 61  ? 0.63471 0.92665 0.80577 -0.01667 0.03005  -0.02633 58  LEU   A CG  
501  C CD1 . LEU   A 61  ? 0.46017 0.72821 0.62740 -0.02139 0.02657  -0.01580 58  LEU   A CD1 
502  C CD2 . LEU   A 61  ? 0.52428 0.81528 0.68549 -0.02154 0.03608  -0.02101 58  LEU   A CD2 
503  N N   . ASN   A 62  ? 0.54750 0.95723 0.76258 -0.03227 0.06274  -0.05934 59  ASN   A N   
504  C CA  . ASN   A 62  ? 0.59532 1.03247 0.82294 -0.04701 0.07490  -0.06233 59  ASN   A CA  
505  C C   . ASN   A 62  ? 0.50454 0.93075 0.71643 -0.06498 0.08676  -0.04800 59  ASN   A C   
506  O O   . ASN   A 62  ? 0.55393 0.98450 0.75367 -0.06677 0.09269  -0.04773 59  ASN   A O   
507  C CB  . ASN   A 62  ? 0.58683 1.06714 0.83067 -0.04166 0.07927  -0.08212 59  ASN   A CB  
508  C CG  . ASN   A 62  ? 0.78806 1.30058 1.05168 -0.05478 0.08830  -0.08916 59  ASN   A CG  
509  O OD1 . ASN   A 62  ? 0.90064 1.43604 1.18482 -0.04557 0.08194  -0.10380 59  ASN   A OD1 
510  N ND2 . ASN   A 62  ? 0.81873 1.33186 1.07528 -0.07664 0.10219  -0.07900 59  ASN   A ND2 
511  N N   . HIS   A 63  ? 0.49607 0.90596 0.70617 -0.07759 0.08914  -0.03644 60  HIS   A N   
512  C CA  . HIS   A 63  ? 0.50794 0.90002 0.70061 -0.09344 0.09731  -0.02179 60  HIS   A CA  
513  C C   . HIS   A 63  ? 0.47182 0.86188 0.67062 -0.10874 0.10201  -0.01704 60  HIS   A C   
514  O O   . HIS   A 63  ? 0.47720 0.86575 0.68925 -0.10425 0.09542  -0.02025 60  HIS   A O   
515  C CB  . HIS   A 63  ? 0.44340 0.79878 0.61915 -0.08729 0.08926  -0.00878 60  HIS   A CB  
516  C CG  . HIS   A 63  ? 0.43962 0.77607 0.59499 -0.09957 0.09493  0.00473  60  HIS   A CG  
517  N ND1 . HIS   A 63  ? 0.50427 0.81810 0.65372 -0.10967 0.09519  0.01630  60  HIS   A ND1 
518  C CD2 . HIS   A 63  ? 0.49254 0.82734 0.62999 -0.10266 0.09937  0.00815  60  HIS   A CD2 
519  C CE1 . HIS   A 63  ? 0.56664 0.86393 0.69495 -0.11788 0.09852  0.02668  60  HIS   A CE1 
520  N NE2 . HIS   A 63  ? 0.47718 0.78691 0.59720 -0.11432 0.10132  0.02238  60  HIS   A NE2 
521  N N   . PRO   A 64  ? 0.46302 0.85091 0.65027 -0.12740 0.11277  -0.00947 61  PRO   A N   
522  C CA  . PRO   A 64  ? 0.42672 0.80963 0.61812 -0.14344 0.11673  -0.00514 61  PRO   A CA  
523  C C   . PRO   A 64  ? 0.55710 0.90437 0.74392 -0.13983 0.10734  0.00538  61  PRO   A C   
524  O O   . PRO   A 64  ? 0.52953 0.87422 0.72457 -0.14791 0.10729  0.00525  61  PRO   A O   
525  C CB  . PRO   A 64  ? 0.49614 0.87543 0.66803 -0.16402 0.12899  0.00315  61  PRO   A CB  
526  C CG  . PRO   A 64  ? 0.55978 0.96194 0.72696 -0.15956 0.13471  -0.00397 61  PRO   A CG  
527  C CD  . PRO   A 64  ? 0.46599 0.85911 0.63549 -0.13597 0.12234  -0.00657 61  PRO   A CD  
528  N N   . ASN   A 65  ? 0.54077 0.86235 0.71561 -0.12833 0.09955  0.01329  62  ASN   A N   
529  C CA  . ASN   A 65  ? 0.46464 0.75657 0.63668 -0.12410 0.09139  0.02136  62  ASN   A CA  
530  C C   . ASN   A 65  ? 0.46594 0.75837 0.64910 -0.10748 0.08178  0.01553  62  ASN   A C   
531  O O   . ASN   A 65  ? 0.51804 0.78787 0.69675 -0.10144 0.07527  0.02164  62  ASN   A O   
532  C CB  . ASN   A 65  ? 0.46650 0.72884 0.61743 -0.12483 0.08928  0.03436  62  ASN   A CB  
533  C CG  . ASN   A 65  ? 0.56286 0.81613 0.69681 -0.14240 0.09715  0.04228  62  ASN   A CG  
534  O OD1 . ASN   A 65  ? 0.63027 0.88398 0.74858 -0.14583 0.10121  0.04575  62  ASN   A OD1 
535  N ND2 . ASN   A 65  ? 0.52193 0.76489 0.65653 -0.15443 0.09903  0.04524  62  ASN   A ND2 
536  N N   . ILE   A 66  ? 0.47062 0.78814 0.66721 -0.10019 0.08048  0.00335  63  ILE   A N   
537  C CA  . ILE   A 66  ? 0.43756 0.75313 0.64150 -0.08574 0.07050  -0.00234 63  ILE   A CA  
538  C C   . ILE   A 66  ? 0.42047 0.75830 0.64169 -0.08578 0.06942  -0.01385 63  ILE   A C   
539  O O   . ILE   A 66  ? 0.50328 0.86990 0.73464 -0.08913 0.07478  -0.02335 63  ILE   A O   
540  C CB  . ILE   A 66  ? 0.46646 0.78522 0.66611 -0.07267 0.06569  -0.00664 63  ILE   A CB  
541  C CG1 . ILE   A 66  ? 0.45620 0.75478 0.63959 -0.07303 0.06599  0.00387  63  ILE   A CG1 
542  C CG2 . ILE   A 66  ? 0.43026 0.74208 0.63342 -0.05950 0.05458  -0.01161 63  ILE   A CG2 
543  C CD1 . ILE   A 66  ? 0.59209 0.89103 0.76988 -0.06133 0.06069  -0.00023 63  ILE   A CD1 
544  N N   . VAL   A 67  ? 0.41949 0.74586 0.64422 -0.08223 0.06254  -0.01392 64  VAL   A N   
545  C CA  . VAL   A 67  ? 0.47055 0.81603 0.71076 -0.08158 0.05944  -0.02491 64  VAL   A CA  
546  C C   . VAL   A 67  ? 0.44547 0.81223 0.69402 -0.06780 0.05334  -0.03779 64  VAL   A C   
547  O O   . VAL   A 67  ? 0.56852 0.92125 0.80881 -0.05452 0.04453  -0.03762 64  VAL   A O   
548  C CB  . VAL   A 67  ? 0.46431 0.79002 0.70224 -0.07903 0.05217  -0.02222 64  VAL   A CB  
549  C CG1 . VAL   A 67  ? 0.47331 0.81828 0.72600 -0.07717 0.04702  -0.03424 64  VAL   A CG1 
550  C CG2 . VAL   A 67  ? 0.47468 0.78025 0.70552 -0.09094 0.05751  -0.01168 64  VAL   A CG2 
551  N N   . LYS   A 68  ? 0.37014 0.77087 0.63511 -0.07110 0.05759  -0.04985 65  LYS   A N   
552  C CA  . LYS   A 68  ? 0.52099 0.94640 0.79582 -0.05706 0.05241  -0.06444 65  LYS   A CA  
553  C C   . LYS   A 68  ? 0.43462 0.85781 0.71504 -0.04180 0.03715  -0.07330 65  LYS   A C   
554  O O   . LYS   A 68  ? 0.50941 0.93205 0.79619 -0.04569 0.03375  -0.07452 65  LYS   A O   
555  C CB  . LYS   A 68  ? 0.53578 1.00357 0.82890 -0.06611 0.06279  -0.07654 65  LYS   A CB  
556  C CG  . LYS   A 68  ? 0.63485 1.10881 0.91915 -0.07752 0.07667  -0.07113 65  LYS   A CG  
557  C CD  . LYS   A 68  ? 0.59815 1.11945 0.90107 -0.08390 0.08650  -0.08671 65  LYS   A CD  
558  C CE  . LYS   A 68  ? 0.73176 1.27946 1.05067 -0.06243 0.07638  -0.10614 65  LYS   A CE  
559  N NZ  . LYS   A 68  ? 0.94222 1.54265 1.28335 -0.06745 0.08621  -0.12446 65  LYS   A NZ  
560  N N   . LEU   A 69  ? 0.50731 0.92696 0.78316 -0.02424 0.02697  -0.07967 66  LEU   A N   
561  C CA  . LEU   A 69  ? 0.48272 0.90307 0.76290 -0.00752 0.01074  -0.09090 66  LEU   A CA  
562  C C   . LEU   A 69  ? 0.53881 1.00403 0.84304 -0.00065 0.01033  -0.11112 66  LEU   A C   
563  O O   . LEU   A 69  ? 0.57463 1.05619 0.88180 0.00606  0.01307  -0.11879 66  LEU   A O   
564  C CB  . LEU   A 69  ? 0.46970 0.85807 0.72959 0.00750  -0.00154 -0.08716 66  LEU   A CB  
565  C CG  . LEU   A 69  ? 0.58736 0.97052 0.84606 0.02690  -0.02074 -0.09868 66  LEU   A CG  
566  C CD1 . LEU   A 69  ? 0.49723 0.87065 0.75518 0.02444  -0.02768 -0.09688 66  LEU   A CD1 
567  C CD2 . LEU   A 69  ? 0.54701 0.89413 0.78184 0.03854  -0.03174 -0.09342 66  LEU   A CD2 
568  N N   . LEU   A 70  ? 0.50514 0.99244 0.82746 -0.00227 0.00695  -0.12104 67  LEU   A N   
569  C CA  . LEU   A 70  ? 0.50502 1.04207 0.85507 0.00182  0.00811  -0.14191 67  LEU   A CA  
570  C C   . LEU   A 70  ? 0.51211 1.05569 0.86742 0.02822  -0.01123 -0.15870 67  LEU   A C   
571  O O   . LEU   A 70  ? 0.67590 1.25185 1.04579 0.03827  -0.01062 -0.17480 67  LEU   A O   
572  C CB  . LEU   A 70  ? 0.55042 1.11159 0.92001 -0.01290 0.01282  -0.14665 67  LEU   A CB  
573  C CG  . LEU   A 70  ? 0.51790 1.07187 0.88229 -0.03941 0.03069  -0.13160 67  LEU   A CG  
574  C CD1 . LEU   A 70  ? 0.50255 1.07740 0.88539 -0.05346 0.03302  -0.13753 67  LEU   A CD1 
575  C CD2 . LEU   A 70  ? 0.54667 1.12048 0.91219 -0.05038 0.04765  -0.13093 67  LEU   A CD2 
576  N N   . ASP   A 71  ? 0.53053 1.04297 0.87256 0.04007  -0.02889 -0.15581 68  ASP   A N   
577  C CA  . ASP   A 71  ? 0.53999 1.05359 0.88401 0.06581  -0.05016 -0.17154 68  ASP   A CA  
578  C C   . ASP   A 71  ? 0.60097 1.06003 0.91382 0.07461  -0.06665 -0.15905 68  ASP   A C   
579  O O   . ASP   A 71  ? 0.54801 0.97947 0.84549 0.06072  -0.06197 -0.14246 68  ASP   A O   
580  C CB  . ASP   A 71  ? 0.64741 1.20522 1.02212 0.07113  -0.05678 -0.19227 68  ASP   A CB  
581  C CG  . ASP   A 71  ? 0.75398 1.32414 1.13686 0.10008  -0.07781 -0.21333 68  ASP   A CG  
582  O OD1 . ASP   A 71  ? 0.86005 1.40544 1.22494 0.11515  -0.08592 -0.21233 68  ASP   A OD1 
583  O OD2 . ASP   A 71  ? 0.78627 1.39054 1.19372 0.10826  -0.08731 -0.23171 68  ASP   A OD2 
584  N N   . VAL   A 72  ? 0.63354 1.07676 0.93594 0.09767  -0.08609 -0.16778 69  VAL   A N   
585  C CA  . VAL   A 72  ? 0.61874 1.00994 0.88922 0.10736  -0.10450 -0.15835 69  VAL   A CA  
586  C C   . VAL   A 72  ? 0.64605 1.04557 0.92345 0.13062  -0.12824 -0.17714 69  VAL   A C   
587  O O   . VAL   A 72  ? 0.74774 1.16204 1.03412 0.15039  -0.13866 -0.19365 69  VAL   A O   
588  C CB  . VAL   A 72  ? 0.67076 1.02209 0.91331 0.11214  -0.10743 -0.14794 69  VAL   A CB  
589  C CG1 . VAL   A 72  ? 0.53780 0.83498 0.74536 0.11989  -0.12643 -0.13853 69  VAL   A CG1 
590  C CG2 . VAL   A 72  ? 0.56130 0.90713 0.79890 0.09049  -0.08539 -0.13078 69  VAL   A CG2 
591  N N   . ILE   A 73  ? 0.71340 1.10356 0.98636 0.12950  -0.13778 -0.17574 70  ILE   A N   
592  C CA  . ILE   A 73  ? 0.69051 1.09214 0.97229 0.15061  -0.16098 -0.19420 70  ILE   A CA  
593  C C   . ILE   A 73  ? 0.64248 0.98487 0.88337 0.16015  -0.18242 -0.18374 70  ILE   A C   
594  O O   . ILE   A 73  ? 0.72678 1.03972 0.94621 0.14440  -0.17709 -0.16636 70  ILE   A O   
595  C CB  . ILE   A 73  ? 0.77432 1.22104 1.08795 0.14123  -0.15545 -0.20460 70  ILE   A CB  
596  C CG1 . ILE   A 73  ? 0.56727 1.06917 0.91698 0.12690  -0.13178 -0.21249 70  ILE   A CG1 
597  C CG2 . ILE   A 73  ? 0.56103 1.02384 0.88674 0.16495  -0.18111 -0.22604 70  ILE   A CG2 
598  C CD1 . ILE   A 73  ? 0.61550 1.16084 0.99597 0.11290  -0.12380 -0.22142 70  ILE   A CD1 
599  N N   . HIS   A 74  ? 0.68049 1.00467 0.90916 0.18583  -0.20679 -0.19480 71  HIS   A N   
600  C CA  . HIS   A 74  ? 0.85955 1.12591 1.04665 0.19721  -0.23097 -0.18714 71  HIS   A CA  
601  C C   . HIS   A 74  ? 0.96860 1.25310 1.16865 0.21833  -0.25507 -0.20715 71  HIS   A C   
602  O O   . HIS   A 74  ? 1.00453 1.31370 1.22419 0.24188  -0.26958 -0.22867 71  HIS   A O   
603  C CB  . HIS   A 74  ? 0.74718 0.96937 0.90420 0.21022  -0.24291 -0.18296 71  HIS   A CB  
604  C CG  . HIS   A 74  ? 0.79872 0.95976 0.91088 0.22356  -0.27052 -0.17707 71  HIS   A CG  
605  N ND1 . HIS   A 74  ? 1.03739 1.16101 1.11798 0.20980  -0.27206 -0.15996 71  HIS   A ND1 
606  C CD2 . HIS   A 74  ? 0.89575 1.02395 0.98644 0.24912  -0.29810 -0.18594 71  HIS   A CD2 
607  C CE1 . HIS   A 74  ? 1.08838 1.15824 1.12829 0.22479  -0.29879 -0.15751 71  HIS   A CE1 
608  N NE2 . HIS   A 74  ? 1.05883 1.12842 1.10353 0.24911  -0.31586 -0.17280 71  HIS   A NE2 
609  N N   . THR   A 75  ? 0.89515 1.16869 1.08473 0.21083  -0.26000 -0.20138 72  THR   A N   
610  C CA  . THR   A 75  ? 1.13413 1.43238 1.34098 0.22736  -0.28051 -0.22066 72  THR   A CA  
611  C C   . THR   A 75  ? 1.30425 1.54514 1.46656 0.24392  -0.31126 -0.21663 72  THR   A C   
612  O O   . THR   A 75  ? 1.48161 1.71765 1.64216 0.27220  -0.33834 -0.23306 72  THR   A O   
613  C CB  . THR   A 75  ? 1.06092 1.39898 1.29534 0.20642  -0.26345 -0.22114 72  THR   A CB  
614  O OG1 . THR   A 75  ? 1.42996 1.77575 1.66823 0.21973  -0.28606 -0.23461 72  THR   A OG1 
615  C CG2 . THR   A 75  ? 1.01277 1.31709 1.22051 0.17899  -0.24373 -0.19503 72  THR   A CG2 
616  N N   . GLU   A 76  ? 1.20368 1.39973 1.32799 0.22734  -0.30840 -0.19558 73  GLU   A N   
617  C CA  . GLU   A 76  ? 1.30237 1.44498 1.38170 0.23983  -0.33661 -0.19117 73  GLU   A CA  
618  C C   . GLU   A 76  ? 1.23369 1.31729 1.26324 0.21829  -0.32616 -0.16318 73  GLU   A C   
619  O O   . GLU   A 76  ? 1.26525 1.34282 1.28386 0.19986  -0.31575 -0.15227 73  GLU   A O   
620  C CB  . GLU   A 76  ? 1.36978 1.53856 1.46466 0.24421  -0.34835 -0.20364 73  GLU   A CB  
621  C CG  . GLU   A 76  ? 1.32099 1.53723 1.45103 0.21903  -0.32049 -0.20239 73  GLU   A CG  
622  C CD  . GLU   A 76  ? 1.48703 1.70490 1.61218 0.21620  -0.33073 -0.20549 73  GLU   A CD  
623  O OE1 . GLU   A 76  ? 1.59799 1.76206 1.67525 0.22058  -0.34851 -0.19525 73  GLU   A OE1 
624  O OE2 . GLU   A 76  ? 1.54837 1.82029 1.71588 0.20857  -0.32103 -0.21816 73  GLU   A OE2 
625  N N   . ASN   A 77  ? 1.17084 1.21152 1.17031 0.22059  -0.32910 -0.15268 74  ASN   A N   
626  C CA  . ASN   A 77  ? 1.24559 1.23422 1.20080 0.19896  -0.31737 -0.12734 74  ASN   A CA  
627  C C   . ASN   A 77  ? 1.10894 1.12681 1.08550 0.17035  -0.28288 -0.11622 74  ASN   A C   
628  O O   . ASN   A 77  ? 1.03155 1.01826 0.97798 0.15033  -0.27148 -0.09783 74  ASN   A O   
629  C CB  . ASN   A 77  ? 1.28110 1.21414 1.18350 0.19929  -0.33695 -0.11712 74  ASN   A CB  
630  C CG  . ASN   A 77  ? 1.52544 1.42443 1.40287 0.22900  -0.37428 -0.12791 74  ASN   A CG  
631  O OD1 . ASN   A 77  ? 1.56383 1.41984 1.41232 0.23745  -0.38645 -0.12324 74  ASN   A OD1 
632  N ND2 . ASN   A 77  ? 1.59110 1.50774 1.47898 0.24548  -0.39402 -0.14302 74  ASN   A ND2 
633  N N   . LYS   A 78  ? 1.02882 1.10638 1.05646 0.16825  -0.26649 -0.12789 75  LYS   A N   
634  C CA  . LYS   A 78  ? 1.00729 1.11321 1.05712 0.14338  -0.23572 -0.11902 75  LYS   A CA  
635  C C   . LYS   A 78  ? 0.99420 1.13853 1.07991 0.14318  -0.22022 -0.12565 75  LYS   A C   
636  O O   . LYS   A 78  ? 0.80885 0.97928 0.91739 0.16210  -0.23102 -0.14325 75  LYS   A O   
637  C CB  . LYS   A 78  ? 1.03507 1.17599 1.10891 0.13601  -0.23039 -0.12595 75  LYS   A CB  
638  C CG  . LYS   A 78  ? 1.11374 1.21886 1.15154 0.13357  -0.24287 -0.11895 75  LYS   A CG  
639  C CD  . LYS   A 78  ? 1.25362 1.39568 1.31790 0.12815  -0.23966 -0.12863 75  LYS   A CD  
640  C CE  . LYS   A 78  ? 1.22634 1.41574 1.33113 0.14654  -0.25288 -0.15247 75  LYS   A CE  
641  N NZ  . LYS   A 78  ? 1.16042 1.38767 1.29298 0.13917  -0.24955 -0.16269 75  LYS   A NZ  
642  N N   . LEU   A 79  ? 0.83498 0.98300 0.92474 0.12216  -0.19520 -0.11219 76  LEU   A N   
643  C CA  . LEU   A 79  ? 0.82142 1.00185 0.94003 0.11851  -0.17832 -0.11548 76  LEU   A CA  
644  C C   . LEU   A 79  ? 0.79152 1.01011 0.93938 0.09892  -0.15476 -0.11344 76  LEU   A C   
645  O O   . LEU   A 79  ? 0.75195 0.95405 0.88670 0.08092  -0.14146 -0.09848 76  LEU   A O   
646  C CB  . LEU   A 79  ? 0.74982 0.89473 0.84319 0.11238  -0.17233 -0.10100 76  LEU   A CB  
647  C CG  . LEU   A 79  ? 0.74180 0.91044 0.85634 0.11520  -0.16242 -0.10634 76  LEU   A CG  
648  C CD1 . LEU   A 79  ? 0.70091 0.88463 0.82787 0.14080  -0.18127 -0.12648 76  LEU   A CD1 
649  C CD2 . LEU   A 79  ? 0.62125 0.75243 0.70905 0.10610  -0.15637 -0.09063 76  LEU   A CD2 
650  N N   . TYR   A 80  ? 0.65670 0.92572 0.84334 0.10215  -0.14995 -0.12909 77  TYR   A N   
651  C CA  . TYR   A 80  ? 0.68738 0.99191 0.90138 0.08316  -0.12882 -0.12821 77  TYR   A CA  
652  C C   . TYR   A 80  ? 0.71258 1.03693 0.94211 0.07483  -0.10988 -0.12552 77  TYR   A C   
653  O O   . TYR   A 80  ? 0.68256 1.02721 0.92571 0.08720  -0.11327 -0.13731 77  TYR   A O   
654  C CB  . TYR   A 80  ? 0.74493 1.09356 0.99099 0.08796  -0.13455 -0.14706 77  TYR   A CB  
655  C CG  . TYR   A 80  ? 0.78675 1.12042 1.02039 0.08972  -0.14847 -0.14799 77  TYR   A CG  
656  C CD1 . TYR   A 80  ? 0.77735 1.10399 1.00621 0.07072  -0.13675 -0.13761 77  TYR   A CD1 
657  C CD2 . TYR   A 80  ? 0.91758 1.24319 1.14312 0.11137  -0.17444 -0.16004 77  TYR   A CD2 
658  C CE1 . TYR   A 80  ? 0.87954 1.19257 1.09551 0.07221  -0.14932 -0.13916 77  TYR   A CE1 
659  C CE2 . TYR   A 80  ? 0.91291 1.22366 1.12448 0.11308  -0.18808 -0.16088 77  TYR   A CE2 
660  C CZ  . TYR   A 80  ? 0.98025 1.28543 1.18702 0.09294  -0.17483 -0.15042 77  TYR   A CZ  
661  O OH  . TYR   A 80  ? 1.14574 1.43610 1.33708 0.09455  -0.18825 -0.15191 77  TYR   A OH  
662  N N   . LEU   A 81  ? 0.63696 0.95490 0.86332 0.05486  -0.09083 -0.11080 78  LEU   A N   
663  C CA  . LEU   A 81  ? 0.58845 0.92210 0.82630 0.04481  -0.07255 -0.10629 78  LEU   A CA  
664  C C   . LEU   A 81  ? 0.58496 0.95346 0.84874 0.02836  -0.05680 -0.10890 78  LEU   A C   
665  O O   . LEU   A 81  ? 0.55913 0.91645 0.81784 0.01468  -0.05006 -0.09970 78  LEU   A O   
666  C CB  . LEU   A 81  ? 0.61749 0.91421 0.83001 0.03559  -0.06469 -0.08755 78  LEU   A CB  
667  C CG  . LEU   A 81  ? 0.66703 0.93183 0.85555 0.04670  -0.07474 -0.08338 78  LEU   A CG  
668  C CD1 . LEU   A 81  ? 0.58753 0.82153 0.75256 0.05943  -0.09564 -0.08506 78  LEU   A CD1 
669  C CD2 . LEU   A 81  ? 0.58811 0.82843 0.76028 0.03326  -0.06256 -0.06636 78  LEU   A CD2 
670  N N   . VAL   A 82  ? 0.45975 0.86971 0.75010 0.02912  -0.05092 -0.12194 79  VAL   A N   
671  C CA  . VAL   A 82  ? 0.46205 0.90648 0.77665 0.01190  -0.03633 -0.12572 79  VAL   A CA  
672  C C   . VAL   A 82  ? 0.53046 0.97200 0.84141 -0.00420 -0.01689 -0.11303 79  VAL   A C   
673  O O   . VAL   A 82  ? 0.48912 0.94118 0.80202 -0.00033 -0.01186 -0.11532 79  VAL   A O   
674  C CB  . VAL   A 82  ? 0.52277 1.01749 0.86868 0.01899  -0.03930 -0.14779 79  VAL   A CB  
675  C CG1 . VAL   A 82  ? 0.47194 1.00073 0.84129 -0.00225 -0.02413 -0.15134 79  VAL   A CG1 
676  C CG2 . VAL   A 82  ? 0.44512 0.94010 0.79297 0.03893  -0.06209 -0.16125 79  VAL   A CG2 
677  N N   . PHE   A 83  ? 0.42611 0.85219 0.73052 -0.02124 -0.00709 -0.10032 80  PHE   A N   
678  C CA  . PHE   A 83  ? 0.49827 0.91740 0.79703 -0.03641 0.00930  -0.08763 80  PHE   A CA  
679  C C   . PHE   A 83  ? 0.50137 0.94672 0.81775 -0.05536 0.02213  -0.09041 80  PHE   A C   
680  O O   . PHE   A 83  ? 0.47271 0.93650 0.80435 -0.05916 0.01878  -0.09991 80  PHE   A O   
681  C CB  . PHE   A 83  ? 0.48705 0.86494 0.76285 -0.04104 0.01031  -0.07067 80  PHE   A CB  
682  C CG  . PHE   A 83  ? 0.47659 0.82628 0.73217 -0.02777 0.00124  -0.06512 80  PHE   A CG  
683  C CD1 . PHE   A 83  ? 0.48109 0.81293 0.72530 -0.01693 -0.01315 -0.06732 80  PHE   A CD1 
684  C CD2 . PHE   A 83  ? 0.44273 0.78161 0.68843 -0.02754 0.00676  -0.05728 80  PHE   A CD2 
685  C CE1 . PHE   A 83  ? 0.59013 0.89301 0.81283 -0.00759 -0.02112 -0.06136 80  PHE   A CE1 
686  C CE2 . PHE   A 83  ? 0.49546 0.80776 0.72246 -0.01761 -0.00150 -0.05233 80  PHE   A CE2 
687  C CZ  . PHE   A 83  ? 0.44796 0.74167 0.66306 -0.00846 -0.01506 -0.05407 80  PHE   A CZ  
688  N N   . GLU   A 84  ? 0.45747 0.90226 0.76966 -0.06811 0.03628  -0.08172 81  GLU   A N   
689  C CA  . GLU   A 84  ? 0.43916 0.89663 0.75962 -0.08959 0.04909  -0.07970 81  GLU   A CA  
690  C C   . GLU   A 84  ? 0.47112 0.89766 0.78062 -0.09852 0.04821  -0.06890 81  GLU   A C   
691  O O   . GLU   A 84  ? 0.49017 0.88362 0.78181 -0.09178 0.04368  -0.05846 81  GLU   A O   
692  C CB  . GLU   A 84  ? 0.46425 0.92363 0.77719 -0.09978 0.06283  -0.07215 81  GLU   A CB  
693  C CG  . GLU   A 84  ? 0.59954 1.03413 0.89867 -0.11842 0.07241  -0.05700 81  GLU   A CG  
694  C CD  . GLU   A 84  ? 0.64832 1.07634 0.93329 -0.12446 0.08245  -0.04771 81  GLU   A CD  
695  O OE1 . GLU   A 84  ? 0.58246 1.00761 0.86072 -0.11069 0.07923  -0.04749 81  GLU   A OE1 
696  O OE2 . GLU   A 84  ? 0.65319 1.07678 0.93174 -0.14332 0.09278  -0.04055 81  GLU   A OE2 
697  N N   . PHE   A 85  ? 0.46316 0.90167 0.78393 -0.11398 0.05248  -0.07264 82  PHE   A N   
698  C CA  . PHE   A 85  ? 0.43481 0.84668 0.74734 -0.12122 0.05001  -0.06595 82  PHE   A CA  
699  C C   . PHE   A 85  ? 0.42617 0.81664 0.72640 -0.13867 0.06114  -0.05274 82  PHE   A C   
700  O O   . PHE   A 85  ? 0.49599 0.90258 0.80155 -0.15432 0.07157  -0.05314 82  PHE   A O   
701  C CB  . PHE   A 85  ? 0.43430 0.86795 0.76516 -0.12668 0.04501  -0.07899 82  PHE   A CB  
702  C CG  . PHE   A 85  ? 0.50091 0.90796 0.82322 -0.13489 0.04259  -0.07372 82  PHE   A CG  
703  C CD1 . PHE   A 85  ? 0.44013 0.82215 0.74951 -0.12201 0.03213  -0.07123 82  PHE   A CD1 
704  C CD2 . PHE   A 85  ? 0.52348 0.92919 0.84876 -0.15612 0.05083  -0.07157 82  PHE   A CD2 
705  C CE1 . PHE   A 85  ? 0.51957 0.87854 0.82081 -0.12863 0.03023  -0.06800 82  PHE   A CE1 
706  C CE2 . PHE   A 85  ? 0.52622 0.90560 0.84296 -0.16244 0.04756  -0.06797 82  PHE   A CE2 
707  C CZ  . PHE   A 85  ? 0.43804 0.79547 0.74359 -0.14790 0.03741  -0.06684 82  PHE   A CZ  
708  N N   . LEU   A 86  ? 0.50544 0.85937 0.78823 -0.13595 0.05848  -0.04162 83  LEU   A N   
709  C CA  . LEU   A 86  ? 0.41330 0.74075 0.68319 -0.14960 0.06492  -0.03020 83  LEU   A CA  
710  C C   . LEU   A 86  ? 0.47431 0.77947 0.73984 -0.14976 0.05862  -0.02999 83  LEU   A C   
711  O O   . LEU   A 86  ? 0.42226 0.72076 0.68520 -0.13608 0.05043  -0.03257 83  LEU   A O   
712  C CB  . LEU   A 86  ? 0.51577 0.82073 0.76842 -0.14398 0.06768  -0.01770 83  LEU   A CB  
713  C CG  . LEU   A 86  ? 0.59856 0.92008 0.85061 -0.14536 0.07475  -0.01628 83  LEU   A CG  
714  C CD1 . LEU   A 86  ? 0.50081 0.83910 0.75865 -0.12783 0.06932  -0.02308 83  LEU   A CD1 
715  C CD2 . LEU   A 86  ? 0.49258 0.78692 0.72533 -0.14883 0.07889  -0.00241 83  LEU   A CD2 
716  N N   . HIS   A 87  ? 0.44718 0.73893 0.70960 -0.16581 0.06234  -0.02700 84  HIS   A N   
717  C CA  . HIS   A 87  ? 0.59667 0.87416 0.85884 -0.16801 0.05625  -0.03095 84  HIS   A CA  
718  C C   . HIS   A 87  ? 0.56398 0.80649 0.80959 -0.15868 0.05235  -0.02357 84  HIS   A C   
719  O O   . HIS   A 87  ? 0.68181 0.91371 0.92604 -0.15642 0.04653  -0.02831 84  HIS   A O   
720  C CB  . HIS   A 87  ? 0.51235 0.78819 0.77766 -0.18996 0.06082  -0.03209 84  HIS   A CB  
721  C CG  . HIS   A 87  ? 0.61589 0.85548 0.86221 -0.19916 0.06453  -0.01970 84  HIS   A CG  
722  N ND1 . HIS   A 87  ? 0.72060 0.95148 0.95523 -0.20069 0.07067  -0.00907 84  HIS   A ND1 
723  C CD2 . HIS   A 87  ? 0.76016 0.96799 0.99573 -0.20624 0.06145  -0.01685 84  HIS   A CD2 
724  C CE1 . HIS   A 87  ? 0.70814 0.90268 0.92515 -0.20786 0.07045  0.00022  84  HIS   A CE1 
725  N NE2 . HIS   A 87  ? 0.76270 0.94225 0.98023 -0.21105 0.06485  -0.00451 84  HIS   A NE2 
726  N N   . GLN   A 88  ? 0.60817 0.83466 0.84198 -0.15289 0.05517  -0.01349 85  GLN   A N   
727  C CA  . GLN   A 88  ? 0.55097 0.74780 0.77195 -0.14512 0.05205  -0.00823 85  GLN   A CA  
728  C C   . GLN   A 88  ? 0.64260 0.83437 0.85625 -0.13413 0.05340  -0.00063 85  GLN   A C   
729  O O   . GLN   A 88  ? 0.51309 0.71268 0.72596 -0.13702 0.05785  0.00419  85  GLN   A O   
730  C CB  . GLN   A 88  ? 0.65427 0.82431 0.86636 -0.15680 0.05296  -0.00375 85  GLN   A CB  
731  C CG  . GLN   A 88  ? 0.68691 0.82796 0.88805 -0.14736 0.04865  -0.00130 85  GLN   A CG  
732  C CD  . GLN   A 88  ? 0.72787 0.83938 0.91936 -0.15767 0.04701  0.00137  85  GLN   A CD  
733  O OE1 . GLN   A 88  ? 0.95437 1.04662 1.14134 -0.15269 0.04204  -0.00256 85  GLN   A OE1 
734  N NE2 . GLN   A 88  ? 0.81860 0.92491 1.00497 -0.17247 0.05105  0.00779  85  GLN   A NE2 
735  N N   . ASP   A 89  ? 0.46493 0.64480 0.67308 -0.12239 0.04983  -0.00036 86  ASP   A N   
736  C CA  . ASP   A 89  ? 0.55455 0.72807 0.75644 -0.11304 0.05059  0.00610  86  ASP   A CA  
737  C C   . ASP   A 89  ? 0.58897 0.73769 0.78232 -0.11384 0.05055  0.01219  86  ASP   A C   
738  O O   . ASP   A 89  ? 0.57216 0.70471 0.76263 -0.11922 0.04885  0.01069  86  ASP   A O   
739  C CB  . ASP   A 89  ? 0.55854 0.73455 0.75895 -0.10160 0.04751  0.00269  86  ASP   A CB  
740  C CG  . ASP   A 89  ? 0.69009 0.85313 0.88713 -0.09957 0.04514  -0.00204 86  ASP   A CG  
741  O OD1 . ASP   A 89  ? 0.76547 0.91328 0.95828 -0.09618 0.04553  0.00013  86  ASP   A OD1 
742  O OD2 . ASP   A 89  ? 1.05160 1.22033 1.25011 -0.10047 0.04224  -0.00895 86  ASP   A OD2 
743  N N   . LEU   A 90  ? 0.53337 0.67800 0.72213 -0.10767 0.05109  0.01848  87  LEU   A N   
744  C CA  . LEU   A 90  ? 0.58792 0.70905 0.76811 -0.10636 0.04902  0.02407  87  LEU   A CA  
745  C C   . LEU   A 90  ? 0.59037 0.69810 0.77057 -0.09827 0.04511  0.01898  87  LEU   A C   
746  O O   . LEU   A 90  ? 0.58558 0.67050 0.75943 -0.09877 0.04155  0.02008  87  LEU   A O   
747  C CB  . LEU   A 90  ? 0.51386 0.63646 0.69026 -0.10027 0.04916  0.03053  87  LEU   A CB  
748  C CG  . LEU   A 90  ? 0.49163 0.58990 0.65833 -0.09684 0.04479  0.03618  87  LEU   A CG  
749  C CD1 . LEU   A 90  ? 0.59321 0.67223 0.74811 -0.10950 0.04482  0.04195  87  LEU   A CD1 
750  C CD2 . LEU   A 90  ? 0.51654 0.61936 0.68115 -0.08931 0.04367  0.04085  87  LEU   A CD2 
751  N N   . LYS   A 91  ? 0.60518 0.72550 0.79073 -0.09095 0.04550  0.01294  88  LYS   A N   
752  C CA  . LYS   A 91  ? 0.54240 0.65420 0.72807 -0.08339 0.04341  0.00659  88  LYS   A CA  
753  C C   . LYS   A 91  ? 0.58797 0.68593 0.77145 -0.08855 0.04099  0.00131  88  LYS   A C   
754  O O   . LYS   A 91  ? 0.63835 0.71832 0.81884 -0.08387 0.03749  -0.00185 88  LYS   A O   
755  C CB  . LYS   A 91  ? 0.60381 0.73212 0.79220 -0.07792 0.04568  0.00169  88  LYS   A CB  
756  C CG  . LYS   A 91  ? 0.73313 0.85982 0.92274 -0.06890 0.04597  -0.00363 88  LYS   A CG  
757  C CD  . LYS   A 91  ? 0.79660 0.91728 0.98431 -0.06791 0.04534  -0.01289 88  LYS   A CD  
758  C CE  . LYS   A 91  ? 1.05749 1.19176 1.24188 -0.06790 0.04865  -0.01783 88  LYS   A CE  
759  N NZ  . LYS   A 91  ? 1.08218 1.22410 1.26365 -0.07406 0.04791  -0.01445 88  LYS   A NZ  
760  N N   . LYS   A 92  ? 0.57155 0.67784 0.75705 -0.09762 0.04185  -0.00084 89  LYS   A N   
761  C CA  . LYS   A 92  ? 0.58391 0.67757 0.76772 -0.10446 0.03907  -0.00625 89  LYS   A CA  
762  C C   . LYS   A 92  ? 0.69659 0.76707 0.87383 -0.11280 0.03712  -0.00054 89  LYS   A C   
763  O O   . LYS   A 92  ? 0.64350 0.69267 0.81571 -0.11531 0.03298  -0.00438 89  LYS   A O   
764  C CB  . LYS   A 92  ? 0.67978 0.79153 0.86935 -0.11226 0.03960  -0.01077 89  LYS   A CB  
765  C CG  . LYS   A 92  ? 0.93220 1.03523 1.12112 -0.11756 0.03589  -0.01919 89  LYS   A CG  
766  C CD  . LYS   A 92  ? 0.98533 1.10988 1.18131 -0.12243 0.03471  -0.02527 89  LYS   A CD  
767  C CE  . LYS   A 92  ? 0.96223 1.09784 1.16608 -0.13627 0.03661  -0.02316 89  LYS   A CE  
768  N NZ  . LYS   A 92  ? 1.00378 1.16512 1.21792 -0.13869 0.03430  -0.03083 89  LYS   A NZ  
769  N N   . PHE   A 93  ? 0.66149 0.73325 0.83610 -0.11748 0.03959  0.00862  90  PHE   A N   
770  C CA  . PHE   A 93  ? 0.63894 0.68518 0.80216 -0.12690 0.03771  0.01578  90  PHE   A CA  
771  C C   . PHE   A 93  ? 0.63707 0.65606 0.79115 -0.11540 0.03126  0.01780  90  PHE   A C   
772  O O   . PHE   A 93  ? 0.68686 0.67485 0.82946 -0.11953 0.02573  0.01932  90  PHE   A O   
773  C CB  . PHE   A 93  ? 0.66392 0.72154 0.82486 -0.13588 0.04301  0.02443  90  PHE   A CB  
774  C CG  . PHE   A 93  ? 0.67232 0.70154 0.81634 -0.14604 0.04150  0.03391  90  PHE   A CG  
775  C CD1 . PHE   A 93  ? 0.71853 0.73374 0.85576 -0.16403 0.04226  0.03486  90  PHE   A CD1 
776  C CD2 . PHE   A 93  ? 0.66812 0.68349 0.80127 -0.13863 0.03878  0.04202  90  PHE   A CD2 
777  C CE1 . PHE   A 93  ? 0.70329 0.68796 0.82024 -0.17541 0.04072  0.04483  90  PHE   A CE1 
778  C CE2 . PHE   A 93  ? 0.84691 0.83204 0.95984 -0.14801 0.03613  0.05168  90  PHE   A CE2 
779  C CZ  . PHE   A 93  ? 0.76200 0.73023 0.86533 -0.16695 0.03732  0.05365  90  PHE   A CZ  
780  N N   . MET   A 94  ? 0.61755 0.64724 0.77656 -0.10089 0.03101  0.01712  91  MET   A N   
781  C CA  . MET   A 94  ? 0.65075 0.66033 0.80515 -0.08766 0.02408  0.01631  91  MET   A CA  
782  C C   . MET   A 94  ? 0.64021 0.63873 0.79670 -0.08043 0.01988  0.00516  91  MET   A C   
783  O O   . MET   A 94  ? 0.69012 0.66094 0.83898 -0.07362 0.01181  0.00348  91  MET   A O   
784  C CB  . MET   A 94  ? 0.66275 0.69227 0.82509 -0.07553 0.02562  0.01656  91  MET   A CB  
785  C CG  . MET   A 94  ? 0.69836 0.73919 0.85823 -0.08103 0.02925  0.02617  91  MET   A CG  
786  S SD  . MET   A 94  ? 0.89418 0.96280 1.06557 -0.06951 0.03196  0.02413  91  MET   A SD  
787  C CE  . MET   A 94  ? 0.75356 0.80525 0.92384 -0.05460 0.02298  0.02233  91  MET   A CE  
788  N N   . ASP   A 95  ? 0.55182 0.57029 0.71696 -0.08087 0.02433  -0.00311 92  ASP   A N   
789  C CA  . ASP   A 95  ? 0.75009 0.75928 0.91561 -0.07496 0.02108  -0.01470 92  ASP   A CA  
790  C C   . ASP   A 95  ? 0.64208 0.62235 0.79776 -0.08523 0.01573  -0.01497 92  ASP   A C   
791  O O   . ASP   A 95  ? 0.75635 0.71185 0.90635 -0.07821 0.00864  -0.02135 92  ASP   A O   
792  C CB  . ASP   A 95  ? 0.66088 0.69638 0.83370 -0.07474 0.02685  -0.02236 92  ASP   A CB  
793  C CG  . ASP   A 95  ? 0.76057 0.81990 0.94034 -0.06525 0.03170  -0.02339 92  ASP   A CG  
794  O OD1 . ASP   A 95  ? 0.78735 0.84523 0.96931 -0.05759 0.03030  -0.02003 92  ASP   A OD1 
795  O OD2 . ASP   A 95  ? 0.75312 0.83147 0.93492 -0.06611 0.03627  -0.02755 92  ASP   A OD2 
796  N N   . ALA   A 96  ? 0.65109 0.63450 0.80497 -0.10212 0.01879  -0.00906 93  ALA   A N   
797  C CA  . ALA   A 96  ? 0.68246 0.63862 0.82650 -0.11570 0.01442  -0.00840 93  ALA   A CA  
798  C C   . ALA   A 96  ? 0.70711 0.62581 0.83512 -0.11593 0.00743  -0.00020 93  ALA   A C   
799  O O   . ALA   A 96  ? 0.79433 0.67935 0.91028 -0.12188 0.00049  -0.00154 93  ALA   A O   
800  C CB  . ALA   A 96  ? 0.63553 0.60948 0.78376 -0.13477 0.02043  -0.00459 93  ALA   A CB  
801  N N   . SER   A 97  ? 0.71607 0.63736 0.84173 -0.10948 0.00792  0.00819  94  SER   A N   
802  C CA  . SER   A 97  ? 0.70494 0.58981 0.81262 -0.10818 -0.00016 0.01688  94  SER   A CA  
803  C C   . SER   A 97  ? 0.82186 0.69403 0.93016 -0.08520 -0.00925 0.01074  94  SER   A C   
804  O O   . SER   A 97  ? 0.89631 0.74086 0.99070 -0.07960 -0.01779 0.01739  94  SER   A O   
805  C CB  . SER   A 97  ? 0.76447 0.65873 0.86680 -0.11600 0.00491  0.02988  94  SER   A CB  
806  O OG  . SER   A 97  ? 0.78711 0.70283 0.89372 -0.13506 0.01465  0.03289  94  SER   A OG  
807  N N   . ALA   A 98  ? 0.76887 0.66126 0.89239 -0.07178 -0.00787 -0.00247 95  ALA   A N   
808  C CA  . ALA   A 98  ? 0.82659 0.71801 0.95584 -0.04962 -0.01432 -0.01046 95  ALA   A CA  
809  C C   . ALA   A 98  ? 0.83107 0.67730 0.94577 -0.04111 -0.02865 -0.01396 95  ALA   A C   
810  O O   . ALA   A 98  ? 0.96212 0.79583 1.07469 -0.02496 -0.03788 -0.01490 95  ALA   A O   
811  C CB  . ALA   A 98  ? 0.86942 0.79373 1.01631 -0.04022 -0.00780 -0.02449 95  ALA   A CB  
812  N N   . LEU   A 99  ? 0.83641 0.65667 0.94073 -0.05110 -0.03202 -0.01667 96  LEU   A N   
813  C CA  . LEU   A 99  ? 0.95484 0.72709 1.04289 -0.04286 -0.04714 -0.02064 96  LEU   A CA  
814  C C   . LEU   A 99  ? 1.07501 0.80628 1.13835 -0.05205 -0.05555 -0.00461 96  LEU   A C   
815  O O   . LEU   A 99  ? 1.09670 0.79589 1.14809 -0.03698 -0.06955 -0.00452 96  LEU   A O   
816  C CB  . LEU   A 99  ? 0.97825 0.73419 1.06204 -0.05129 -0.04862 -0.02956 96  LEU   A CB  
817  C CG  . LEU   A 99  ? 0.99082 0.78002 1.09337 -0.04166 -0.04219 -0.04653 96  LEU   A CG  
818  C CD1 . LEU   A 99  ? 1.03234 0.79732 1.12670 -0.04871 -0.04692 -0.05569 96  LEU   A CD1 
819  C CD2 . LEU   A 99  ? 0.92002 0.72185 1.03431 -0.01513 -0.04603 -0.05906 96  LEU   A CD2 
820  N N   . THR   A 100 ? 1.16538 0.89755 1.21993 -0.07660 -0.04748 0.00849  97  THR   A N   
821  C CA  . THR   A 100 ? 1.20560 0.89840 1.23278 -0.08961 -0.05348 0.02450  97  THR   A CA  
822  C C   . THR   A 100 ? 1.06207 0.76908 1.08801 -0.08427 -0.05167 0.03491  97  THR   A C   
823  O O   . THR   A 100 ? 1.07076 0.73992 1.07127 -0.08676 -0.06085 0.04649  97  THR   A O   
824  C CB  . THR   A 100 ? 1.31239 1.00224 1.33069 -0.12035 -0.04449 0.03268  97  THR   A CB  
825  O OG1 . THR   A 100 ? 1.29646 1.04043 1.33667 -0.12843 -0.02849 0.03259  97  THR   A OG1 
826  C CG2 . THR   A 100 ? 1.38456 1.05298 1.40034 -0.12714 -0.04883 0.02293  97  THR   A CG2 
827  N N   . GLY   A 101 ? 1.11799 0.87562 1.16822 -0.07741 -0.04099 0.03119  98  GLY   A N   
828  C CA  . GLY   A 101 ? 0.93437 0.70779 0.98438 -0.07358 -0.03881 0.04020  98  GLY   A CA  
829  C C   . GLY   A 101 ? 0.91678 0.69921 0.95743 -0.09736 -0.02789 0.05352  98  GLY   A C   
830  O O   . GLY   A 101 ? 1.05156 0.80723 1.07355 -0.11726 -0.02749 0.06058  98  GLY   A O   
831  N N   . ILE   A 102 ? 0.95823 0.77893 1.01179 -0.09623 -0.01874 0.05610  99  ILE   A N   
832  C CA  . ILE   A 102 ? 0.89119 0.72333 0.93637 -0.11652 -0.00843 0.06725  99  ILE   A CA  
833  C C   . ILE   A 102 ? 0.93332 0.72681 0.94759 -0.12117 -0.01628 0.08101  99  ILE   A C   
834  O O   . ILE   A 102 ? 0.92625 0.70610 0.93492 -0.10313 -0.02720 0.08201  99  ILE   A O   
835  C CB  . ILE   A 102 ? 0.92443 0.80530 0.99073 -0.11172 0.00178  0.06493  99  ILE   A CB  
836  C CG1 . ILE   A 102 ? 0.83631 0.74945 0.92872 -0.10477 0.00708  0.05173  99  ILE   A CG1 
837  C CG2 . ILE   A 102 ? 0.83142 0.72869 0.89219 -0.13166 0.01310  0.07316  99  ILE   A CG2 
838  C CD1 . ILE   A 102 ? 0.80877 0.76440 0.91924 -0.09953 0.01536  0.04936  99  ILE   A CD1 
839  N N   . PRO   A 103 ? 0.98682 0.76155 0.97951 -0.14512 -0.01162 0.09139  100 PRO   A N   
840  C CA  . PRO   A 103 ? 0.94395 0.67862 0.90175 -0.15142 -0.01887 0.10580  100 PRO   A CA  
841  C C   . PRO   A 103 ? 0.93559 0.69187 0.89417 -0.14208 -0.01710 0.11058  100 PRO   A C   
842  O O   . PRO   A 103 ? 0.92043 0.72282 0.89959 -0.14411 -0.00455 0.10727  100 PRO   A O   
843  C CB  . PRO   A 103 ? 1.10979 0.83564 1.05030 -0.18328 -0.00844 0.11414  100 PRO   A CB  
844  C CG  . PRO   A 103 ? 0.92763 0.67026 0.89004 -0.18999 -0.00296 0.10289  100 PRO   A CG  
845  C CD  . PRO   A 103 ? 0.85904 0.64589 0.85668 -0.16833 -0.00046 0.08977  100 PRO   A CD  
846  N N   . LEU   A 104 ? 0.97872 0.69931 0.91368 -0.13087 -0.03136 0.11780  101 LEU   A N   
847  C CA  . LEU   A 104 ? 0.97974 0.71707 0.91342 -0.12088 -0.03217 0.12192  101 LEU   A CA  
848  C C   . LEU   A 104 ? 1.01589 0.77377 0.93971 -0.14183 -0.01718 0.13074  101 LEU   A C   
849  O O   . LEU   A 104 ? 0.87640 0.67335 0.81743 -0.13489 -0.01055 0.12754  101 LEU   A O   
850  C CB  . LEU   A 104 ? 1.02863 0.71846 0.93403 -0.10663 -0.05222 0.12869  101 LEU   A CB  
851  C CG  . LEU   A 104 ? 1.17242 0.87402 1.07309 -0.09522 -0.05635 0.13293  101 LEU   A CG  
852  C CD1 . LEU   A 104 ? 1.01946 0.77373 0.96102 -0.07717 -0.05192 0.11957  101 LEU   A CD1 
853  C CD2 . LEU   A 104 ? 1.32247 0.97331 1.19351 -0.08040 -0.07883 0.13897  101 LEU   A CD2 
854  N N   . PRO   A 105 ? 1.01194 0.74698 0.90895 -0.16752 -0.01110 0.14089  102 PRO   A N   
855  C CA  . PRO   A 105 ? 1.05589 0.82028 0.94890 -0.18701 0.00556  0.14594  102 PRO   A CA  
856  C C   . PRO   A 105 ? 0.96002 0.78333 0.89210 -0.18791 0.02060  0.13385  102 PRO   A C   
857  O O   . PRO   A 105 ? 0.90868 0.76628 0.84737 -0.19074 0.03081  0.13350  102 PRO   A O   
858  C CB  . PRO   A 105 ? 1.07555 0.80512 0.93627 -0.21622 0.00979  0.15648  102 PRO   A CB  
859  C CG  . PRO   A 105 ? 1.06871 0.73649 0.90203 -0.20840 -0.00970 0.16251  102 PRO   A CG  
860  C CD  . PRO   A 105 ? 0.93170 0.61056 0.79689 -0.18044 -0.01979 0.14880  102 PRO   A CD  
861  N N   . LEU   A 106 ? 0.81633 0.65071 0.77286 -0.18468 0.02115  0.12346  103 LEU   A N   
862  C CA  . LEU   A 106 ? 0.84172 0.72822 0.83284 -0.18402 0.03302  0.11200  103 LEU   A CA  
863  C C   . LEU   A 106 ? 0.82796 0.74199 0.84157 -0.15998 0.02990  0.10480  103 LEU   A C   
864  O O   . LEU   A 106 ? 0.77689 0.73138 0.80928 -0.15904 0.03914  0.09947  103 LEU   A O   
865  C CB  . LEU   A 106 ? 0.75553 0.64243 0.76189 -0.18932 0.03377  0.10351  103 LEU   A CB  
866  C CG  . LEU   A 106 ? 0.77724 0.71358 0.81520 -0.19170 0.04495  0.09210  103 LEU   A CG  
867  C CD1 . LEU   A 106 ? 0.75578 0.71915 0.79236 -0.21126 0.05866  0.09447  103 LEU   A CD1 
868  C CD2 . LEU   A 106 ? 0.74373 0.67502 0.79297 -0.19613 0.04324  0.08396  103 LEU   A CD2 
869  N N   . ILE   A 107 ? 0.82797 0.72074 0.84008 -0.14062 0.01654  0.10374  104 ILE   A N   
870  C CA  . ILE   A 107 ? 0.86849 0.78663 0.90010 -0.12012 0.01368  0.09742  104 ILE   A CA  
871  C C   . ILE   A 107 ? 0.73439 0.66364 0.75589 -0.12076 0.01634  0.10397  104 ILE   A C   
872  O O   . ILE   A 107 ? 0.65939 0.62365 0.69897 -0.11474 0.02200  0.09875  104 ILE   A O   
873  C CB  . ILE   A 107 ? 0.81723 0.71203 0.84960 -0.10004 -0.00132 0.09373  104 ILE   A CB  
874  C CG1 . ILE   A 107 ? 0.91304 0.80209 0.95801 -0.09767 -0.00296 0.08459  104 ILE   A CG1 
875  C CG2 . ILE   A 107 ? 0.66548 0.58730 0.71658 -0.08160 -0.00389 0.08770  104 ILE   A CG2 
876  C CD1 . ILE   A 107 ? 0.88143 0.75157 0.92982 -0.07679 -0.01704 0.07803  104 ILE   A CD1 
877  N N   . LYS   A 108 ? 0.75844 0.65552 0.74833 -0.12840 0.01170  0.11553  105 LYS   A N   
878  C CA  . LYS   A 108 ? 0.88637 0.79141 0.86237 -0.13004 0.01408  0.12191  105 LYS   A CA  
879  C C   . LYS   A 108 ? 0.75818 0.69949 0.74236 -0.14537 0.03096  0.11990  105 LYS   A C   
880  O O   . LYS   A 108 ? 0.78586 0.75391 0.77702 -0.14019 0.03503  0.11757  105 LYS   A O   
881  C CB  . LYS   A 108 ? 0.78344 0.64211 0.71876 -0.13722 0.00552  0.13543  105 LYS   A CB  
882  C CG  . LYS   A 108 ? 0.91872 0.77983 0.83485 -0.13685 0.00530  0.14230  105 LYS   A CG  
883  C CD  . LYS   A 108 ? 1.06779 0.87701 0.93910 -0.14339 -0.00527 0.15643  105 LYS   A CD  
884  C CE  . LYS   A 108 ? 1.14125 0.91356 1.00753 -0.12362 -0.02616 0.15619  105 LYS   A CE  
885  N NZ  . LYS   A 108 ? 1.32239 1.04014 1.14162 -0.12727 -0.03961 0.17029  105 LYS   A NZ  
886  N N   . SER   A 109 ? 0.78826 0.73195 0.77288 -0.16377 0.04024  0.11943  106 SER   A N   
887  C CA  . SER   A 109 ? 0.70494 0.68689 0.70072 -0.17737 0.05575  0.11505  106 SER   A CA  
888  C C   . SER   A 109 ? 0.71815 0.74089 0.74892 -0.16426 0.05899  0.10232  106 SER   A C   
889  O O   . SER   A 109 ? 0.65643 0.71093 0.69617 -0.16368 0.06639  0.09805  106 SER   A O   
890  C CB  . SER   A 109 ? 0.78593 0.76220 0.77606 -0.20070 0.06397  0.11625  106 SER   A CB  
891  O OG  . SER   A 109 ? 0.80011 0.82004 0.80838 -0.21117 0.07814  0.10838  106 SER   A OG  
892  N N   . TYR   A 110 ? 0.66517 0.68587 0.71384 -0.15371 0.05314  0.09589  107 TYR   A N   
893  C CA  . TYR   A 110 ? 0.64549 0.69992 0.72279 -0.14246 0.05547  0.08489  107 TYR   A CA  
894  C C   . TYR   A 110 ? 0.61105 0.67673 0.69262 -0.12668 0.05145  0.08400  107 TYR   A C   
895  O O   . TYR   A 110 ? 0.53410 0.62916 0.62869 -0.12352 0.05651  0.07830  107 TYR   A O   
896  C CB  . TYR   A 110 ? 0.57478 0.62159 0.66577 -0.13555 0.05019  0.07870  107 TYR   A CB  
897  C CG  . TYR   A 110 ? 0.61977 0.67170 0.71748 -0.14959 0.05581  0.07439  107 TYR   A CG  
898  C CD1 . TYR   A 110 ? 0.59704 0.66943 0.69565 -0.16572 0.06598  0.07369  107 TYR   A CD1 
899  C CD2 . TYR   A 110 ? 0.67364 0.71237 0.77794 -0.14655 0.05087  0.06954  107 TYR   A CD2 
900  C CE1 . TYR   A 110 ? 0.65688 0.73710 0.76407 -0.17905 0.07053  0.06844  107 TYR   A CE1 
901  C CE2 . TYR   A 110 ? 0.60414 0.64755 0.71471 -0.15957 0.05497  0.06488  107 TYR   A CE2 
902  C CZ  . TYR   A 110 ? 0.68972 0.75427 0.80240 -0.17608 0.06454  0.06442  107 TYR   A CZ  
903  O OH  . TYR   A 110 ? 0.67152 0.74357 0.79270 -0.18952 0.06803  0.05856  107 TYR   A OH  
904  N N   . LEU   A 111 ? 0.62004 0.66206 0.69091 -0.11623 0.04123  0.08878  108 LEU   A N   
905  C CA  . LEU   A 111 ? 0.66873 0.72157 0.74429 -0.10235 0.03662  0.08740  108 LEU   A CA  
906  C C   . LEU   A 111 ? 0.66654 0.73123 0.73035 -0.10813 0.04206  0.09099  108 LEU   A C   
907  O O   . LEU   A 111 ? 0.62390 0.71133 0.69847 -0.10100 0.04345  0.08610  108 LEU   A O   
908  C CB  . LEU   A 111 ? 0.62131 0.64738 0.68767 -0.09042 0.02355  0.09093  108 LEU   A CB  
909  C CG  . LEU   A 111 ? 0.61145 0.64897 0.68427 -0.07635 0.01735  0.08858  108 LEU   A CG  
910  C CD1 . LEU   A 111 ? 0.53454 0.59889 0.63484 -0.06803 0.01965  0.07825  108 LEU   A CD1 
911  C CD2 . LEU   A 111 ? 0.72075 0.73104 0.78153 -0.06543 0.00319  0.09223  108 LEU   A CD2 
912  N N   . PHE   A 112 ? 0.60293 0.65127 0.64286 -0.12180 0.04529  0.09924  109 PHE   A N   
913  C CA  . PHE   A 112 ? 0.62808 0.68855 0.65443 -0.12863 0.05189  0.10193  109 PHE   A CA  
914  C C   . PHE   A 112 ? 0.62625 0.72565 0.67271 -0.13175 0.06290  0.09224  109 PHE   A C   
915  O O   . PHE   A 112 ? 0.57173 0.69044 0.62130 -0.12562 0.06448  0.08834  109 PHE   A O   
916  C CB  . PHE   A 112 ? 0.68902 0.72499 0.68464 -0.14641 0.05540  0.11236  109 PHE   A CB  
917  C CG  . PHE   A 112 ? 0.70726 0.75270 0.68377 -0.15406 0.06226  0.11568  109 PHE   A CG  
918  C CD1 . PHE   A 112 ? 0.69717 0.72885 0.65557 -0.14462 0.05370  0.12083  109 PHE   A CD1 
919  C CD2 . PHE   A 112 ? 0.75642 0.82632 0.73338 -0.17055 0.07714  0.11243  109 PHE   A CD2 
920  C CE1 . PHE   A 112 ? 0.77576 0.81566 0.71440 -0.15154 0.06004  0.12327  109 PHE   A CE1 
921  C CE2 . PHE   A 112 ? 0.79452 0.87538 0.75344 -0.17753 0.08449  0.11404  109 PHE   A CE2 
922  C CZ  . PHE   A 112 ? 0.81404 0.87866 0.75247 -0.16807 0.07602  0.11978  109 PHE   A CZ  
923  N N   . GLN   A 113 ? 0.55783 0.66831 0.61812 -0.14021 0.06919  0.08733  110 GLN   A N   
924  C CA  . GLN   A 113 ? 0.55654 0.70372 0.63703 -0.14131 0.07748  0.07677  110 GLN   A CA  
925  C C   . GLN   A 113 ? 0.56430 0.72591 0.66437 -0.12401 0.07190  0.06919  110 GLN   A C   
926  O O   . GLN   A 113 ? 0.58296 0.76882 0.69153 -0.11944 0.07488  0.06222  110 GLN   A O   
927  C CB  . GLN   A 113 ? 0.60303 0.75772 0.69450 -0.15351 0.08328  0.07265  110 GLN   A CB  
928  C CG  . GLN   A 113 ? 0.55928 0.70202 0.63173 -0.17461 0.09046  0.07941  110 GLN   A CG  
929  C CD  . GLN   A 113 ? 0.76771 0.91533 0.85231 -0.18682 0.09439  0.07492  110 GLN   A CD  
930  O OE1 . GLN   A 113 ? 0.62901 0.80913 0.73630 -0.18661 0.09905  0.06384  110 GLN   A OE1 
931  N NE2 . GLN   A 113 ? 0.67740 0.79109 0.74643 -0.19667 0.09099  0.08288  110 GLN   A NE2 
932  N N   . LEU   A 114 ? 0.49269 0.63925 0.59918 -0.11470 0.06382  0.06983  111 LEU   A N   
933  C CA  . LEU   A 114 ? 0.54039 0.69852 0.66248 -0.10102 0.05926  0.06354  111 LEU   A CA  
934  C C   . LEU   A 114 ? 0.50298 0.66399 0.61864 -0.09312 0.05582  0.06470  111 LEU   A C   
935  O O   . LEU   A 114 ? 0.47807 0.65563 0.60300 -0.08654 0.05555  0.05851  111 LEU   A O   
936  C CB  . LEU   A 114 ? 0.59981 0.74273 0.72851 -0.09416 0.05264  0.06356  111 LEU   A CB  
937  C CG  . LEU   A 114 ? 0.64149 0.78304 0.77961 -0.09860 0.05440  0.05975  111 LEU   A CG  
938  C CD1 . LEU   A 114 ? 0.54686 0.67151 0.68792 -0.09073 0.04763  0.05959  111 LEU   A CD1 
939  C CD2 . LEU   A 114 ? 0.50110 0.66629 0.65449 -0.09705 0.05764  0.05115  111 LEU   A CD2 
940  N N   . LEU   A 115 ? 0.50661 0.64924 0.60463 -0.09353 0.05193  0.07246  112 LEU   A N   
941  C CA  . LEU   A 115 ? 0.56457 0.70937 0.65488 -0.08664 0.04791  0.07329  112 LEU   A CA  
942  C C   . LEU   A 115 ? 0.53799 0.70183 0.62321 -0.09129 0.05539  0.06989  112 LEU   A C   
943  O O   . LEU   A 115 ? 0.61972 0.79319 0.70590 -0.08387 0.05287  0.06600  112 LEU   A O   
944  C CB  . LEU   A 115 ? 0.53924 0.65840 0.60951 -0.08568 0.04057  0.08224  112 LEU   A CB  
945  C CG  . LEU   A 115 ? 0.57022 0.67337 0.64693 -0.07597 0.03026  0.08308  112 LEU   A CG  
946  C CD1 . LEU   A 115 ? 0.55523 0.62927 0.60891 -0.07581 0.02213  0.09203  112 LEU   A CD1 
947  C CD2 . LEU   A 115 ? 0.52365 0.64045 0.61551 -0.06433 0.02479  0.07697  112 LEU   A CD2 
948  N N   . GLN   A 116 ? 0.53803 0.70860 0.61836 -0.10376 0.06462  0.07016  113 GLN   A N   
949  C CA  . GLN   A 116 ? 0.47562 0.66981 0.55410 -0.10785 0.07289  0.06430  113 GLN   A CA  
950  C C   . GLN   A 116 ? 0.51514 0.73378 0.61577 -0.09945 0.07322  0.05250  113 GLN   A C   
951  O O   . GLN   A 116 ? 0.48733 0.71947 0.58846 -0.09239 0.07265  0.04628  113 GLN   A O   
952  C CB  . GLN   A 116 ? 0.53913 0.73778 0.60885 -0.12524 0.08366  0.06643  113 GLN   A CB  
953  C CG  . GLN   A 116 ? 0.55025 0.72374 0.59012 -0.13553 0.08418  0.07839  113 GLN   A CG  
954  C CD  . GLN   A 116 ? 0.74088 0.91825 0.77072 -0.15616 0.09601  0.08072  113 GLN   A CD  
955  O OE1 . GLN   A 116 ? 0.84817 1.03112 0.89208 -0.16354 0.09962  0.07783  113 GLN   A OE1 
956  N NE2 . GLN   A 116 ? 0.83243 1.00735 0.83694 -0.16678 0.10239  0.08561  113 GLN   A NE2 
957  N N   . GLY   A 117 ? 0.47513 0.69747 0.59220 -0.09969 0.07308  0.04901  114 GLY   A N   
958  C CA  . GLY   A 117 ? 0.52188 0.76184 0.65645 -0.09084 0.07096  0.03877  114 GLY   A CA  
959  C C   . GLY   A 117 ? 0.47906 0.71083 0.61484 -0.07833 0.06208  0.03823  114 GLY   A C   
960  O O   . GLY   A 117 ? 0.53035 0.77335 0.67208 -0.07048 0.05941  0.03050  114 GLY   A O   
961  N N   . LEU   A 118 ? 0.52093 0.73293 0.65103 -0.07645 0.05681  0.04568  115 LEU   A N   
962  C CA  . LEU   A 118 ? 0.59886 0.80537 0.73123 -0.06702 0.04914  0.04474  115 LEU   A CA  
963  C C   . LEU   A 118 ? 0.54479 0.75330 0.66621 -0.06327 0.04696  0.04412  115 LEU   A C   
964  O O   . LEU   A 118 ? 0.56183 0.77337 0.68593 -0.05636 0.04224  0.03920  115 LEU   A O   
965  C CB  . LEU   A 118 ? 0.50423 0.69429 0.63756 -0.06575 0.04433  0.05048  115 LEU   A CB  
966  C CG  . LEU   A 118 ? 0.58797 0.77624 0.72815 -0.05869 0.03790  0.04820  115 LEU   A CG  
967  C CD1 . LEU   A 118 ? 0.52693 0.72248 0.67686 -0.05733 0.03854  0.04220  115 LEU   A CD1 
968  C CD2 . LEU   A 118 ? 0.54191 0.71910 0.68531 -0.05698 0.03388  0.05180  115 LEU   A CD2 
969  N N   . ALA   A 119 ? 0.49549 0.70008 0.60206 -0.06840 0.04992  0.04916  116 ALA   A N   
970  C CA  . ALA   A 119 ? 0.61965 0.82692 0.71328 -0.06533 0.04846  0.04788  116 ALA   A CA  
971  C C   . ALA   A 119 ? 0.54627 0.77415 0.64402 -0.06272 0.05269  0.03758  116 ALA   A C   
972  O O   . ALA   A 119 ? 0.51267 0.74328 0.60577 -0.05577 0.04858  0.03270  116 ALA   A O   
973  C CB  . ALA   A 119 ? 0.55913 0.75640 0.63205 -0.07289 0.05139  0.05592  116 ALA   A CB  
974  N N   . PHE   A 120 ? 0.52809 0.77099 0.63517 -0.06751 0.05996  0.03297  117 PHE   A N   
975  C CA  . PHE   A 120 ? 0.54640 0.81134 0.66146 -0.06243 0.06232  0.02076  117 PHE   A CA  
976  C C   . PHE   A 120 ? 0.50309 0.76427 0.62815 -0.05107 0.05302  0.01494  117 PHE   A C   
977  O O   . PHE   A 120 ? 0.62614 0.89361 0.74994 -0.04241 0.04919  0.00645  117 PHE   A O   
978  C CB  . PHE   A 120 ? 0.59040 0.87427 0.71588 -0.07050 0.07125  0.01639  117 PHE   A CB  
979  C CG  . PHE   A 120 ? 0.52259 0.83406 0.65811 -0.06471 0.07388  0.00182  117 PHE   A CG  
980  C CD1 . PHE   A 120 ? 0.61074 0.94136 0.73888 -0.06794 0.08194  -0.00394 117 PHE   A CD1 
981  C CD2 . PHE   A 120 ? 0.55722 0.87572 0.70869 -0.05562 0.06789  -0.00690 117 PHE   A CD2 
982  C CE1 . PHE   A 120 ? 0.59194 0.95143 0.73174 -0.06092 0.08411  -0.01976 117 PHE   A CE1 
983  C CE2 . PHE   A 120 ? 0.57156 0.91531 0.73310 -0.04785 0.06819  -0.02180 117 PHE   A CE2 
984  C CZ  . PHE   A 120 ? 0.46701 0.83297 0.62445 -0.04992 0.07642  -0.02906 117 PHE   A CZ  
985  N N   . CYS   A 121 ? 0.42115 0.67042 0.55410 -0.05133 0.04912  0.01915  118 CYS   A N   
986  C CA  . CYS   A 121 ? 0.44210 0.68397 0.58012 -0.04321 0.04067  0.01530  118 CYS   A CA  
987  C C   . CYS   A 121 ? 0.47809 0.70793 0.60691 -0.03838 0.03369  0.01647  118 CYS   A C   
988  O O   . CYS   A 121 ? 0.57780 0.80503 0.70496 -0.03109 0.02726  0.01001  118 CYS   A O   
989  C CB  . CYS   A 121 ? 0.52142 0.75292 0.66672 -0.04639 0.03934  0.02022  118 CYS   A CB  
990  S SG  . CYS   A 121 ? 0.52812 0.77139 0.68518 -0.05073 0.04442  0.01684  118 CYS   A SG  
991  N N   . HIS   A 122 ? 0.44651 0.66748 0.56868 -0.04213 0.03358  0.02423  119 HIS   A N   
992  C CA  . HIS   A 122 ? 0.51894 0.72976 0.63443 -0.03844 0.02613  0.02494  119 HIS   A CA  
993  C C   . HIS   A 122 ? 0.52644 0.74281 0.63097 -0.03382 0.02503  0.01908  119 HIS   A C   
994  O O   . HIS   A 122 ? 0.50316 0.71272 0.60371 -0.02867 0.01756  0.01501  119 HIS   A O   
995  C CB  . HIS   A 122 ? 0.46445 0.66606 0.57771 -0.04213 0.02471  0.03346  119 HIS   A CB  
996  C CG  . HIS   A 122 ? 0.54455 0.74104 0.66921 -0.04475 0.02450  0.03696  119 HIS   A CG  
997  N ND1 . HIS   A 122 ? 0.58521 0.77505 0.71130 -0.04640 0.02297  0.04283  119 HIS   A ND1 
998  C CD2 . HIS   A 122 ? 0.51858 0.71549 0.65257 -0.04526 0.02514  0.03452  119 HIS   A CD2 
999  C CE1 . HIS   A 122 ? 0.59385 0.78254 0.73123 -0.04779 0.02370  0.04294  119 HIS   A CE1 
1000 N NE2 . HIS   A 122 ? 0.51451 0.70698 0.65572 -0.04792 0.02541  0.03851  119 HIS   A NE2 
1001 N N   . SER   A 123 ? 0.51102 0.73951 0.60955 -0.03647 0.03263  0.01801  120 SER   A N   
1002 C CA  . SER   A 123 ? 0.55767 0.79483 0.64564 -0.03180 0.03300  0.01047  120 SER   A CA  
1003 C C   . SER   A 123 ? 0.59552 0.84107 0.69045 -0.02273 0.02979  -0.00188 120 SER   A C   
1004 O O   . SER   A 123 ? 0.61216 0.85885 0.69932 -0.01534 0.02555  -0.00992 120 SER   A O   
1005 C CB  . SER   A 123 ? 0.54181 0.79225 0.62103 -0.03897 0.04381  0.01175  120 SER   A CB  
1006 O OG  . SER   A 123 ? 0.63650 0.90387 0.72789 -0.04249 0.05169  0.00743  120 SER   A OG  
1007 N N   . HIS   A 124 ? 0.52066 0.77068 0.62888 -0.02221 0.03053  -0.00418 121 HIS   A N   
1008 C CA  . HIS   A 124 ? 0.54793 0.80037 0.66182 -0.01208 0.02416  -0.01515 121 HIS   A CA  
1009 C C   . HIS   A 124 ? 0.55344 0.78206 0.66529 -0.00909 0.01315  -0.01248 121 HIS   A C   
1010 O O   . HIS   A 124 ? 0.58519 0.80854 0.69882 -0.00159 0.00604  -0.01932 121 HIS   A O   
1011 C CB  . HIS   A 124 ? 0.53837 0.80779 0.66627 -0.01276 0.02915  -0.01975 121 HIS   A CB  
1012 C CG  . HIS   A 124 ? 0.53932 0.83704 0.67080 -0.01421 0.03907  -0.02771 121 HIS   A CG  
1013 N ND1 . HIS   A 124 ? 0.60184 0.90695 0.72611 -0.02515 0.04954  -0.02132 121 HIS   A ND1 
1014 C CD2 . HIS   A 124 ? 0.57429 0.89560 0.71524 -0.00657 0.04014  -0.04225 121 HIS   A CD2 
1015 C CE1 . HIS   A 124 ? 0.57659 0.90947 0.70510 -0.02635 0.05829  -0.03107 121 HIS   A CE1 
1016 N NE2 . HIS   A 124 ? 0.66620 1.01193 0.80701 -0.01457 0.05295  -0.04479 121 HIS   A NE2 
1017 N N   . ARG   A 125 ? 0.50897 0.72322 0.61649 -0.01520 0.01130  -0.00308 122 ARG   A N   
1018 C CA  . ARG   A 125 ? 0.58746 0.78132 0.69262 -0.01576 0.00256  -0.00040 122 ARG   A CA  
1019 C C   . ARG   A 125 ? 0.66302 0.85124 0.77503 -0.01756 0.00181  0.00123  122 ARG   A C   
1020 O O   . ARG   A 125 ? 0.60148 0.77494 0.70836 -0.01420 -0.00622 -0.00186 122 ARG   A O   
1021 C CB  . ARG   A 125 ? 0.62888 0.81147 0.72346 -0.00795 -0.00723 -0.00836 122 ARG   A CB  
1022 C CG  . ARG   A 125 ? 0.64762 0.82850 0.73310 -0.00817 -0.00925 -0.00827 122 ARG   A CG  
1023 C CD  . ARG   A 125 ? 0.73017 0.91348 0.80644 0.00232  -0.01367 -0.02006 122 ARG   A CD  
1024 N NE  . ARG   A 125 ? 0.87543 1.05270 0.95235 0.01109  -0.02003 -0.02864 122 ARG   A NE  
1025 C CZ  . ARG   A 125 ? 0.92600 1.07913 0.99433 0.01441  -0.03192 -0.03142 122 ARG   A CZ  
1026 N NH1 . ARG   A 125 ? 0.87830 1.01377 0.93878 0.00829  -0.03773 -0.02700 122 ARG   A NH1 
1027 N NH2 . ARG   A 125 ? 0.98765 1.13325 1.05451 0.02372  -0.03897 -0.03908 122 ARG   A NH2 
1028 N N   . VAL   A 126 ? 0.53236 0.72973 0.65351 -0.02330 0.00955  0.00633  123 VAL   A N   
1029 C CA  . VAL   A 126 ? 0.45816 0.65129 0.58506 -0.02564 0.00959  0.00797  123 VAL   A CA  
1030 C C   . VAL   A 126 ? 0.49583 0.68652 0.62808 -0.03434 0.01440  0.01672  123 VAL   A C   
1031 O O   . VAL   A 126 ? 0.52619 0.72532 0.66226 -0.03774 0.02055  0.02052  123 VAL   A O   
1032 C CB  . VAL   A 126 ? 0.51659 0.72552 0.65132 -0.02256 0.01337  0.00233  123 VAL   A CB  
1033 C CG1 . VAL   A 126 ? 0.51520 0.71858 0.65438 -0.02533 0.01276  0.00440  123 VAL   A CG1 
1034 C CG2 . VAL   A 126 ? 0.63133 0.84537 0.76322 -0.01158 0.00746  -0.00890 123 VAL   A CG2 
1035 N N   . LEU   A 127 ? 0.54522 0.72362 0.67640 -0.03800 0.01138  0.01939  124 LEU   A N   
1036 C CA  . LEU   A 127 ? 0.51790 0.69656 0.65610 -0.04482 0.01596  0.02501  124 LEU   A CA  
1037 C C   . LEU   A 127 ? 0.55712 0.73753 0.69943 -0.04597 0.01900  0.02444  124 LEU   A C   
1038 O O   . LEU   A 127 ? 0.58145 0.75533 0.71830 -0.04339 0.01471  0.02106  124 LEU   A O   
1039 C CB  . LEU   A 127 ? 0.49164 0.66016 0.62716 -0.04991 0.01267  0.02687  124 LEU   A CB  
1040 C CG  . LEU   A 127 ? 0.64269 0.80746 0.77342 -0.04949 0.00751  0.02612  124 LEU   A CG  
1041 C CD1 . LEU   A 127 ? 0.57900 0.73642 0.70915 -0.05743 0.00539  0.02730  124 LEU   A CD1 
1042 C CD2 . LEU   A 127 ? 0.58047 0.75537 0.71602 -0.04767 0.00972  0.02817  124 LEU   A CD2 
1043 N N   . HIS   A 128 ? 0.48671 0.67380 0.63715 -0.04934 0.02505  0.02744  125 HIS   A N   
1044 C CA  . HIS   A 128 ? 0.41044 0.59870 0.56477 -0.05110 0.02763  0.02647  125 HIS   A CA  
1045 C C   . HIS   A 128 ? 0.46194 0.64149 0.61423 -0.05522 0.02725  0.02778  125 HIS   A C   
1046 O O   . HIS   A 128 ? 0.48760 0.66084 0.63404 -0.05527 0.02482  0.02578  125 HIS   A O   
1047 C CB  . HIS   A 128 ? 0.39198 0.58752 0.55382 -0.05389 0.03360  0.02869  125 HIS   A CB  
1048 C CG  . HIS   A 128 ? 0.50537 0.70323 0.67148 -0.05577 0.03573  0.02645  125 HIS   A CG  
1049 N ND1 . HIS   A 128 ? 0.47593 0.66794 0.64307 -0.05832 0.03652  0.02690  125 HIS   A ND1 
1050 C CD2 . HIS   A 128 ? 0.43230 0.63934 0.60229 -0.05580 0.03716  0.02267  125 HIS   A CD2 
1051 C CE1 . HIS   A 128 ? 0.53390 0.72899 0.70392 -0.05935 0.03751  0.02399  125 HIS   A CE1 
1052 N NE2 . HIS   A 128 ? 0.51298 0.71780 0.68583 -0.05810 0.03770  0.02131  125 HIS   A NE2 
1053 N N   . ARG   A 129 ? 0.43740 0.61747 0.59400 -0.05869 0.02951  0.03047  126 ARG   A N   
1054 C CA  . ARG   A 129 ? 0.52671 0.70311 0.68259 -0.06413 0.03081  0.03057  126 ARG   A CA  
1055 C C   . ARG   A 129 ? 0.42491 0.60194 0.58283 -0.06639 0.03498  0.02939  126 ARG   A C   
1056 O O   . ARG   A 129 ? 0.52765 0.70134 0.68129 -0.07162 0.03675  0.02867  126 ARG   A O   
1057 C CB  . ARG   A 129 ? 0.44331 0.60797 0.58632 -0.06692 0.02598  0.03018  126 ARG   A CB  
1058 C CG  . ARG   A 129 ? 0.53353 0.69520 0.67282 -0.06463 0.02075  0.03015  126 ARG   A CG  
1059 C CD  . ARG   A 129 ? 0.57732 0.72329 0.70255 -0.06958 0.01557  0.03013  126 ARG   A CD  
1060 N NE  . ARG   A 129 ? 0.55853 0.69053 0.67029 -0.06775 0.01140  0.02927  126 ARG   A NE  
1061 C CZ  . ARG   A 129 ? 0.79507 0.90675 0.88910 -0.07190 0.00541  0.03002  126 ARG   A CZ  
1062 N NH1 . ARG   A 129 ? 0.69195 0.79589 0.78037 -0.08003 0.00402  0.03155  126 ARG   A NH1 
1063 N NH2 . ARG   A 129 ? 0.73106 0.82848 0.81160 -0.06821 -0.00021 0.02908  126 ARG   A NH2 
1064 N N   . ASP   A 130 ? 0.47261 0.65362 0.63576 -0.06377 0.03690  0.02887  127 ASP   A N   
1065 C CA  . ASP   A 130 ? 0.47296 0.65407 0.63838 -0.06577 0.04033  0.02696  127 ASP   A CA  
1066 C C   . ASP   A 130 ? 0.49112 0.67597 0.66463 -0.06428 0.04257  0.02719  127 ASP   A C   
1067 O O   . ASP   A 130 ? 0.49310 0.67790 0.66693 -0.06498 0.04319  0.02507  127 ASP   A O   
1068 C CB  . ASP   A 130 ? 0.40637 0.58124 0.56178 -0.06615 0.03751  0.02481  127 ASP   A CB  
1069 C CG  . ASP   A 130 ? 0.73070 0.90311 0.88328 -0.06982 0.04072  0.02269  127 ASP   A CG  
1070 O OD1 . ASP   A 130 ? 0.54284 0.71932 0.70100 -0.07239 0.04560  0.02206  127 ASP   A OD1 
1071 O OD2 . ASP   A 130 ? 0.80196 0.96931 0.94670 -0.06939 0.03786  0.02063  127 ASP   A OD2 
1072 N N   . LEU   A 131 ? 0.45704 0.64334 0.63551 -0.06280 0.04290  0.02980  128 LEU   A N   
1073 C CA  . LEU   A 131 ? 0.49604 0.68040 0.67785 -0.06280 0.04420  0.03144  128 LEU   A CA  
1074 C C   . LEU   A 131 ? 0.50437 0.68531 0.69118 -0.06258 0.04582  0.02897  128 LEU   A C   
1075 O O   . LEU   A 131 ? 0.65128 0.83284 0.84283 -0.05974 0.04520  0.02807  128 LEU   A O   
1076 C CB  . LEU   A 131 ? 0.44953 0.63239 0.63002 -0.06093 0.04235  0.03571  128 LEU   A CB  
1077 C CG  . LEU   A 131 ? 0.56315 0.75002 0.73782 -0.06084 0.04142  0.03715  128 LEU   A CG  
1078 C CD1 . LEU   A 131 ? 0.61369 0.79734 0.78411 -0.05933 0.03944  0.04152  128 LEU   A CD1 
1079 C CD2 . LEU   A 131 ? 0.46180 0.65328 0.63577 -0.06392 0.04414  0.03557  128 LEU   A CD2 
1080 N N   . LYS   A 132 ? 0.52499 0.70372 0.71161 -0.06494 0.04735  0.02645  129 LYS   A N   
1081 C CA  . LYS   A 132 ? 0.57389 0.74790 0.76394 -0.06436 0.04853  0.02286  129 LYS   A CA  
1082 C C   . LYS   A 132 ? 0.44924 0.61711 0.63837 -0.06803 0.04858  0.02301  129 LYS   A C   
1083 O O   . LYS   A 132 ? 0.51622 0.68856 0.70366 -0.07163 0.04881  0.02403  129 LYS   A O   
1084 C CB  . LYS   A 132 ? 0.48287 0.66069 0.67141 -0.06514 0.05067  0.01771  129 LYS   A CB  
1085 C CG  . LYS   A 132 ? 0.44415 0.62299 0.62534 -0.06802 0.04976  0.01705  129 LYS   A CG  
1086 C CD  . LYS   A 132 ? 0.46175 0.64049 0.63601 -0.06979 0.05142  0.01348  129 LYS   A CD  
1087 C CE  . LYS   A 132 ? 0.61660 0.79215 0.78032 -0.07110 0.04779  0.01313  129 LYS   A CE  
1088 N NZ  . LYS   A 132 ? 0.73273 0.90381 0.88426 -0.07413 0.04895  0.01064  129 LYS   A NZ  
1089 N N   . PRO   A 133 ? 0.50503 0.66314 0.69573 -0.06734 0.04803  0.02106  130 PRO   A N   
1090 C CA  . PRO   A 133 ? 0.49068 0.64047 0.67939 -0.07314 0.04781  0.02147  130 PRO   A CA  
1091 C C   . PRO   A 133 ? 0.44748 0.60554 0.63685 -0.07779 0.04897  0.01744  130 PRO   A C   
1092 O O   . PRO   A 133 ? 0.53206 0.69120 0.72185 -0.08444 0.04947  0.01812  130 PRO   A O   
1093 C CB  . PRO   A 133 ? 0.46862 0.60453 0.65795 -0.06977 0.04573  0.01795  130 PRO   A CB  
1094 C CG  . PRO   A 133 ? 0.65719 0.79467 0.84985 -0.06138 0.04411  0.01773  130 PRO   A CG  
1095 C CD  . PRO   A 133 ? 0.55071 0.70494 0.74545 -0.06115 0.04698  0.01751  130 PRO   A CD  
1096 N N   . GLN   A 134 ? 0.46276 0.62704 0.65144 -0.07504 0.04910  0.01299  131 GLN   A N   
1097 C CA  . GLN   A 134 ? 0.48119 0.65181 0.66862 -0.07768 0.04784  0.00887  131 GLN   A CA  
1098 C C   . GLN   A 134 ? 0.50102 0.68250 0.68977 -0.07865 0.04675  0.01068  131 GLN   A C   
1099 O O   . GLN   A 134 ? 0.50736 0.69639 0.69881 -0.08112 0.04488  0.00662  131 GLN   A O   
1100 C CB  . GLN   A 134 ? 0.55409 0.72526 0.73529 -0.07475 0.04748  0.00500  131 GLN   A CB  
1101 C CG  . GLN   A 134 ? 0.62966 0.79416 0.80965 -0.07382 0.04920  0.00002  131 GLN   A CG  
1102 C CD  . GLN   A 134 ? 0.79335 0.95750 0.97611 -0.06981 0.05214  0.00055  131 GLN   A CD  
1103 O OE1 . GLN   A 134 ? 0.58109 0.74761 0.76733 -0.06820 0.05214  0.00551  131 GLN   A OE1 
1104 N NE2 . GLN   A 134 ? 0.90069 1.06377 1.08249 -0.06778 0.05443  -0.00584 131 GLN   A NE2 
1105 N N   . ASN   A 135 ? 0.38991 0.57377 0.57765 -0.07607 0.04732  0.01530  132 ASN   A N   
1106 C CA  . ASN   A 135 ? 0.48616 0.68058 0.67461 -0.07528 0.04615  0.01561  132 ASN   A CA  
1107 C C   . ASN   A 135 ? 0.46842 0.66713 0.66012 -0.08013 0.04923  0.01859  132 ASN   A C   
1108 O O   . ASN   A 135 ? 0.43550 0.64497 0.62802 -0.07925 0.04945  0.01820  132 ASN   A O   
1109 C CB  . ASN   A 135 ? 0.47947 0.67290 0.66258 -0.07014 0.04442  0.01804  132 ASN   A CB  
1110 C CG  . ASN   A 135 ? 0.49138 0.68089 0.66730 -0.06763 0.04110  0.01524  132 ASN   A CG  
1111 O OD1 . ASN   A 135 ? 0.61661 0.80685 0.79109 -0.06780 0.03852  0.01083  132 ASN   A OD1 
1112 N ND2 . ASN   A 135 ? 0.47557 0.66007 0.64547 -0.06625 0.04076  0.01779  132 ASN   A ND2 
1113 N N   . LEU   A 136 ? 0.52797 0.71705 0.71952 -0.08545 0.05142  0.02128  133 LEU   A N   
1114 C CA  . LEU   A 136 ? 0.47370 0.66230 0.66359 -0.09281 0.05468  0.02540  133 LEU   A CA  
1115 C C   . LEU   A 136 ? 0.52852 0.71962 0.72270 -0.10234 0.05643  0.02176  133 LEU   A C   
1116 O O   . LEU   A 136 ? 0.49863 0.67685 0.69219 -0.10422 0.05491  0.02059  133 LEU   A O   
1117 C CB  . LEU   A 136 ? 0.41305 0.58328 0.59543 -0.09205 0.05401  0.03237  133 LEU   A CB  
1118 C CG  . LEU   A 136 ? 0.48052 0.64987 0.66127 -0.08282 0.05147  0.03445  133 LEU   A CG  
1119 C CD1 . LEU   A 136 ? 0.61355 0.76645 0.78816 -0.08069 0.04896  0.04003  133 LEU   A CD1 
1120 C CD2 . LEU   A 136 ? 0.42157 0.60457 0.60149 -0.08119 0.05228  0.03468  133 LEU   A CD2 
1121 N N   . LEU   A 137 ? 0.43716 0.64629 0.63651 -0.10840 0.05954  0.01871  134 LEU   A N   
1122 C CA  . LEU   A 137 ? 0.48685 0.70519 0.69379 -0.11834 0.06116  0.01306  134 LEU   A CA  
1123 C C   . LEU   A 137 ? 0.56726 0.78382 0.76990 -0.13278 0.06743  0.01764  134 LEU   A C   
1124 O O   . LEU   A 137 ? 0.57275 0.79411 0.76989 -0.13430 0.07137  0.02192  134 LEU   A O   
1125 C CB  . LEU   A 137 ? 0.40509 0.65006 0.62388 -0.11447 0.05938  0.00334  134 LEU   A CB  
1126 C CG  . LEU   A 137 ? 0.37495 0.61813 0.59298 -0.10119 0.05228  -0.00023 134 LEU   A CG  
1127 C CD1 . LEU   A 137 ? 0.39068 0.65698 0.61819 -0.09588 0.04820  -0.00992 134 LEU   A CD1 
1128 C CD2 . LEU   A 137 ? 0.54595 0.77350 0.76100 -0.10120 0.04907  -0.00123 134 LEU   A CD2 
1129 N N   . ILE   A 138 ? 0.48372 0.69180 0.68672 -0.14438 0.06825  0.01673  135 ILE   A N   
1130 C CA  . ILE   A 138 ? 0.54646 0.74788 0.74185 -0.16152 0.07416  0.02185  135 ILE   A CA  
1131 C C   . ILE   A 138 ? 0.64034 0.86338 0.84899 -0.17500 0.07757  0.01308  135 ILE   A C   
1132 O O   . ILE   A 138 ? 0.60148 0.83405 0.82219 -0.17078 0.07296  0.00429  135 ILE   A O   
1133 C CB  . ILE   A 138 ? 0.55846 0.72146 0.73768 -0.16508 0.07086  0.03036  135 ILE   A CB  
1134 C CG1 . ILE   A 138 ? 0.66886 0.82087 0.85312 -0.16495 0.06571  0.02450  135 ILE   A CG1 
1135 C CG2 . ILE   A 138 ? 0.54518 0.69125 0.71482 -0.15048 0.06646  0.03692  135 ILE   A CG2 
1136 C CD1 . ILE   A 138 ? 0.75315 0.86659 0.92233 -0.16579 0.06081  0.03054  135 ILE   A CD1 
1137 N N   . ASN   A 139 ? 0.54237 0.77418 0.74817 -0.19209 0.08574  0.01507  136 ASN   A N   
1138 C CA  . ASN   A 139 ? 0.54993 0.80407 0.76893 -0.20879 0.09036  0.00661  136 ASN   A CA  
1139 C C   . ASN   A 139 ? 0.66902 0.89512 0.87250 -0.22992 0.09355  0.01443  136 ASN   A C   
1140 O O   . ASN   A 139 ? 0.62617 0.81394 0.80863 -0.22878 0.09036  0.02577  136 ASN   A O   
1141 C CB  . ASN   A 139 ? 0.60934 0.90525 0.84126 -0.21299 0.09854  -0.00084 136 ASN   A CB  
1142 C CG  . ASN   A 139 ? 0.62591 0.91659 0.84051 -0.22188 0.10734  0.00869  136 ASN   A CG  
1143 O OD1 . ASN   A 139 ? 0.64074 0.89478 0.83245 -0.22671 0.10677  0.02168  136 ASN   A OD1 
1144 N ND2 . ASN   A 139 ? 0.59267 0.92024 0.81739 -0.22333 0.11483  0.00134  136 ASN   A ND2 
1145 N N   . THR   A 140 ? 0.61281 0.85791 0.82665 -0.24941 0.09904  0.00765  137 THR   A N   
1146 C CA  . THR   A 140 ? 0.72437 0.94302 0.92333 -0.27305 0.10205  0.01406  137 THR   A CA  
1147 C C   . THR   A 140 ? 0.73618 0.95129 0.91691 -0.29156 0.11289  0.02358  137 THR   A C   
1148 O O   . THR   A 140 ? 0.77355 0.96932 0.94012 -0.31562 0.11709  0.02899  137 THR   A O   
1149 C CB  . THR   A 140 ? 0.66443 0.90555 0.88302 -0.28808 0.10296  0.00176  137 THR   A CB  
1150 O OG1 . THR   A 140 ? 0.80722 1.09979 1.04686 -0.29552 0.11206  -0.00887 137 THR   A OG1 
1151 C CG2 . THR   A 140 ? 0.62955 0.87142 0.86221 -0.26999 0.09149  -0.00740 137 THR   A CG2 
1152 N N   . GLU   A 141 ? 0.70065 0.93196 0.87904 -0.28180 0.11730  0.02582  138 GLU   A N   
1153 C CA  . GLU   A 141 ? 0.75498 0.98497 0.91391 -0.29833 0.12804  0.03432  138 GLU   A CA  
1154 C C   . GLU   A 141 ? 0.69593 0.88988 0.82802 -0.28591 0.12319  0.04842  138 GLU   A C   
1155 O O   . GLU   A 141 ? 0.70416 0.90078 0.82014 -0.29291 0.13074  0.05462  138 GLU   A O   
1156 C CB  . GLU   A 141 ? 0.70569 0.99131 0.88483 -0.30038 0.13887  0.02252  138 GLU   A CB  
1157 C CG  . GLU   A 141 ? 0.82641 1.15360 1.03467 -0.31292 0.14352  0.00663  138 GLU   A CG  
1158 C CD  . GLU   A 141 ? 0.90521 1.29028 1.13586 -0.31174 0.15304  -0.00751 138 GLU   A CD  
1159 O OE1 . GLU   A 141 ? 0.79286 1.18520 1.01832 -0.29679 0.15415  -0.00610 138 GLU   A OE1 
1160 O OE2 . GLU   A 141 ? 0.82241 1.23713 1.07203 -0.31782 0.15538  -0.02031 138 GLU   A OE2 
1161 N N   . GLY   A 142 ? 0.74825 0.91067 0.87565 -0.26750 0.11071  0.05255  139 GLY   A N   
1162 C CA  . GLY   A 142 ? 0.65281 0.78131 0.75702 -0.25534 0.10435  0.06456  139 GLY   A CA  
1163 C C   . GLY   A 142 ? 0.62867 0.77712 0.74112 -0.23358 0.10266  0.06204  139 GLY   A C   
1164 O O   . GLY   A 142 ? 0.66542 0.79005 0.75971 -0.22422 0.09768  0.07119  139 GLY   A O   
1165 N N   . ALA   A 143 ? 0.54779 0.73721 0.68609 -0.22492 0.10530  0.04965  140 ALA   A N   
1166 C CA  . ALA   A 143 ? 0.64543 0.85241 0.79064 -0.20546 0.10323  0.04658  140 ALA   A CA  
1167 C C   . ALA   A 143 ? 0.59245 0.79172 0.74859 -0.18486 0.09261  0.04332  140 ALA   A C   
1168 O O   . ALA   A 143 ? 0.54350 0.73815 0.70914 -0.18474 0.08858  0.03885  140 ALA   A O   
1169 C CB  . ALA   A 143 ? 0.58423 0.83823 0.74865 -0.20679 0.11110  0.03439  140 ALA   A CB  
1170 N N   . ILE   A 144 ? 0.49655 0.69448 0.65004 -0.16858 0.08844  0.04534  141 ILE   A N   
1171 C CA  . ILE   A 144 ? 0.47501 0.67067 0.63835 -0.15040 0.08022  0.04172  141 ILE   A CA  
1172 C C   . ILE   A 144 ? 0.58791 0.80624 0.75808 -0.13848 0.08021  0.03694  141 ILE   A C   
1173 O O   . ILE   A 144 ? 0.54313 0.76637 0.70425 -0.13987 0.08388  0.04006  141 ILE   A O   
1174 C CB  . ILE   A 144 ? 0.42695 0.58887 0.57763 -0.14284 0.07287  0.04993  141 ILE   A CB  
1175 C CG1 . ILE   A 144 ? 0.51401 0.67738 0.67583 -0.12700 0.06645  0.04492  141 ILE   A CG1 
1176 C CG2 . ILE   A 144 ? 0.55975 0.71004 0.69351 -0.14079 0.07237  0.05856  141 ILE   A CG2 
1177 C CD1 . ILE   A 144 ? 0.52938 0.66563 0.68383 -0.11934 0.05969  0.04952  141 ILE   A CD1 
1178 N N   . LYS   A 145 ? 0.53347 0.76363 0.71729 -0.12709 0.07555  0.02921  142 LYS   A N   
1179 C CA  . LYS   A 145 ? 0.50491 0.75545 0.69513 -0.11654 0.07434  0.02303  142 LYS   A CA  
1180 C C   . LYS   A 145 ? 0.51907 0.76071 0.71099 -0.10246 0.06644  0.02214  142 LYS   A C   
1181 O O   . LYS   A 145 ? 0.45966 0.69132 0.65447 -0.10093 0.06293  0.02138  142 LYS   A O   
1182 C CB  . LYS   A 145 ? 0.39219 0.67347 0.59779 -0.11924 0.07707  0.01140  142 LYS   A CB  
1183 C CG  . LYS   A 145 ? 0.50072 0.79645 0.70678 -0.13615 0.08681  0.01060  142 LYS   A CG  
1184 C CD  . LYS   A 145 ? 0.45595 0.78937 0.68072 -0.13713 0.08966  -0.00345 142 LYS   A CD  
1185 C CE  . LYS   A 145 ? 0.37846 0.72878 0.60403 -0.15722 0.10128  -0.00459 142 LYS   A CE  
1186 N NZ  . LYS   A 145 ? 0.63657 1.03063 0.88171 -0.15692 0.10548  -0.02008 142 LYS   A NZ  
1187 N N   . LEU   A 146 ? 0.41543 0.66059 0.60421 -0.09326 0.06401  0.02185  143 LEU   A N   
1188 C CA  . LEU   A 146 ? 0.40336 0.64151 0.59218 -0.08215 0.05717  0.02066  143 LEU   A CA  
1189 C C   . LEU   A 146 ? 0.42266 0.67369 0.61999 -0.07695 0.05313  0.01140  143 LEU   A C   
1190 O O   . LEU   A 146 ? 0.44053 0.71143 0.64462 -0.07628 0.05409  0.00408  143 LEU   A O   
1191 C CB  . LEU   A 146 ? 0.43250 0.66863 0.61408 -0.07547 0.05512  0.02295  143 LEU   A CB  
1192 C CG  . LEU   A 146 ? 0.52892 0.75295 0.70041 -0.07833 0.05688  0.03139  143 LEU   A CG  
1193 C CD1 . LEU   A 146 ? 0.48386 0.70834 0.64943 -0.07113 0.05360  0.03150  143 LEU   A CD1 
1194 C CD2 . LEU   A 146 ? 0.53209 0.73767 0.70212 -0.07861 0.05456  0.03679  143 LEU   A CD2 
1195 N N   . ALA   A 147 ? 0.41378 0.65388 0.60998 -0.07276 0.04815  0.01102  144 ALA   A N   
1196 C CA  . ALA   A 147 ? 0.37193 0.61854 0.57186 -0.06727 0.04220  0.00325  144 ALA   A CA  
1197 C C   . ALA   A 147 ? 0.59675 0.82718 0.78671 -0.06066 0.03623  0.00533  144 ALA   A C   
1198 O O   . ALA   A 147 ? 0.50056 0.71846 0.68444 -0.06158 0.03787  0.01172  144 ALA   A O   
1199 C CB  . ALA   A 147 ? 0.53176 0.78212 0.73880 -0.07323 0.04286  -0.00048 144 ALA   A CB  
1200 N N   . ASP   A 148 ? 0.57439 0.80536 0.76214 -0.05445 0.02881  -0.00061 145 ASP   A N   
1201 C CA  . ASP   A 148 ? 0.60127 0.81474 0.77548 -0.04992 0.02249  0.00120  145 ASP   A CA  
1202 C C   . ASP   A 148 ? 0.53555 0.74107 0.70199 -0.04693 0.02134  0.00514  145 ASP   A C   
1203 O O   . ASP   A 148 ? 0.54160 0.73786 0.70392 -0.05098 0.02506  0.01141  145 ASP   A O   
1204 C CB  . ASP   A 148 ? 0.51853 0.71977 0.68780 -0.05554 0.02560  0.00532  145 ASP   A CB  
1205 C CG  . ASP   A 148 ? 0.79034 0.97544 0.94368 -0.05337 0.01964  0.00579  145 ASP   A CG  
1206 O OD1 . ASP   A 148 ? 0.68751 0.86653 0.83193 -0.04736 0.01188  0.00414  145 ASP   A OD1 
1207 O OD2 . ASP   A 148 ? 0.85372 1.03094 1.00172 -0.05787 0.02251  0.00751  145 ASP   A OD2 
1208 N N   . PHE   A 149 ? 0.57906 0.78918 0.74433 -0.03929 0.01551  0.00016  146 PHE   A N   
1209 C CA  . PHE   A 149 ? 0.53893 0.73954 0.69524 -0.03563 0.01238  0.00234  146 PHE   A CA  
1210 C C   . PHE   A 149 ? 0.61176 0.79069 0.75110 -0.03155 0.00253  0.00251  146 PHE   A C   
1211 O O   . PHE   A 149 ? 0.63498 0.80464 0.76565 -0.02636 -0.00356 0.00148  146 PHE   A O   
1212 C CB  . PHE   A 149 ? 0.47881 0.69562 0.64190 -0.02935 0.01176  -0.00408 146 PHE   A CB  
1213 C CG  . PHE   A 149 ? 0.53909 0.76952 0.71045 -0.03566 0.02183  -0.00096 146 PHE   A CG  
1214 C CD1 . PHE   A 149 ? 0.56275 0.80731 0.74489 -0.04250 0.02903  -0.00135 146 PHE   A CD1 
1215 C CD2 . PHE   A 149 ? 0.47054 0.69712 0.63649 -0.03547 0.02325  0.00260  146 PHE   A CD2 
1216 C CE1 . PHE   A 149 ? 0.40480 0.65668 0.58963 -0.04948 0.03746  0.00274  146 PHE   A CE1 
1217 C CE2 . PHE   A 149 ? 0.45197 0.68755 0.62127 -0.04118 0.03125  0.00620  146 PHE   A CE2 
1218 C CZ  . PHE   A 149 ? 0.48131 0.72821 0.65879 -0.04841 0.03836  0.00677  146 PHE   A CZ  
1219 N N   . GLY   A 150 ? 0.57985 0.74824 0.71176 -0.03445 0.00054  0.00390  147 GLY   A N   
1220 C CA  . GLY   A 150 ? 0.58021 0.72405 0.69101 -0.03287 -0.00860 0.00547  147 GLY   A CA  
1221 C C   . GLY   A 150 ? 0.64693 0.77518 0.74638 -0.04026 -0.00596 0.01269  147 GLY   A C   
1222 O O   . GLY   A 150 ? 0.70740 0.81433 0.78864 -0.03902 -0.01423 0.01391  147 GLY   A O   
1223 N N   . LEU   A 151 ? 0.62041 0.75834 0.73013 -0.04807 0.00461  0.01696  148 LEU   A N   
1224 C CA  . LEU   A 151 ? 0.57134 0.70095 0.67537 -0.05543 0.00772  0.02212  148 LEU   A CA  
1225 C C   . LEU   A 151 ? 0.57587 0.71212 0.68699 -0.05254 0.00773  0.02204  148 LEU   A C   
1226 O O   . LEU   A 151 ? 0.57878 0.71197 0.68877 -0.05840 0.01005  0.02537  148 LEU   A O   
1227 C CB  . LEU   A 151 ? 0.61327 0.75080 0.72506 -0.06389 0.01771  0.02493  148 LEU   A CB  
1228 C CG  . LEU   A 151 ? 0.76026 0.88950 0.86123 -0.06889 0.01888  0.02509  148 LEU   A CG  
1229 C CD1 . LEU   A 151 ? 0.72960 0.86934 0.84003 -0.07581 0.02904  0.02573  148 LEU   A CD1 
1230 C CD2 . LEU   A 151 ? 0.71442 0.82037 0.79098 -0.07330 0.01261  0.02763  148 LEU   A CD2 
1231 N N   . ALA   A 152 ? 0.56625 0.71318 0.68467 -0.04408 0.00533  0.01745  149 ALA   A N   
1232 C CA  . ALA   A 152 ? 0.54999 0.70378 0.67293 -0.04108 0.00567  0.01670  149 ALA   A CA  
1233 C C   . ALA   A 152 ? 0.51189 0.64815 0.62018 -0.03724 -0.00388 0.01495  149 ALA   A C   
1234 O O   . ALA   A 152 ? 0.61938 0.73835 0.71391 -0.03432 -0.01231 0.01326  149 ALA   A O   
1235 C CB  . ALA   A 152 ? 0.41703 0.59042 0.55166 -0.03498 0.00804  0.01153  149 ALA   A CB  
1236 N N   . ARG   A 153 ? 0.59810 0.73634 0.70741 -0.03709 -0.00367 0.01533  150 ARG   A N   
1237 C CA  . ARG   A 153 ? 0.64649 0.76731 0.74198 -0.03348 -0.01315 0.01288  150 ARG   A CA  
1238 C C   . ARG   A 153 ? 0.64997 0.78212 0.75065 -0.02871 -0.01241 0.00973  150 ARG   A C   
1239 O O   . ARG   A 153 ? 0.64450 0.78972 0.75454 -0.03327 -0.00511 0.01327  150 ARG   A O   
1240 C CB  . ARG   A 153 ? 0.70973 0.81121 0.79361 -0.04442 -0.01479 0.01852  150 ARG   A CB  
1241 C CG  . ARG   A 153 ? 0.88806 0.96514 0.95389 -0.04240 -0.02609 0.01638  150 ARG   A CG  
1242 C CD  . ARG   A 153 ? 0.95758 1.02093 1.01521 -0.05656 -0.02550 0.02177  150 ARG   A CD  
1243 N NE  . ARG   A 153 ? 1.04633 1.08197 1.08420 -0.05624 -0.03718 0.02004  150 ARG   A NE  
1244 C CZ  . ARG   A 153 ? 1.09816 1.10333 1.11322 -0.06019 -0.04534 0.02213  150 ARG   A CZ  
1245 N NH1 . ARG   A 153 ? 1.13153 1.13118 1.14000 -0.06507 -0.04269 0.02606  150 ARG   A NH1 
1246 N NH2 . ARG   A 153 ? 1.16261 1.13960 1.15854 -0.05940 -0.05718 0.02027  150 ARG   A NH2 
1247 N N   . ALA   A 154 ? 0.64448 0.77050 0.73755 -0.01869 -0.02083 0.00247  151 ALA   A N   
1248 C CA  . ALA   A 154 ? 0.72981 0.86370 0.82366 -0.01406 -0.02110 -0.00155 151 ALA   A CA  
1249 C C   . ALA   A 154 ? 0.66329 0.77937 0.74715 -0.02046 -0.02570 0.00201  151 ALA   A C   
1250 O O   . ALA   A 154 ? 0.80732 0.89896 0.87740 -0.02272 -0.03404 0.00259  151 ALA   A O   
1251 C CB  . ALA   A 154 ? 0.52715 0.66306 0.61747 0.00021  -0.02852 -0.01294 151 ALA   A CB  
1252 N N   . PHE   A 155 ? 0.65267 0.77974 0.74221 -0.02422 -0.02092 0.00443  152 PHE   A N   
1253 C CA  . PHE   A 155 ? 0.66851 0.78292 0.75154 -0.03071 -0.02548 0.00656  152 PHE   A CA  
1254 C C   . PHE   A 155 ? 0.75698 0.86803 0.83169 -0.02263 -0.03218 -0.00053 152 PHE   A C   
1255 O O   . PHE   A 155 ? 0.80237 0.92928 0.88015 -0.01436 -0.02908 -0.00535 152 PHE   A O   
1256 C CB  . PHE   A 155 ? 0.70226 0.82973 0.79691 -0.03965 -0.01827 0.01298  152 PHE   A CB  
1257 C CG  . PHE   A 155 ? 0.67933 0.82536 0.78077 -0.03536 -0.01309 0.01303  152 PHE   A CG  
1258 C CD1 . PHE   A 155 ? 0.66512 0.81193 0.76162 -0.03317 -0.01694 0.01081  152 PHE   A CD1 
1259 C CD2 . PHE   A 155 ? 0.70392 0.86430 0.81428 -0.03478 -0.00479 0.01572  152 PHE   A CD2 
1260 C CE1 . PHE   A 155 ? 0.73480 0.89542 0.83284 -0.03030 -0.01250 0.01187  152 PHE   A CE1 
1261 C CE2 . PHE   A 155 ? 0.72971 0.90274 0.84196 -0.03302 -0.00019 0.01708  152 PHE   A CE2 
1262 C CZ  . PHE   A 155 ? 0.64481 0.81750 0.74976 -0.03075 -0.00399 0.01549  152 PHE   A CZ  
1263 N N   . GLY   A 156 ? 0.73880 0.82870 0.80176 -0.02609 -0.04117 -0.00165 153 GLY   A N   
1264 C CA  . GLY   A 156 ? 0.90395 0.98779 0.95759 -0.01910 -0.04867 -0.00893 153 GLY   A CA  
1265 C C   . GLY   A 156 ? 1.02656 1.12255 1.08535 -0.02388 -0.04592 -0.00681 153 GLY   A C   
1266 O O   . GLY   A 156 ? 0.96618 1.07352 1.03613 -0.03249 -0.03954 0.00013  153 GLY   A O   
1267 N N   . VAL   A 157 ? 1.10351 1.19682 1.15339 -0.01689 -0.05184 -0.01392 154 VAL   A N   
1268 C CA  . VAL   A 157 ? 1.12048 1.22177 1.17098 -0.01981 -0.05229 -0.01335 154 VAL   A CA  
1269 C C   . VAL   A 157 ? 1.13794 1.21724 1.17599 -0.02203 -0.06447 -0.01843 154 VAL   A C   
1270 O O   . VAL   A 157 ? 1.17752 1.24740 1.20308 -0.01225 -0.07147 -0.02746 154 VAL   A O   
1271 C CB  . VAL   A 157 ? 1.08680 1.20670 1.13547 -0.01038 -0.04723 -0.01736 154 VAL   A CB  
1272 C CG1 . VAL   A 157 ? 0.98503 1.11020 1.03090 -0.01319 -0.04920 -0.01598 154 VAL   A CG1 
1273 C CG2 . VAL   A 157 ? 0.98458 1.12350 1.04406 -0.01022 -0.03541 -0.01245 154 VAL   A CG2 
1274 N N   . PRO   A 158 ? 1.05491 1.12624 1.09631 -0.03535 -0.06731 -0.01384 155 PRO   A N   
1275 C CA  . PRO   A 158 ? 1.05969 1.14399 1.11694 -0.04683 -0.05975 -0.00547 155 PRO   A CA  
1276 C C   . PRO   A 158 ? 1.02691 1.10314 1.08538 -0.05210 -0.05558 -0.00090 155 PRO   A C   
1277 O O   . PRO   A 158 ? 0.88945 0.94534 0.93468 -0.04836 -0.06085 -0.00355 155 PRO   A O   
1278 C CB  . PRO   A 158 ? 1.02666 1.10573 1.08512 -0.05841 -0.06637 -0.00630 155 PRO   A CB  
1279 C CG  . PRO   A 158 ? 1.02959 1.07957 1.06889 -0.05809 -0.07744 -0.01220 155 PRO   A CG  
1280 C CD  . PRO   A 158 ? 1.07904 1.12723 1.10805 -0.04054 -0.07916 -0.01847 155 PRO   A CD  
1281 N N   . VAL   A 159 ? 0.92818 1.01924 1.00130 -0.05992 -0.04701 0.00536  156 VAL   A N   
1282 C CA  . VAL   A 159 ? 0.92397 1.00865 0.99725 -0.06592 -0.04236 0.00969  156 VAL   A CA  
1283 C C   . VAL   A 159 ? 0.90059 0.96630 0.96557 -0.08094 -0.04676 0.01086  156 VAL   A C   
1284 O O   . VAL   A 159 ? 0.90737 0.97010 0.97165 -0.08781 -0.05212 0.00840  156 VAL   A O   
1285 C CB  . VAL   A 159 ? 0.86068 0.96841 0.95196 -0.06825 -0.03142 0.01465  156 VAL   A CB  
1286 C CG1 . VAL   A 159 ? 0.79817 0.92283 0.89582 -0.05675 -0.02751 0.01433  156 VAL   A CG1 
1287 C CG2 . VAL   A 159 ? 0.79831 0.91808 0.90268 -0.07993 -0.02939 0.01591  156 VAL   A CG2 
1288 N N   . ARG   A 160 ? 0.91958 0.97171 0.97671 -0.08727 -0.04469 0.01458  157 ARG   A N   
1289 C CA  . ARG   A 160 ? 0.95598 0.99188 1.00424 -0.10541 -0.04567 0.01743  157 ARG   A CA  
1290 C C   . ARG   A 160 ? 0.87219 0.92208 0.93011 -0.11422 -0.03423 0.02239  157 ARG   A C   
1291 O O   . ARG   A 160 ? 0.81994 0.88989 0.89148 -0.10550 -0.02708 0.02328  157 ARG   A O   
1292 C CB  . ARG   A 160 ? 0.86996 0.86590 0.88987 -0.10595 -0.05685 0.01705  157 ARG   A CB  
1293 C CG  . ARG   A 160 ? 0.99467 0.97640 1.00250 -0.09941 -0.05705 0.01975  157 ARG   A CG  
1294 C CD  . ARG   A 160 ? 1.07072 1.00805 1.04759 -0.10112 -0.07047 0.01970  157 ARG   A CD  
1295 N NE  . ARG   A 160 ? 1.12436 1.04465 1.08654 -0.10014 -0.07123 0.02386  157 ARG   A NE  
1296 C CZ  . ARG   A 160 ? 1.07551 0.98758 1.03112 -0.08187 -0.07826 0.02016  157 ARG   A CZ  
1297 N NH1 . ARG   A 160 ? 1.13512 1.05587 1.09777 -0.06342 -0.08381 0.01175  157 ARG   A NH1 
1298 N NH2 . ARG   A 160 ? 1.03681 0.93315 0.97845 -0.08218 -0.07983 0.02410  157 ARG   A NH2 
1299 N N   . THR   A 161 ? 0.78344 0.82225 0.83309 -0.13265 -0.03222 0.02522  158 THR   A N   
1300 C CA  . THR   A 161 ? 0.85857 0.91165 0.91598 -0.14262 -0.02061 0.02864  158 THR   A CA  
1301 C C   . THR   A 161 ? 0.95529 0.99579 1.00056 -0.13393 -0.01987 0.03189  158 THR   A C   
1302 O O   . THR   A 161 ? 0.99083 0.99854 1.01040 -0.13468 -0.02774 0.03408  158 THR   A O   
1303 C CB  . THR   A 161 ? 0.81035 0.85311 0.85772 -0.16642 -0.01808 0.03052  158 THR   A CB  
1304 O OG1 . THR   A 161 ? 0.93162 0.98937 0.99317 -0.17458 -0.01951 0.02604  158 THR   A OG1 
1305 C CG2 . THR   A 161 ? 0.92821 0.98968 0.98405 -0.17684 -0.00463 0.03249  158 THR   A CG2 
1306 N N   . TYR   A 162 ? 0.83682 0.90173 0.89971 -0.12540 -0.01175 0.03177  159 TYR   A N   
1307 C CA  . TYR   A 162 ? 0.83327 0.89080 0.88822 -0.11696 -0.01097 0.03371  159 TYR   A CA  
1308 C C   . TYR   A 162 ? 0.85608 0.91865 0.91006 -0.12882 -0.00130 0.03673  159 TYR   A C   
1309 O O   . TYR   A 162 ? 0.80603 0.87675 0.86383 -0.14457 0.00503  0.03699  159 TYR   A O   
1310 C CB  . TYR   A 162 ? 0.83799 0.91636 0.91034 -0.10008 -0.00898 0.03120  159 TYR   A CB  
1311 C CG  . TYR   A 162 ? 0.80604 0.88055 0.87674 -0.08792 -0.01733 0.02746  159 TYR   A CG  
1312 C CD1 . TYR   A 162 ? 0.80541 0.85234 0.85565 -0.08594 -0.02851 0.02570  159 TYR   A CD1 
1313 C CD2 . TYR   A 162 ? 0.86799 0.96466 0.95529 -0.07853 -0.01440 0.02536  159 TYR   A CD2 
1314 C CE1 . TYR   A 162 ? 0.89841 0.94340 0.94710 -0.07398 -0.03582 0.02051  159 TYR   A CE1 
1315 C CE2 . TYR   A 162 ? 0.72838 0.82299 0.81229 -0.06831 -0.02080 0.02134  159 TYR   A CE2 
1316 C CZ  . TYR   A 162 ? 0.87976 0.95024 0.94552 -0.06561 -0.03115 0.01821  159 TYR   A CZ  
1317 O OH  . TYR   A 162 ? 0.81609 0.88605 0.87849 -0.05455 -0.03723 0.01249  159 TYR   A OH  
1318 N N   . TPO   A 163 ? 0.85644 0.91606 0.90573 -0.12147 -0.00006 0.03791  160 TPO   A N   
1319 C CA  . TPO   A 163 ? 0.85304 0.91469 0.89743 -0.13129 0.00833  0.04023  160 TPO   A CA  
1320 C CB  . TPO   A 163 ? 0.87785 0.93305 0.91543 -0.11992 0.00608  0.04061  160 TPO   A CB  
1321 C CG2 . TPO   A 163 ? 0.76917 0.82501 0.79892 -0.12985 0.01425  0.04254  160 TPO   A CG2 
1322 O OG1 . TPO   A 163 ? 0.95471 0.97982 0.96948 -0.11350 -0.00683 0.04150  160 TPO   A OG1 
1323 P P   . TPO   A 163 ? 0.85373 0.88323 0.87693 -0.09136 -0.01529 0.03650  160 TPO   A P   
1324 O O1P . TPO   A 163 ? 1.00354 0.99659 0.99794 -0.08749 -0.02987 0.03677  160 TPO   A O1P 
1325 O O2P . TPO   A 163 ? 0.79913 0.84693 0.84130 -0.08714 -0.01377 0.03363  160 TPO   A O2P 
1326 O O3P . TPO   A 163 ? 0.79861 0.84673 0.83449 -0.08570 -0.00884 0.03527  160 TPO   A O3P 
1327 C C   . TPO   A 163 ? 0.83752 0.93292 0.90767 -0.13633 0.02069  0.03751  160 TPO   A C   
1328 O O   . TPO   A 163 ? 0.85100 0.96792 0.94301 -0.12519 0.02273  0.03470  160 TPO   A O   
1329 N N   . HIS   A 164 ? 0.74101 0.84010 0.80714 -0.15335 0.02858  0.03787  161 HIS   A N   
1330 C CA  . HIS   A 164 ? 1.00217 1.13487 1.09309 -0.15819 0.04001  0.03305  161 HIS   A CA  
1331 C C   . HIS   A 164 ? 1.02148 1.16558 1.11816 -0.15227 0.04718  0.03153  161 HIS   A C   
1332 O O   . HIS   A 164 ? 0.99925 1.12414 1.07676 -0.14999 0.04482  0.03483  161 HIS   A O   
1333 C CB  . HIS   A 164 ? 0.96527 1.10168 1.05091 -0.18023 0.04686  0.03216  161 HIS   A CB  
1334 C CG  . HIS   A 164 ? 1.11609 1.23017 1.17215 -0.19410 0.05044  0.03673  161 HIS   A CG  
1335 N ND1 . HIS   A 164 ? 1.18130 1.31119 1.23909 -0.20166 0.06255  0.03419  161 HIS   A ND1 
1336 C CD2 . HIS   A 164 ? 1.20087 1.27576 1.22226 -0.20121 0.04259  0.04354  161 HIS   A CD2 
1337 C CE1 . HIS   A 164 ? 1.21490 1.31659 1.23909 -0.21404 0.06270  0.03995  161 HIS   A CE1 
1338 N NE2 . HIS   A 164 ? 1.33453 1.40107 1.33560 -0.21381 0.04999  0.04606  161 HIS   A NE2 
1339 N N   . GLU   A 165 ? 1.11817 1.29273 1.24105 -0.14900 0.05459  0.02570  162 GLU   A N   
1340 C CA  . GLU   A 165 ? 1.08619 1.27338 1.21653 -0.14422 0.06184  0.02247  162 GLU   A CA  
1341 C C   . GLU   A 165 ? 0.95058 1.12442 1.07538 -0.12980 0.05600  0.02543  162 GLU   A C   
1342 O O   . GLU   A 165 ? 1.24730 1.41128 1.35873 -0.13014 0.05757  0.02642  162 GLU   A O   
1343 C CB  . GLU   A 165 ? 1.00808 1.19289 1.12242 -0.15989 0.07079  0.02192  162 GLU   A CB  
1344 C CG  . GLU   A 165 ? 1.02976 1.23361 1.15193 -0.17674 0.07908  0.01740  162 GLU   A CG  
1345 C CD  . GLU   A 165 ? 1.30890 1.51069 1.41212 -0.19433 0.08960  0.01698  162 GLU   A CD  
1346 O OE1 . GLU   A 165 ? 1.42827 1.62070 1.51836 -0.19041 0.09148  0.01809  162 GLU   A OE1 
1347 O OE2 . GLU   A 165 ? 1.38987 1.59957 1.49029 -0.21316 0.09614  0.01533  162 GLU   A OE2 
1348 N N   . VAL   A 166 ? 0.85280 1.02760 0.98774 -0.11785 0.04932  0.02630  163 VAL   A N   
1349 C CA  . VAL   A 166 ? 0.84458 1.01241 0.97836 -0.10541 0.04492  0.02786  163 VAL   A CA  
1350 C C   . VAL   A 166 ? 0.74504 0.93065 0.89858 -0.09781 0.04933  0.02438  163 VAL   A C   
1351 O O   . VAL   A 166 ? 0.76826 0.97095 0.93677 -0.09966 0.05405  0.02026  163 VAL   A O   
1352 C CB  . VAL   A 166 ? 0.81074 0.96940 0.94162 -0.09795 0.03613  0.03025  163 VAL   A CB  
1353 C CG1 . VAL   A 166 ? 0.87087 1.00611 0.97895 -0.10285 0.02949  0.03295  163 VAL   A CG1 
1354 C CG2 . VAL   A 166 ? 0.50282 0.67477 0.64877 -0.09665 0.03539  0.02892  163 VAL   A CG2 
1355 N N   . VAL   A 167 ? 0.59756 0.77896 0.75122 -0.08930 0.04712  0.02526  164 VAL   A N   
1356 C CA  . VAL   A 167 ? 0.69105 0.88239 0.85911 -0.08238 0.04961  0.02297  164 VAL   A CA  
1357 C C   . VAL   A 167 ? 0.58897 0.78697 0.75982 -0.08560 0.05634  0.01828  164 VAL   A C   
1358 O O   . VAL   A 167 ? 0.50270 0.70802 0.67342 -0.09321 0.06127  0.01538  164 VAL   A O   
1359 C CB  . VAL   A 167 ? 0.56838 0.76998 0.75126 -0.07751 0.04796  0.02253  164 VAL   A CB  
1360 C CG1 . VAL   A 167 ? 0.56500 0.76895 0.75722 -0.07005 0.04819  0.02163  164 VAL   A CG1 
1361 C CG2 . VAL   A 167 ? 0.57367 0.76936 0.75155 -0.07539 0.04185  0.02633  164 VAL   A CG2 
1362 N N   . THR   A 168 ? 0.54866 0.74501 0.72179 -0.08067 0.05697  0.01673  165 THR   A N   
1363 C CA  . THR   A 168 ? 0.49873 0.70157 0.67548 -0.08166 0.06280  0.01082  165 THR   A CA  
1364 C C   . THR   A 168 ? 0.54805 0.76746 0.74192 -0.07960 0.06604  0.00534  165 THR   A C   
1365 O O   . THR   A 168 ? 0.56495 0.78802 0.76946 -0.07405 0.06194  0.00656  165 THR   A O   
1366 C CB  . THR   A 168 ? 0.58922 0.78620 0.76736 -0.07595 0.06123  0.00977  165 THR   A CB  
1367 O OG1 . THR   A 168 ? 0.62011 0.80604 0.78636 -0.07661 0.05693  0.01357  165 THR   A OG1 
1368 C CG2 . THR   A 168 ? 0.47876 0.67946 0.65675 -0.07691 0.06650  0.00281  165 THR   A CG2 
1369 N N   . LEU   A 169 ? 0.42060 0.65104 0.61669 -0.08363 0.07308  -0.00168 166 LEU   A N   
1370 C CA  . LEU   A 169 ? 0.52055 0.77219 0.73405 -0.08301 0.07680  -0.00922 166 LEU   A CA  
1371 C C   . LEU   A 169 ? 0.56574 0.82133 0.79660 -0.06978 0.07134  -0.01244 166 LEU   A C   
1372 O O   . LEU   A 169 ? 0.44003 0.70657 0.68414 -0.06615 0.06805  -0.01423 166 LEU   A O   
1373 C CB  . LEU   A 169 ? 0.43671 0.70149 0.64932 -0.08911 0.08649  -0.01795 166 LEU   A CB  
1374 C CG  . LEU   A 169 ? 0.53253 0.82560 0.76445 -0.09062 0.09221  -0.02821 166 LEU   A CG  
1375 C CD1 . LEU   A 169 ? 0.45747 0.75647 0.69021 -0.10013 0.09173  -0.02430 166 LEU   A CD1 
1376 C CD2 . LEU   A 169 ? 0.44909 0.75633 0.67766 -0.09787 0.10352  -0.03752 166 LEU   A CD2 
1377 N N   . TRP   A 170 ? 0.45144 0.69609 0.68085 -0.06270 0.06918  -0.01322 167 TRP   A N   
1378 C CA  . TRP   A 170 ? 0.41221 0.65490 0.65382 -0.05060 0.06302  -0.01611 167 TRP   A CA  
1379 C C   . TRP   A 170 ? 0.48972 0.72339 0.73111 -0.04694 0.05502  -0.00783 167 TRP   A C   
1380 O O   . TRP   A 170 ? 0.42138 0.65535 0.67230 -0.03756 0.04877  -0.01000 167 TRP   A O   
1381 C CB  . TRP   A 170 ? 0.42992 0.65740 0.66598 -0.04634 0.06173  -0.01728 167 TRP   A CB  
1382 C CG  . TRP   A 170 ? 0.50682 0.74327 0.74521 -0.04597 0.06798  -0.02808 167 TRP   A CG  
1383 C CD1 . TRP   A 170 ? 0.46280 0.72046 0.70621 -0.05060 0.07609  -0.03624 167 TRP   A CD1 
1384 C CD2 . TRP   A 170 ? 0.50064 0.72550 0.73542 -0.04159 0.06708  -0.03269 167 TRP   A CD2 
1385 N NE1 . TRP   A 170 ? 0.52582 0.78690 0.76844 -0.04859 0.08080  -0.04600 167 TRP   A NE1 
1386 C CE2 . TRP   A 170 ? 0.54776 0.78795 0.78519 -0.04242 0.07471  -0.04415 167 TRP   A CE2 
1387 C CE3 . TRP   A 170 ? 0.51227 0.71533 0.74110 -0.03834 0.06087  -0.02861 167 TRP   A CE3 
1388 C CZ2 . TRP   A 170 ? 0.56011 0.79363 0.79427 -0.03836 0.07542  -0.05210 167 TRP   A CZ2 
1389 C CZ3 . TRP   A 170 ? 0.58910 0.78451 0.81524 -0.03542 0.06117  -0.03602 167 TRP   A CZ3 
1390 C CH2 . TRP   A 170 ? 0.60548 0.81560 0.83418 -0.03459 0.06796  -0.04786 167 TRP   A CH2 
1391 N N   . TYR   A 171 ? 0.33916 0.56421 0.56866 -0.05332 0.05435  0.00091  168 TYR   A N   
1392 C CA  . TYR   A 171 ? 0.45556 0.67217 0.68201 -0.05065 0.04786  0.00840  168 TYR   A CA  
1393 C C   . TYR   A 171 ? 0.46509 0.68957 0.69118 -0.05540 0.04721  0.01053  168 TYR   A C   
1394 O O   . TYR   A 171 ? 0.40092 0.61795 0.62035 -0.05510 0.04292  0.01678  168 TYR   A O   
1395 C CB  . TYR   A 171 ? 0.40897 0.60992 0.62295 -0.05280 0.04702  0.01510  168 TYR   A CB  
1396 C CG  . TYR   A 171 ? 0.48734 0.67979 0.70101 -0.05051 0.04775  0.01246  168 TYR   A CG  
1397 C CD1 . TYR   A 171 ? 0.44650 0.62795 0.66175 -0.04440 0.04279  0.01344  168 TYR   A CD1 
1398 C CD2 . TYR   A 171 ? 0.42717 0.62006 0.63686 -0.05463 0.05238  0.00882  168 TYR   A CD2 
1399 C CE1 . TYR   A 171 ? 0.52378 0.69440 0.73756 -0.04299 0.04256  0.01065  168 TYR   A CE1 
1400 C CE2 . TYR   A 171 ? 0.48262 0.66730 0.69194 -0.05271 0.05239  0.00540  168 TYR   A CE2 
1401 C CZ  . TYR   A 171 ? 0.53484 0.70824 0.74675 -0.04712 0.04755  0.00617  168 TYR   A CZ  
1402 O OH  . TYR   A 171 ? 0.56362 0.72565 0.77378 -0.04593 0.04667  0.00258  168 TYR   A OH  
1403 N N   . ARG   A 172 ? 0.33894 0.57861 0.57155 -0.06062 0.05167  0.00479  169 ARG   A N   
1404 C CA  . ARG   A 172 ? 0.44307 0.68850 0.67397 -0.06785 0.05136  0.00631  169 ARG   A CA  
1405 C C   . ARG   A 172 ? 0.36938 0.62759 0.61512 -0.06249 0.04596  0.00290  169 ARG   A C   
1406 O O   . ARG   A 172 ? 0.39941 0.67252 0.66113 -0.05681 0.04605  -0.00519 169 ARG   A O   
1407 C CB  . ARG   A 172 ? 0.42417 0.67845 0.65212 -0.07935 0.05939  0.00229  169 ARG   A CB  
1408 C CG  . ARG   A 172 ? 0.46305 0.71748 0.68459 -0.08975 0.05890  0.00486  169 ARG   A CG  
1409 C CD  . ARG   A 172 ? 0.46175 0.72037 0.67510 -0.10371 0.06731  0.00229  169 ARG   A CD  
1410 N NE  . ARG   A 172 ? 0.45848 0.70154 0.65451 -0.10536 0.07005  0.00530  169 ARG   A NE  
1411 C CZ  . ARG   A 172 ? 0.62609 0.86850 0.80990 -0.11642 0.07728  0.00375  169 ARG   A CZ  
1412 N NH1 . ARG   A 172 ? 0.41541 0.67269 0.60219 -0.12883 0.08415  -0.00062 169 ARG   A NH1 
1413 N NH2 . ARG   A 172 ? 0.51513 0.74219 0.68262 -0.11589 0.07768  0.00631  169 ARG   A NH2 
1414 N N   . ALA   A 173 ? 0.42297 0.67583 0.66345 -0.06334 0.04039  0.00792  170 ALA   A N   
1415 C CA  . ALA   A 173 ? 0.32422 0.58696 0.57631 -0.05766 0.03326  0.00523  170 ALA   A CA  
1416 C C   . ALA   A 173 ? 0.43132 0.71857 0.69980 -0.06391 0.03642  -0.00391 170 ALA   A C   
1417 O O   . ALA   A 173 ? 0.46124 0.75313 0.72587 -0.07623 0.04413  -0.00525 170 ALA   A O   
1418 C CB  . ALA   A 173 ? 0.41652 0.66743 0.65663 -0.05822 0.02710  0.01210  170 ALA   A CB  
1419 N N   . PRO   A 174 ? 0.41796 0.72148 0.70424 -0.05612 0.03025  -0.01072 171 PRO   A N   
1420 C CA  . PRO   A 174 ? 0.32875 0.66162 0.63469 -0.06266 0.03387  -0.02160 171 PRO   A CA  
1421 C C   . PRO   A 174 ? 0.43689 0.77226 0.73781 -0.07708 0.03478  -0.01959 171 PRO   A C   
1422 O O   . PRO   A 174 ? 0.39129 0.74620 0.70102 -0.08983 0.04234  -0.02627 171 PRO   A O   
1423 C CB  . PRO   A 174 ? 0.42862 0.77580 0.75418 -0.04766 0.02360  -0.02937 171 PRO   A CB  
1424 C CG  . PRO   A 174 ? 0.34318 0.66375 0.65275 -0.03787 0.01321  -0.01912 171 PRO   A CG  
1425 C CD  . PRO   A 174 ? 0.38586 0.68209 0.67465 -0.04125 0.01927  -0.00950 171 PRO   A CD  
1426 N N   . GLU   A 175 ? 0.37764 0.69346 0.66360 -0.07634 0.02757  -0.01112 172 GLU   A N   
1427 C CA  . GLU   A 175 ? 0.47674 0.79072 0.75574 -0.08976 0.02721  -0.00962 172 GLU   A CA  
1428 C C   . GLU   A 175 ? 0.48412 0.78572 0.74610 -0.10420 0.03632  -0.00551 172 GLU   A C   
1429 O O   . GLU   A 175 ? 0.48991 0.79502 0.74917 -0.11939 0.03918  -0.00706 172 GLU   A O   
1430 C CB  . GLU   A 175 ? 0.44295 0.73789 0.70829 -0.08408 0.01711  -0.00273 172 GLU   A CB  
1431 C CG  . GLU   A 175 ? 0.47787 0.74667 0.72208 -0.07858 0.01715  0.00669  172 GLU   A CG  
1432 C CD  . GLU   A 175 ? 0.46214 0.72673 0.70795 -0.06406 0.01312  0.00889  172 GLU   A CD  
1433 O OE1 . GLU   A 175 ? 0.45964 0.73867 0.72189 -0.05738 0.01175  0.00307  172 GLU   A OE1 
1434 O OE2 . GLU   A 175 ? 0.40896 0.65551 0.63900 -0.05959 0.01106  0.01590  172 GLU   A OE2 
1435 N N   . ILE   A 176 ? 0.42320 0.70892 0.67228 -0.10038 0.04015  -0.00034 173 ILE   A N   
1436 C CA  . ILE   A 176 ? 0.40496 0.67825 0.63668 -0.11258 0.04749  0.00299  173 ILE   A CA  
1437 C C   . ILE   A 176 ? 0.47478 0.76998 0.71716 -0.12302 0.05798  -0.00482 173 ILE   A C   
1438 O O   . ILE   A 176 ? 0.47391 0.76670 0.70543 -0.13973 0.06365  -0.00434 173 ILE   A O   
1439 C CB  . ILE   A 176 ? 0.36806 0.62128 0.58513 -0.10475 0.04758  0.00918  173 ILE   A CB  
1440 C CG1 . ILE   A 176 ? 0.46236 0.69920 0.67082 -0.09519 0.03878  0.01522  173 ILE   A CG1 
1441 C CG2 . ILE   A 176 ? 0.44082 0.67856 0.63740 -0.11592 0.05261  0.01262  173 ILE   A CG2 
1442 C CD1 . ILE   A 176 ? 0.60705 0.82948 0.80107 -0.10172 0.03366  0.01853  173 ILE   A CD1 
1443 N N   . LEU   A 177 ? 0.39365 0.70969 0.65595 -0.11367 0.06063  -0.01259 174 LEU   A N   
1444 C CA  . LEU   A 177 ? 0.44027 0.78172 0.71484 -0.12202 0.07150  -0.02244 174 LEU   A CA  
1445 C C   . LEU   A 177 ? 0.49420 0.86069 0.78327 -0.13531 0.07414  -0.02980 174 LEU   A C   
1446 O O   . LEU   A 177 ? 0.45627 0.84021 0.74763 -0.15032 0.08541  -0.03587 174 LEU   A O   
1447 C CB  . LEU   A 177 ? 0.50713 0.86518 0.80150 -0.10605 0.07144  -0.03104 174 LEU   A CB  
1448 C CG  . LEU   A 177 ? 0.42684 0.76320 0.70896 -0.09517 0.07029  -0.02575 174 LEU   A CG  
1449 C CD1 . LEU   A 177 ? 0.38769 0.73465 0.68871 -0.07757 0.06565  -0.03344 174 LEU   A CD1 
1450 C CD2 . LEU   A 177 ? 0.47027 0.80225 0.73755 -0.10568 0.08107  -0.02579 174 LEU   A CD2 
1451 N N   . LEU   A 178 ? 0.56700 0.93667 0.86549 -0.13117 0.06427  -0.02990 175 LEU   A N   
1452 C CA  . LEU   A 178 ? 0.50791 0.90169 0.82140 -0.14431 0.06523  -0.03737 175 LEU   A CA  
1453 C C   . LEU   A 178 ? 0.60572 0.97702 0.89618 -0.16263 0.06470  -0.02906 175 LEU   A C   
1454 O O   . LEU   A 178 ? 0.59263 0.97989 0.89257 -0.17635 0.06496  -0.03426 175 LEU   A O   
1455 C CB  . LEU   A 178 ? 0.54882 0.95931 0.88551 -0.12971 0.05321  -0.04358 175 LEU   A CB  
1456 C CG  . LEU   A 178 ? 0.58310 1.02228 0.94756 -0.11343 0.05229  -0.05586 175 LEU   A CG  
1457 C CD1 . LEU   A 178 ? 0.50357 0.95050 0.88420 -0.09737 0.03709  -0.05972 175 LEU   A CD1 
1458 C CD2 . LEU   A 178 ? 0.37049 0.84929 0.75656 -0.12575 0.06455  -0.07025 175 LEU   A CD2 
1459 N N   . GLY   A 179 ? 0.59990 0.93447 0.86084 -0.16281 0.06294  -0.01722 176 GLY   A N   
1460 C CA  . GLY   A 179 ? 0.61889 0.92710 0.85414 -0.17924 0.06169  -0.00970 176 GLY   A CA  
1461 C C   . GLY   A 179 ? 0.58918 0.88387 0.82078 -0.17666 0.04934  -0.00672 176 GLY   A C   
1462 O O   . GLY   A 179 ? 0.71209 1.00339 0.93803 -0.19330 0.04833  -0.00726 176 GLY   A O   
1463 N N   . CYS   A 180 ? 0.50527 0.79111 0.73823 -0.15712 0.04008  -0.00372 177 CYS   A N   
1464 C CA  . CYS   A 180 ? 0.65339 0.92545 0.88019 -0.15326 0.02843  -0.00129 177 CYS   A CA  
1465 C C   . CYS   A 180 ? 0.66141 0.89708 0.85734 -0.16106 0.02502  0.00660  177 CYS   A C   
1466 O O   . CYS   A 180 ? 0.60454 0.82071 0.78248 -0.16000 0.02812  0.01228  177 CYS   A O   
1467 C CB  . CYS   A 180 ? 0.61905 0.88947 0.85087 -0.13159 0.02085  0.00044  177 CYS   A CB  
1468 S SG  . CYS   A 180 ? 0.71904 0.96656 0.93309 -0.11976 0.02322  0.00865  177 CYS   A SG  
1469 N N   . LYS   A 181 ? 0.69579 0.92141 0.88530 -0.16809 0.01722  0.00609  178 LYS   A N   
1470 C CA  . LYS   A 181 ? 0.74164 0.92963 0.90105 -0.17345 0.01127  0.01232  178 LYS   A CA  
1471 C C   . LYS   A 181 ? 0.72632 0.89510 0.87358 -0.15381 0.00454  0.01675  178 LYS   A C   
1472 O O   . LYS   A 181 ? 0.85941 1.00571 0.98731 -0.15146 0.00481  0.02170  178 LYS   A O   
1473 C CB  . LYS   A 181 ? 0.80381 0.98540 0.96009 -0.18494 0.00349  0.00941  178 LYS   A CB  
1474 C CG  . LYS   A 181 ? 1.01314 1.20136 1.16981 -0.21087 0.01017  0.00693  178 LYS   A CG  
1475 C CD  . LYS   A 181 ? 1.09734 1.27939 1.25225 -0.22248 0.00139  0.00337  178 LYS   A CD  
1476 C CE  . LYS   A 181 ? 1.18307 1.32281 1.30931 -0.21511 -0.01144 0.00834  178 LYS   A CE  
1477 N NZ  . LYS   A 181 ? 1.14915 1.25062 1.24278 -0.22163 -0.01085 0.01628  178 LYS   A NZ  
1478 N N   . TYR   A 182 ? 0.66727 0.84562 0.82523 -0.13992 -0.00168 0.01445  179 TYR   A N   
1479 C CA  . TYR   A 182 ? 0.72359 0.88875 0.87161 -0.12284 -0.00673 0.01739  179 TYR   A CA  
1480 C C   . TYR   A 182 ? 0.78523 0.96924 0.94856 -0.11017 -0.00193 0.01783  179 TYR   A C   
1481 O O   . TYR   A 182 ? 0.86529 1.07266 1.04863 -0.11028 0.00093  0.01441  179 TYR   A O   
1482 C CB  . TYR   A 182 ? 0.69941 0.85765 0.84251 -0.11707 -0.01727 0.01491  179 TYR   A CB  
1483 C CG  . TYR   A 182 ? 0.77517 0.91592 0.90575 -0.13043 -0.02364 0.01305  179 TYR   A CG  
1484 C CD1 . TYR   A 182 ? 0.74127 0.85083 0.84756 -0.13526 -0.02669 0.01602  179 TYR   A CD1 
1485 C CD2 . TYR   A 182 ? 0.80596 0.95955 0.94798 -0.13802 -0.02804 0.00794  179 TYR   A CD2 
1486 C CE1 . TYR   A 182 ? 0.87528 0.96352 0.96687 -0.14828 -0.03368 0.01478  179 TYR   A CE1 
1487 C CE2 . TYR   A 182 ? 0.81148 0.94744 0.94134 -0.15205 -0.03419 0.00606  179 TYR   A CE2 
1488 C CZ  . TYR   A 182 ? 0.90546 1.00701 1.00899 -0.15757 -0.03690 0.00991  179 TYR   A CZ  
1489 O OH  . TYR   A 182 ? 0.92422 1.00309 1.01251 -0.17236 -0.04410 0.00850  179 TYR   A OH  
1490 N N   . TYR   A 183 ? 0.71786 0.89127 0.87163 -0.09921 -0.00177 0.02129  180 TYR   A N   
1491 C CA  . TYR   A 183 ? 0.76656 0.95236 0.93055 -0.08791 0.00150  0.02249  180 TYR   A CA  
1492 C C   . TYR   A 183 ? 0.62440 0.79811 0.77554 -0.07741 -0.00110 0.02481  180 TYR   A C   
1493 O O   . TYR   A 183 ? 0.71963 0.87674 0.85582 -0.07751 -0.00432 0.02479  180 TYR   A O   
1494 C CB  . TYR   A 183 ? 0.73889 0.93329 0.91116 -0.09057 0.01035  0.02310  180 TYR   A CB  
1495 C CG  . TYR   A 183 ? 0.73074 0.90927 0.88826 -0.09379 0.01352  0.02588  180 TYR   A CG  
1496 C CD1 . TYR   A 183 ? 0.59660 0.76821 0.74780 -0.08455 0.01378  0.02818  180 TYR   A CD1 
1497 C CD2 . TYR   A 183 ? 0.69722 0.86786 0.84632 -0.10680 0.01594  0.02595  180 TYR   A CD2 
1498 C CE1 . TYR   A 183 ? 0.74553 0.90364 0.88407 -0.08608 0.01480  0.02966  180 TYR   A CE1 
1499 C CE2 . TYR   A 183 ? 0.65180 0.80494 0.78424 -0.10890 0.01699  0.02880  180 TYR   A CE2 
1500 C CZ  . TYR   A 183 ? 0.68600 0.83342 0.81410 -0.09746 0.01568  0.03024  180 TYR   A CZ  
1501 O OH  . TYR   A 183 ? 0.69254 0.82346 0.80482 -0.09817 0.01490  0.03205  180 TYR   A OH  
1502 N N   . SER   A 184 ? 0.58537 0.76745 0.74189 -0.06845 0.00001  0.02621  181 SER   A N   
1503 C CA  . SER   A 184 ? 0.73847 0.91430 0.88469 -0.06025 -0.00031 0.02757  181 SER   A CA  
1504 C C   . SER   A 184 ? 0.60715 0.79043 0.75927 -0.05561 0.00510  0.03061  181 SER   A C   
1505 O O   . SER   A 184 ? 0.64379 0.83011 0.80290 -0.05803 0.01033  0.03155  181 SER   A O   
1506 C CB  . SER   A 184 ? 0.69551 0.86851 0.83347 -0.05556 -0.00705 0.02571  181 SER   A CB  
1507 O OG  . SER   A 184 ? 0.82353 1.00571 0.96794 -0.05296 -0.00918 0.02672  181 SER   A OG  
1508 N N   . THR   A 185 ? 0.62215 0.80672 0.76939 -0.04984 0.00374  0.03213  182 THR   A N   
1509 C CA  . THR   A 185 ? 0.55524 0.74202 0.70269 -0.04720 0.00874  0.03565  182 THR   A CA  
1510 C C   . THR   A 185 ? 0.49569 0.68608 0.65365 -0.04714 0.00945  0.03783  182 THR   A C   
1511 O O   . THR   A 185 ? 0.58188 0.77088 0.74064 -0.04664 0.01369  0.04053  182 THR   A O   
1512 C CB  . THR   A 185 ? 0.53137 0.71704 0.66684 -0.04329 0.00758  0.03702  182 THR   A CB  
1513 O OG1 . THR   A 185 ? 0.59993 0.78488 0.73303 -0.04125 0.00076  0.03742  182 THR   A OG1 
1514 C CG2 . THR   A 185 ? 0.55817 0.74287 0.68478 -0.04135 0.00737  0.03260  182 THR   A CG2 
1515 N N   . ALA   A 186 ? 0.50087 0.69636 0.66759 -0.04740 0.00485  0.03561  183 ALA   A N   
1516 C CA  . ALA   A 186 ? 0.47718 0.67759 0.65513 -0.04449 0.00376  0.03556  183 ALA   A CA  
1517 C C   . ALA   A 186 ? 0.52959 0.73332 0.71702 -0.04713 0.01046  0.03417  183 ALA   A C   
1518 O O   . ALA   A 186 ? 0.45494 0.65889 0.64851 -0.04312 0.01037  0.03433  183 ALA   A O   
1519 C CB  . ALA   A 186 ? 0.41567 0.62606 0.60445 -0.04381 -0.00296 0.03095  183 ALA   A CB  
1520 N N   . VAL   A 187 ? 0.46358 0.66753 0.65015 -0.05324 0.01528  0.03261  184 VAL   A N   
1521 C CA  . VAL   A 187 ? 0.46588 0.67291 0.65930 -0.05614 0.02145  0.03081  184 VAL   A CA  
1522 C C   . VAL   A 187 ? 0.43632 0.63630 0.62530 -0.05340 0.02473  0.03395  184 VAL   A C   
1523 O O   . VAL   A 187 ? 0.45819 0.65974 0.65389 -0.05276 0.02785  0.03239  184 VAL   A O   
1524 C CB  . VAL   A 187 ? 0.56587 0.77129 0.75489 -0.06415 0.02458  0.02914  184 VAL   A CB  
1525 C CG1 . VAL   A 187 ? 0.48756 0.69916 0.68056 -0.06981 0.02179  0.02605  184 VAL   A CG1 
1526 C CG2 . VAL   A 187 ? 0.62031 0.81403 0.79497 -0.06363 0.02362  0.03165  184 VAL   A CG2 
1527 N N   . ASP   A 188 ? 0.48045 0.67385 0.65859 -0.05228 0.02430  0.03736  185 ASP   A N   
1528 C CA  . ASP   A 188 ? 0.52344 0.71220 0.69812 -0.05201 0.02788  0.03988  185 ASP   A CA  
1529 C C   . ASP   A 188 ? 0.48614 0.66933 0.66059 -0.04871 0.02561  0.04310  185 ASP   A C   
1530 O O   . ASP   A 188 ? 0.50708 0.68496 0.68229 -0.04939 0.02810  0.04412  185 ASP   A O   
1531 C CB  . ASP   A 188 ? 0.51760 0.70550 0.68247 -0.05265 0.02898  0.04086  185 ASP   A CB  
1532 C CG  . ASP   A 188 ? 0.51104 0.70023 0.67436 -0.05397 0.02946  0.03722  185 ASP   A CG  
1533 O OD1 . ASP   A 188 ? 0.45720 0.64570 0.62445 -0.05638 0.03082  0.03548  185 ASP   A OD1 
1534 O OD2 . ASP   A 188 ? 0.49062 0.68055 0.64725 -0.05212 0.02795  0.03565  185 ASP   A OD2 
1535 N N   . ILE   A 189 ? 0.45399 0.63579 0.62551 -0.04501 0.01968  0.04464  186 ILE   A N   
1536 C CA  . ILE   A 189 ? 0.41281 0.58476 0.58038 -0.04072 0.01497  0.04816  186 ILE   A CA  
1537 C C   . ILE   A 189 ? 0.48679 0.66036 0.66774 -0.03647 0.01314  0.04401  186 ILE   A C   
1538 O O   . ILE   A 189 ? 0.49606 0.65767 0.67400 -0.03389 0.01139  0.04601  186 ILE   A O   
1539 C CB  . ILE   A 189 ? 0.46001 0.62988 0.62001 -0.03672 0.00731  0.05005  186 ILE   A CB  
1540 C CG1 . ILE   A 189 ? 0.59705 0.76534 0.74204 -0.04041 0.00991  0.05311  186 ILE   A CG1 
1541 C CG2 . ILE   A 189 ? 0.47951 0.63548 0.63286 -0.03095 -0.00012 0.05379  186 ILE   A CG2 
1542 C CD1 . ILE   A 189 ? 0.61019 0.76856 0.74150 -0.04474 0.01464  0.05875  186 ILE   A CD1 
1543 N N   . TRP   A 190 ? 0.38567 0.57376 0.58082 -0.03617 0.01358  0.03751  187 TRP   A N   
1544 C CA  . TRP   A 190 ? 0.44547 0.64031 0.65522 -0.03231 0.01360  0.03117  187 TRP   A CA  
1545 C C   . TRP   A 190 ? 0.43491 0.62336 0.64340 -0.03489 0.01982  0.03106  187 TRP   A C   
1546 O O   . TRP   A 190 ? 0.40267 0.58389 0.61396 -0.02957 0.01742  0.02926  187 TRP   A O   
1547 C CB  . TRP   A 190 ? 0.39457 0.60906 0.61837 -0.03551 0.01600  0.02395  187 TRP   A CB  
1548 C CG  . TRP   A 190 ? 0.39508 0.62192 0.63537 -0.03193 0.01760  0.01533  187 TRP   A CG  
1549 C CD1 . TRP   A 190 ? 0.39354 0.62348 0.63714 -0.03526 0.02525  0.01163  187 TRP   A CD1 
1550 C CD2 . TRP   A 190 ? 0.41563 0.65512 0.67165 -0.02337 0.01100  0.00779  187 TRP   A CD2 
1551 N NE1 . TRP   A 190 ? 0.38515 0.62959 0.64535 -0.02960 0.02495  0.00190  187 TRP   A NE1 
1552 C CE2 . TRP   A 190 ? 0.38716 0.63879 0.65667 -0.02174 0.01602  -0.00112 187 TRP   A CE2 
1553 C CE3 . TRP   A 190 ? 0.45228 0.69501 0.71244 -0.01615 0.00059  0.00668  187 TRP   A CE3 
1554 C CZ2 . TRP   A 190 ? 0.32946 0.59867 0.61857 -0.01251 0.01140  -0.01214 187 TRP   A CZ2 
1555 C CZ3 . TRP   A 190 ? 0.47909 0.73820 0.75868 -0.00677 -0.00526 -0.00373 187 TRP   A CZ3 
1556 C CH2 . TRP   A 190 ? 0.36376 0.63708 0.65870 -0.00472 0.00037  -0.01353 187 TRP   A CH2 
1557 N N   . SER   A 191 ? 0.38270 0.57255 0.58642 -0.04228 0.02651  0.03226  188 SER   A N   
1558 C CA  . SER   A 191 ? 0.42665 0.61123 0.62871 -0.04515 0.03158  0.03168  188 SER   A CA  
1559 C C   . SER   A 191 ? 0.47384 0.64235 0.66746 -0.04405 0.02943  0.03655  188 SER   A C   
1560 O O   . SER   A 191 ? 0.48132 0.64249 0.67680 -0.04278 0.02981  0.03445  188 SER   A O   
1561 C CB  . SER   A 191 ? 0.39428 0.58153 0.59051 -0.05181 0.03638  0.03249  188 SER   A CB  
1562 O OG  . SER   A 191 ? 0.46666 0.66326 0.66613 -0.05460 0.03774  0.02919  188 SER   A OG  
1563 N N   . LEU   A 192 ? 0.37378 0.53553 0.55636 -0.04541 0.02724  0.04286  189 LEU   A N   
1564 C CA  . LEU   A 192 ? 0.47496 0.61979 0.64587 -0.04748 0.02603  0.04857  189 LEU   A CA  
1565 C C   . LEU   A 192 ? 0.47104 0.60139 0.64081 -0.03994 0.01805  0.04899  189 LEU   A C   
1566 O O   . LEU   A 192 ? 0.53828 0.65099 0.70075 -0.04129 0.01668  0.05142  189 LEU   A O   
1567 C CB  . LEU   A 192 ? 0.42298 0.56605 0.58055 -0.05171 0.02668  0.05458  189 LEU   A CB  
1568 C CG  . LEU   A 192 ? 0.66929 0.80926 0.81856 -0.06098 0.03296  0.05763  189 LEU   A CG  
1569 C CD1 . LEU   A 192 ? 0.63849 0.79136 0.79835 -0.06397 0.03857  0.05188  189 LEU   A CD1 
1570 C CD2 . LEU   A 192 ? 0.66549 0.80891 0.80278 -0.06473 0.03483  0.06145  189 LEU   A CD2 
1571 N N   . GLY   A 193 ? 0.47417 0.61096 0.65096 -0.03177 0.01168  0.04595  190 GLY   A N   
1572 C CA  . GLY   A 193 ? 0.51180 0.63710 0.69036 -0.02161 0.00218  0.04384  190 GLY   A CA  
1573 C C   . GLY   A 193 ? 0.52132 0.64795 0.71195 -0.01777 0.00362  0.03597  190 GLY   A C   
1574 O O   . GLY   A 193 ? 0.48892 0.59616 0.67458 -0.01200 -0.00284 0.03577  190 GLY   A O   
1575 N N   . CYS   A 194 ? 0.39070 0.53803 0.59499 -0.02099 0.01161  0.02924  191 CYS   A N   
1576 C CA  . CYS   A 194 ? 0.48928 0.63903 0.70277 -0.01866 0.01462  0.02125  191 CYS   A CA  
1577 C C   . CYS   A 194 ? 0.50297 0.63302 0.70459 -0.02444 0.01685  0.02543  191 CYS   A C   
1578 O O   . CYS   A 194 ? 0.49807 0.61540 0.70010 -0.01950 0.01351  0.02127  191 CYS   A O   
1579 C CB  . CYS   A 194 ? 0.44039 0.61399 0.66529 -0.02367 0.02354  0.01482  191 CYS   A CB  
1580 S SG  . CYS   A 194 ? 0.44809 0.64739 0.68894 -0.02034 0.02237  0.00817  191 CYS   A SG  
1581 N N   . ILE   A 195 ? 0.47413 0.60235 0.66588 -0.03482 0.02208  0.03250  192 ILE   A N   
1582 C CA  . ILE   A 195 ? 0.60268 0.71585 0.78483 -0.04243 0.02460  0.03590  192 ILE   A CA  
1583 C C   . ILE   A 195 ? 0.54419 0.62994 0.71216 -0.04135 0.01717  0.04210  192 ILE   A C   
1584 O O   . ILE   A 195 ? 0.58119 0.64874 0.74339 -0.04386 0.01576  0.04187  192 ILE   A O   
1585 C CB  . ILE   A 195 ? 0.53311 0.65593 0.71082 -0.05277 0.03149  0.04010  192 ILE   A CB  
1586 C CG1 . ILE   A 195 ? 0.55422 0.69691 0.74179 -0.05355 0.03683  0.03411  192 ILE   A CG1 
1587 C CG2 . ILE   A 195 ? 0.53184 0.64236 0.70096 -0.06218 0.03400  0.04332  192 ILE   A CG2 
1588 C CD1 . ILE   A 195 ? 0.61724 0.76993 0.80143 -0.05997 0.04093  0.03657  192 ILE   A CD1 
1589 N N   . PHE   A 196 ? 0.58577 0.66559 0.74558 -0.03806 0.01149  0.04785  193 PHE   A N   
1590 C CA  . PHE   A 196 ? 0.55119 0.60067 0.69274 -0.03669 0.00271  0.05484  193 PHE   A CA  
1591 C C   . PHE   A 196 ? 0.57605 0.60917 0.72128 -0.02505 -0.00646 0.04852  193 PHE   A C   
1592 O O   . PHE   A 196 ? 0.58905 0.59489 0.72163 -0.02808 -0.01002 0.05115  193 PHE   A O   
1593 C CB  . PHE   A 196 ? 0.51635 0.56480 0.64901 -0.03282 -0.00310 0.06049  193 PHE   A CB  
1594 C CG  . PHE   A 196 ? 0.59678 0.61094 0.70459 -0.03259 -0.01277 0.06958  193 PHE   A CG  
1595 C CD1 . PHE   A 196 ? 0.68249 0.66866 0.77379 -0.04112 -0.01300 0.07488  193 PHE   A CD1 
1596 C CD2 . PHE   A 196 ? 0.62859 0.63657 0.72743 -0.02460 -0.02245 0.07301  193 PHE   A CD2 
1597 C CE1 . PHE   A 196 ? 0.68969 0.63948 0.75346 -0.04245 -0.02250 0.08444  193 PHE   A CE1 
1598 C CE2 . PHE   A 196 ? 0.65799 0.63064 0.72948 -0.02435 -0.03265 0.08222  193 PHE   A CE2 
1599 C CZ  . PHE   A 196 ? 0.58770 0.52980 0.64036 -0.03369 -0.03255 0.08846  193 PHE   A CZ  
1600 N N   . ALA   A 197 ? 0.60605 0.65620 0.76899 -0.01186 -0.01047 0.03909  194 ALA   A N   
1601 C CA  . ALA   A 197 ? 0.56086 0.60045 0.73057 0.00171  -0.01936 0.03006  194 ALA   A CA  
1602 C C   . ALA   A 197 ? 0.60009 0.63760 0.77441 -0.00201 -0.01343 0.02380  194 ALA   A C   
1603 O O   . ALA   A 197 ? 0.67624 0.69055 0.84583 0.00508  -0.02128 0.01982  194 ALA   A O   
1604 C CB  . ALA   A 197 ? 0.61573 0.68309 0.80775 0.01491  -0.02236 0.01890  194 ALA   A CB  
1605 N N   . GLU   A 198 ? 0.53474 0.59405 0.71669 -0.01237 -0.00095 0.02245  195 GLU   A N   
1606 C CA  . GLU   A 198 ? 0.65768 0.71577 0.84281 -0.01611 0.00417  0.01617  195 GLU   A CA  
1607 C C   . GLU   A 198 ? 0.71349 0.74074 0.88054 -0.02559 0.00201  0.02335  195 GLU   A C   
1608 O O   . GLU   A 198 ? 0.68685 0.69919 0.85253 -0.02399 -0.00043 0.01757  195 GLU   A O   
1609 C CB  . GLU   A 198 ? 0.58623 0.67226 0.78046 -0.02470 0.01614  0.01387  195 GLU   A CB  
1610 C CG  . GLU   A 198 ? 0.60480 0.69636 0.80530 -0.02490 0.02076  0.00410  195 GLU   A CG  
1611 C CD  . GLU   A 198 ? 0.65853 0.77412 0.86412 -0.03260 0.03068  0.00247  195 GLU   A CD  
1612 O OE1 . GLU   A 198 ? 0.58668 0.72012 0.79725 -0.03298 0.03353  0.00419  195 GLU   A OE1 
1613 O OE2 . GLU   A 198 ? 0.58787 0.70231 0.79089 -0.03827 0.03452  -0.00055 195 GLU   A OE2 
1614 N N   . MET   A 199 ? 0.62790 0.64572 0.78052 -0.03645 0.00324  0.03521  196 MET   A N   
1615 C CA  . MET   A 199 ? 0.68047 0.66858 0.81440 -0.04797 0.00154  0.04252  196 MET   A CA  
1616 C C   . MET   A 199 ? 0.70852 0.65877 0.82776 -0.03941 -0.01213 0.04408  196 MET   A C   
1617 O O   . MET   A 199 ? 0.70728 0.62892 0.81366 -0.04592 -0.01544 0.04560  196 MET   A O   
1618 C CB  . MET   A 199 ? 0.69120 0.68148 0.81285 -0.06209 0.00719  0.05386  196 MET   A CB  
1619 C CG  . MET   A 199 ? 0.59775 0.61869 0.73053 -0.07210 0.01922  0.05204  196 MET   A CG  
1620 S SD  . MET   A 199 ? 0.73968 0.76302 0.85815 -0.08897 0.02608  0.06269  196 MET   A SD  
1621 C CE  . MET   A 199 ? 0.58868 0.61591 0.70177 -0.07932 0.02166  0.06786  196 MET   A CE  
1622 N N   . VAL   A 200 ? 0.71185 0.66005 0.83221 -0.02468 -0.02137 0.04321  197 VAL   A N   
1623 C CA  . VAL   A 200 ? 0.79834 0.70817 0.90299 -0.01394 -0.03719 0.04448  197 VAL   A CA  
1624 C C   . VAL   A 200 ? 0.88057 0.78597 0.99772 0.00048  -0.04336 0.03018  197 VAL   A C   
1625 O O   . VAL   A 200 ? 0.83447 0.70222 0.93640 0.00247  -0.05300 0.03012  197 VAL   A O   
1626 C CB  . VAL   A 200 ? 0.75608 0.66659 0.85773 -0.00208 -0.04663 0.04768  197 VAL   A CB  
1627 C CG1 . VAL   A 200 ? 0.82517 0.69525 0.91098 0.01259  -0.06581 0.04735  197 VAL   A CG1 
1628 C CG2 . VAL   A 200 ? 0.71118 0.62185 0.79617 -0.01658 -0.04101 0.06162  197 VAL   A CG2 
1629 N N   . THR   A 201 ? 0.79365 0.73642 0.93717 0.01009  -0.03781 0.01744  198 THR   A N   
1630 C CA  . THR   A 201 ? 0.76687 0.71217 0.92438 0.02526  -0.04250 0.00151  198 THR   A CA  
1631 C C   . THR   A 201 ? 0.80582 0.75972 0.96923 0.01660  -0.03219 -0.00512 198 THR   A C   
1632 O O   . THR   A 201 ? 0.85735 0.81109 1.02961 0.02797  -0.03535 -0.01890 198 THR   A O   
1633 C CB  . THR   A 201 ? 0.80698 0.79010 0.98970 0.04015  -0.04201 -0.01028 198 THR   A CB  
1634 O OG1 . THR   A 201 ? 0.83504 0.85607 1.03072 0.02896  -0.02656 -0.00948 198 THR   A OG1 
1635 C CG2 . THR   A 201 ? 0.72221 0.69687 0.90025 0.05083  -0.05468 -0.00568 198 THR   A CG2 
1636 N N   . ARG   A 202 ? 0.86466 0.82675 1.02343 -0.00219 -0.02075 0.00318  199 ARG   A N   
1637 C CA  . ARG   A 202 ? 0.91189 0.88453 1.07593 -0.01094 -0.01155 -0.00281 199 ARG   A CA  
1638 C C   . ARG   A 202 ? 0.82391 0.83089 1.00863 -0.00166 -0.00507 -0.01696 199 ARG   A C   
1639 O O   . ARG   A 202 ? 0.83336 0.84253 1.02145 -0.00130 -0.00210 -0.02672 199 ARG   A O   
1640 C CB  . ARG   A 202 ? 1.06955 1.00559 1.22003 -0.01310 -0.01871 -0.00503 199 ARG   A CB  
1641 C CG  . ARG   A 202 ? 1.12531 1.03222 1.25441 -0.03087 -0.01993 0.00926  199 ARG   A CG  
1642 C CD  . ARG   A 202 ? 1.03645 0.90444 1.14574 -0.02563 -0.03352 0.01743  199 ARG   A CD  
1643 N NE  . ARG   A 202 ? 1.06955 0.89799 1.16726 -0.01841 -0.04597 0.01155  199 ARG   A NE  
1644 C CZ  . ARG   A 202 ? 1.14135 0.96185 1.24523 0.00375  -0.05727 -0.00006 199 ARG   A CZ  
1645 N NH1 . ARG   A 202 ? 1.23118 1.08279 1.35411 0.01984  -0.05717 -0.00722 199 ARG   A NH1 
1646 N NH2 . ARG   A 202 ? 1.19385 0.97479 1.28503 0.00988  -0.06936 -0.00566 199 ARG   A NH2 
1647 N N   . ARG   A 203 ? 0.74196 0.77591 0.93927 0.00446  -0.00248 -0.01826 200 ARG   A N   
1648 C CA  . ARG   A 203 ? 0.77056 0.83840 0.98633 0.01102  0.00460  -0.03114 200 ARG   A CA  
1649 C C   . ARG   A 203 ? 0.73179 0.82705 0.95625 0.00834  0.00987  -0.02658 200 ARG   A C   
1650 O O   . ARG   A 203 ? 0.66316 0.75139 0.88439 0.01113  0.00330  -0.01908 200 ARG   A O   
1651 C CB  . ARG   A 203 ? 0.70875 0.77501 0.93466 0.02987  -0.00359 -0.04611 200 ARG   A CB  
1652 C CG  . ARG   A 203 ? 0.87453 0.98058 1.12214 0.03801  0.00239  -0.05888 200 ARG   A CG  
1653 C CD  . ARG   A 203 ? 1.01579 1.12330 1.27506 0.05705  -0.00480 -0.07696 200 ARG   A CD  
1654 N NE  . ARG   A 203 ? 1.16612 1.23498 1.41468 0.06894  -0.02188 -0.07487 200 ARG   A NE  
1655 C CZ  . ARG   A 203 ? 1.12161 1.18451 1.37295 0.08092  -0.03399 -0.07337 200 ARG   A CZ  
1656 N NH1 . ARG   A 203 ? 1.04751 1.14301 1.31466 0.08263  -0.03083 -0.07449 200 ARG   A NH1 
1657 N NH2 . ARG   A 203 ? 1.19829 1.21945 1.43450 0.09104  -0.05064 -0.07064 200 ARG   A NH2 
1658 N N   . ALA   A 204 ? 0.64204 0.76565 0.87482 0.00220  0.02107  -0.03082 201 ALA   A N   
1659 C CA  . ALA   A 204 ? 0.58280 0.73014 0.82213 -0.00218 0.02613  -0.02677 201 ALA   A CA  
1660 C C   . ALA   A 204 ? 0.50137 0.66040 0.75420 0.01036  0.01963  -0.03260 201 ALA   A C   
1661 O O   . ALA   A 204 ? 0.54711 0.71334 0.81174 0.02254  0.01645  -0.04577 201 ALA   A O   
1662 C CB  . ALA   A 204 ? 0.49419 0.66607 0.73782 -0.01011 0.03797  -0.03196 201 ALA   A CB  
1663 N N   . LEU   A 205 ? 0.43403 0.59618 0.68570 0.00809  0.01702  -0.02393 202 LEU   A N   
1664 C CA  . LEU   A 205 ? 0.39570 0.56822 0.65966 0.01997  0.00882  -0.02891 202 LEU   A CA  
1665 C C   . LEU   A 205 ? 0.45162 0.66189 0.73680 0.02139  0.01609  -0.04201 202 LEU   A C   
1666 O O   . LEU   A 205 ? 0.48984 0.71367 0.79147 0.03472  0.01098  -0.05513 202 LEU   A O   
1667 C CB  . LEU   A 205 ? 0.43823 0.60380 0.69317 0.01590  0.00433  -0.01628 202 LEU   A CB  
1668 C CG  . LEU   A 205 ? 0.55058 0.72251 0.81462 0.02799  -0.00679 -0.01948 202 LEU   A CG  
1669 C CD1 . LEU   A 205 ? 0.51582 0.66652 0.77874 0.04449  -0.02056 -0.02506 202 LEU   A CD1 
1670 C CD2 . LEU   A 205 ? 0.43386 0.59563 0.68401 0.02204  -0.01025 -0.00606 202 LEU   A CD2 
1671 N N   . PHE   A 206 ? 0.40492 0.63250 0.68948 0.00750  0.02772  -0.03924 203 PHE   A N   
1672 C CA  . PHE   A 206 ? 0.40196 0.66415 0.70268 0.00388  0.03658  -0.04990 203 PHE   A CA  
1673 C C   . PHE   A 206 ? 0.47319 0.73973 0.76554 -0.00815 0.04911  -0.05084 203 PHE   A C   
1674 O O   . PHE   A 206 ? 0.51382 0.78283 0.79683 -0.02149 0.05562  -0.04316 203 PHE   A O   
1675 C CB  . PHE   A 206 ? 0.39928 0.67603 0.70415 -0.00291 0.03689  -0.04480 203 PHE   A CB  
1676 C CG  . PHE   A 206 ? 0.42615 0.69548 0.73452 0.00759  0.02363  -0.04169 203 PHE   A CG  
1677 C CD1 . PHE   A 206 ? 0.46778 0.74839 0.79376 0.02320  0.01479  -0.05366 203 PHE   A CD1 
1678 C CD2 . PHE   A 206 ? 0.45637 0.70851 0.74991 0.00245  0.01949  -0.02779 203 PHE   A CD2 
1679 C CE1 . PHE   A 206 ? 0.48358 0.75516 0.81011 0.03351  0.00080  -0.05059 203 PHE   A CE1 
1680 C CE2 . PHE   A 206 ? 0.43364 0.67772 0.72693 0.01149  0.00716  -0.02462 203 PHE   A CE2 
1681 C CZ  . PHE   A 206 ? 0.48559 0.73797 0.79437 0.02697  -0.00277 -0.03543 203 PHE   A CZ  
1682 N N   . PRO   A 207 ? 0.42815 0.69369 0.72174 -0.00312 0.05162  -0.06055 204 PRO   A N   
1683 C CA  . PRO   A 207 ? 0.48548 0.75316 0.76810 -0.01412 0.06254  -0.06170 204 PRO   A CA  
1684 C C   . PRO   A 207 ? 0.62978 0.93007 0.92160 -0.02099 0.07423  -0.07225 204 PRO   A C   
1685 O O   . PRO   A 207 ? 0.60678 0.92176 0.90521 -0.01730 0.07995  -0.08607 204 PRO   A O   
1686 C CB  . PRO   A 207 ? 0.59269 0.84310 0.87192 -0.00484 0.05857  -0.06817 204 PRO   A CB  
1687 C CG  . PRO   A 207 ? 0.53389 0.78975 0.83031 0.01216  0.04982  -0.07878 204 PRO   A CG  
1688 C CD  . PRO   A 207 ? 0.47640 0.73340 0.77792 0.01362  0.04276  -0.07040 204 PRO   A CD  
1689 N N   . GLY   A 208 ? 0.45954 0.77147 0.75061 -0.03234 0.07840  -0.06616 205 GLY   A N   
1690 C CA  . GLY   A 208 ? 0.54015 0.88193 0.83791 -0.04248 0.09006  -0.07481 205 GLY   A CA  
1691 C C   . GLY   A 208 ? 0.49836 0.83482 0.77480 -0.05702 0.10044  -0.07179 205 GLY   A C   
1692 O O   . GLY   A 208 ? 0.59151 0.90207 0.84813 -0.06089 0.09765  -0.06073 205 GLY   A O   
1693 N N   . ASP   A 209 ? 0.61929 0.98202 0.89960 -0.06538 0.11248  -0.08260 206 ASP   A N   
1694 C CA  . ASP   A 209 ? 0.65142 1.00973 0.90841 -0.08036 0.12283  -0.08053 206 ASP   A CA  
1695 C C   . ASP   A 209 ? 0.55047 0.91760 0.79761 -0.09990 0.13076  -0.07503 206 ASP   A C   
1696 O O   . ASP   A 209 ? 0.72935 1.08298 0.95019 -0.11342 0.13632  -0.06879 206 ASP   A O   
1697 C CB  . ASP   A 209 ? 0.63245 1.01009 0.89400 -0.07730 0.13215  -0.09724 206 ASP   A CB  
1698 C CG  . ASP   A 209 ? 0.72794 1.14472 1.01952 -0.07133 0.13682  -0.11432 206 ASP   A CG  
1699 O OD1 . ASP   A 209 ? 0.74661 1.18798 1.04354 -0.08518 0.14582  -0.11669 206 ASP   A OD1 
1700 O OD2 . ASP   A 209 ? 0.94804 1.37071 1.25796 -0.05275 0.13073  -0.12599 206 ASP   A OD2 
1701 N N   . SER   A 210 ? 0.60518 0.99258 0.87112 -0.10200 0.13042  -0.07733 207 SER   A N   
1702 C CA  . SER   A 210 ? 0.61358 1.00604 0.87031 -0.12149 0.13624  -0.07141 207 SER   A CA  
1703 C C   . SER   A 210 ? 0.52734 0.91878 0.79795 -0.11720 0.12598  -0.06555 207 SER   A C   
1704 O O   . SER   A 210 ? 0.48048 0.87036 0.76765 -0.09971 0.11569  -0.06705 207 SER   A O   
1705 C CB  . SER   A 210 ? 0.60352 1.03346 0.87025 -0.13449 0.15148  -0.08538 207 SER   A CB  
1706 O OG  . SER   A 210 ? 0.55098 1.01580 0.85379 -0.12374 0.15020  -0.09964 207 SER   A OG  
1707 N N   . GLU   A 211 ? 0.48242 0.87215 0.74354 -0.13384 0.12821  -0.05867 208 GLU   A N   
1708 C CA  . GLU   A 211 ? 0.48944 0.87806 0.76188 -0.13088 0.11844  -0.05372 208 GLU   A CA  
1709 C C   . GLU   A 211 ? 0.44397 0.86956 0.75169 -0.12236 0.11758  -0.06804 208 GLU   A C   
1710 O O   . GLU   A 211 ? 0.51091 0.93407 0.83254 -0.10800 0.10562  -0.06697 208 GLU   A O   
1711 C CB  . GLU   A 211 ? 0.55351 0.93088 0.80703 -0.15132 0.12064  -0.04461 208 GLU   A CB  
1712 C CG  . GLU   A 211 ? 0.54365 0.88020 0.76322 -0.15537 0.11603  -0.02978 208 GLU   A CG  
1713 C CD  . GLU   A 211 ? 0.97644 1.29643 1.17845 -0.17114 0.11346  -0.02067 208 GLU   A CD  
1714 O OE1 . GLU   A 211 ? 0.92370 1.25265 1.14080 -0.17045 0.10799  -0.02136 208 GLU   A OE1 
1715 O OE2 . GLU   A 211 ? 1.24965 1.54565 1.42122 -0.18391 0.11582  -0.01308 208 GLU   A OE2 
1716 N N   . ILE   A 212 ? 0.46022 0.92114 0.78233 -0.13078 0.12983  -0.08228 209 ILE   A N   
1717 C CA  . ILE   A 212 ? 0.43880 0.93959 0.79763 -0.12134 0.12840  -0.09864 209 ILE   A CA  
1718 C C   . ILE   A 212 ? 0.50966 1.01221 0.88425 -0.09570 0.12072  -0.10751 209 ILE   A C   
1719 O O   . ILE   A 212 ? 0.51357 1.02960 0.91258 -0.07948 0.11003  -0.11485 209 ILE   A O   
1720 C CB  . ILE   A 212 ? 0.45920 1.00179 0.83031 -0.13950 0.14503  -0.11292 209 ILE   A CB  
1721 C CG1 . ILE   A 212 ? 0.53293 1.12108 0.94539 -0.13077 0.14220  -0.13082 209 ILE   A CG1 
1722 C CG2 . ILE   A 212 ? 0.47414 1.02375 0.83622 -0.14123 0.15785  -0.12095 209 ILE   A CG2 
1723 C CD1 . ILE   A 212 ? 0.56382 1.14867 0.98466 -0.13178 0.13032  -0.12439 209 ILE   A CD1 
1724 N N   . ASP   A 213 ? 0.42440 0.91060 0.78358 -0.09136 0.12452  -0.10691 210 ASP   A N   
1725 C CA  . ASP   A 213 ? 0.34557 0.82709 0.71597 -0.06793 0.11619  -0.11456 210 ASP   A CA  
1726 C C   . ASP   A 213 ? 0.48139 0.92709 0.84372 -0.05473 0.09978  -0.10079 210 ASP   A C   
1727 O O   . ASP   A 213 ? 0.45667 0.90065 0.83352 -0.03516 0.08842  -0.10640 210 ASP   A O   
1728 C CB  . ASP   A 213 ? 0.40353 0.87635 0.75810 -0.06863 0.12469  -0.11801 210 ASP   A CB  
1729 C CG  . ASP   A 213 ? 0.59330 1.05810 0.95759 -0.04531 0.11568  -0.12663 210 ASP   A CG  
1730 O OD1 . ASP   A 213 ? 0.50556 1.00004 0.89664 -0.03228 0.11474  -0.14482 210 ASP   A OD1 
1731 O OD2 . ASP   A 213 ? 0.53374 0.96243 0.87901 -0.04005 0.10897  -0.11595 210 ASP   A OD2 
1732 N N   . GLN   A 214 ? 0.38277 0.79893 0.72062 -0.06517 0.09811  -0.08319 211 GLN   A N   
1733 C CA  . GLN   A 214 ? 0.34150 0.72806 0.67172 -0.05539 0.08439  -0.07056 211 GLN   A CA  
1734 C C   . GLN   A 214 ? 0.41956 0.81931 0.76856 -0.04847 0.07488  -0.07286 211 GLN   A C   
1735 O O   . GLN   A 214 ? 0.41462 0.80091 0.76755 -0.03283 0.06232  -0.07085 211 GLN   A O   
1736 C CB  . GLN   A 214 ? 0.37775 0.73660 0.68085 -0.06813 0.08530  -0.05411 211 GLN   A CB  
1737 C CG  . GLN   A 214 ? 0.39772 0.72883 0.69184 -0.05984 0.07335  -0.04185 211 GLN   A CG  
1738 C CD  . GLN   A 214 ? 0.53315 0.84351 0.82047 -0.04898 0.06918  -0.04007 211 GLN   A CD  
1739 O OE1 . GLN   A 214 ? 0.44709 0.75691 0.72952 -0.05021 0.07539  -0.04486 211 GLN   A OE1 
1740 N NE2 . GLN   A 214 ? 0.47246 0.76468 0.75768 -0.03951 0.05868  -0.03319 211 GLN   A NE2 
1741 N N   . LEU   A 215 ? 0.44359 0.86842 0.80264 -0.06093 0.08024  -0.07703 212 LEU   A N   
1742 C CA  . LEU   A 215 ? 0.42568 0.86548 0.80323 -0.05556 0.07077  -0.08029 212 LEU   A CA  
1743 C C   . LEU   A 215 ? 0.49531 0.96019 0.90142 -0.03669 0.06431  -0.09702 212 LEU   A C   
1744 O O   . LEU   A 215 ? 0.43075 0.89028 0.84520 -0.02183 0.04973  -0.09683 212 LEU   A O   
1745 C CB  . LEU   A 215 ? 0.43534 0.89701 0.81708 -0.07580 0.07882  -0.08204 212 LEU   A CB  
1746 C CG  . LEU   A 215 ? 0.52916 1.00019 0.92330 -0.07547 0.06893  -0.08187 212 LEU   A CG  
1747 C CD1 . LEU   A 215 ? 0.39734 0.83007 0.76871 -0.07258 0.05851  -0.06479 212 LEU   A CD1 
1748 C CD2 . LEU   A 215 ? 0.54967 1.04631 0.95030 -0.09779 0.07889  -0.08671 212 LEU   A CD2 
1749 N N   . PHE   A 216 ? 0.39861 0.89026 0.81866 -0.03617 0.07423  -0.11227 213 PHE   A N   
1750 C CA  . PHE   A 216 ? 0.42991 0.94719 0.87865 -0.01608 0.06738  -0.13084 213 PHE   A CA  
1751 C C   . PHE   A 216 ? 0.44727 0.93128 0.88740 0.00562  0.05390  -0.12741 213 PHE   A C   
1752 O O   . PHE   A 216 ? 0.52509 1.01436 0.98230 0.02575  0.04000  -0.13660 213 PHE   A O   
1753 C CB  . PHE   A 216 ? 0.41122 0.96755 0.87649 -0.02134 0.08273  -0.14958 213 PHE   A CB  
1754 C CG  . PHE   A 216 ? 0.40112 0.99993 0.88374 -0.04018 0.09416  -0.15843 213 PHE   A CG  
1755 C CD1 . PHE   A 216 ? 0.51544 1.11444 0.99927 -0.04990 0.08882  -0.15023 213 PHE   A CD1 
1756 C CD2 . PHE   A 216 ? 0.41471 1.05372 0.91182 -0.04921 0.11057  -0.17565 213 PHE   A CD2 
1757 C CE1 . PHE   A 216 ? 0.59163 1.22847 1.09097 -0.06930 0.09909  -0.15848 213 PHE   A CE1 
1758 C CE2 . PHE   A 216 ? 0.42206 1.10058 0.93417 -0.06943 0.12210  -0.18375 213 PHE   A CE2 
1759 C CZ  . PHE   A 216 ? 0.49080 1.16630 1.00332 -0.07979 0.11585  -0.17461 213 PHE   A CZ  
1760 N N   . ARG   A 217 ? 0.35128 0.80007 0.76445 0.00165  0.05685  -0.11465 214 ARG   A N   
1761 C CA  . ARG   A 217 ? 0.42748 0.84065 0.82924 0.01849  0.04409  -0.10922 214 ARG   A CA  
1762 C C   . ARG   A 217 ? 0.46351 0.85317 0.85767 0.02471  0.02902  -0.09663 214 ARG   A C   
1763 O O   . ARG   A 217 ? 0.47651 0.84808 0.87100 0.04256  0.01444  -0.09767 214 ARG   A O   
1764 C CB  . ARG   A 217 ? 0.34597 0.72990 0.72179 0.01015  0.05112  -0.09871 214 ARG   A CB  
1765 C CG  . ARG   A 217 ? 0.52144 0.92047 0.90151 0.01020  0.06193  -0.11238 214 ARG   A CG  
1766 C CD  . ARG   A 217 ? 0.53229 0.90118 0.88635 0.00280  0.06662  -0.10219 214 ARG   A CD  
1767 N NE  . ARG   A 217 ? 0.61653 0.99918 0.97246 0.00283  0.07663  -0.11574 214 ARG   A NE  
1768 C CZ  . ARG   A 217 ? 0.72696 1.10380 1.08850 0.01893  0.07130  -0.12728 214 ARG   A CZ  
1769 N NH1 . ARG   A 217 ? 0.67594 1.03054 1.04028 0.03597  0.05541  -0.12616 214 ARG   A NH1 
1770 N NH2 . ARG   A 217 ? 0.67611 1.06752 1.03806 0.01773  0.08165  -0.14033 214 ARG   A NH2 
1771 N N   . ILE   A 218 ? 0.41083 0.79829 0.79572 0.01018  0.03178  -0.08481 215 ILE   A N   
1772 C CA  . ILE   A 218 ? 0.41785 0.78765 0.79591 0.01528  0.01842  -0.07453 215 ILE   A CA  
1773 C C   . ILE   A 218 ? 0.43216 0.82727 0.83562 0.02880  0.00723  -0.08758 215 ILE   A C   
1774 O O   . ILE   A 218 ? 0.45665 0.83354 0.85699 0.04420  -0.00884 -0.08511 215 ILE   A O   
1775 C CB  . ILE   A 218 ? 0.45013 0.81375 0.81319 -0.00285 0.02418  -0.06128 215 ILE   A CB  
1776 C CG1 . ILE   A 218 ? 0.37190 0.70812 0.70974 -0.01251 0.03172  -0.04879 215 ILE   A CG1 
1777 C CG2 . ILE   A 218 ? 0.48110 0.83188 0.83867 0.00223  0.01106  -0.05315 215 ILE   A CG2 
1778 C CD1 . ILE   A 218 ? 0.32048 0.65208 0.64412 -0.02942 0.03792  -0.03854 215 ILE   A CD1 
1779 N N   . PHE   A 219 ? 0.45086 0.88851 0.87917 0.02288  0.01515  -0.10213 216 PHE   A N   
1780 C CA  . PHE   A 219 ? 0.41281 0.88127 0.86991 0.03577  0.00453  -0.11737 216 PHE   A CA  
1781 C C   . PHE   A 219 ? 0.55189 1.01823 1.02083 0.06081  -0.00745 -0.13004 216 PHE   A C   
1782 O O   . PHE   A 219 ? 0.50164 0.97086 0.98256 0.07837  -0.02472 -0.13634 216 PHE   A O   
1783 C CB  . PHE   A 219 ? 0.37313 0.89185 0.85621 0.02201  0.01786  -0.13230 216 PHE   A CB  
1784 C CG  . PHE   A 219 ? 0.35885 0.88032 0.83258 -0.00148 0.02592  -0.12195 216 PHE   A CG  
1785 C CD1 . PHE   A 219 ? 0.29760 0.78111 0.74358 -0.00683 0.02074  -0.10223 216 PHE   A CD1 
1786 C CD2 . PHE   A 219 ? 0.37725 0.93954 0.86963 -0.01867 0.03865  -0.13294 216 PHE   A CD2 
1787 C CE1 . PHE   A 219 ? 0.40063 0.88434 0.83727 -0.02679 0.02670  -0.09402 216 PHE   A CE1 
1788 C CE2 . PHE   A 219 ? 0.36225 0.92255 0.84361 -0.04081 0.04478  -0.12340 216 PHE   A CE2 
1789 C CZ  . PHE   A 219 ? 0.43058 0.95037 0.88398 -0.04375 0.03799  -0.10415 216 PHE   A CZ  
1790 N N   . ARG   A 220 ? 0.48745 0.94718 0.95208 0.06357  0.00013  -0.13452 217 ARG   A N   
1791 C CA  . ARG   A 220 ? 0.49963 0.95626 0.97524 0.08788  -0.01144 -0.14847 217 ARG   A CA  
1792 C C   . ARG   A 220 ? 0.50215 0.90901 0.95511 0.10303  -0.03102 -0.13567 217 ARG   A C   
1793 O O   . ARG   A 220 ? 0.66590 1.06679 1.12769 0.12612  -0.04756 -0.14626 217 ARG   A O   
1794 C CB  . ARG   A 220 ? 0.58485 1.04336 1.05794 0.08567  0.00174  -0.15587 217 ARG   A CB  
1795 C CG  . ARG   A 220 ? 0.67899 1.19202 1.18359 0.08528  0.01380  -0.17980 217 ARG   A CG  
1796 C CD  . ARG   A 220 ? 0.77282 1.28416 1.27009 0.08266  0.02688  -0.18625 217 ARG   A CD  
1797 N NE  . ARG   A 220 ? 0.95014 1.41265 1.42500 0.09577  0.01580  -0.17827 217 ARG   A NE  
1798 C CZ  . ARG   A 220 ? 0.96881 1.41907 1.45113 0.12113  -0.00062 -0.18952 217 ARG   A CZ  
1799 N NH1 . ARG   A 220 ? 0.80600 1.29059 1.31948 0.13924  -0.00939 -0.21031 217 ARG   A NH1 
1800 N NH2 . ARG   A 220 ? 0.94661 1.34835 1.40437 0.12852  -0.00938 -0.18022 217 ARG   A NH2 
1801 N N   . THR   A 221 ? 0.44955 0.82020 0.87244 0.09038  -0.02976 -0.11360 218 THR   A N   
1802 C CA  . THR   A 221 ? 0.59653 0.91835 0.99314 0.09982  -0.04534 -0.09944 218 THR   A CA  
1803 C C   . THR   A 221 ? 0.57828 0.89324 0.96940 0.10214  -0.05831 -0.09100 218 THR   A C   
1804 O O   . THR   A 221 ? 0.57450 0.86629 0.95841 0.11945  -0.07744 -0.09033 218 THR   A O   
1805 C CB  . THR   A 221 ? 0.58713 0.87516 0.95411 0.08432  -0.03541 -0.08177 218 THR   A CB  
1806 O OG1 . THR   A 221 ? 0.55346 0.84841 0.92472 0.08184  -0.02386 -0.09016 218 THR   A OG1 
1807 C CG2 . THR   A 221 ? 0.70418 0.94247 1.04338 0.09177  -0.04975 -0.06813 218 THR   A CG2 
1808 N N   . LEU   A 222 ? 0.53081 0.86312 0.92298 0.08516  -0.04918 -0.08467 219 LEU   A N   
1809 C CA  . LEU   A 222 ? 0.51891 0.84423 0.90329 0.08514  -0.06007 -0.07619 219 LEU   A CA  
1810 C C   . LEU   A 222 ? 0.49976 0.86735 0.91519 0.09082  -0.06598 -0.09184 219 LEU   A C   
1811 O O   . LEU   A 222 ? 0.54841 0.91397 0.95978 0.09124  -0.07595 -0.08696 219 LEU   A O   
1812 C CB  . LEU   A 222 ? 0.50923 0.82336 0.87308 0.06375  -0.04830 -0.05956 219 LEU   A CB  
1813 C CG  . LEU   A 222 ? 0.45454 0.73103 0.78918 0.05634  -0.04216 -0.04431 219 LEU   A CG  
1814 C CD1 . LEU   A 222 ? 0.48050 0.75467 0.80106 0.03689  -0.03041 -0.03220 219 LEU   A CD1 
1815 C CD2 . LEU   A 222 ? 0.65164 0.88776 0.96303 0.06800  -0.05781 -0.03464 219 LEU   A CD2 
1816 N N   . GLY   A 223 ? 0.43647 0.84395 0.88302 0.09466  -0.05988 -0.11140 220 GLY   A N   
1817 C CA  . GLY   A 223 ? 0.36334 0.81761 0.84334 0.09778  -0.06358 -0.12839 220 GLY   A CA  
1818 C C   . GLY   A 223 ? 0.34070 0.82349 0.82812 0.07255  -0.04675 -0.12691 220 GLY   A C   
1819 O O   . GLY   A 223 ? 0.40010 0.85871 0.86215 0.05625  -0.03976 -0.10930 220 GLY   A O   
1820 N N   . THR   A 224 ? 0.34417 0.87802 0.86572 0.06881  -0.04033 -0.14591 221 THR   A N   
1821 C CA  . THR   A 224 ? 0.42341 0.98384 0.95174 0.04347  -0.02574 -0.14534 221 THR   A CA  
1822 C C   . THR   A 224 ? 0.34866 0.89960 0.86952 0.04029  -0.03779 -0.13649 221 THR   A C   
1823 O O   . THR   A 224 ? 0.37228 0.93942 0.91180 0.05549  -0.05453 -0.14687 221 THR   A O   
1824 C CB  . THR   A 224 ? 0.31049 0.93063 0.87849 0.03960  -0.01672 -0.16924 221 THR   A CB  
1825 O OG1 . THR   A 224 ? 0.42562 1.05447 0.99906 0.04391  -0.00565 -0.17864 221 THR   A OG1 
1826 C CG2 . THR   A 224 ? 0.42057 1.06355 0.99122 0.00984  -0.00074 -0.16726 221 THR   A CG2 
1827 N N   . PRO   A 225 ? 0.40222 0.92769 0.89638 0.02221  -0.03102 -0.11878 222 PRO   A N   
1828 C CA  . PRO   A 225 ? 0.47345 0.98599 0.95711 0.02073  -0.04323 -0.11040 222 PRO   A CA  
1829 C C   . PRO   A 225 ? 0.45195 1.00724 0.96317 0.00964  -0.04293 -0.12350 222 PRO   A C   
1830 O O   . PRO   A 225 ? 0.46093 1.05080 0.99163 -0.00585 -0.02798 -0.13402 222 PRO   A O   
1831 C CB  . PRO   A 225 ? 0.46803 0.94349 0.91653 0.00461  -0.03373 -0.09009 222 PRO   A CB  
1832 C CG  . PRO   A 225 ? 0.50238 0.98834 0.95239 -0.01064 -0.01382 -0.09185 222 PRO   A CG  
1833 C CD  . PRO   A 225 ? 0.31706 0.82342 0.78847 0.00381  -0.01314 -0.10651 222 PRO   A CD  
1834 N N   . ASP   A 226 ? 0.45610 1.00848 0.96754 0.01669  -0.05978 -0.12293 223 ASP   A N   
1835 C CA  . ASP   A 226 ? 0.39287 0.98225 0.92829 0.00537  -0.06190 -0.13435 223 ASP   A CA  
1836 C C   . ASP   A 226 ? 0.42181 0.98374 0.93242 -0.00257 -0.06958 -0.12065 223 ASP   A C   
1837 O O   . ASP   A 226 ? 0.42646 0.94424 0.90220 -0.00132 -0.07001 -0.10279 223 ASP   A O   
1838 C CB  . ASP   A 226 ? 0.32229 0.94931 0.89379 0.02539  -0.07795 -0.15511 223 ASP   A CB  
1839 C CG  . ASP   A 226 ? 0.44756 1.04274 1.00388 0.05266  -0.10142 -0.14983 223 ASP   A CG  
1840 O OD1 . ASP   A 226 ? 0.58847 1.13420 1.10669 0.05454  -0.10326 -0.13011 223 ASP   A OD1 
1841 O OD2 . ASP   A 226 ? 0.59918 1.21910 1.18117 0.07203  -0.11841 -0.16593 223 ASP   A OD2 
1842 N N   . GLU   A 227 ? 0.34760 0.93692 0.87656 -0.01098 -0.07558 -0.13005 224 GLU   A N   
1843 C CA  . GLU   A 227 ? 0.40335 0.96832 0.90925 -0.01982 -0.08236 -0.11893 224 GLU   A CA  
1844 C C   . GLU   A 227 ? 0.50614 1.03698 0.98899 0.00165  -0.10188 -0.10975 224 GLU   A C   
1845 O O   . GLU   A 227 ? 0.52462 1.02202 0.97664 -0.00320 -0.10434 -0.09573 224 GLU   A O   
1846 C CB  . GLU   A 227 ? 0.34894 0.95223 0.88142 -0.03346 -0.08585 -0.13285 224 GLU   A CB  
1847 C CG  . GLU   A 227 ? 0.45906 1.08147 0.99911 -0.06323 -0.06557 -0.13547 224 GLU   A CG  
1848 C CD  . GLU   A 227 ? 0.61769 1.19697 1.11916 -0.08009 -0.05728 -0.11674 224 GLU   A CD  
1849 O OE1 . GLU   A 227 ? 0.63135 1.17603 1.10673 -0.07184 -0.06874 -0.10544 224 GLU   A OE1 
1850 O OE2 . GLU   A 227 ? 0.58029 1.16004 1.07649 -0.10112 -0.03973 -0.11389 224 GLU   A OE2 
1851 N N   . VAL   A 228 ? 0.46264 0.99999 0.95798 0.02539  -0.11617 -0.11771 225 VAL   A N   
1852 C CA  . VAL   A 228 ? 0.51462 1.01649 0.98419 0.04495  -0.13566 -0.10840 225 VAL   A CA  
1853 C C   . VAL   A 228 ? 0.51407 0.96773 0.94484 0.04580  -0.12830 -0.08858 225 VAL   A C   
1854 O O   . VAL   A 228 ? 0.55956 0.97938 0.95758 0.04392  -0.13223 -0.07433 225 VAL   A O   
1855 C CB  . VAL   A 228 ? 0.61117 1.12955 1.10263 0.07087  -0.15487 -0.12261 225 VAL   A CB  
1856 C CG1 . VAL   A 228 ? 0.63621 1.10918 1.09319 0.08993  -0.17411 -0.11013 225 VAL   A CG1 
1857 C CG2 . VAL   A 228 ? 0.43582 1.00327 0.96560 0.07079  -0.16489 -0.14288 225 VAL   A CG2 
1858 N N   . VAL   A 229 ? 0.52248 0.97410 0.95685 0.04830  -0.11732 -0.08847 226 VAL   A N   
1859 C CA  . VAL   A 229 ? 0.57232 0.98096 0.97255 0.04845  -0.11056 -0.07103 226 VAL   A CA  
1860 C C   . VAL   A 229 ? 0.60022 0.99726 0.98301 0.02643  -0.09274 -0.05975 226 VAL   A C   
1861 O O   . VAL   A 229 ? 0.59628 0.95841 0.94879 0.02482  -0.08850 -0.04484 226 VAL   A O   
1862 C CB  . VAL   A 229 ? 0.50299 0.91137 0.91189 0.05867  -0.10599 -0.07529 226 VAL   A CB  
1863 C CG1 . VAL   A 229 ? 0.70059 1.12442 1.13108 0.08191  -0.12469 -0.08994 226 VAL   A CG1 
1864 C CG2 . VAL   A 229 ? 0.64125 1.07813 1.07036 0.04288  -0.08536 -0.08258 226 VAL   A CG2 
1865 N N   . TRP   A 230 ? 0.50757 0.93238 0.90797 0.00923  -0.08286 -0.06688 227 TRP   A N   
1866 C CA  . TRP   A 230 ? 0.48691 0.89917 0.87063 -0.01091 -0.06719 -0.05735 227 TRP   A CA  
1867 C C   . TRP   A 230 ? 0.50294 0.93904 0.90063 -0.02736 -0.06567 -0.06482 227 TRP   A C   
1868 O O   . TRP   A 230 ? 0.43595 0.90222 0.85636 -0.03987 -0.05537 -0.07484 227 TRP   A O   
1869 C CB  . TRP   A 230 ? 0.44790 0.86227 0.83432 -0.01757 -0.05031 -0.05668 227 TRP   A CB  
1870 C CG  . TRP   A 230 ? 0.51535 0.91177 0.88109 -0.03556 -0.03639 -0.04619 227 TRP   A CG  
1871 C CD1 . TRP   A 230 ? 0.56641 0.94574 0.91307 -0.04548 -0.03743 -0.03843 227 TRP   A CD1 
1872 C CD2 . TRP   A 230 ? 0.45700 0.84945 0.81808 -0.04410 -0.02103 -0.04324 227 TRP   A CD2 
1873 N NE1 . TRP   A 230 ? 0.56095 0.92543 0.89191 -0.05867 -0.02457 -0.03106 227 TRP   A NE1 
1874 C CE2 . TRP   A 230 ? 0.46270 0.83478 0.80157 -0.05844 -0.01444 -0.03342 227 TRP   A CE2 
1875 C CE3 . TRP   A 230 ? 0.46418 0.86756 0.83677 -0.04014 -0.01314 -0.04873 227 TRP   A CE3 
1876 C CZ2 . TRP   A 230 ? 0.48937 0.85119 0.81676 -0.06866 -0.00123 -0.02838 227 TRP   A CZ2 
1877 C CZ3 . TRP   A 230 ? 0.47463 0.86864 0.83546 -0.05143 0.00108  -0.04363 227 TRP   A CZ3 
1878 C CH2 . TRP   A 230 ? 0.56403 0.93718 0.90220 -0.06546 0.00648  -0.03324 227 TRP   A CH2 
1879 N N   . PRO   A 231 ? 0.55237 0.97504 0.93545 -0.02903 -0.07544 -0.06042 228 PRO   A N   
1880 C CA  . PRO   A 231 ? 0.48801 0.93034 0.88299 -0.04523 -0.07589 -0.06781 228 PRO   A CA  
1881 C C   . PRO   A 231 ? 0.48955 0.92771 0.87732 -0.06786 -0.05871 -0.06375 228 PRO   A C   
1882 O O   . PRO   A 231 ? 0.54393 0.95004 0.90380 -0.07143 -0.05239 -0.05106 228 PRO   A O   
1883 C CB  . PRO   A 231 ? 0.57300 0.99137 0.94497 -0.04011 -0.08977 -0.06128 228 PRO   A CB  
1884 C CG  . PRO   A 231 ? 0.51238 0.91065 0.87006 -0.01817 -0.10006 -0.05502 228 PRO   A CG  
1885 C CD  . PRO   A 231 ? 0.57290 0.96281 0.92785 -0.01602 -0.08733 -0.04968 228 PRO   A CD  
1886 N N   . GLY   A 232 ? 0.56540 1.03664 0.97809 -0.08340 -0.05152 -0.07518 229 GLY   A N   
1887 C CA  . GLY   A 232 ? 0.53949 1.00637 0.94384 -0.10690 -0.03619 -0.07184 229 GLY   A CA  
1888 C C   . GLY   A 232 ? 0.49417 0.96969 0.90368 -0.11118 -0.02018 -0.07236 229 GLY   A C   
1889 O O   . GLY   A 232 ? 0.62319 1.09242 1.02213 -0.13109 -0.00742 -0.06879 229 GLY   A O   
1890 N N   . VAL   A 233 ? 0.47873 0.96601 0.90185 -0.09310 -0.02127 -0.07680 230 VAL   A N   
1891 C CA  . VAL   A 233 ? 0.47607 0.96978 0.90221 -0.09575 -0.00653 -0.07781 230 VAL   A CA  
1892 C C   . VAL   A 233 ? 0.57158 1.10564 1.02248 -0.11460 0.00574  -0.09129 230 VAL   A C   
1893 O O   . VAL   A 233 ? 0.39775 0.93047 0.84052 -0.12858 0.02128  -0.08906 230 VAL   A O   
1894 C CB  . VAL   A 233 ? 0.46736 0.96241 0.90202 -0.07117 -0.01239 -0.08073 230 VAL   A CB  
1895 C CG1 . VAL   A 233 ? 0.36913 0.90227 0.83837 -0.05834 -0.02336 -0.09787 230 VAL   A CG1 
1896 C CG2 . VAL   A 233 ? 0.41361 0.90937 0.84665 -0.07326 0.00227  -0.08075 230 VAL   A CG2 
1897 N N   . THR   A 234 ? 0.45076 1.02195 0.93125 -0.11640 -0.00078 -0.10578 231 THR   A N   
1898 C CA  . THR   A 234 ? 0.46741 1.08293 0.97448 -0.13591 0.01176  -0.12050 231 THR   A CA  
1899 C C   . THR   A 234 ? 0.48492 1.08826 0.97339 -0.16703 0.02225  -0.11367 231 THR   A C   
1900 O O   . THR   A 234 ? 0.57719 1.21041 1.07918 -0.18835 0.03655  -0.12263 231 THR   A O   
1901 C CB  . THR   A 234 ? 0.54885 1.21072 1.09556 -0.12861 0.00053  -0.13955 231 THR   A CB  
1902 O OG1 . THR   A 234 ? 0.49248 1.13930 1.03127 -0.12891 -0.01475 -0.13523 231 THR   A OG1 
1903 C CG2 . THR   A 234 ? 0.49136 1.16683 1.05747 -0.09766 -0.00996 -0.14859 231 THR   A CG2 
1904 N N   . SER   A 235 ? 0.52077 1.08043 0.97745 -0.17038 0.01544  -0.09860 232 SER   A N   
1905 C CA  . SER   A 235 ? 0.64755 1.18700 1.08174 -0.19788 0.02236  -0.09119 232 SER   A CA  
1906 C C   . SER   A 235 ? 0.66781 1.16662 1.06602 -0.20348 0.03217  -0.07593 232 SER   A C   
1907 O O   . SER   A 235 ? 0.64988 1.12465 1.02403 -0.22491 0.03681  -0.06842 232 SER   A O   
1908 C CB  . SER   A 235 ? 0.58783 1.10549 1.01023 -0.19822 0.00700  -0.08674 232 SER   A CB  
1909 O OG  . SER   A 235 ? 0.62840 1.18390 1.08352 -0.19423 -0.00328 -0.10144 232 SER   A OG  
1910 N N   . MET   A 236 ? 0.52230 1.01158 0.91555 -0.18485 0.03428  -0.07161 233 MET   A N   
1911 C CA  . MET   A 236 ? 0.57395 1.02586 0.93442 -0.18799 0.04165  -0.05802 233 MET   A CA  
1912 C C   . MET   A 236 ? 0.61565 1.07957 0.97293 -0.21049 0.05913  -0.06069 233 MET   A C   
1913 O O   . MET   A 236 ? 0.65041 1.15719 1.03560 -0.21640 0.06765  -0.07446 233 MET   A O   
1914 C CB  . MET   A 236 ? 0.57035 1.01074 0.92810 -0.16288 0.03854  -0.05373 233 MET   A CB  
1915 C CG  . MET   A 236 ? 0.60478 1.03283 0.96260 -0.14223 0.02225  -0.05064 233 MET   A CG  
1916 S SD  . MET   A 236 ? 0.71654 1.11814 1.05972 -0.11843 0.01889  -0.04119 233 MET   A SD  
1917 C CE  . MET   A 236 ? 0.66187 1.02292 0.96802 -0.12978 0.02565  -0.02684 233 MET   A CE  
1918 N N   . PRO   A 237 ? 0.66313 1.08993 0.98556 -0.22318 0.06437  -0.04832 234 PRO   A N   
1919 C CA  . PRO   A 237 ? 0.75246 1.18548 1.06506 -0.24869 0.08028  -0.04940 234 PRO   A CA  
1920 C C   . PRO   A 237 ? 0.54961 1.01382 0.87900 -0.24447 0.09333  -0.05833 234 PRO   A C   
1921 O O   . PRO   A 237 ? 0.67056 1.16566 1.01108 -0.26415 0.10688  -0.06767 234 PRO   A O   
1922 C CB  . PRO   A 237 ? 0.70964 1.08887 0.97797 -0.25490 0.07868  -0.03304 234 PRO   A CB  
1923 C CG  . PRO   A 237 ? 0.73996 1.09157 0.99940 -0.24056 0.06209  -0.02635 234 PRO   A CG  
1924 C CD  . PRO   A 237 ? 0.60912 0.98697 0.89868 -0.21609 0.05508  -0.03373 234 PRO   A CD  
1925 N N   . ASP   A 238 ? 0.59358 1.05092 0.92451 -0.22029 0.09003  -0.05643 235 ASP   A N   
1926 C CA  . ASP   A 238 ? 0.61531 1.09765 0.95947 -0.21451 0.10121  -0.06515 235 ASP   A CA  
1927 C C   . ASP   A 238 ? 0.58947 1.11634 0.97539 -0.19719 0.09787  -0.08181 235 ASP   A C   
1928 O O   . ASP   A 238 ? 0.56574 1.11384 0.96522 -0.18812 0.10505  -0.09101 235 ASP   A O   
1929 C CB  . ASP   A 238 ? 0.58896 1.03752 0.91018 -0.19931 0.09959  -0.05465 235 ASP   A CB  
1930 C CG  . ASP   A 238 ? 0.82102 1.22904 1.10184 -0.21500 0.10323  -0.04062 235 ASP   A CG  
1931 O OD1 . ASP   A 238 ? 0.88264 1.29232 1.15170 -0.24010 0.11208  -0.04050 235 ASP   A OD1 
1932 O OD2 . ASP   A 238 ? 0.91036 1.28457 1.17061 -0.20255 0.09674  -0.03008 235 ASP   A OD2 
1933 N N   . TYR   A 239 ? 0.58174 1.12219 0.98744 -0.19127 0.08600  -0.08667 236 TYR   A N   
1934 C CA  . TYR   A 239 ? 0.57190 1.15436 1.01705 -0.17394 0.08046  -0.10351 236 TYR   A CA  
1935 C C   . TYR   A 239 ? 0.44528 1.07084 0.91225 -0.18845 0.09249  -0.11929 236 TYR   A C   
1936 O O   . TYR   A 239 ? 0.54957 1.17222 1.00554 -0.21123 0.09793  -0.11702 236 TYR   A O   
1937 C CB  . TYR   A 239 ? 0.57233 1.15176 1.02758 -0.16180 0.06206  -0.10317 236 TYR   A CB  
1938 C CG  . TYR   A 239 ? 0.56072 1.18006 1.05479 -0.14151 0.05293  -0.12049 236 TYR   A CG  
1939 C CD1 . TYR   A 239 ? 0.55956 1.16697 1.05580 -0.11305 0.04213  -0.11988 236 TYR   A CD1 
1940 C CD2 . TYR   A 239 ? 0.50021 1.16691 1.02709 -0.15060 0.05416  -0.13761 236 TYR   A CD2 
1941 C CE1 . TYR   A 239 ? 0.42066 1.06005 0.94963 -0.09273 0.03139  -0.13578 236 TYR   A CE1 
1942 C CE2 . TYR   A 239 ? 0.50792 1.20449 1.06570 -0.12845 0.04336  -0.15298 236 TYR   A CE2 
1943 C CZ  . TYR   A 239 ? 0.49639 1.18554 1.06021 -0.10012 0.03178  -0.15399 236 TYR   A CZ  
1944 O OH  . TYR   A 239 ? 0.60853 1.32706 1.20341 -0.07728 0.01901  -0.17036 236 TYR   A OH  
1945 N N   . LYS   A 240 ? 0.51060 1.16376 0.99968 -0.17157 0.09456  -0.13316 237 LYS   A N   
1946 C CA  . LYS   A 240 ? 0.53795 1.22474 1.04278 -0.17779 0.10337  -0.14810 237 LYS   A CA  
1947 C C   . LYS   A 240 ? 0.59892 1.31989 1.14125 -0.15416 0.09054  -0.16503 237 LYS   A C   
1948 O O   . LYS   A 240 ? 0.48815 1.20845 1.04207 -0.12877 0.08056  -0.16821 237 LYS   A O   
1949 C CB  . LYS   A 240 ? 0.64869 1.33863 1.14250 -0.18084 0.11950  -0.15169 237 LYS   A CB  
1950 C CG  . LYS   A 240 ? 0.71177 1.38208 1.17200 -0.21040 0.13498  -0.14165 237 LYS   A CG  
1951 C CD  . LYS   A 240 ? 0.73384 1.35842 1.16091 -0.21838 0.13314  -0.12144 237 LYS   A CD  
1952 C CE  . LYS   A 240 ? 0.85173 1.45326 1.24218 -0.24535 0.14703  -0.11188 237 LYS   A CE  
1953 N NZ  . LYS   A 240 ? 0.92306 1.53856 1.30912 -0.24566 0.16106  -0.11998 237 LYS   A NZ  
1954 N N   . PRO   A 241 ? 0.56094 1.31059 1.12201 -0.16124 0.08934  -0.17635 238 PRO   A N   
1955 C CA  . PRO   A 241 ? 0.61285 1.39653 1.20930 -0.13764 0.07687  -0.19444 238 PRO   A CA  
1956 C C   . PRO   A 241 ? 0.62314 1.42788 1.23303 -0.12081 0.08250  -0.20898 238 PRO   A C   
1957 O O   . PRO   A 241 ? 0.58141 1.40524 1.21678 -0.09505 0.06923  -0.22258 238 PRO   A O   
1958 C CB  . PRO   A 241 ? 0.48194 1.29239 1.09184 -0.15497 0.07873  -0.20338 238 PRO   A CB  
1959 C CG  . PRO   A 241 ? 0.69147 1.47280 1.27265 -0.18365 0.08514  -0.18647 238 PRO   A CG  
1960 C CD  . PRO   A 241 ? 0.60055 1.35040 1.15073 -0.19062 0.09721  -0.17292 238 PRO   A CD  
1961 N N   . SER   A 242 ? 0.58212 1.38227 1.17410 -0.13394 0.10061  -0.20702 239 SER   A N   
1962 C CA  . SER   A 242 ? 0.52924 1.34866 1.13161 -0.11954 0.10704  -0.22152 239 SER   A CA  
1963 C C   . SER   A 242 ? 0.47031 1.26687 1.06798 -0.09616 0.09950  -0.21685 239 SER   A C   
1964 O O   . SER   A 242 ? 0.58323 1.39094 1.18704 -0.08330 0.10410  -0.22829 239 SER   A O   
1965 C CB  . SER   A 242 ? 0.66888 1.49248 1.25170 -0.14404 0.12930  -0.22170 239 SER   A CB  
1966 O OG  . SER   A 242 ? 0.79132 1.57503 1.33836 -0.16056 0.13661  -0.20110 239 SER   A OG  
1967 N N   . PHE   A 243 ? 0.41441 1.17996 1.00127 -0.09092 0.08826  -0.20128 240 PHE   A N   
1968 C CA  . PHE   A 243 ? 0.50145 1.24578 1.08514 -0.06905 0.08020  -0.19721 240 PHE   A CA  
1969 C C   . PHE   A 243 ? 0.50116 1.26568 1.11347 -0.03790 0.06564  -0.21518 240 PHE   A C   
1970 O O   . PHE   A 243 ? 0.57974 1.36142 1.21218 -0.02841 0.05215  -0.22338 240 PHE   A O   
1971 C CB  . PHE   A 243 ? 0.49078 1.20332 1.06144 -0.06854 0.06894  -0.17948 240 PHE   A CB  
1972 C CG  . PHE   A 243 ? 0.54910 1.23327 1.08757 -0.09382 0.08137  -0.16125 240 PHE   A CG  
1973 C CD1 . PHE   A 243 ? 0.52219 1.20320 1.04188 -0.11068 0.09979  -0.15964 240 PHE   A CD1 
1974 C CD2 . PHE   A 243 ? 0.59882 1.24564 1.11460 -0.09791 0.07204  -0.14292 240 PHE   A CD2 
1975 C CE1 . PHE   A 243 ? 0.52716 1.17830 1.01453 -0.13240 0.10889  -0.14278 240 PHE   A CE1 
1976 C CE2 . PHE   A 243 ? 0.57261 1.18544 1.05359 -0.11795 0.08076  -0.12561 240 PHE   A CE2 
1977 C CZ  . PHE   A 243 ? 0.60076 1.21787 1.06958 -0.13549 0.09892  -0.12610 240 PHE   A CZ  
1978 N N   . PRO   A 244 ? 0.46875 1.23041 1.08262 -0.02104 0.06677  -0.22232 241 PRO   A N   
1979 C CA  . PRO   A 244 ? 0.43293 1.20761 1.07104 0.01060  0.05045  -0.23936 241 PRO   A CA  
1980 C C   . PRO   A 244 ? 0.51783 1.27102 1.16004 0.03105  0.02674  -0.23225 241 PRO   A C   
1981 O O   . PRO   A 244 ? 0.46662 1.18979 1.09069 0.02500  0.02409  -0.21404 241 PRO   A O   
1982 C CB  . PRO   A 244 ? 0.47447 1.24106 1.10628 0.02104  0.05757  -0.24476 241 PRO   A CB  
1983 C CG  . PRO   A 244 ? 0.57748 1.34205 1.18674 -0.00841 0.08132  -0.23645 241 PRO   A CG  
1984 C CD  . PRO   A 244 ? 0.54183 1.28877 1.13461 -0.03045 0.08291  -0.21687 241 PRO   A CD  
1985 N N   . LYS   A 245 ? 0.39020 1.15680 1.05377 0.05565  0.00859  -0.24682 242 LYS   A N   
1986 C CA  . LYS   A 245 ? 0.40765 1.15317 1.07358 0.07764  -0.01688 -0.24173 242 LYS   A CA  
1987 C C   . LYS   A 245 ? 0.47383 1.19446 1.13732 0.10635  -0.03001 -0.24480 242 LYS   A C   
1988 O O   . LYS   A 245 ? 0.57413 1.30636 1.25140 0.12685  -0.03721 -0.26248 242 LYS   A O   
1989 C CB  . LYS   A 245 ? 0.35680 1.12695 1.04359 0.08746  -0.03143 -0.25487 242 LYS   A CB  
1990 C CG  . LYS   A 245 ? 0.34027 1.13333 1.03045 0.05978  -0.02076 -0.25252 242 LYS   A CG  
1991 C CD  . LYS   A 245 ? 0.38443 1.15099 1.05449 0.04326  -0.02097 -0.23074 242 LYS   A CD  
1992 C CE  . LYS   A 245 ? 0.38718 1.17214 1.05910 0.01660  -0.01260 -0.22879 242 LYS   A CE  
1993 N NZ  . LYS   A 245 ? 0.65584 1.41370 1.30699 0.00092  -0.01341 -0.20888 242 LYS   A NZ  
1994 N N   . TRP   A 246 ? 0.35166 1.01320 0.97468 0.10386  -0.03240 -0.22034 243 TRP   A N   
1995 C CA  . TRP   A 246 ? 0.45555 1.07191 1.05888 0.12653  -0.04612 -0.21530 243 TRP   A CA  
1996 C C   . TRP   A 246 ? 0.55870 1.13376 1.14251 0.14047  -0.07008 -0.20124 243 TRP   A C   
1997 O O   . TRP   A 246 ? 0.53579 1.09999 1.10585 0.12647  -0.07078 -0.18628 243 TRP   A O   
1998 C CB  . TRP   A 246 ? 0.43360 1.01187 1.00349 0.11278  -0.03132 -0.19828 243 TRP   A CB  
1999 C CG  . TRP   A 246 ? 0.56733 1.17612 1.14966 0.10414  -0.01083 -0.21204 243 TRP   A CG  
2000 C CD1 . TRP   A 246 ? 0.45987 1.08222 1.05775 0.12245  -0.01196 -0.23136 243 TRP   A CD1 
2001 C CD2 . TRP   A 246 ? 0.55469 1.18125 1.13149 0.07512  0.01333  -0.20747 243 TRP   A CD2 
2002 N NE1 . TRP   A 246 ? 0.55565 1.20590 1.15853 0.10603  0.01116  -0.23951 243 TRP   A NE1 
2003 C CE2 . TRP   A 246 ? 0.63497 1.28699 1.22385 0.07644  0.02676  -0.22440 243 TRP   A CE2 
2004 C CE3 . TRP   A 246 ? 0.52199 1.14324 1.08285 0.04863  0.02397  -0.19107 243 TRP   A CE3 
2005 C CZ2 . TRP   A 246 ? 0.54422 1.21563 1.12756 0.05105  0.05069  -0.22424 243 TRP   A CZ2 
2006 C CZ3 . TRP   A 246 ? 0.65437 1.29244 1.20983 0.02427  0.04642  -0.19080 243 TRP   A CZ3 
2007 C CH2 . TRP   A 246 ? 0.55617 1.21871 1.12182 0.02505  0.05973  -0.20672 243 TRP   A CH2 
2008 N N   . ALA   A 247 ? 0.51100 1.06100 1.09130 0.16809  -0.09014 -0.20632 244 ALA   A N   
2009 C CA  . ALA   A 247 ? 0.59197 1.09698 1.14829 0.18224  -0.11393 -0.19258 244 ALA   A CA  
2010 C C   . ALA   A 247 ? 0.49246 0.93501 1.00275 0.17381  -0.11145 -0.16666 244 ALA   A C   
2011 O O   . ALA   A 247 ? 0.65011 1.07779 1.15021 0.17024  -0.10038 -0.16480 244 ALA   A O   
2012 C CB  . ALA   A 247 ? 0.54232 1.04570 1.11354 0.21640  -0.13922 -0.21013 244 ALA   A CB  
2013 N N   . ARG   A 248 ? 0.54019 0.94816 1.02302 0.17005  -0.12159 -0.14752 245 ARG   A N   
2014 C CA  . ARG   A 248 ? 0.60108 0.95300 1.04111 0.16106  -0.11940 -0.12351 245 ARG   A CA  
2015 C C   . ARG   A 248 ? 0.67636 0.98720 1.10009 0.18120  -0.13410 -0.12387 245 ARG   A C   
2016 O O   . ARG   A 248 ? 0.77243 1.07492 1.20081 0.20503  -0.15674 -0.13284 245 ARG   A O   
2017 C CB  . ARG   A 248 ? 0.65089 0.97789 1.06587 0.15446  -0.12807 -0.10553 245 ARG   A CB  
2018 C CG  . ARG   A 248 ? 0.63821 0.91306 1.01040 0.14270  -0.12378 -0.08154 245 ARG   A CG  
2019 C CD  . ARG   A 248 ? 0.80336 1.05456 1.15026 0.13911  -0.13398 -0.06616 245 ARG   A CD  
2020 N NE  . ARG   A 248 ? 0.80371 1.01155 1.11200 0.12582  -0.12751 -0.04474 245 ARG   A NE  
2021 C CZ  . ARG   A 248 ? 0.80667 1.01771 1.10521 0.10459  -0.11056 -0.03378 245 ARG   A CZ  
2022 N NH1 . ARG   A 248 ? 0.71536 0.96516 1.03587 0.09306  -0.09863 -0.04028 245 ARG   A NH1 
2023 N NH2 . ARG   A 248 ? 0.80035 0.97450 1.06590 0.09446  -0.10595 -0.01646 245 ARG   A NH2 
2024 N N   . GLN   A 249 ? 0.71390 0.99765 1.11781 0.17184  -0.12246 -0.11459 246 GLN   A N   
2025 C CA  . GLN   A 249 ? 0.82578 1.06631 1.21127 0.18775  -0.13529 -0.11395 246 GLN   A CA  
2026 C C   . GLN   A 249 ? 0.87136 1.05363 1.21489 0.18721  -0.14936 -0.09189 246 GLN   A C   
2027 O O   . GLN   A 249 ? 0.80994 0.98120 1.13335 0.16816  -0.14086 -0.07392 246 GLN   A O   
2028 C CB  . GLN   A 249 ? 0.84428 1.07986 1.22558 0.17697  -0.11753 -0.11391 246 GLN   A CB  
2029 C CG  . GLN   A 249 ? 0.92042 1.20899 1.33854 0.17867  -0.10399 -0.13663 246 GLN   A CG  
2030 C CD  . GLN   A 249 ? 1.05855 1.33813 1.46863 0.16943  -0.08846 -0.13664 246 GLN   A CD  
2031 O OE1 . GLN   A 249 ? 1.15741 1.39217 1.53650 0.16163  -0.08817 -0.12009 246 GLN   A OE1 
2032 N NE2 . GLN   A 249 ? 1.10403 1.42755 1.54174 0.16942  -0.07524 -0.15587 246 GLN   A NE2 
2033 N N   . ASP   A 250 ? 0.90969 1.05386 1.23881 0.20845  -0.17138 -0.09399 247 ASP   A N   
2034 C CA  . ASP   A 250 ? 0.89758 0.98110 1.18215 0.20717  -0.18512 -0.07293 247 ASP   A CA  
2035 C C   . ASP   A 250 ? 0.93107 0.98403 1.18780 0.18460  -0.16842 -0.05529 247 ASP   A C   
2036 O O   . ASP   A 250 ? 1.05941 1.10939 1.32080 0.18359  -0.16025 -0.06129 247 ASP   A O   
2037 C CB  . ASP   A 250 ? 0.99037 1.03542 1.26345 0.23474  -0.21284 -0.07983 247 ASP   A CB  
2038 C CG  . ASP   A 250 ? 1.20797 1.19441 1.43545 0.23586  -0.23158 -0.05963 247 ASP   A CG  
2039 O OD1 . ASP   A 250 ? 1.27012 1.23243 1.46725 0.21276  -0.22000 -0.03824 247 ASP   A OD1 
2040 O OD2 . ASP   A 250 ? 1.33725 1.30190 1.55842 0.26017  -0.25834 -0.06578 247 ASP   A OD2 
2041 N N   . PHE   A 251 ? 0.88624 0.91840 1.11467 0.16667  -0.16351 -0.03470 248 PHE   A N   
2042 C CA  . PHE   A 251 ? 0.97677 0.98493 1.18100 0.14439  -0.14750 -0.01878 248 PHE   A CA  
2043 C C   . PHE   A 251 ? 1.09779 1.05176 1.27354 0.14858  -0.15765 -0.01278 248 PHE   A C   
2044 O O   . PHE   A 251 ? 1.09021 1.02739 1.25077 0.13105  -0.14447 -0.00317 248 PHE   A O   
2045 C CB  . PHE   A 251 ? 0.94416 0.94364 1.12486 0.12641  -0.14152 -0.00016 248 PHE   A CB  
2046 C CG  . PHE   A 251 ? 0.81006 0.85445 1.01132 0.11025  -0.12107 -0.00128 248 PHE   A CG  
2047 C CD1 . PHE   A 251 ? 0.82871 0.92171 1.06698 0.11643  -0.11729 -0.01773 248 PHE   A CD1 
2048 C CD2 . PHE   A 251 ? 0.77360 0.81120 0.95661 0.08867  -0.10609 0.01346  248 PHE   A CD2 
2049 C CE1 . PHE   A 251 ? 0.82605 0.95464 1.07916 0.10048  -0.09962 -0.01787 248 PHE   A CE1 
2050 C CE2 . PHE   A 251 ? 0.74491 0.81922 0.94446 0.07544  -0.08957 0.01214  248 PHE   A CE2 
2051 C CZ  . PHE   A 251 ? 0.85276 0.96986 1.08556 0.08092  -0.08670 -0.00273 248 PHE   A CZ  
2052 N N   . SER   A 252 ? 1.22068 1.14593 1.38840 0.17129  -0.18165 -0.01864 249 SER   A N   
2053 C CA  . SER   A 252 ? 1.24123 1.11449 1.38436 0.17713  -0.19263 -0.01607 249 SER   A CA  
2054 C C   . SER   A 252 ? 1.26942 1.16189 1.43720 0.18030  -0.18237 -0.03197 249 SER   A C   
2055 O O   . SER   A 252 ? 1.34756 1.20086 1.49503 0.17651  -0.18389 -0.02787 249 SER   A O   
2056 C CB  . SER   A 252 ? 1.36139 1.19900 1.49074 0.20375  -0.22325 -0.02057 249 SER   A CB  
2057 O OG  . SER   A 252 ? 1.63093 1.44561 1.73186 0.20034  -0.23380 -0.00482 249 SER   A OG  
2058 N N   . LYS   A 253 ? 1.15280 1.10393 1.36224 0.18600  -0.17187 -0.05016 250 LYS   A N   
2059 C CA  . LYS   A 253 ? 1.14610 1.12113 1.37851 0.18673  -0.15918 -0.06554 250 LYS   A CA  
2060 C C   . LYS   A 253 ? 1.08574 1.08933 1.32461 0.16059  -0.13204 -0.05904 250 LYS   A C   
2061 O O   . LYS   A 253 ? 1.16609 1.16998 1.40762 0.15468  -0.12137 -0.06391 250 LYS   A O   
2062 C CB  . LYS   A 253 ? 1.13075 1.15394 1.40442 0.20893  -0.16370 -0.09170 250 LYS   A CB  
2063 C CG  . LYS   A 253 ? 1.30796 1.30979 1.58100 0.23890  -0.19260 -0.10208 250 LYS   A CG  
2064 C CD  . LYS   A 253 ? 1.37710 1.42983 1.69436 0.26130  -0.19527 -0.13188 250 LYS   A CD  
2065 C CE  . LYS   A 253 ? 1.37528 1.49651 1.72788 0.25072  -0.17747 -0.13961 250 LYS   A CE  
2066 N NZ  . LYS   A 253 ? 1.23025 1.35484 1.57869 0.24968  -0.18700 -0.12977 250 LYS   A NZ  
2067 N N   . VAL   A 254 ? 0.98714 1.01313 1.22747 0.14580  -0.12198 -0.04881 251 VAL   A N   
2068 C CA  . VAL   A 254 ? 0.92299 0.97255 1.16704 0.12234  -0.09854 -0.04232 251 VAL   A CA  
2069 C C   . VAL   A 254 ? 0.94004 0.94895 1.15207 0.10510  -0.09364 -0.02477 251 VAL   A C   
2070 O O   . VAL   A 254 ? 0.98102 0.99326 1.19415 0.09396  -0.08052 -0.02570 251 VAL   A O   
2071 C CB  . VAL   A 254 ? 0.86759 0.94993 1.12154 0.11309  -0.09134 -0.03761 251 VAL   A CB  
2072 C CG1 . VAL   A 254 ? 0.73222 0.83421 0.98732 0.09044  -0.06942 -0.03094 251 VAL   A CG1 
2073 C CG2 . VAL   A 254 ? 0.86662 0.99228 1.15447 0.12798  -0.09559 -0.05623 251 VAL   A CG2 
2074 N N   . VAL   A 255 ? 0.98073 0.95189 1.16339 0.10190  -0.10401 -0.00908 252 VAL   A N   
2075 C CA  . VAL   A 255 ? 0.90636 0.83837 1.05757 0.08452  -0.10013 0.00720  252 VAL   A CA  
2076 C C   . VAL   A 255 ? 1.04516 0.92176 1.16731 0.09474  -0.12086 0.01277  252 VAL   A C   
2077 O O   . VAL   A 255 ? 1.09376 0.94355 1.18986 0.09183  -0.12986 0.02636  252 VAL   A O   
2078 C CB  . VAL   A 255 ? 0.87746 0.81682 1.01607 0.06499  -0.08905 0.02278  252 VAL   A CB  
2079 C CG1 . VAL   A 255 ? 0.89537 0.87263 1.05256 0.05037  -0.06810 0.02008  252 VAL   A CG1 
2080 C CG2 . VAL   A 255 ? 0.87220 0.82558 1.01442 0.07363  -0.09746 0.02361  252 VAL   A CG2 
2081 N N   . PRO   A 256 ? 1.05653 0.91236 1.17970 0.10685  -0.12964 0.00256  253 PRO   A N   
2082 C CA  . PRO   A 256 ? 1.09301 0.89063 1.18633 0.11833  -0.15206 0.00707  253 PRO   A CA  
2083 C C   . PRO   A 256 ? 1.15713 0.90729 1.20832 0.09659  -0.15139 0.02929  253 PRO   A C   
2084 O O   . PRO   A 256 ? 1.19828 0.90947 1.21973 0.10046  -0.16745 0.04018  253 PRO   A O   
2085 C CB  . PRO   A 256 ? 1.15673 0.94571 1.26108 0.13060  -0.15618 -0.00894 253 PRO   A CB  
2086 C CG  . PRO   A 256 ? 1.06694 0.91892 1.21387 0.13610  -0.14182 -0.02684 253 PRO   A CG  
2087 C CD  . PRO   A 256 ? 1.02947 0.91618 1.18247 0.11412  -0.12151 -0.01614 253 PRO   A CD  
2088 N N   . PRO   A 257 ? 1.09574 0.84723 1.14170 0.07308  -0.13374 0.03635  254 PRO   A N   
2089 C CA  . PRO   A 257 ? 1.12789 0.83485 1.13411 0.05124  -0.13303 0.05598  254 PRO   A CA  
2090 C C   . PRO   A 257 ? 1.21830 0.92947 1.20781 0.03964  -0.12917 0.07107  254 PRO   A C   
2091 O O   . PRO   A 257 ? 1.19817 0.87006 1.15095 0.02303  -0.13065 0.08733  254 PRO   A O   
2092 C CB  . PRO   A 257 ? 1.09271 0.81449 1.10712 0.03033  -0.11358 0.05581  254 PRO   A CB  
2093 C CG  . PRO   A 257 ? 1.09964 0.85550 1.14933 0.04498  -0.10996 0.03609  254 PRO   A CG  
2094 C CD  . PRO   A 257 ? 1.00518 0.79609 1.07837 0.06428  -0.11445 0.02696  254 PRO   A CD  
2095 N N   . LEU   A 258 ? 1.15436 0.91073 1.16793 0.04680  -0.12417 0.06593  255 LEU   A N   
2096 C CA  . LEU   A 258 ? 1.09576 0.86103 1.09573 0.03495  -0.11836 0.07858  255 LEU   A CA  
2097 C C   . LEU   A 258 ? 1.15281 0.88242 1.12513 0.04732  -0.13955 0.08575  255 LEU   A C   
2098 O O   . LEU   A 258 ? 1.19822 0.92686 1.18225 0.07172  -0.15680 0.07493  255 LEU   A O   
2099 C CB  . LEU   A 258 ? 1.01733 0.84246 1.05268 0.03678  -0.10526 0.06990  255 LEU   A CB  
2100 C CG  . LEU   A 258 ? 1.03356 0.88033 1.06408 0.01608  -0.08800 0.07988  255 LEU   A CG  
2101 C CD1 . LEU   A 258 ? 0.88205 0.71515 0.89836 -0.00623 -0.07491 0.08781  255 LEU   A CD1 
2102 C CD2 . LEU   A 258 ? 0.83417 0.73552 0.90047 0.01857  -0.07607 0.06937  255 LEU   A CD2 
2103 N N   . ASP   A 259 ? 1.15605 0.85745 1.09125 0.03055  -0.13845 0.10326  256 ASP   A N   
2104 C CA  . ASP   A 259 ? 1.22616 0.89058 1.12843 0.03951  -0.15806 0.11240  256 ASP   A CA  
2105 C C   . ASP   A 259 ? 1.20800 0.91206 1.12826 0.04960  -0.15888 0.10797  256 ASP   A C   
2106 O O   . ASP   A 259 ? 1.01935 0.77669 0.97669 0.04923  -0.14457 0.09806  256 ASP   A O   
2107 C CB  . ASP   A 259 ? 1.31599 0.93618 1.16914 0.01520  -0.15477 0.13283  256 ASP   A CB  
2108 C CG  . ASP   A 259 ? 1.41558 1.07094 1.27324 -0.00996 -0.12926 0.13901  256 ASP   A CG  
2109 O OD1 . ASP   A 259 ? 1.40422 1.10331 1.29783 -0.01419 -0.11268 0.12924  256 ASP   A OD1 
2110 O OD2 . ASP   A 259 ? 1.49997 1.13898 1.32420 -0.02495 -0.12629 0.15302  256 ASP   A OD2 
2111 N N   . GLU   A 260 ? 1.29549 0.97075 1.18673 0.05802  -0.17669 0.11570  257 GLU   A N   
2112 C CA  . GLU   A 260 ? 1.26405 0.97365 1.17218 0.07026  -0.18150 0.10985  257 GLU   A CA  
2113 C C   . GLU   A 260 ? 1.17922 0.92255 1.08945 0.05017  -0.16039 0.11615  257 GLU   A C   
2114 O O   . GLU   A 260 ? 1.04778 0.83425 0.98557 0.05674  -0.15713 0.10747  257 GLU   A O   
2115 C CB  . GLU   A 260 ? 1.21456 0.88186 1.08866 0.08556  -0.20823 0.11610  257 GLU   A CB  
2116 C CG  . GLU   A 260 ? 1.58966 1.21809 1.41075 0.06677  -0.20765 0.13694  257 GLU   A CG  
2117 C CD  . GLU   A 260 ? 1.72567 1.37813 1.54464 0.06883  -0.20907 0.13838  257 GLU   A CD  
2118 O OE1 . GLU   A 260 ? 1.60732 1.31526 1.46873 0.07429  -0.20018 0.12554  257 GLU   A OE1 
2119 O OE2 . GLU   A 260 ? 1.67410 1.28813 1.44697 0.06440  -0.21949 0.15235  257 GLU   A OE2 
2120 N N   . ASP   A 261 ? 1.16472 0.89005 1.04692 0.02562  -0.14613 0.13006  258 ASP   A N   
2121 C CA  . ASP   A 261 ? 0.99613 0.75686 0.88384 0.00783  -0.12531 0.13337  258 ASP   A CA  
2122 C C   . ASP   A 261 ? 1.01521 0.82498 0.94739 0.00462  -0.10724 0.12119  258 ASP   A C   
2123 O O   . ASP   A 261 ? 0.83373 0.68407 0.78645 0.00233  -0.09664 0.11636  258 ASP   A O   
2124 C CB  . ASP   A 261 ? 1.12924 0.86067 0.97609 -0.01754 -0.11477 0.14977  258 ASP   A CB  
2125 C CG  . ASP   A 261 ? 1.36184 1.05287 1.16107 -0.01841 -0.12859 0.16319  258 ASP   A CG  
2126 O OD1 . ASP   A 261 ? 1.42356 1.11035 1.22276 0.00203  -0.14744 0.15940  258 ASP   A OD1 
2127 O OD2 . ASP   A 261 ? 1.27105 0.93542 1.03229 -0.04018 -0.12058 0.17713  258 ASP   A OD2 
2128 N N   . GLY   A 262 ? 0.96078 0.76492 0.90598 0.00454  -0.10450 0.11605  259 GLY   A N   
2129 C CA  . GLY   A 262 ? 0.90337 0.75062 0.88744 0.00221  -0.08890 0.10459  259 GLY   A CA  
2130 C C   . GLY   A 262 ? 0.79615 0.67949 0.81673 0.02131  -0.09403 0.08953  259 GLY   A C   
2131 O O   . GLY   A 262 ? 0.70897 0.63368 0.75558 0.01756  -0.08111 0.08295  259 GLY   A O   
2132 N N   . ARG   A 263 ? 0.81922 0.68728 0.84182 0.04172  -0.11336 0.08332  260 ARG   A N   
2133 C CA  . ARG   A 263 ? 0.83989 0.74555 0.89886 0.05932  -0.11838 0.06744  260 ARG   A CA  
2134 C C   . ARG   A 263 ? 0.78186 0.71496 0.84646 0.05828  -0.11685 0.06799  260 ARG   A C   
2135 O O   . ARG   A 263 ? 0.74255 0.71809 0.83989 0.06145  -0.11043 0.05666  260 ARG   A O   
2136 C CB  . ARG   A 263 ? 0.91934 0.80311 0.97846 0.08288  -0.14138 0.05962  260 ARG   A CB  
2137 C CG  . ARG   A 263 ? 0.91153 0.76571 0.96546 0.08693  -0.14559 0.05683  260 ARG   A CG  
2138 C CD  . ARG   A 263 ? 1.11961 0.96192 1.18238 0.11435  -0.16853 0.04412  260 ARG   A CD  
2139 N NE  . ARG   A 263 ? 1.15315 0.97335 1.19479 0.12627  -0.18903 0.04948  260 ARG   A NE  
2140 C CZ  . ARG   A 263 ? 1.21187 0.97390 1.21107 0.12891  -0.20625 0.06179  260 ARG   A CZ  
2141 N NH1 . ARG   A 263 ? 1.33458 1.05343 1.30789 0.11938  -0.20541 0.07024  260 ARG   A NH1 
2142 N NH2 . ARG   A 263 ? 1.23061 0.97559 1.21103 0.14060  -0.22543 0.06585  260 ARG   A NH2 
2143 N N   . SER   A 264 ? 0.80183 0.71014 0.83310 0.05292  -0.12266 0.08088  261 SER   A N   
2144 C CA  . SER   A 264 ? 0.79161 0.72321 0.82490 0.05134  -0.12155 0.08143  261 SER   A CA  
2145 C C   . SER   A 264 ? 0.72190 0.68691 0.76964 0.03457  -0.09944 0.08117  261 SER   A C   
2146 O O   . SER   A 264 ? 0.72855 0.72933 0.80083 0.03663  -0.09554 0.07280  261 SER   A O   
2147 C CB  . SER   A 264 ? 0.77131 0.66604 0.76095 0.04816  -0.13182 0.09566  261 SER   A CB  
2148 O OG  . SER   A 264 ? 0.89149 0.80829 0.88025 0.04376  -0.12799 0.09661  261 SER   A OG  
2149 N N   . LEU   A 265 ? 0.73678 0.68987 0.76914 0.01771  -0.08565 0.08979  262 LEU   A N   
2150 C CA  . LEU   A 265 ? 0.63609 0.61929 0.68170 0.00363  -0.06638 0.08860  262 LEU   A CA  
2151 C C   . LEU   A 265 ? 0.64096 0.65730 0.72426 0.00784  -0.05946 0.07565  262 LEU   A C   
2152 O O   . LEU   A 265 ? 0.57706 0.62400 0.67770 0.00460  -0.05133 0.07055  262 LEU   A O   
2153 C CB  . LEU   A 265 ? 0.68521 0.65141 0.71033 -0.01411 -0.05419 0.09817  262 LEU   A CB  
2154 C CG  . LEU   A 265 ? 0.63381 0.63020 0.67336 -0.02711 -0.03556 0.09561  262 LEU   A CG  
2155 C CD1 . LEU   A 265 ? 0.59888 0.61564 0.63728 -0.02856 -0.03255 0.09532  262 LEU   A CD1 
2156 C CD2 . LEU   A 265 ? 0.59352 0.57535 0.61555 -0.04407 -0.02486 0.10325  262 LEU   A CD2 
2157 N N   . LEU   A 266 ? 0.58301 0.59184 0.67714 0.01473  -0.06286 0.07004  263 LEU   A N   
2158 C CA  . LEU   A 266 ? 0.63726 0.67675 0.76419 0.01774  -0.05542 0.05757  263 LEU   A CA  
2159 C C   . LEU   A 266 ? 0.58261 0.65189 0.73342 0.02830  -0.06085 0.04706  263 LEU   A C   
2160 O O   . LEU   A 266 ? 0.55477 0.65522 0.72710 0.02366  -0.05061 0.04013  263 LEU   A O   
2161 C CB  . LEU   A 266 ? 0.61302 0.63703 0.74467 0.02477  -0.05955 0.05238  263 LEU   A CB  
2162 C CG  . LEU   A 266 ? 0.60956 0.66354 0.77204 0.02765  -0.05138 0.03891  263 LEU   A CG  
2163 C CD1 . LEU   A 266 ? 0.57074 0.64137 0.73710 0.01150  -0.03382 0.04115  263 LEU   A CD1 
2164 C CD2 . LEU   A 266 ? 0.63816 0.67451 0.80330 0.03742  -0.05797 0.03235  263 LEU   A CD2 
2165 N N   . SER   A 267 ? 0.56933 0.62873 0.71570 0.04192  -0.07760 0.04562  264 SER   A N   
2166 C CA  . SER   A 267 ? 0.61665 0.70670 0.78711 0.05122  -0.08371 0.03466  264 SER   A CA  
2167 C C   . SER   A 267 ? 0.60950 0.71904 0.78002 0.04004  -0.07550 0.03767  264 SER   A C   
2168 O O   . SER   A 267 ? 0.57529 0.71752 0.77057 0.03834  -0.07025 0.02840  264 SER   A O   
2169 C CB  . SER   A 267 ? 0.59672 0.67007 0.75941 0.06856  -0.10543 0.03300  264 SER   A CB  
2170 O OG  . SER   A 267 ? 0.85896 0.91558 1.02467 0.08181  -0.11504 0.02739  264 SER   A OG  
2171 N N   . GLN   A 268 ? 0.55633 0.64559 0.69817 0.03164  -0.07409 0.05010  265 GLN   A N   
2172 C CA  . GLN   A 268 ? 0.57745 0.68261 0.71718 0.02283  -0.06778 0.05197  265 GLN   A CA  
2173 C C   . GLN   A 268 ? 0.49764 0.62184 0.64948 0.01024  -0.05028 0.05022  265 GLN   A C   
2174 O O   . GLN   A 268 ? 0.60032 0.74451 0.76104 0.00541  -0.04584 0.04679  265 GLN   A O   
2175 C CB  . GLN   A 268 ? 0.58567 0.66518 0.69036 0.01795  -0.07066 0.06432  265 GLN   A CB  
2176 C CG  . GLN   A 268 ? 0.52692 0.58300 0.61361 0.03021  -0.08979 0.06739  265 GLN   A CG  
2177 C CD  . GLN   A 268 ? 0.66423 0.69400 0.71201 0.02323  -0.09126 0.08022  265 GLN   A CD  
2178 O OE1 . GLN   A 268 ? 0.77212 0.76742 0.79230 0.02460  -0.09906 0.08909  265 GLN   A OE1 
2179 N NE2 . GLN   A 268 ? 0.68370 0.72829 0.72720 0.01526  -0.08384 0.08096  265 GLN   A NE2 
2180 N N   . MET   A 269 ? 0.57996 0.69623 0.73090 0.00503  -0.04153 0.05230  266 MET   A N   
2181 C CA  . MET   A 269 ? 0.51740 0.65083 0.68014 -0.00496 -0.02705 0.04960  266 MET   A CA  
2182 C C   . MET   A 269 ? 0.50653 0.66470 0.69711 -0.00181 -0.02468 0.03815  266 MET   A C   
2183 O O   . MET   A 269 ? 0.49977 0.67339 0.69895 -0.01001 -0.01453 0.03549  266 MET   A O   
2184 C CB  . MET   A 269 ? 0.47311 0.59076 0.62555 -0.01194 -0.01931 0.05487  266 MET   A CB  
2185 C CG  . MET   A 269 ? 0.52450 0.62056 0.64936 -0.01897 -0.01848 0.06585  266 MET   A CG  
2186 S SD  . MET   A 269 ? 0.61218 0.69257 0.72816 -0.02924 -0.00952 0.07050  266 MET   A SD  
2187 C CE  . MET   A 269 ? 0.50030 0.60774 0.63044 -0.03833 0.00470  0.06592  266 MET   A CE  
2188 N N   . LEU   A 270 ? 0.50301 0.66518 0.70681 0.00983  -0.03404 0.03081  267 LEU   A N   
2189 C CA  . LEU   A 270 ? 0.44320 0.63243 0.67439 0.01250  -0.03098 0.01828  267 LEU   A CA  
2190 C C   . LEU   A 270 ? 0.50335 0.71445 0.75065 0.01802  -0.03905 0.01030  267 LEU   A C   
2191 O O   . LEU   A 270 ? 0.44064 0.67530 0.71214 0.02310  -0.03972 -0.00191 267 LEU   A O   
2192 C CB  . LEU   A 270 ? 0.39823 0.58107 0.63701 0.02199  -0.03401 0.01227  267 LEU   A CB  
2193 C CG  . LEU   A 270 ? 0.52059 0.68579 0.74783 0.01534  -0.02537 0.01752  267 LEU   A CG  
2194 C CD1 . LEU   A 270 ? 0.46995 0.62806 0.70491 0.02602  -0.02995 0.00980  267 LEU   A CD1 
2195 C CD2 . LEU   A 270 ? 0.44041 0.62275 0.67354 0.00229  -0.01054 0.01663  267 LEU   A CD2 
2196 N N   . HIS   A 271 ? 0.49364 0.69919 0.72845 0.01677  -0.04505 0.01592  268 HIS   A N   
2197 C CA  . HIS   A 271 ? 0.48060 0.70759 0.73039 0.02009  -0.05284 0.00819  268 HIS   A CA  
2198 C C   . HIS   A 271 ? 0.57509 0.83075 0.84463 0.00867  -0.04162 0.00068  268 HIS   A C   
2199 O O   . HIS   A 271 ? 0.46369 0.71580 0.72460 -0.00344 -0.03019 0.00585  268 HIS   A O   
2200 C CB  . HIS   A 271 ? 0.54819 0.76117 0.77669 0.01905  -0.06006 0.01629  268 HIS   A CB  
2201 C CG  . HIS   A 271 ? 0.67918 0.90412 0.91728 0.02819  -0.07490 0.00936  268 HIS   A CG  
2202 N ND1 . HIS   A 271 ? 0.66154 0.91719 0.92339 0.02410  -0.07440 -0.00114 268 HIS   A ND1 
2203 C CD2 . HIS   A 271 ? 0.70583 0.91550 0.93197 0.04075  -0.09149 0.01123  268 HIS   A CD2 
2204 C CE1 . HIS   A 271 ? 0.81925 1.08115 1.08636 0.03420  -0.09009 -0.00649 268 HIS   A CE1 
2205 N NE2 . HIS   A 271 ? 0.84243 1.07593 1.08736 0.04534  -0.10131 0.00098  268 HIS   A NE2 
2206 N N   . TYR   A 272 ? 0.46664 0.75069 0.76226 0.01230  -0.04537 -0.01209 269 TYR   A N   
2207 C CA  . TYR   A 272 ? 0.42450 0.73564 0.73740 -0.00099 -0.03454 -0.01934 269 TYR   A CA  
2208 C C   . TYR   A 272 ? 0.50164 0.80861 0.80224 -0.01293 -0.03299 -0.01349 269 TYR   A C   
2209 O O   . TYR   A 272 ? 0.52528 0.83136 0.82027 -0.02639 -0.02179 -0.01055 269 TYR   A O   
2210 C CB  . TYR   A 272 ? 0.38254 0.72848 0.72689 0.00430  -0.03926 -0.03534 269 TYR   A CB  
2211 C CG  . TYR   A 272 ? 0.45317 0.81383 0.81547 0.01059  -0.03417 -0.04535 269 TYR   A CG  
2212 C CD1 . TYR   A 272 ? 0.42301 0.78872 0.78564 -0.00112 -0.01804 -0.04566 269 TYR   A CD1 
2213 C CD2 . TYR   A 272 ? 0.44570 0.81465 0.82364 0.02920  -0.04650 -0.05548 269 TYR   A CD2 
2214 C CE1 . TYR   A 272 ? 0.43472 0.81452 0.81263 0.00480  -0.01304 -0.05595 269 TYR   A CE1 
2215 C CE2 . TYR   A 272 ? 0.40654 0.78946 0.80123 0.03644  -0.04229 -0.06653 269 TYR   A CE2 
2216 C CZ  . TYR   A 272 ? 0.47153 0.86066 0.86623 0.02376  -0.02489 -0.06687 269 TYR   A CZ  
2217 O OH  . TYR   A 272 ? 0.43028 0.83376 0.84045 0.03116  -0.02044 -0.07888 269 TYR   A OH  
2218 N N   . ASP   A 273 ? 0.43632 0.73872 0.73092 -0.00743 -0.04529 -0.01219 270 ASP   A N   
2219 C CA  . ASP   A 273 ? 0.48151 0.78019 0.76498 -0.01713 -0.04576 -0.00865 270 ASP   A CA  
2220 C C   . ASP   A 273 ? 0.52413 0.79575 0.78008 -0.02173 -0.03929 0.00349  270 ASP   A C   
2221 O O   . ASP   A 273 ? 0.46675 0.71807 0.70474 -0.01393 -0.04368 0.01100  270 ASP   A O   
2222 C CB  . ASP   A 273 ? 0.51670 0.81644 0.79907 -0.00839 -0.06174 -0.01099 270 ASP   A CB  
2223 C CG  . ASP   A 273 ? 0.62314 0.92311 0.89801 -0.01833 -0.06347 -0.01063 270 ASP   A CG  
2224 O OD1 . ASP   A 273 ? 0.55588 0.85040 0.82301 -0.03098 -0.05305 -0.00726 270 ASP   A OD1 
2225 O OD2 . ASP   A 273 ? 0.69048 0.99451 0.96620 -0.01279 -0.07659 -0.01422 270 ASP   A OD2 
2226 N N   . PRO   A 274 ? 0.55028 0.82057 0.80139 -0.03432 -0.02940 0.00528  271 PRO   A N   
2227 C CA  . PRO   A 274 ? 0.51361 0.76169 0.74126 -0.03688 -0.02429 0.01458  271 PRO   A CA  
2228 C C   . PRO   A 274 ? 0.57790 0.81282 0.78697 -0.03314 -0.03212 0.01888  271 PRO   A C   
2229 O O   . PRO   A 274 ? 0.55306 0.77174 0.74335 -0.03156 -0.02930 0.02588  271 PRO   A O   
2230 C CB  . PRO   A 274 ? 0.39194 0.64233 0.61980 -0.04981 -0.01554 0.01334  271 PRO   A CB  
2231 C CG  . PRO   A 274 ? 0.48330 0.75609 0.73364 -0.05533 -0.01227 0.00499  271 PRO   A CG  
2232 C CD  . PRO   A 274 ? 0.40687 0.69510 0.67258 -0.04700 -0.02262 -0.00142 271 PRO   A CD  
2233 N N   . ASN   A 275 ? 0.62707 0.87026 0.84100 -0.03226 -0.04163 0.01398  272 ASN   A N   
2234 C CA  . ASN   A 275 ? 0.53179 0.76266 0.72648 -0.02809 -0.04986 0.01715  272 ASN   A CA  
2235 C C   . ASN   A 275 ? 0.60922 0.82909 0.79267 -0.01671 -0.05718 0.02206  272 ASN   A C   
2236 O O   . ASN   A 275 ? 0.71793 0.92234 0.87810 -0.01423 -0.05989 0.02772  272 ASN   A O   
2237 C CB  . ASN   A 275 ? 0.52547 0.76803 0.72854 -0.03104 -0.05891 0.00967  272 ASN   A CB  
2238 C CG  . ASN   A 275 ? 0.82879 1.07754 1.03918 -0.04446 -0.05256 0.00558  272 ASN   A CG  
2239 O OD1 . ASN   A 275 ? 0.78150 1.01795 0.98012 -0.04978 -0.04436 0.00965  272 ASN   A OD1 
2240 N ND2 . ASN   A 275 ? 0.93713 1.20452 1.16638 -0.05043 -0.05693 -0.00283 272 ASN   A ND2 
2241 N N   . LYS   A 276 ? 0.55189 0.77820 0.74967 -0.00977 -0.06081 0.01960  273 LYS   A N   
2242 C CA  . LYS   A 276 ? 0.60560 0.81602 0.79007 0.00129  -0.06955 0.02474  273 LYS   A CA  
2243 C C   . LYS   A 276 ? 0.60758 0.80197 0.78188 0.00099  -0.06103 0.03228  273 LYS   A C   
2244 O O   . LYS   A 276 ? 0.53404 0.70799 0.68931 0.00693  -0.06671 0.03918  273 LYS   A O   
2245 C CB  . LYS   A 276 ? 0.61177 0.83576 0.81661 0.01199  -0.08203 0.01636  273 LYS   A CB  
2246 C CG  . LYS   A 276 ? 0.70952 0.95109 0.92588 0.01294  -0.09282 0.00783  273 LYS   A CG  
2247 C CD  . LYS   A 276 ? 0.74152 0.96447 0.93028 0.01691  -0.10333 0.01363  273 LYS   A CD  
2248 C CE  . LYS   A 276 ? 0.86050 1.10062 1.06137 0.01944  -0.11673 0.00410  273 LYS   A CE  
2249 N NZ  . LYS   A 276 ? 1.02567 1.24650 1.19718 0.02442  -0.12818 0.00930  273 LYS   A NZ  
2250 N N   . ARG   A 277 ? 0.48722 0.68873 0.67192 -0.00655 -0.04828 0.03120  274 ARG   A N   
2251 C CA  . ARG   A 277 ? 0.48036 0.66858 0.65765 -0.00761 -0.04049 0.03702  274 ARG   A CA  
2252 C C   . ARG   A 277 ? 0.54476 0.71376 0.69450 -0.01122 -0.03731 0.04655  274 ARG   A C   
2253 O O   . ARG   A 277 ? 0.57798 0.74928 0.71911 -0.01636 -0.03406 0.04709  274 ARG   A O   
2254 C CB  . ARG   A 277 ? 0.41834 0.61871 0.61020 -0.01556 -0.02813 0.03343  274 ARG   A CB  
2255 C CG  . ARG   A 277 ? 0.42465 0.61633 0.61628 -0.01540 -0.02170 0.03603  274 ARG   A CG  
2256 C CD  . ARG   A 277 ? 0.43445 0.63964 0.64045 -0.02245 -0.01122 0.03116  274 ARG   A CD  
2257 N NE  . ARG   A 277 ? 0.45604 0.68257 0.68374 -0.02185 -0.01283 0.02167  274 ARG   A NE  
2258 C CZ  . ARG   A 277 ? 0.43513 0.67554 0.67253 -0.03080 -0.00508 0.01713  274 ARG   A CZ  
2259 N NH1 . ARG   A 277 ? 0.36084 0.59402 0.58785 -0.03901 0.00297  0.02114  274 ARG   A NH1 
2260 N NH2 . ARG   A 277 ? 0.36477 0.62687 0.62199 -0.03186 -0.00586 0.00798  274 ARG   A NH2 
2261 N N   . ILE   A 278 ? 0.56363 0.71348 0.69892 -0.00886 -0.03840 0.05334  275 ILE   A N   
2262 C CA  . ILE   A 278 ? 0.52175 0.65455 0.62950 -0.01381 -0.03517 0.06221  275 ILE   A CA  
2263 C C   . ILE   A 278 ? 0.61246 0.75359 0.72057 -0.02352 -0.02127 0.06218  275 ILE   A C   
2264 O O   . ILE   A 278 ? 0.49083 0.64138 0.61517 -0.02648 -0.01411 0.05858  275 ILE   A O   
2265 C CB  . ILE   A 278 ? 0.58447 0.69279 0.67593 -0.01215 -0.03840 0.06982  275 ILE   A CB  
2266 C CG1 . ILE   A 278 ? 0.60424 0.69453 0.66338 -0.01852 -0.03647 0.07926  275 ILE   A CG1 
2267 C CG2 . ILE   A 278 ? 0.49542 0.60371 0.59801 -0.01637 -0.02929 0.06927  275 ILE   A CG2 
2268 C CD1 . ILE   A 278 ? 0.54995 0.60982 0.58629 -0.01813 -0.04234 0.08824  275 ILE   A CD1 
2269 N N   . SER   A 279 ? 0.62198 0.76043 0.71173 -0.02766 -0.01812 0.06516  276 SER   A N   
2270 C CA  . SER   A 279 ? 0.60806 0.75552 0.69792 -0.03471 -0.00657 0.06356  276 SER   A CA  
2271 C C   . SER   A 279 ? 0.60146 0.74044 0.68119 -0.04147 0.00181  0.06925  276 SER   A C   
2272 O O   . SER   A 279 ? 0.53862 0.66026 0.60380 -0.04221 -0.00136 0.07611  276 SER   A O   
2273 C CB  . SER   A 279 ? 0.64561 0.79745 0.72235 -0.03514 -0.00674 0.06155  276 SER   A CB  
2274 O OG  . SER   A 279 ? 0.59523 0.73489 0.64673 -0.03696 -0.00734 0.06789  276 SER   A OG  
2275 N N   . ALA   A 280 ? 0.43884 0.58919 0.52562 -0.04675 0.01171  0.06603  277 ALA   A N   
2276 C CA  . ALA   A 280 ? 0.63007 0.77689 0.71044 -0.05484 0.02039  0.06973  277 ALA   A CA  
2277 C C   . ALA   A 280 ? 0.65833 0.79690 0.71336 -0.06067 0.02294  0.07558  277 ALA   A C   
2278 O O   . ALA   A 280 ? 0.64420 0.76764 0.68601 -0.06731 0.02483  0.08265  277 ALA   A O   
2279 C CB  . ALA   A 280 ? 0.51184 0.67576 0.60530 -0.05796 0.02888  0.06332  277 ALA   A CB  
2280 N N   . LYS   A 281 ? 0.67612 0.82279 0.72189 -0.05907 0.02295  0.07267  278 LYS   A N   
2281 C CA  . LYS   A 281 ? 0.62358 0.76403 0.64279 -0.06547 0.02653  0.07758  278 LYS   A CA  
2282 C C   . LYS   A 281 ? 0.72355 0.83814 0.72208 -0.06405 0.01669  0.08698  278 LYS   A C   
2283 O O   . LYS   A 281 ? 0.65654 0.75549 0.63190 -0.07301 0.01994  0.09512  278 LYS   A O   
2284 C CB  . LYS   A 281 ? 0.72968 0.88448 0.74327 -0.06223 0.02765  0.07074  278 LYS   A CB  
2285 C CG  . LYS   A 281 ? 0.73525 0.89020 0.72234 -0.07064 0.03525  0.07353  278 LYS   A CG  
2286 C CD  . LYS   A 281 ? 0.87073 1.03843 0.85041 -0.06557 0.03495  0.06562  278 LYS   A CD  
2287 C CE  . LYS   A 281 ? 1.07841 1.24961 1.03133 -0.07522 0.04480  0.06730  278 LYS   A CE  
2288 N NZ  . LYS   A 281 ? 1.26879 1.44764 1.20854 -0.06938 0.04263  0.06027  278 LYS   A NZ  
2289 N N   . ALA   A 282 ? 0.64526 0.75453 0.65109 -0.05326 0.00400  0.08570  279 ALA   A N   
2290 C CA  . ALA   A 282 ? 0.68006 0.76482 0.66789 -0.04897 -0.00823 0.09316  279 ALA   A CA  
2291 C C   . ALA   A 282 ? 0.72138 0.78707 0.70855 -0.05133 -0.00952 0.09926  279 ALA   A C   
2292 O O   . ALA   A 282 ? 0.75811 0.79681 0.71937 -0.05317 -0.01574 0.10825  279 ALA   A O   
2293 C CB  . ALA   A 282 ? 0.59702 0.68610 0.59855 -0.03633 -0.02181 0.08778  279 ALA   A CB  
2294 N N   . ALA   A 283 ? 0.67633 0.75289 0.68910 -0.05130 -0.00458 0.09451  280 ALA   A N   
2295 C CA  . ALA   A 283 ? 0.78924 0.84759 0.80178 -0.05339 -0.00572 0.09886  280 ALA   A CA  
2296 C C   . ALA   A 283 ? 0.67957 0.72312 0.66801 -0.06824 0.00308  0.10713  280 ALA   A C   
2297 O O   . ALA   A 283 ? 0.77522 0.79074 0.74785 -0.07110 -0.00180 0.11450  280 ALA   A O   
2298 C CB  . ALA   A 283 ? 0.62123 0.69648 0.66453 -0.05140 -0.00088 0.09114  280 ALA   A CB  
2299 N N   . LEU   A 284 ? 0.72154 0.78345 0.70661 -0.07808 0.01575  0.10530  281 LEU   A N   
2300 C CA  . LEU   A 284 ? 0.70422 0.75746 0.66722 -0.09463 0.02595  0.11194  281 LEU   A CA  
2301 C C   . LEU   A 284 ? 0.77458 0.79835 0.69900 -0.09877 0.01971  0.12290  281 LEU   A C   
2302 O O   . LEU   A 284 ? 0.81563 0.81844 0.71626 -0.11288 0.02404  0.13163  281 LEU   A O   
2303 C CB  . LEU   A 284 ? 0.71586 0.80102 0.68670 -0.10212 0.04039  0.10473  281 LEU   A CB  
2304 C CG  . LEU   A 284 ? 0.66568 0.77636 0.66949 -0.10026 0.04672  0.09484  281 LEU   A CG  
2305 C CD1 . LEU   A 284 ? 0.73165 0.87348 0.74312 -0.10270 0.05703  0.08584  281 LEU   A CD1 
2306 C CD2 . LEU   A 284 ? 0.63545 0.73741 0.64282 -0.11061 0.05155  0.09774  281 LEU   A CD2 
2307 N N   . ALA   A 285 ? 0.77465 0.79477 0.69059 -0.08762 0.00903  0.12278  282 ALA   A N   
2308 C CA  . ALA   A 285 ? 0.73878 0.72910 0.61578 -0.08940 0.00049  0.13298  282 ALA   A CA  
2309 C C   . ALA   A 285 ? 0.82796 0.78357 0.69610 -0.07920 -0.01761 0.13915  282 ALA   A C   
2310 O O   . ALA   A 285 ? 0.88930 0.81464 0.72283 -0.07864 -0.02816 0.14818  282 ALA   A O   
2311 C CB  . ALA   A 285 ? 0.83252 0.83619 0.70308 -0.08192 -0.00333 0.12875  282 ALA   A CB  
2312 N N   . HIS   A 286 ? 0.84197 0.80079 0.73908 -0.07051 -0.02201 0.13385  283 HIS   A N   
2313 C CA  . HIS   A 286 ? 0.92161 0.85108 0.81448 -0.05807 -0.03989 0.13671  283 HIS   A CA  
2314 C C   . HIS   A 286 ? 0.92432 0.81113 0.78179 -0.06925 -0.04224 0.14935  283 HIS   A C   
2315 O O   . HIS   A 286 ? 0.95879 0.84596 0.81085 -0.08679 -0.02775 0.15277  283 HIS   A O   
2316 C CB  . HIS   A 286 ? 0.83287 0.77981 0.76582 -0.04755 -0.04132 0.12635  283 HIS   A CB  
2317 C CG  . HIS   A 286 ? 0.82732 0.75468 0.76414 -0.03031 -0.06045 0.12448  283 HIS   A CG  
2318 N ND1 . HIS   A 286 ? 0.79971 0.69241 0.72290 -0.02924 -0.06843 0.12961  283 HIS   A ND1 
2319 C CD2 . HIS   A 286 ? 0.84532 0.78389 0.79892 -0.01299 -0.07385 0.11676  283 HIS   A CD2 
2320 C CE1 . HIS   A 286 ? 0.93373 0.81758 0.86565 -0.01012 -0.08642 0.12443  283 HIS   A CE1 
2321 N NE2 . HIS   A 286 ? 0.86194 0.77537 0.81356 -0.00042 -0.08959 0.11635  283 HIS   A NE2 
2322 N N   . PRO   A 287 ? 1.00887 0.85718 0.84097 -0.05971 -0.06131 0.15615  284 PRO   A N   
2323 C CA  . PRO   A 287 ? 1.07387 0.87384 0.86649 -0.07085 -0.06573 0.16943  284 PRO   A CA  
2324 C C   . PRO   A 287 ? 1.06926 0.85979 0.87610 -0.07582 -0.06173 0.16806  284 PRO   A C   
2325 O O   . PRO   A 287 ? 1.19563 0.94544 0.97096 -0.08767 -0.06407 0.17866  284 PRO   A O   
2326 C CB  . PRO   A 287 ? 1.06794 0.83179 0.83808 -0.05290 -0.09122 0.17352  284 PRO   A CB  
2327 C CG  . PRO   A 287 ? 1.05188 0.84645 0.83692 -0.04027 -0.09548 0.16582  284 PRO   A CG  
2328 C CD  . PRO   A 287 ? 0.98635 0.83269 0.81972 -0.03983 -0.08010 0.15252  284 PRO   A CD  
2329 N N   . PHE   A 288 ? 1.00991 0.83522 0.86152 -0.06761 -0.05626 0.15524  285 PHE   A N   
2330 C CA  . PHE   A 288 ? 1.06129 0.88192 0.92714 -0.07353 -0.05060 0.15271  285 PHE   A CA  
2331 C C   . PHE   A 288 ? 0.98177 0.80884 0.83795 -0.09908 -0.03094 0.15772  285 PHE   A C   
2332 O O   . PHE   A 288 ? 0.96812 0.77593 0.81969 -0.10939 -0.02830 0.16032  285 PHE   A O   
2333 C CB  . PHE   A 288 ? 0.88712 0.74550 0.80069 -0.05982 -0.04829 0.13766  285 PHE   A CB  
2334 C CG  . PHE   A 288 ? 0.85091 0.70373 0.77930 -0.06274 -0.04489 0.13353  285 PHE   A CG  
2335 C CD1 . PHE   A 288 ? 0.96186 0.77515 0.87760 -0.05497 -0.05963 0.13554  285 PHE   A CD1 
2336 C CD2 . PHE   A 288 ? 0.74783 0.63357 0.70188 -0.07203 -0.02843 0.12682  285 PHE   A CD2 
2337 C CE1 . PHE   A 288 ? 0.96063 0.76784 0.88906 -0.05732 -0.05701 0.13074  285 PHE   A CE1 
2338 C CE2 . PHE   A 288 ? 0.82080 0.70123 0.78730 -0.07463 -0.02602 0.12248  285 PHE   A CE2 
2339 C CZ  . PHE   A 288 ? 0.87825 0.71975 0.83208 -0.06765 -0.03985 0.12429  285 PHE   A CZ  
2340 N N   . PHE   A 289 ? 1.02681 0.88136 0.88037 -0.10930 -0.01757 0.15795  286 PHE   A N   
2341 C CA  . PHE   A 289 ? 1.13084 0.99858 0.97781 -0.13307 0.00168  0.16047  286 PHE   A CA  
2342 C C   . PHE   A 289 ? 1.31189 1.15728 1.11362 -0.14996 0.00533  0.17291  286 PHE   A C   
2343 O O   . PHE   A 289 ? 1.39357 1.25824 1.19032 -0.16982 0.02298  0.17335  286 PHE   A O   
2344 C CB  . PHE   A 289 ? 0.94636 0.86772 0.82792 -0.13235 0.01611  0.14848  286 PHE   A CB  
2345 C CG  . PHE   A 289 ? 0.82551 0.76970 0.74815 -0.11721 0.01351  0.13672  286 PHE   A CG  
2346 C CD1 . PHE   A 289 ? 0.75150 0.69543 0.69047 -0.12194 0.01732  0.13320  286 PHE   A CD1 
2347 C CD2 . PHE   A 289 ? 0.69775 0.66368 0.64114 -0.09975 0.00768  0.12899  286 PHE   A CD2 
2348 C CE1 . PHE   A 289 ? 0.78899 0.75337 0.76227 -0.10897 0.01558  0.12253  286 PHE   A CE1 
2349 C CE2 . PHE   A 289 ? 0.72823 0.71461 0.70621 -0.08835 0.00652  0.11871  286 PHE   A CE2 
2350 C CZ  . PHE   A 289 ? 0.72590 0.71144 0.71796 -0.09272 0.01067  0.11561  286 PHE   A CZ  
2351 N N   . GLN   A 290 ? 1.38770 1.19383 1.15579 -0.14258 -0.01108 0.18234  287 GLN   A N   
2352 C CA  . GLN   A 290 ? 1.51417 1.29709 1.23452 -0.15836 -0.00834 0.19475  287 GLN   A CA  
2353 C C   . GLN   A 290 ? 1.76788 1.52624 1.45985 -0.18651 0.00279  0.20485  287 GLN   A C   
2354 O O   . GLN   A 290 ? 1.80595 1.56094 1.46510 -0.20661 0.01397  0.21252  287 GLN   A O   
2355 C CB  . GLN   A 290 ? 1.46498 1.20467 1.15287 -0.14327 -0.03158 0.20314  287 GLN   A CB  
2356 C CG  . GLN   A 290 ? 1.58082 1.26802 1.25165 -0.13796 -0.04943 0.21021  287 GLN   A CG  
2357 C CD  . GLN   A 290 ? 1.82757 1.47740 1.47341 -0.11750 -0.07535 0.21516  287 GLN   A CD  
2358 O OE1 . GLN   A 290 ? 2.01392 1.66482 1.63866 -0.11481 -0.07900 0.21853  287 GLN   A OE1 
2359 N NE2 . GLN   A 290 ? 1.78855 1.40590 1.43714 -0.10180 -0.09441 0.21436  287 GLN   A NE2 
2360 N N   . ASP   A 291 ? 1.74912 1.49082 1.45232 -0.18946 0.00037  0.20444  288 ASP   A N   
2361 C CA  . ASP   A 291 ? 1.75202 1.47401 1.43357 -0.21797 0.01174  0.21230  288 ASP   A CA  
2362 C C   . ASP   A 291 ? 1.83386 1.60878 1.54972 -0.23319 0.03485  0.20168  288 ASP   A C   
2363 O O   . ASP   A 291 ? 1.97030 1.74159 1.66920 -0.26084 0.04879  0.20671  288 ASP   A O   
2364 C CB  . ASP   A 291 ? 1.80671 1.48177 1.48164 -0.21427 -0.00334 0.21635  288 ASP   A CB  
2365 C CG  . ASP   A 291 ? 1.73949 1.43837 1.46394 -0.19054 -0.01002 0.20184  288 ASP   A CG  
2366 O OD1 . ASP   A 291 ? 1.65580 1.40187 1.41591 -0.17585 -0.00550 0.19041  288 ASP   A OD1 
2367 O OD2 . ASP   A 291 ? 1.66533 1.33443 1.39127 -0.18720 -0.01978 0.20169  288 ASP   A OD2 
2368 N N   . VAL   A 292 ? 1.73431 1.55758 1.49688 -0.21632 0.03859  0.18692  289 VAL   A N   
2369 C CA  . VAL   A 292 ? 1.66330 1.53638 1.45963 -0.22717 0.05762  0.17554  289 VAL   A CA  
2370 C C   . VAL   A 292 ? 1.69002 1.60364 1.48676 -0.23348 0.07249  0.17088  289 VAL   A C   
2371 O O   . VAL   A 292 ? 1.71798 1.66573 1.52735 -0.25043 0.09017  0.16453  289 VAL   A O   
2372 C CB  . VAL   A 292 ? 1.54748 1.44722 1.39135 -0.20654 0.05312  0.16210  289 VAL   A CB  
2373 C CG1 . VAL   A 292 ? 1.42460 1.36759 1.30023 -0.21788 0.06961  0.15105  289 VAL   A CG1 
2374 C CG2 . VAL   A 292 ? 1.52204 1.38189 1.36418 -0.19637 0.03686  0.16521  289 VAL   A CG2 
2375 N N   . THR   A 293 ? 1.61291 1.52464 1.39663 -0.21973 0.06519  0.17262  290 THR   A N   
2376 C CA  . THR   A 293 ? 1.58834 1.53766 1.37261 -0.22256 0.07763  0.16655  290 THR   A CA  
2377 C C   . THR   A 293 ? 1.72368 1.64364 1.46146 -0.22491 0.07172  0.17797  290 THR   A C   
2378 O O   . THR   A 293 ? 1.76329 1.63849 1.47663 -0.21583 0.05380  0.18818  290 THR   A O   
2379 C CB  . THR   A 293 ? 1.44975 1.43872 1.27506 -0.19939 0.07517  0.15206  290 THR   A CB  
2380 O OG1 . THR   A 293 ? 1.42264 1.44539 1.24641 -0.20173 0.08642  0.14530  290 THR   A OG1 
2381 C CG2 . THR   A 293 ? 1.32743 1.29325 1.15282 -0.17572 0.05473  0.15440  290 THR   A CG2 
2382 N N   . LYS   A 294 ? 1.72419 1.67060 1.44953 -0.23651 0.08650  0.17514  291 LYS   A N   
2383 C CA  . LYS   A 294 ? 1.80457 1.73202 1.48753 -0.23794 0.08295  0.18328  291 LYS   A CA  
2384 C C   . LYS   A 294 ? 1.81357 1.78272 1.51601 -0.22259 0.08610  0.17017  291 LYS   A C   
2385 O O   . LYS   A 294 ? 1.78091 1.79747 1.51441 -0.22476 0.10093  0.15645  291 LYS   A O   
2386 C CB  . LYS   A 294 ? 1.86084 1.77725 1.50131 -0.26949 0.09892  0.19278  291 LYS   A CB  
2387 C CG  . LYS   A 294 ? 1.85678 1.70761 1.44060 -0.27859 0.08593  0.21276  291 LYS   A CG  
2388 C CD  . LYS   A 294 ? 1.94697 1.75723 1.53709 -0.27094 0.06902  0.21923  291 LYS   A CD  
2389 C CE  . LYS   A 294 ? 1.98136 1.72177 1.51411 -0.27543 0.05188  0.23834  291 LYS   A CE  
2390 N NZ  . LYS   A 294 ? 1.86256 1.56305 1.40251 -0.26426 0.03334  0.24251  291 LYS   A NZ  
2391 N N   . PRO   A 295 ? 1.81895 1.77097 1.50405 -0.20638 0.07123  0.17317  292 PRO   A N   
2392 C CA  . PRO   A 295 ? 1.77604 1.76430 1.48117 -0.19036 0.07177  0.16002  292 PRO   A CA  
2393 C C   . PRO   A 295 ? 1.81018 1.82794 1.49928 -0.20504 0.09081  0.15450  292 PRO   A C   
2394 O O   . PRO   A 295 ? 1.67686 1.67851 1.32592 -0.22663 0.10025  0.16408  292 PRO   A O   
2395 C CB  . PRO   A 295 ? 1.61598 1.57194 1.29978 -0.17289 0.04991  0.16654  292 PRO   A CB  
2396 C CG  . PRO   A 295 ? 1.71627 1.62040 1.35164 -0.18602 0.04313  0.18443  292 PRO   A CG  
2397 C CD  . PRO   A 295 ? 1.75976 1.65713 1.40543 -0.20142 0.05169  0.18808  292 PRO   A CD  
2398 N N   . VAL   A 296 ? 2.01313 2.07414 1.73313 -0.19329 0.09637  0.13823  293 VAL   A N   
2399 C CA  . VAL   A 296 ? 1.87713 1.97239 1.58792 -0.20235 0.11346  0.12871  293 VAL   A CA  
2400 C C   . VAL   A 296 ? 1.84954 1.93003 1.52691 -0.19381 0.10434  0.13120  293 VAL   A C   
2401 O O   . VAL   A 296 ? 2.01789 2.07704 1.69745 -0.17506 0.08459  0.13399  293 VAL   A O   
2402 C CB  . VAL   A 296 ? 1.79494 1.94118 1.55362 -0.19205 0.12189  0.10878  293 VAL   A CB  
2403 C CG1 . VAL   A 296 ? 1.70523 1.86384 1.49638 -0.19897 0.12826  0.10640  293 VAL   A CG1 
2404 C CG2 . VAL   A 296 ? 1.70981 1.85872 1.49128 -0.16563 0.10556  0.10117  293 VAL   A CG2 
2405 N N   . PRO   A 297 ? 1.64697 1.73892 1.29277 -0.20731 0.11791  0.12968  294 PRO   A N   
2406 C CA  . PRO   A 297 ? 1.64007 1.72044 1.25430 -0.19809 0.10903  0.13017  294 PRO   A CA  
2407 C C   . PRO   A 297 ? 1.57110 1.68192 1.22039 -0.17443 0.10260  0.11272  294 PRO   A C   
2408 O O   . PRO   A 297 ? 1.63206 1.78540 1.31312 -0.17229 0.11512  0.09662  294 PRO   A O   
2409 C CB  . PRO   A 297 ? 1.58768 1.68113 1.16417 -0.22084 0.12966  0.13005  294 PRO   A CB  
2410 C CG  . PRO   A 297 ? 1.60127 1.73455 1.20854 -0.23538 0.15089  0.12046  294 PRO   A CG  
2411 C CD  . PRO   A 297 ? 1.64241 1.75862 1.27818 -0.23296 0.14221  0.12724  294 PRO   A CD  
2412 N N   . HIS   A 298 ? 1.51825 1.60606 1.16130 -0.15666 0.08194  0.11556  295 HIS   A N   
2413 C CA  . HIS   A 298 ? 1.63530 1.74475 1.30932 -0.13515 0.07303  0.10069  295 HIS   A CA  
2414 C C   . HIS   A 298 ? 1.55150 1.67145 1.19850 -0.13258 0.07542  0.09262  295 HIS   A C   
2415 O O   . HIS   A 298 ? 1.60689 1.69843 1.21114 -0.13512 0.06732  0.10236  295 HIS   A O   
2416 C CB  . HIS   A 298 ? 1.73773 1.82102 1.42489 -0.11812 0.04958  0.10617  295 HIS   A CB  
2417 C CG  . HIS   A 298 ? 1.78805 1.86770 1.50890 -0.11667 0.04701  0.10961  295 HIS   A CG  
2418 N ND1 . HIS   A 298 ? 1.84055 1.94338 1.58585 -0.12627 0.06290  0.10511  295 HIS   A ND1 
2419 C CD2 . HIS   A 298 ? 1.84079 1.89794 1.57511 -0.10635 0.03025  0.11588  295 HIS   A CD2 
2420 C CE1 . HIS   A 298 ? 1.85274 1.94523 1.62295 -0.12224 0.05601  0.10917  295 HIS   A CE1 
2421 N NE2 . HIS   A 298 ? 1.85555 1.92114 1.61996 -0.11014 0.03682  0.11542  295 HIS   A NE2 
2422 N N   . LEU   A 299 ? 1.55477 1.71407 1.22530 -0.12667 0.08547  0.07427  296 LEU   A N   
2423 C CA  . LEU   A 299 ? 1.51945 1.69149 1.16962 -0.12080 0.08660  0.06309  296 LEU   A CA  
2424 C C   . LEU   A 299 ? 1.65679 1.81064 1.31063 -0.10109 0.06352  0.06154  296 LEU   A C   
2425 O O   . LEU   A 299 ? 1.56595 1.73001 1.25857 -0.08678 0.05507  0.05280  296 LEU   A O   
2426 C CB  . LEU   A 299 ? 1.34383 1.56252 1.02141 -0.11770 0.10209  0.04214  296 LEU   A CB  
2427 C CG  . LEU   A 299 ? 1.39663 1.63224 1.06023 -0.10785 0.10247  0.02627  296 LEU   A CG  
2428 C CD1 . LEU   A 299 ? 1.29073 1.52183 0.90265 -0.12361 0.11387  0.03112  296 LEU   A CD1 
2429 C CD2 . LEU   A 299 ? 1.25716 1.53621 0.95666 -0.09922 0.11282  0.00396  296 LEU   A CD2 
2430 N N   . ARG   A 300 ? 1.95499 2.08137 1.56736 -0.10124 0.05290  0.07000  297 ARG   A N   
2431 C CA  . ARG   A 300 ? 1.96614 2.07531 1.57980 -0.08393 0.02991  0.06856  297 ARG   A CA  
2432 C C   . ARG   A 300 ? 1.92898 2.05704 1.53462 -0.07522 0.03034  0.05186  297 ARG   A C   
2433 O O   . ARG   A 300 ? 1.96044 2.07344 1.52837 -0.07381 0.02267  0.05326  297 ARG   A O   
2434 C CB  . ARG   A 300 ? 2.07859 2.14598 1.65350 -0.08647 0.01463  0.08615  297 ARG   A CB  
2435 C CG  . ARG   A 300 ? 2.15243 2.19733 1.73451 -0.09283 0.01164  0.10158  297 ARG   A CG  
2436 C CD  . ARG   A 300 ? 2.31485 2.31539 1.85807 -0.09190 -0.00706 0.11764  297 ARG   A CD  
2437 N NE  . ARG   A 300 ? 2.50088 2.47807 2.05195 -0.09565 -0.01178 0.13078  297 ARG   A NE  
2438 C CZ  . ARG   A 300 ? 2.52646 2.46251 2.04980 -0.09311 -0.02970 0.14485  297 ARG   A CZ  
2439 N NH1 . ARG   A 300 ? 2.46062 2.37358 1.94566 -0.08710 -0.04537 0.14862  297 ARG   A NH1 
2440 N NH2 . ARG   A 300 ? 2.56501 2.48158 2.09855 -0.09563 -0.03322 0.15463  297 ARG   A NH2 
2441 N N   . LEU   A 301 ? 1.66974 1.82982 1.31079 -0.06850 0.03842  0.03526  298 LEU   A N   
2442 C CA  . LEU   A 301 ? 1.77938 1.95837 1.41783 -0.05837 0.03860  0.01679  298 LEU   A CA  
2443 C C   . LEU   A 301 ? 1.91188 2.09824 1.59178 -0.04181 0.02629  0.00486  298 LEU   A C   
2444 O O   . LEU   A 301 ? 1.92250 2.09751 1.62905 -0.03846 0.01623  0.01205  298 LEU   A O   
2445 C CB  . LEU   A 301 ? 1.70026 1.91320 1.33434 -0.06665 0.06224  0.00473  298 LEU   A CB  
2446 C CG  . LEU   A 301 ? 1.64270 1.87886 1.27647 -0.05469 0.06399  -0.01749 298 LEU   A CG  
2447 C CD1 . LEU   A 301 ? 1.75689 1.97280 1.34928 -0.05098 0.05242  -0.01686 298 LEU   A CD1 
2448 C CD2 . LEU   A 301 ? 1.54412 1.81845 1.17748 -0.06304 0.08842  -0.03034 298 LEU   A CD2 
2449 N N   . GLY   B 9   ? 1.06245 1.35351 0.95835 0.07663  -0.00135 -0.15004 102 GLY   B N   
2450 C CA  . GLY   B 9   ? 1.29035 1.56024 1.17699 0.06237  -0.00451 -0.12850 102 GLY   B CA  
2451 C C   . GLY   B 9   ? 1.28435 1.53586 1.19229 0.05695  -0.01144 -0.11401 102 GLY   B C   
2452 O O   . GLY   B 9   ? 1.22145 1.47029 1.14798 0.06455  -0.01644 -0.12017 102 GLY   B O   
2453 N N   . SER   B 10  ? 1.27337 1.51181 1.17740 0.04438  -0.01231 -0.09535 103 SER   B N   
2454 C CA  . SER   B 10  ? 1.21376 1.43719 1.13706 0.03804  -0.01750 -0.08154 103 SER   B CA  
2455 C C   . SER   B 10  ? 1.38905 1.58623 1.30680 0.03580  -0.03294 -0.07509 103 SER   B C   
2456 O O   . SER   B 10  ? 1.39409 1.58707 1.29517 0.03072  -0.03452 -0.06840 103 SER   B O   
2457 C CB  . SER   B 10  ? 1.33116 1.56517 1.25941 0.02531  -0.00464 -0.06618 103 SER   B CB  
2458 O OG  . SER   B 10  ? 1.23466 1.45544 1.18133 0.02006  -0.00945 -0.05427 103 SER   B OG  
2459 N N   . PRO   B 11  ? 1.21732 1.39634 1.14746 0.03865  -0.04496 -0.07702 104 PRO   B N   
2460 C CA  . PRO   B 11  ? 1.13713 1.29461 1.06460 0.03439  -0.05900 -0.07211 104 PRO   B CA  
2461 C C   . PRO   B 11  ? 1.08318 1.23623 1.02593 0.02329  -0.05915 -0.05610 104 PRO   B C   
2462 O O   . PRO   B 11  ? 1.00455 1.14517 0.94771 0.01877  -0.06982 -0.05242 104 PRO   B O   
2463 C CB  . PRO   B 11  ? 1.05439 1.19380 0.98550 0.04150  -0.07092 -0.08329 104 PRO   B CB  
2464 C CG  . PRO   B 11  ? 1.08643 1.23422 1.03223 0.04544  -0.06360 -0.08525 104 PRO   B CG  
2465 C CD  . PRO   B 11  ? 1.08920 1.26572 1.03331 0.04637  -0.04736 -0.08579 104 PRO   B CD  
2466 N N   . LEU   B 12  ? 1.10172 1.26589 1.05785 0.01903  -0.04806 -0.04794 105 LEU   B N   
2467 C CA  . LEU   B 12  ? 1.08746 1.24792 1.05893 0.00993  -0.04818 -0.03456 105 LEU   B CA  
2468 C C   . LEU   B 12  ? 1.06976 1.23086 1.03156 0.00522  -0.04943 -0.02550 105 LEU   B C   
2469 O O   . LEU   B 12  ? 1.18025 1.34836 1.12391 0.00625  -0.04371 -0.02522 105 LEU   B O   
2470 C CB  . LEU   B 12  ? 0.95103 1.12251 0.93710 0.00722  -0.03635 -0.02919 105 LEU   B CB  
2471 C CG  . LEU   B 12  ? 0.94124 1.11196 0.93754 0.01266  -0.03608 -0.03724 105 LEU   B CG  
2472 C CD1 . LEU   B 12  ? 0.81680 1.00079 0.82683 0.00948  -0.02457 -0.03188 105 LEU   B CD1 
2473 C CD2 . LEU   B 12  ? 1.02115 1.17153 1.02424 0.01083  -0.04785 -0.03749 105 LEU   B CD2 
2474 N N   . PRO   B 13  ? 1.04139 1.19548 1.01391 0.00008  -0.05714 -0.01857 106 PRO   B N   
2475 C CA  . PRO   B 13  ? 1.03553 1.18923 1.00048 -0.00241 -0.06052 -0.01018 106 PRO   B CA  
2476 C C   . PRO   B 13  ? 1.11385 1.27358 1.08207 -0.00632 -0.04963 0.00071  106 PRO   B C   
2477 O O   . PRO   B 13  ? 1.10333 1.26968 1.08166 -0.00790 -0.03931 0.00141  106 PRO   B O   
2478 C CB  . PRO   B 13  ? 1.11170 1.26004 1.09331 -0.00584 -0.07229 -0.00937 106 PRO   B CB  
2479 C CG  . PRO   B 13  ? 1.13432 1.28219 1.13564 -0.00928 -0.06849 -0.01068 106 PRO   B CG  
2480 C CD  . PRO   B 13  ? 1.12613 1.27274 1.11799 -0.00391 -0.06342 -0.01881 106 PRO   B CD  
2481 N N   . VAL   B 14  ? 1.11659 1.27206 1.07502 -0.00760 -0.05347 0.00895  107 VAL   B N   
2482 C CA  . VAL   B 14  ? 1.13478 1.29050 1.09360 -0.01170 -0.04546 0.01989  107 VAL   B CA  
2483 C C   . VAL   B 14  ? 1.03360 1.19246 1.02109 -0.01439 -0.04365 0.02269  107 VAL   B C   
2484 O O   . VAL   B 14  ? 0.95091 1.10875 0.95436 -0.01406 -0.05282 0.02170  107 VAL   B O   
2485 C CB  . VAL   B 14  ? 1.10628 1.25124 1.04699 -0.01101 -0.05371 0.02788  107 VAL   B CB  
2486 C CG1 . VAL   B 14  ? 1.08507 1.22639 0.99163 -0.01119 -0.05028 0.02790  107 VAL   B CG1 
2487 C CG2 . VAL   B 14  ? 1.21642 1.35813 1.16624 -0.00688 -0.07029 0.02440  107 VAL   B CG2 
2488 N N   . LEU   B 15  ? 0.99827 1.16279 0.99258 -0.01771 -0.03148 0.02524  108 LEU   B N   
2489 C CA  . LEU   B 15  ? 1.08650 1.25399 1.10520 -0.02041 -0.02844 0.02739  108 LEU   B CA  
2490 C C   . LEU   B 15  ? 1.06366 1.22697 1.08389 -0.02320 -0.02622 0.03746  108 LEU   B C   
2491 O O   . LEU   B 15  ? 1.14437 1.30445 1.14796 -0.02593 -0.01993 0.04305  108 LEU   B O   
2492 C CB  . LEU   B 15  ? 1.01704 1.19252 1.04295 -0.02121 -0.01846 0.02262  108 LEU   B CB  
2493 C CG  . LEU   B 15  ? 1.09458 1.27134 1.11646 -0.01644 -0.02139 0.01158  108 LEU   B CG  
2494 C CD1 . LEU   B 15  ? 0.95297 1.13748 0.98314 -0.01515 -0.01346 0.00634  108 LEU   B CD1 
2495 C CD2 . LEU   B 15  ? 1.05550 1.22407 1.08576 -0.01600 -0.03297 0.00812  108 LEU   B CD2 
2496 N N   . SER   B 16  ? 0.98139 1.14433 1.02070 -0.02305 -0.03137 0.03916  109 SER   B N   
2497 C CA  . SER   B 16  ? 1.13152 1.28886 1.17361 -0.02371 -0.03107 0.04709  109 SER   B CA  
2498 C C   . SER   B 16  ? 1.22576 1.38585 1.27542 -0.02853 -0.01900 0.05000  109 SER   B C   
2499 O O   . SER   B 16  ? 1.21668 1.36870 1.25960 -0.03063 -0.01629 0.05718  109 SER   B O   
2500 C CB  . SER   B 16  ? 1.12898 1.28903 1.19104 -0.02065 -0.04062 0.04534  109 SER   B CB  
2501 O OG  . SER   B 16  ? 1.20197 1.37206 1.28584 -0.02382 -0.03691 0.04002  109 SER   B OG  
2502 N N   . TRP   B 17  ? 1.01848 1.18766 1.08038 -0.03030 -0.01290 0.04444  110 TRP   B N   
2503 C CA  . TRP   B 17  ? 0.98047 1.15372 1.05205 -0.03424 -0.00310 0.04580  110 TRP   B CA  
2504 C C   . TRP   B 17  ? 0.92101 1.09925 0.98062 -0.03742 0.00670  0.04543  110 TRP   B C   
2505 O O   . TRP   B 17  ? 0.96912 1.15077 1.03483 -0.04171 0.01460  0.04729  110 TRP   B O   
2506 C CB  . TRP   B 17  ? 0.89895 1.07800 0.98859 -0.03442 -0.00274 0.04010  110 TRP   B CB  
2507 C CG  . TRP   B 17  ? 0.89608 1.07562 0.98329 -0.03194 -0.00824 0.03305  110 TRP   B CG  
2508 C CD1 . TRP   B 17  ? 1.02570 1.20259 1.11435 -0.03081 -0.01762 0.03067  110 TRP   B CD1 
2509 C CD2 . TRP   B 17  ? 0.91555 1.09744 0.99869 -0.03004 -0.00587 0.02649  110 TRP   B CD2 
2510 N NE1 . TRP   B 17  ? 0.94280 1.11742 1.02656 -0.02949 -0.02105 0.02385  110 TRP   B NE1 
2511 C CE2 . TRP   B 17  ? 0.92934 1.10603 1.00921 -0.02792 -0.01447 0.02101  110 TRP   B CE2 
2512 C CE3 . TRP   B 17  ? 0.81684 1.00530 0.89955 -0.02935 0.00174  0.02362  110 TRP   B CE3 
2513 C CZ2 . TRP   B 17  ? 0.85585 1.02994 0.92988 -0.02417 -0.01640 0.01316  110 TRP   B CZ2 
2514 C CZ3 . TRP   B 17  ? 0.75834 0.94777 0.83750 -0.02447 -0.00027 0.01493  110 TRP   B CZ3 
2515 C CH2 . TRP   B 17  ? 0.76286 0.94330 0.83666 -0.02144 -0.00961 0.00997  110 TRP   B CH2 
2516 N N   . ALA   B 18  ? 0.96536 1.14605 1.00887 -0.03580 0.00665  0.04200  111 ALA   B N   
2517 C CA  . ALA   B 18  ? 1.03019 1.22042 1.06297 -0.03939 0.01710  0.03988  111 ALA   B CA  
2518 C C   . ALA   B 18  ? 1.11123 1.30131 1.12220 -0.03723 0.01510  0.03708  111 ALA   B C   
2519 O O   . ALA   B 18  ? 1.20132 1.38362 1.20729 -0.03226 0.00472  0.03601  111 ALA   B O   
2520 C CB  . ALA   B 18  ? 1.00484 1.20915 1.05253 -0.03744 0.02236  0.03091  111 ALA   B CB  
2521 N N   . ASN   B 19  ? 1.09472 1.29509 1.09275 -0.04175 0.02548  0.03511  112 ASN   B N   
2522 C CA  . ASN   B 19  ? 1.23853 1.44177 1.21444 -0.03999 0.02564  0.03065  112 ASN   B CA  
2523 C C   . ASN   B 19  ? 1.20549 1.41610 1.18918 -0.03005 0.02009  0.01770  112 ASN   B C   
2524 O O   . ASN   B 19  ? 1.19615 1.41913 1.19577 -0.02674 0.02372  0.00925  112 ASN   B O   
2525 C CB  . ASN   B 19  ? 1.32106 1.53832 1.28346 -0.04864 0.04032  0.02972  112 ASN   B CB  
2526 C CG  . ASN   B 19  ? 1.52817 1.74841 1.46362 -0.04831 0.04198  0.02565  112 ASN   B CG  
2527 O OD1 . ASN   B 19  ? 1.51523 1.72092 1.43661 -0.04329 0.03105  0.02758  112 ASN   B OD1 
2528 N ND2 . ASN   B 19  ? 1.45215 1.69326 1.38060 -0.05391 0.05584  0.01897  112 ASN   B ND2 
2529 N N   . ARG   B 20  ? 1.21744 1.41829 1.18886 -0.02493 0.00977  0.01589  113 ARG   B N   
2530 C CA  . ARG   B 20  ? 1.13406 1.33679 1.10974 -0.01606 0.00267  0.00374  113 ARG   B CA  
2531 C C   . ARG   B 20  ? 1.20127 1.42200 1.17311 -0.01226 0.01134  -0.00867 113 ARG   B C   
2532 O O   . ARG   B 20  ? 1.02641 1.25091 1.01002 -0.00458 0.00801  -0.01934 113 ARG   B O   
2533 C CB  . ARG   B 20  ? 1.20693 1.39719 1.16684 -0.01266 -0.00927 0.00341  113 ARG   B CB  
2534 C CG  . ARG   B 20  ? 1.30027 1.48845 1.23173 -0.01610 -0.00631 0.00816  113 ARG   B CG  
2535 C CD  . ARG   B 20  ? 1.28213 1.45991 1.19703 -0.01088 -0.01913 0.00459  113 ARG   B CD  
2536 N NE  . ARG   B 20  ? 1.29070 1.47371 1.20649 -0.00326 -0.02226 -0.01008 113 ARG   B NE  
2537 C CZ  . ARG   B 20  ? 1.35805 1.55220 1.25805 -0.00018 -0.01523 -0.01991 113 ARG   B CZ  
2538 N NH1 . ARG   B 20  ? 1.40715 1.61034 1.28853 -0.00619 -0.00305 -0.01633 113 ARG   B NH1 
2539 N NH2 . ARG   B 20  ? 1.31945 1.51532 1.22151 0.00868  -0.02049 -0.03426 113 ARG   B NH2 
2540 N N   . GLU   B 21  ? 1.58269 1.81455 1.53729 -0.01762 0.02222  -0.00805 114 GLU   B N   
2541 C CA  . GLU   B 21  ? 1.49016 1.74549 1.44388 -0.01453 0.03233  -0.02163 114 GLU   B CA  
2542 C C   . GLU   B 21  ? 1.40406 1.67547 1.38187 -0.01569 0.04015  -0.02488 114 GLU   B C   
2543 O O   . GLU   B 21  ? 1.41728 1.70417 1.40648 -0.00678 0.04092  -0.03930 114 GLU   B O   
2544 C CB  . GLU   B 21  ? 1.60800 1.87278 1.53569 -0.02295 0.04370  -0.01973 114 GLU   B CB  
2545 C CG  . GLU   B 21  ? 1.82121 2.07100 1.72120 -0.02089 0.03562  -0.01806 114 GLU   B CG  
2546 C CD  . GLU   B 21  ? 2.06222 2.31849 1.93181 -0.03109 0.04742  -0.01461 114 GLU   B CD  
2547 O OE1 . GLU   B 21  ? 2.03888 2.30991 1.90972 -0.04203 0.06225  -0.01174 114 GLU   B OE1 
2548 O OE2 . GLU   B 21  ? 2.10845 2.35453 1.95149 -0.02926 0.04184  -0.01479 114 GLU   B OE2 
2549 N N   . GLU   B 22  ? 1.28502 1.55209 1.27049 -0.02556 0.04466  -0.01247 115 GLU   B N   
2550 C CA  . GLU   B 22  ? 1.17664 1.45907 1.18404 -0.02770 0.05184  -0.01536 115 GLU   B CA  
2551 C C   . GLU   B 22  ? 0.92317 1.20053 0.95066 -0.01675 0.04162  -0.02205 115 GLU   B C   
2552 O O   . GLU   B 22  ? 0.91903 1.21331 0.96052 -0.01075 0.04400  -0.03352 115 GLU   B O   
2553 C CB  . GLU   B 22  ? 1.23396 1.50779 1.24322 -0.04034 0.05678  -0.00043 115 GLU   B CB  
2554 C CG  . GLU   B 22  ? 1.20300 1.49304 1.23323 -0.04448 0.06465  -0.00310 115 GLU   B CG  
2555 C CD  . GLU   B 22  ? 1.30053 1.57865 1.33071 -0.05687 0.06843  0.01115  115 GLU   B CD  
2556 O OE1 . GLU   B 22  ? 1.34688 1.60184 1.36361 -0.05953 0.06251  0.02290  115 GLU   B OE1 
2557 O OE2 . GLU   B 22  ? 1.22552 1.51719 1.26928 -0.06327 0.07630  0.00970  115 GLU   B OE2 
2558 N N   . VAL   B 23  ? 0.88084 1.13502 0.90918 -0.01438 0.02980  -0.01545 116 VAL   B N   
2559 C CA  . VAL   B 23  ? 0.83861 1.08366 0.88123 -0.00663 0.02013  -0.02026 116 VAL   B CA  
2560 C C   . VAL   B 23  ? 0.90808 1.15742 0.94720 0.00564  0.01463  -0.03590 116 VAL   B C   
2561 O O   . VAL   B 23  ? 0.69842 0.94945 0.74874 0.01332  0.01066  -0.04428 116 VAL   B O   
2562 C CB  . VAL   B 23  ? 0.75866 0.98081 0.80143 -0.00893 0.00991  -0.01097 116 VAL   B CB  
2563 C CG1 . VAL   B 23  ? 0.70208 0.91233 0.75480 -0.00356 0.00051  -0.01549 116 VAL   B CG1 
2564 C CG2 . VAL   B 23  ? 0.72016 0.93883 0.76851 -0.01841 0.01436  0.00221  116 VAL   B CG2 
2565 N N   . TRP   B 24  ? 0.83956 1.08921 0.86151 0.00855  0.01326  -0.04063 117 TRP   B N   
2566 C CA  . TRP   B 24  ? 0.89084 1.14294 0.90777 0.02142  0.00709  -0.05687 117 TRP   B CA  
2567 C C   . TRP   B 24  ? 0.91019 1.19155 0.93448 0.02707  0.01674  -0.07049 117 TRP   B C   
2568 O O   . TRP   B 24  ? 0.75368 1.03758 0.78546 0.03988  0.01021  -0.08429 117 TRP   B O   
2569 C CB  . TRP   B 24  ? 0.89369 1.13873 0.88918 0.02265  0.00311  -0.05873 117 TRP   B CB  
2570 C CG  . TRP   B 24  ? 0.86836 1.11113 0.85671 0.03639  -0.00531 -0.07573 117 TRP   B CG  
2571 C CD1 . TRP   B 24  ? 1.07126 1.33330 1.04941 0.04352  0.00029  -0.09001 117 TRP   B CD1 
2572 C CD2 . TRP   B 24  ? 0.86814 1.08675 0.85757 0.04435  -0.02108 -0.08092 117 TRP   B CD2 
2573 N NE1 . TRP   B 24  ? 1.02326 1.27408 0.99686 0.05743  -0.01206 -0.10460 117 TRP   B NE1 
2574 C CE2 . TRP   B 24  ? 0.89283 1.11485 0.87215 0.05760  -0.02574 -0.09866 117 TRP   B CE2 
2575 C CE3 . TRP   B 24  ? 0.81200 1.00602 0.80864 0.04059  -0.03135 -0.07263 117 TRP   B CE3 
2576 C CZ2 . TRP   B 24  ? 0.89707 1.09463 0.87208 0.06748  -0.04176 -0.10764 117 TRP   B CZ2 
2577 C CZ3 . TRP   B 24  ? 0.88652 1.05744 0.87816 0.04821  -0.04594 -0.08072 117 TRP   B CZ3 
2578 C CH2 . TRP   B 24  ? 0.86071 1.03149 0.84102 0.06170  -0.05176 -0.09773 117 TRP   B CH2 
2579 N N   . LYS   B 25  ? 0.93073 1.23424 0.95270 0.01745  0.03175  -0.06744 118 LYS   B N   
2580 C CA  . LYS   B 25  ? 0.82495 1.16217 0.85693 0.02055  0.04265  -0.08139 118 LYS   B CA  
2581 C C   . LYS   B 25  ? 0.75889 1.10233 0.81510 0.02438  0.04056  -0.08446 118 LYS   B C   
2582 O O   . LYS   B 25  ? 0.80441 1.16883 0.87283 0.03565  0.04035  -0.10131 118 LYS   B O   
2583 C CB  . LYS   B 25  ? 1.03520 1.39249 1.05810 0.00507  0.06003  -0.07533 118 LYS   B CB  
2584 C CG  . LYS   B 25  ? 1.28131 1.63553 1.27634 0.00151  0.06320  -0.07414 118 LYS   B CG  
2585 C CD  . LYS   B 25  ? 1.31920 1.68853 1.30880 0.01590  0.06121  -0.09478 118 LYS   B CD  
2586 C CE  . LYS   B 25  ? 1.36549 1.72986 1.32463 0.01209  0.06374  -0.09331 118 LYS   B CE  
2587 N NZ  . LYS   B 25  ? 1.51059 1.88889 1.46309 0.02690  0.06142  -0.11467 118 LYS   B NZ  
2588 N N   . ILE   B 26  ? 0.75410 1.08015 0.81732 0.01606  0.03829  -0.06937 119 ILE   B N   
2589 C CA  . ILE   B 26  ? 0.78502 1.11365 0.86834 0.01932  0.03518  -0.07133 119 ILE   B CA  
2590 C C   . ILE   B 26  ? 0.68094 0.99339 0.76646 0.03560  0.01928  -0.08147 119 ILE   B C   
2591 O O   . ILE   B 26  ? 0.70415 1.02874 0.80276 0.04593  0.01579  -0.09367 119 ILE   B O   
2592 C CB  . ILE   B 26  ? 0.79217 1.10366 0.87961 0.00698  0.03599  -0.05332 119 ILE   B CB  
2593 C CG1 . ILE   B 26  ? 0.80982 1.13695 0.89630 -0.00832 0.05095  -0.04518 119 ILE   B CG1 
2594 C CG2 . ILE   B 26  ? 0.64440 0.95078 0.74799 0.01172  0.02938  -0.05486 119 ILE   B CG2 
2595 C CD1 . ILE   B 26  ? 0.87134 1.17821 0.95729 -0.01941 0.05079  -0.02768 119 ILE   B CD1 
2596 N N   . MET   B 27  ? 0.62447 0.90806 0.69631 0.03793  0.00842  -0.07691 120 MET   B N   
2597 C CA  . MET   B 27  ? 0.70497 0.96763 0.77381 0.05170  -0.00748 -0.08599 120 MET   B CA  
2598 C C   . MET   B 27  ? 0.74912 1.02928 0.81684 0.06769  -0.00972 -0.10686 120 MET   B C   
2599 O O   . MET   B 27  ? 0.70994 0.98323 0.78191 0.08204  -0.02112 -0.11852 120 MET   B O   
2600 C CB  . MET   B 27  ? 0.76177 0.99261 0.81569 0.04811  -0.01729 -0.07755 120 MET   B CB  
2601 C CG  . MET   B 27  ? 0.66511 0.87935 0.72249 0.03456  -0.01702 -0.05978 120 MET   B CG  
2602 S SD  . MET   B 27  ? 0.80163 0.98845 0.84508 0.02848  -0.02639 -0.05182 120 MET   B SD  
2603 C CE  . MET   B 27  ? 0.93378 1.09313 0.96843 0.03993  -0.04367 -0.06291 120 MET   B CE  
2604 N N   . LEU   B 28  ? 0.70264 1.00494 0.76330 0.06600  0.00056  -0.11246 121 LEU   B N   
2605 C CA  . LEU   B 28  ? 0.75018 1.07449 0.81088 0.08131  0.00032  -0.13437 121 LEU   B CA  
2606 C C   . LEU   B 28  ? 0.76201 1.12358 0.84424 0.08546  0.00887  -0.14622 121 LEU   B C   
2607 O O   . LEU   B 28  ? 0.85336 1.22660 0.94381 0.10343  0.00153  -0.16580 121 LEU   B O   
2608 C CB  . LEU   B 28  ? 0.77511 1.11242 0.81909 0.07689  0.00971  -0.13692 121 LEU   B CB  
2609 C CG  . LEU   B 28  ? 0.82707 1.13255 0.84935 0.07585  -0.00017 -0.13038 121 LEU   B CG  
2610 C CD1 . LEU   B 28  ? 0.87191 1.19423 0.87652 0.07258  0.00971  -0.13491 121 LEU   B CD1 
2611 C CD2 . LEU   B 28  ? 0.84676 1.12561 0.86488 0.09229  -0.01937 -0.14165 121 LEU   B CD2 
2612 N N   . ASN   B 29  ? 0.76289 1.14340 0.85483 0.06940  0.02341  -0.13558 122 ASN   B N   
2613 C CA  . ASN   B 29  ? 0.95659 1.37678 1.07023 0.07047  0.03299  -0.14734 122 ASN   B CA  
2614 C C   . ASN   B 29  ? 0.87604 1.28932 1.00645 0.08319  0.01961  -0.15359 122 ASN   B C   
2615 O O   . ASN   B 29  ? 0.96518 1.40919 1.11317 0.09496  0.01956  -0.17235 122 ASN   B O   
2616 C CB  . ASN   B 29  ? 0.94615 1.38225 1.06354 0.04814  0.05048  -0.13301 122 ASN   B CB  
2617 C CG  . ASN   B 29  ? 1.08980 1.54785 1.19340 0.03695  0.06679  -0.13391 122 ASN   B CG  
2618 O OD1 . ASN   B 29  ? 1.04051 1.49220 1.12653 0.04310  0.06427  -0.13911 122 ASN   B OD1 
2619 N ND2 . ASN   B 29  ? 1.20829 1.69078 1.31769 0.01948  0.08341  -0.12884 122 ASN   B ND2 
2620 N N   . LYS   B 30  ? 1.01264 1.38714 1.13754 0.08108  0.00800  -0.13896 123 LYS   B N   
2621 C CA  . LYS   B 30  ? 1.07460 1.43782 1.21010 0.09259  -0.00571 -0.14376 123 LYS   B CA  
2622 C C   . LYS   B 30  ? 1.04358 1.39211 1.17276 0.11550  -0.02358 -0.16084 123 LYS   B C   
2623 O O   . LYS   B 30  ? 1.06890 1.41549 1.20726 0.12951  -0.03563 -0.17078 123 LYS   B O   
2624 C CB  . LYS   B 30  ? 1.06749 1.39405 1.19651 0.08188  -0.01148 -0.12321 123 LYS   B CB  
2625 C CG  . LYS   B 30  ? 1.05643 1.33939 1.16519 0.08517  -0.02564 -0.11670 123 LYS   B CG  
2626 C CD  . LYS   B 30  ? 0.93347 1.18456 1.03967 0.08331  -0.03668 -0.10645 123 LYS   B CD  
2627 C CE  . LYS   B 30  ? 0.83239 1.09009 0.94777 0.06604  -0.02519 -0.09077 123 LYS   B CE  
2628 N NZ  . LYS   B 30  ? 0.78483 1.01485 0.89713 0.06427  -0.03474 -0.08235 123 LYS   B NZ  
2629 N N   . GLU   B 31  ? 1.07089 1.40706 1.18321 0.12023  -0.02688 -0.16489 124 GLU   B N   
2630 C CA  . GLU   B 31  ? 1.21362 1.53555 1.31873 0.14286  -0.04413 -0.18311 124 GLU   B CA  
2631 C C   . GLU   B 31  ? 1.25341 1.61923 1.37752 0.15988  -0.04177 -0.20850 124 GLU   B C   
2632 O O   . GLU   B 31  ? 1.34853 1.70529 1.47371 0.18215  -0.05889 -0.22546 124 GLU   B O   
2633 C CB  . GLU   B 31  ? 1.42777 1.73056 1.51120 0.14293  -0.04673 -0.18301 124 GLU   B CB  
2634 C CG  . GLU   B 31  ? 1.61483 1.88437 1.68403 0.16299  -0.06849 -0.19609 124 GLU   B CG  
2635 C CD  . GLU   B 31  ? 1.50568 1.72495 1.55263 0.15382  -0.07929 -0.18012 124 GLU   B CD  
2636 O OE1 . GLU   B 31  ? 1.18086 1.38711 1.22772 0.13543  -0.07425 -0.15930 124 GLU   B OE1 
2637 O OE2 . GLU   B 31  ? 1.24559 1.43957 1.27579 0.16473  -0.09276 -0.18939 124 GLU   B OE2 
2638 N N   . LYS   B 32  ? 1.31288 1.72628 1.45170 0.14952  -0.02116 -0.21204 125 LYS   B N   
2639 C CA  . LYS   B 32  ? 1.07057 1.53394 1.23241 0.16234  -0.01607 -0.23649 125 LYS   B CA  
2640 C C   . LYS   B 32  ? 1.06822 1.54400 1.25268 0.16511  -0.02038 -0.23841 125 LYS   B C   
2641 O O   . LYS   B 32  ? 1.17446 1.68490 1.37961 0.18180  -0.02377 -0.26146 125 LYS   B O   
2642 C CB  . LYS   B 32  ? 1.23595 1.74575 1.40283 0.14671  0.00901  -0.23913 125 LYS   B CB  
2643 C CG  . LYS   B 32  ? 1.27577 1.77975 1.41999 0.14659  0.01325  -0.24163 125 LYS   B CG  
2644 C CD  . LYS   B 32  ? 1.23621 1.75014 1.36910 0.12013  0.03431  -0.22403 125 LYS   B CD  
2645 C CE  . LYS   B 32  ? 1.41142 1.91533 1.51849 0.12045  0.03634  -0.22560 125 LYS   B CE  
2646 N NZ  . LYS   B 32  ? 1.47688 1.98034 1.56741 0.09546  0.05301  -0.20576 125 LYS   B NZ  
2647 N N   . THR   B 33  ? 1.07388 1.52380 1.25540 0.14981  -0.02073 -0.21601 126 THR   B N   
2648 C CA  . THR   B 33  ? 1.01177 1.46785 1.21131 0.15292  -0.02706 -0.21716 126 THR   B CA  
2649 C C   . THR   B 33  ? 0.97705 1.39894 1.16986 0.17653  -0.05337 -0.22591 126 THR   B C   
2650 O O   . THR   B 33  ? 1.05848 1.49713 1.26866 0.19094  -0.06285 -0.24021 126 THR   B O   
2651 C CB  . THR   B 33  ? 1.06806 1.50524 1.26404 0.12973  -0.01947 -0.19123 126 THR   B CB  
2652 O OG1 . THR   B 33  ? 0.97024 1.43250 1.16801 0.10838  0.00291  -0.18243 126 THR   B OG1 
2653 C CG2 . THR   B 33  ? 1.09955 1.54684 1.31417 0.13150  -0.02444 -0.19314 126 THR   B CG2 
2654 N N   . TYR   B 34  ? 1.02030 1.39306 1.18687 0.18044  -0.06632 -0.21778 127 TYR   B N   
2655 C CA  . TYR   B 34  ? 0.95177 1.28143 1.10444 0.19986  -0.09224 -0.22278 127 TYR   B CA  
2656 C C   . TYR   B 34  ? 0.98005 1.31443 1.12940 0.22440  -0.10344 -0.24722 127 TYR   B C   
2657 O O   . TYR   B 34  ? 1.04285 1.36221 1.17530 0.22300  -0.10220 -0.24636 127 TYR   B O   
2658 C CB  . TYR   B 34  ? 0.95749 1.22921 1.08260 0.18693  -0.09961 -0.19929 127 TYR   B CB  
2659 C CG  . TYR   B 34  ? 0.91359 1.17685 1.04120 0.16677  -0.09226 -0.17776 127 TYR   B CG  
2660 C CD1 . TYR   B 34  ? 0.77473 1.05792 0.90913 0.14407  -0.07104 -0.16309 127 TYR   B CD1 
2661 C CD2 . TYR   B 34  ? 0.74111 0.97456 0.86213 0.17105  -0.10736 -0.17260 127 TYR   B CD2 
2662 C CE1 . TYR   B 34  ? 0.82666 1.10187 0.96351 0.12728  -0.06505 -0.14517 127 TYR   B CE1 
2663 C CE2 . TYR   B 34  ? 0.81030 1.03704 0.93285 0.15320  -0.10035 -0.15438 127 TYR   B CE2 
2664 C CZ  . TYR   B 34  ? 0.76712 1.01557 0.89873 0.13188  -0.07916 -0.14136 127 TYR   B CZ  
2665 O OH  . TYR   B 34  ? 0.61897 0.86024 0.75216 0.11570  -0.07297 -0.12486 127 TYR   B OH  
2666 N N   . LEU   B 35  ? 0.98741 1.34304 1.15319 0.24780  -0.11530 -0.27012 128 LEU   B N   
2667 C CA  . LEU   B 35  ? 0.89900 1.26321 1.06496 0.27473  -0.12726 -0.29715 128 LEU   B CA  
2668 C C   . LEU   B 35  ? 0.98497 1.28623 1.12502 0.29423  -0.15763 -0.29892 128 LEU   B C   
2669 O O   . LEU   B 35  ? 1.23237 1.49804 1.36334 0.29403  -0.17184 -0.28746 128 LEU   B O   
2670 C CB  . LEU   B 35  ? 0.90195 1.32791 1.10227 0.29163  -0.12441 -0.32452 128 LEU   B CB  
2671 C CG  . LEU   B 35  ? 0.93638 1.43080 1.15974 0.28142  -0.09690 -0.33613 128 LEU   B CG  
2672 C CD1 . LEU   B 35  ? 0.92922 1.43762 1.15635 0.24738  -0.07239 -0.31132 128 LEU   B CD1 
2673 C CD2 . LEU   B 35  ? 0.95399 1.50784 1.21209 0.30142  -0.09809 -0.36705 128 LEU   B CD2 
2674 N N   . ARG   B 36  ? 1.13470 1.42034 1.26034 0.31046  -0.16774 -0.31342 129 ARG   B N   
2675 C CA  . ARG   B 36  ? 1.27025 1.49601 1.36984 0.33147  -0.19804 -0.31919 129 ARG   B CA  
2676 C C   . ARG   B 36  ? 1.20302 1.44983 1.31034 0.36356  -0.20955 -0.35312 129 ARG   B C   
2677 O O   . ARG   B 36  ? 1.30419 1.59299 1.42231 0.36358  -0.19318 -0.36619 129 ARG   B O   
2678 C CB  . ARG   B 36  ? 1.29666 1.46265 1.36133 0.31538  -0.20237 -0.29810 129 ARG   B CB  
2679 C CG  . ARG   B 36  ? 1.32250 1.45501 1.37483 0.28876  -0.19853 -0.26686 129 ARG   B CG  
2680 C CD  . ARG   B 36  ? 1.40511 1.57179 1.46980 0.26000  -0.16941 -0.24955 129 ARG   B CD  
2681 N NE  . ARG   B 36  ? 1.26195 1.40315 1.31902 0.23673  -0.16523 -0.22262 129 ARG   B NE  
2682 C CZ  . ARG   B 36  ? 1.22583 1.38046 1.28704 0.21096  -0.14464 -0.20366 129 ARG   B CZ  
2683 N NH1 . ARG   B 36  ? 1.36935 1.55873 1.43918 0.20356  -0.12670 -0.20636 129 ARG   B NH1 
2684 N NH2 . ARG   B 36  ? 1.19829 1.32999 1.25331 0.19270  -0.14260 -0.18196 129 ARG   B NH2 
2685 N N   . ASP   B 37  ? 1.25076 1.46736 1.35097 0.39135  -0.23832 -0.36778 130 ASP   B N   
2686 C CA  . ASP   B 37  ? 1.37827 1.60880 1.48489 0.42653  -0.25436 -0.40219 130 ASP   B CA  
2687 C C   . ASP   B 37  ? 1.32361 1.47330 1.39057 0.44215  -0.28566 -0.40162 130 ASP   B C   
2688 O O   . ASP   B 37  ? 1.22662 1.32334 1.27414 0.44562  -0.30728 -0.39030 130 ASP   B O   
2689 C CB  . ASP   B 37  ? 1.34317 1.61825 1.48209 0.45001  -0.26247 -0.42541 130 ASP   B CB  
2690 C CG  . ASP   B 37  ? 1.45091 1.76854 1.60840 0.48109  -0.26847 -0.46372 130 ASP   B CG  
2691 O OD1 . ASP   B 37  ? 1.38751 1.67368 1.52208 0.49331  -0.28038 -0.47303 130 ASP   B OD1 
2692 O OD2 . ASP   B 37  ? 1.42894 1.80694 1.61627 0.48084  -0.25988 -0.47764 130 ASP   B OD2 
2693 N N   . GLN   B 38  ? 1.28532 1.42352 1.33797 0.45057  -0.28835 -0.41362 131 GLN   B N   
2694 C CA  . GLN   B 38  ? 1.34198 1.40097 1.35509 0.46373  -0.31801 -0.41361 131 GLN   B CA  
2695 C C   . GLN   B 38  ? 1.38461 1.42284 1.39534 0.50367  -0.35094 -0.43989 131 GLN   B C   
2696 O O   . GLN   B 38  ? 1.35300 1.31858 1.32782 0.51630  -0.37920 -0.44014 131 GLN   B O   
2697 C CB  . GLN   B 38  ? 1.37388 1.42759 1.37278 0.46232  -0.31237 -0.42099 131 GLN   B CB  
2698 C CG  . GLN   B 38  ? 1.38168 1.49525 1.40454 0.48870  -0.30693 -0.45749 131 GLN   B CG  
2699 C CD  . GLN   B 38  ? 1.40757 1.60382 1.46318 0.47016  -0.26990 -0.45790 131 GLN   B CD  
2700 O OE1 . GLN   B 38  ? 1.39621 1.61350 1.46494 0.44429  -0.25112 -0.43561 131 GLN   B OE1 
2701 N NE2 . GLN   B 38  ? 1.21915 1.46077 1.28579 0.48276  -0.25935 -0.48342 131 GLN   B NE2 
2702 N N   . HIS   B 39  ? 1.31774 1.41629 1.36313 0.51934  -0.34834 -0.45951 132 HIS   B N   
2703 C CA  . HIS   B 39  ? 1.35165 1.43997 1.39197 0.54180  -0.37635 -0.47649 132 HIS   B CA  
2704 C C   . HIS   B 39  ? 1.36358 1.47153 1.42168 0.54099  -0.37906 -0.47279 132 HIS   B C   
2705 O O   . HIS   B 39  ? 1.34834 1.49241 1.42392 0.55565  -0.38757 -0.49338 132 HIS   B O   
2706 C CB  . HIS   B 39  ? 1.44053 1.58726 1.50154 0.55678  -0.37227 -0.50639 132 HIS   B CB  
2707 C CG  . HIS   B 39  ? 1.31459 1.43930 1.35551 0.56061  -0.37383 -0.51232 132 HIS   B CG  
2708 N ND1 . HIS   B 39  ? 1.43539 1.62215 1.49736 0.56144  -0.35380 -0.53049 132 HIS   B ND1 
2709 C CD2 . HIS   B 39  ? 1.50281 1.54921 1.50292 0.56224  -0.39310 -0.50222 132 HIS   B CD2 
2710 C CE1 . HIS   B 39  ? 1.42420 1.57257 1.45984 0.56502  -0.36104 -0.53187 132 HIS   B CE1 
2711 N NE2 . HIS   B 39  ? 1.48855 1.55171 1.48702 0.56518  -0.38492 -0.51506 132 HIS   B NE2 
2712 N N   . PHE   B 40  ? 1.31714 1.40183 1.37099 0.52376  -0.37238 -0.44712 133 PHE   B N   
2713 C CA  . PHE   B 40  ? 1.28962 1.38866 1.35748 0.52203  -0.37598 -0.44214 133 PHE   B CA  
2714 C C   . PHE   B 40  ? 1.29723 1.33477 1.33305 0.53946  -0.41278 -0.44514 133 PHE   B C   
2715 O O   . PHE   B 40  ? 1.33224 1.38696 1.37971 0.54430  -0.41976 -0.44996 133 PHE   B O   
2716 C CB  . PHE   B 40  ? 1.15863 1.24802 1.22769 0.49639  -0.35969 -0.41172 133 PHE   B CB  
2717 C CG  . PHE   B 40  ? 1.16288 1.16238 1.18189 0.47918  -0.37312 -0.38249 133 PHE   B CG  
2718 C CD1 . PHE   B 40  ? 1.19812 1.13569 1.18824 0.48687  -0.40079 -0.37288 133 PHE   B CD1 
2719 C CD2 . PHE   B 40  ? 1.34491 1.32320 1.34536 0.45379  -0.35759 -0.36454 133 PHE   B CD2 
2720 C CE1 . PHE   B 40  ? 1.24170 1.09846 1.18481 0.46805  -0.41127 -0.34607 133 PHE   B CE1 
2721 C CE2 . PHE   B 40  ? 1.30620 1.20682 1.26332 0.43588  -0.36858 -0.33889 133 PHE   B CE2 
2722 C CZ  . PHE   B 40  ? 1.15093 0.99115 1.07916 0.44200  -0.39454 -0.32950 133 PHE   B CZ  
2723 N N   . LEU   B 41  ? 1.33425 1.29922 1.32817 0.54779  -0.43654 -0.44240 134 LEU   B N   
2724 C CA  . LEU   B 41  ? 1.43514 1.33760 1.39351 0.56339  -0.47250 -0.44520 134 LEU   B CA  
2725 C C   . LEU   B 41  ? 1.45988 1.40097 1.43414 0.58874  -0.48663 -0.47792 134 LEU   B C   
2726 O O   . LEU   B 41  ? 1.49519 1.39605 1.44592 0.60353  -0.51585 -0.48376 134 LEU   B O   
2727 C CB  . LEU   B 41  ? 1.40548 1.21913 1.31303 0.56152  -0.49284 -0.43195 134 LEU   B CB  
2728 C CG  . LEU   B 41  ? 1.43970 1.19620 1.32086 0.53637  -0.48726 -0.39792 134 LEU   B CG  
2729 C CD1 . LEU   B 41  ? 1.51866 1.19231 1.35115 0.53140  -0.50500 -0.38707 134 LEU   B CD1 
2730 C CD2 . LEU   B 41  ? 1.37804 1.10684 1.24599 0.53075  -0.49817 -0.38216 134 LEU   B CD2 
2731 N N   . GLU   B 42  ? 1.43285 1.44971 1.44456 0.59355  -0.46706 -0.49952 135 GLU   B N   
2732 C CA  . GLU   B 42  ? 1.42754 1.49244 1.46100 0.61544  -0.47718 -0.53123 135 GLU   B CA  
2733 C C   . GLU   B 42  ? 1.48528 1.59058 1.54484 0.61455  -0.47356 -0.53585 135 GLU   B C   
2734 O O   . GLU   B 42  ? 1.47048 1.59506 1.53841 0.63437  -0.49084 -0.55983 135 GLU   B O   
2735 C CB  . GLU   B 42  ? 1.40432 1.54210 1.47057 0.61687  -0.45434 -0.55141 135 GLU   B CB  
2736 C CG  . GLU   B 42  ? 1.46454 1.56581 1.50559 0.62256  -0.46154 -0.55287 135 GLU   B CG  
2737 C CD  . GLU   B 42  ? 1.47315 1.64708 1.54499 0.62151  -0.43637 -0.57097 135 GLU   B CD  
2738 O OE1 . GLU   B 42  ? 1.35410 1.60422 1.46520 0.61073  -0.40921 -0.57739 135 GLU   B OE1 
2739 O OE2 . GLU   B 42  ? 1.66880 1.82249 1.72391 0.63013  -0.44364 -0.57827 135 GLU   B OE2 
2740 N N   . GLN   B 43  ? 1.38012 1.49873 1.45285 0.59231  -0.45216 -0.51409 136 GLN   B N   
2741 C CA  . GLN   B 43  ? 1.38751 1.53221 1.47907 0.58990  -0.45137 -0.51459 136 GLN   B CA  
2742 C C   . GLN   B 43  ? 1.30851 1.37540 1.35967 0.59905  -0.48417 -0.50456 136 GLN   B C   
2743 O O   . GLN   B 43  ? 1.28681 1.36789 1.34791 0.60418  -0.49177 -0.51109 136 GLN   B O   
2744 C CB  . GLN   B 43  ? 1.33102 1.51287 1.44801 0.56257  -0.41890 -0.49348 136 GLN   B CB  
2745 C CG  . GLN   B 43  ? 1.27435 1.53086 1.42780 0.54939  -0.38434 -0.50049 136 GLN   B CG  
2746 C CD  . GLN   B 43  ? 1.28603 1.57206 1.46002 0.52172  -0.35438 -0.47789 136 GLN   B CD  
2747 O OE1 . GLN   B 43  ? 1.28351 1.63116 1.48650 0.50705  -0.32446 -0.48104 136 GLN   B OE1 
2748 N NE2 . GLN   B 43  ? 1.25721 1.49832 1.41427 0.51361  -0.36272 -0.45457 136 GLN   B NE2 
2749 N N   . HIS   B 44  ? 1.39507 1.37885 1.39906 0.59962  -0.50341 -0.48857 137 HIS   B N   
2750 C CA  . HIS   B 44  ? 1.30115 1.20173 1.25820 0.60539  -0.53509 -0.47690 137 HIS   B CA  
2751 C C   . HIS   B 44  ? 1.55181 1.40133 1.47393 0.62594  -0.56534 -0.49103 137 HIS   B C   
2752 O O   . HIS   B 44  ? 1.60220 1.38643 1.48607 0.61905  -0.57425 -0.47458 137 HIS   B O   
2753 C CB  . HIS   B 44  ? 1.37482 1.21634 1.30216 0.58134  -0.52991 -0.44028 137 HIS   B CB  
2754 C CG  . HIS   B 44  ? 1.31437 1.20836 1.27724 0.56005  -0.49819 -0.42522 137 HIS   B CG  
2755 N ND1 . HIS   B 44  ? 1.30046 1.19823 1.26823 0.55267  -0.49766 -0.41459 137 HIS   B ND1 
2756 C CD2 . HIS   B 44  ? 1.36071 1.30508 1.35482 0.54448  -0.46669 -0.41919 137 HIS   B CD2 
2757 C CE1 . HIS   B 44  ? 1.22117 1.17016 1.22253 0.53329  -0.46775 -0.40245 137 HIS   B CE1 
2758 N NE2 . HIS   B 44  ? 1.34212 1.31982 1.35968 0.52792  -0.44851 -0.40493 137 HIS   B NE2 
2759 N N   . PRO   B 45  ? 1.67065 1.54818 1.60470 0.65089  -0.58228 -0.52177 138 PRO   B N   
2760 C CA  . PRO   B 45  ? 1.69111 1.52657 1.59528 0.67217  -0.61135 -0.53757 138 PRO   B CA  
2761 C C   . PRO   B 45  ? 1.66801 1.39781 1.50948 0.67257  -0.64363 -0.51966 138 PRO   B C   
2762 O O   . PRO   B 45  ? 1.70631 1.38784 1.51579 0.68165  -0.66365 -0.52282 138 PRO   B O   
2763 C CB  . PRO   B 45  ? 1.67566 1.56628 1.60817 0.69810  -0.62319 -0.57362 138 PRO   B CB  
2764 C CG  . PRO   B 45  ? 1.58787 1.56747 1.57465 0.68651  -0.59048 -0.57849 138 PRO   B CG  
2765 C CD  . PRO   B 45  ? 1.55708 1.50978 1.53455 0.66036  -0.57499 -0.54466 138 PRO   B CD  
2766 N N   . LEU   B 46  ? 1.68442 1.37624 1.50581 0.66176  -0.64912 -0.50055 139 LEU   B N   
2767 C CA  . LEU   B 46  ? 1.76700 1.35753 1.52548 0.65882  -0.67862 -0.48231 139 LEU   B CA  
2768 C C   . LEU   B 46  ? 1.78647 1.31818 1.51137 0.63371  -0.67099 -0.45122 139 LEU   B C   
2769 O O   . LEU   B 46  ? 1.77696 1.22246 1.44620 0.62949  -0.69541 -0.43709 139 LEU   B O   
2770 C CB  . LEU   B 46  ? 1.87369 1.44547 1.62146 0.65407  -0.68525 -0.47200 139 LEU   B CB  
2771 C CG  . LEU   B 46  ? 1.93579 1.41344 1.62107 0.65947  -0.72195 -0.46430 139 LEU   B CG  
2772 C CD1 . LEU   B 46  ? 1.73016 1.20119 1.40626 0.69187  -0.75378 -0.49627 139 LEU   B CD1 
2773 C CD2 . LEU   B 46  ? 1.79152 1.25836 1.47048 0.65198  -0.72296 -0.45250 139 LEU   B CD2 
2774 N N   . LEU   B 47  ? 1.67046 1.24571 1.42642 0.61626  -0.63824 -0.44076 140 LEU   B N   
2775 C CA  . LEU   B 47  ? 1.63913 1.16473 1.36800 0.59122  -0.62845 -0.41202 140 LEU   B CA  
2776 C C   . LEU   B 47  ? 1.67402 1.20034 1.40239 0.59696  -0.62794 -0.42210 140 LEU   B C   
2777 O O   . LEU   B 47  ? 1.67944 1.26755 1.44276 0.61584  -0.62302 -0.44932 140 LEU   B O   
2778 C CB  . LEU   B 47  ? 1.52659 1.09474 1.28733 0.56790  -0.59375 -0.39297 140 LEU   B CB  
2779 C CG  . LEU   B 47  ? 1.55415 1.12272 1.31643 0.55820  -0.59072 -0.37874 140 LEU   B CG  
2780 C CD1 . LEU   B 47  ? 1.43012 1.04617 1.22696 0.53644  -0.55641 -0.36134 140 LEU   B CD1 
2781 C CD2 . LEU   B 47  ? 1.59976 1.07112 1.29934 0.54702  -0.61493 -0.35591 140 LEU   B CD2 
2782 N N   . GLN   B 48  ? 1.73401 1.19092 1.42150 0.57881  -0.63250 -0.39953 141 GLN   B N   
2783 C CA  . GLN   B 48  ? 1.72482 1.17309 1.40702 0.57969  -0.63115 -0.40446 141 GLN   B CA  
2784 C C   . GLN   B 48  ? 1.74400 1.19041 1.43114 0.55125  -0.60317 -0.38123 141 GLN   B C   
2785 O O   . GLN   B 48  ? 1.72373 1.14357 1.39830 0.52845  -0.59439 -0.35561 141 GLN   B O   
2786 C CB  . GLN   B 48  ? 1.85191 1.21305 1.47673 0.58434  -0.66576 -0.40118 141 GLN   B CB  
2787 C CG  . GLN   B 48  ? 1.83602 1.19299 1.45200 0.61469  -0.69696 -0.42612 141 GLN   B CG  
2788 C CD  . GLN   B 48  ? 1.80098 1.23865 1.46421 0.64197  -0.69184 -0.46098 141 GLN   B CD  
2789 O OE1 . GLN   B 48  ? 1.95351 1.42598 1.63888 0.64097  -0.67459 -0.46734 141 GLN   B OE1 
2790 N NE2 . GLN   B 48  ? 1.81735 1.28573 1.49563 0.66558  -0.70641 -0.48431 141 GLN   B NE2 
2791 N N   . PRO   B 49  ? 1.69187 1.16680 1.39694 0.55196  -0.58874 -0.39034 142 PRO   B N   
2792 C CA  . PRO   B 49  ? 1.63426 1.11008 1.34547 0.52568  -0.56176 -0.37115 142 PRO   B CA  
2793 C C   . PRO   B 49  ? 1.62108 1.00687 1.28091 0.49850  -0.57101 -0.34100 142 PRO   B C   
2794 O O   . PRO   B 49  ? 1.55381 0.93573 1.21679 0.47317  -0.54981 -0.32105 142 PRO   B O   
2795 C CB  . PRO   B 49  ? 1.55358 1.06709 1.28444 0.53546  -0.55176 -0.39092 142 PRO   B CB  
2796 C CG  . PRO   B 49  ? 1.59808 1.16671 1.35558 0.56619  -0.56115 -0.42189 142 PRO   B CG  
2797 C CD  . PRO   B 49  ? 1.70175 1.22013 1.42783 0.57719  -0.59340 -0.42080 142 PRO   B CD  
2798 N N   . LYS   B 50  ? 1.65551 0.96956 1.26758 0.50139  -0.60160 -0.33721 143 LYS   B N   
2799 C CA  . LYS   B 50  ? 1.72465 0.95457 1.28604 0.47151  -0.60907 -0.30801 143 LYS   B CA  
2800 C C   . LYS   B 50  ? 1.76559 0.97347 1.31368 0.45145  -0.60442 -0.28386 143 LYS   B C   
2801 O O   . LYS   B 50  ? 1.66011 0.82616 1.18457 0.41922  -0.59473 -0.25758 143 LYS   B O   
2802 C CB  . LYS   B 50  ? 1.92607 1.08700 1.43879 0.47968  -0.64319 -0.31066 143 LYS   B CB  
2803 C CG  . LYS   B 50  ? 1.94325 1.01700 1.40039 0.44651  -0.65161 -0.28075 143 LYS   B CG  
2804 C CD  . LYS   B 50  ? 2.03370 1.05490 1.45517 0.45036  -0.67446 -0.28538 143 LYS   B CD  
2805 C CE  . LYS   B 50  ? 2.19971 1.25761 1.64961 0.45325  -0.65863 -0.29809 143 LYS   B CE  
2806 N NZ  . LYS   B 50  ? 2.16682 1.17296 1.58233 0.45625  -0.68060 -0.30193 143 LYS   B NZ  
2807 N N   . MET   B 51  ? 1.70976 0.94689 1.27297 0.46874  -0.61059 -0.29288 144 MET   B N   
2808 C CA  . MET   B 51  ? 1.72092 0.94093 1.27257 0.45116  -0.60611 -0.27095 144 MET   B CA  
2809 C C   . MET   B 51  ? 1.56687 0.82398 1.14920 0.42943  -0.57308 -0.25492 144 MET   B C   
2810 O O   . MET   B 51  ? 1.60789 0.82823 1.16700 0.40224  -0.56700 -0.22781 144 MET   B O   
2811 C CB  . MET   B 51  ? 1.62597 0.88140 1.19562 0.47576  -0.61691 -0.28786 144 MET   B CB  
2812 C CG  . MET   B 51  ? 1.83349 1.05937 1.37777 0.50136  -0.65038 -0.30828 144 MET   B CG  
2813 S SD  . MET   B 51  ? 1.82507 1.09664 1.39408 0.52977  -0.66207 -0.33139 144 MET   B SD  
2814 C CE  . MET   B 51  ? 1.88753 1.11876 1.42431 0.55920  -0.70195 -0.35624 144 MET   B CE  
2815 N N   . ARG   B 52  ? 1.56887 0.89875 1.20176 0.44021  -0.55141 -0.27139 145 ARG   B N   
2816 C CA  . ARG   B 52  ? 1.53255 0.91579 1.19619 0.40944  -0.51388 -0.25453 145 ARG   B CA  
2817 C C   . ARG   B 52  ? 1.47238 0.81226 1.10665 0.37140  -0.50318 -0.23037 145 ARG   B C   
2818 O O   . ARG   B 52  ? 1.47428 0.82559 1.11082 0.33658  -0.48024 -0.20568 145 ARG   B O   
2819 C CB  . ARG   B 52  ? 1.41040 0.88667 1.13003 0.42227  -0.49052 -0.27656 145 ARG   B CB  
2820 C CG  . ARG   B 52  ? 1.33042 0.86793 1.08160 0.38798  -0.45038 -0.25929 145 ARG   B CG  
2821 C CD  . ARG   B 52  ? 1.34037 0.96396 1.14094 0.40064  -0.42905 -0.28116 145 ARG   B CD  
2822 N NE  . ARG   B 52  ? 1.23013 0.90425 1.05551 0.36813  -0.39299 -0.26423 145 ARG   B NE  
2823 C CZ  . ARG   B 52  ? 1.21784 0.88833 1.03742 0.34733  -0.37894 -0.25533 145 ARG   B CZ  
2824 N NH1 . ARG   B 52  ? 1.27872 0.89879 1.06923 0.35345  -0.39631 -0.26138 145 ARG   B NH1 
2825 N NH2 . ARG   B 52  ? 1.16464 0.88177 1.00744 0.32022  -0.34801 -0.24050 145 ARG   B NH2 
2826 N N   . ALA   B 53  ? 1.55486 0.84574 1.16220 0.37772  -0.52004 -0.23835 146 ALA   B N   
2827 C CA  . ALA   B 53  ? 1.46089 0.70886 1.03995 0.34159  -0.51222 -0.21722 146 ALA   B CA  
2828 C C   . ALA   B 53  ? 1.59628 0.76931 1.12658 0.31650  -0.52396 -0.19036 146 ALA   B C   
2829 O O   . ALA   B 53  ? 1.52384 0.69219 1.04669 0.27720  -0.50410 -0.16629 146 ALA   B O   
2830 C CB  . ALA   B 53  ? 1.48032 0.68973 1.03998 0.35595  -0.53052 -0.23396 146 ALA   B CB  
2831 N N   . ILE   B 54  ? 1.63481 0.74923 1.13075 0.33876  -0.55636 -0.19468 147 ILE   B N   
2832 C CA  . ILE   B 54  ? 1.64491 0.68823 1.08955 0.31369  -0.56771 -0.16882 147 ILE   B CA  
2833 C C   . ILE   B 54  ? 1.67085 0.75190 1.13300 0.29058  -0.54309 -0.14915 147 ILE   B C   
2834 O O   . ILE   B 54  ? 1.64074 0.68707 1.07405 0.25378  -0.53414 -0.12309 147 ILE   B O   
2835 C CB  . ILE   B 54  ? 1.81294 0.82036 1.22448 0.33479  -0.59971 -0.17732 147 ILE   B CB  
2836 C CG1 . ILE   B 54  ? 1.79937 0.78994 1.20001 0.35429  -0.61964 -0.19670 147 ILE   B CG1 
2837 C CG2 . ILE   B 54  ? 1.89680 0.83290 1.25119 0.30563  -0.60979 -0.15075 147 ILE   B CG2 
2838 C CD1 . ILE   B 54  ? 2.03656 0.99689 1.40898 0.37960  -0.65258 -0.20984 147 ILE   B CD1 
2839 N N   . LEU   B 55  ? 1.58041 0.73865 1.09122 0.30949  -0.53002 -0.16177 148 LEU   B N   
2840 C CA  . LEU   B 55  ? 1.57570 0.77646 1.10601 0.28808  -0.50592 -0.14473 148 LEU   B CA  
2841 C C   . LEU   B 55  ? 1.50943 0.75610 1.06528 0.25118  -0.46892 -0.12944 148 LEU   B C   
2842 O O   . LEU   B 55  ? 1.49875 0.73463 1.04087 0.21801  -0.45422 -0.10577 148 LEU   B O   
2843 C CB  . LEU   B 55  ? 1.43829 0.70848 1.01410 0.31811  -0.50317 -0.16389 148 LEU   B CB  
2844 C CG  . LEU   B 55  ? 1.49775 0.81189 1.09443 0.29899  -0.48042 -0.14858 148 LEU   B CG  
2845 C CD1 . LEU   B 55  ? 1.47050 0.71478 1.01585 0.28635  -0.49728 -0.12855 148 LEU   B CD1 
2846 C CD2 . LEU   B 55  ? 1.56239 0.95154 1.20901 0.32691  -0.47575 -0.16969 148 LEU   B CD2 
2847 N N   . LEU   B 56  ? 1.47586 0.77460 1.06837 0.25708  -0.45390 -0.14348 149 LEU   B N   
2848 C CA  . LEU   B 56  ? 1.35371 0.69619 0.97079 0.22494  -0.42101 -0.13047 149 LEU   B CA  
2849 C C   . LEU   B 56  ? 1.42775 0.70982 1.00513 0.19135  -0.42219 -0.11057 149 LEU   B C   
2850 O O   . LEU   B 56  ? 1.41057 0.70978 0.99412 0.15788  -0.39893 -0.09144 149 LEU   B O   
2851 C CB  . LEU   B 56  ? 1.35013 0.75204 1.00718 0.23962  -0.40849 -0.15021 149 LEU   B CB  
2852 C CG  . LEU   B 56  ? 1.22271 0.69825 0.92571 0.26614  -0.39983 -0.16925 149 LEU   B CG  
2853 C CD1 . LEU   B 56  ? 1.28754 0.81749 1.02387 0.27618  -0.38592 -0.18705 149 LEU   B CD1 
2854 C CD2 . LEU   B 56  ? 1.20904 0.73022 0.93643 0.24814  -0.37646 -0.15444 149 LEU   B CD2 
2855 N N   . ASP   B 57  ? 1.48341 0.69450 1.01988 0.19949  -0.44951 -0.11561 150 ASP   B N   
2856 C CA  . ASP   B 57  ? 1.55359 0.70221 1.04882 0.16578  -0.45249 -0.09695 150 ASP   B CA  
2857 C C   . ASP   B 57  ? 1.65433 0.76516 1.11723 0.14014  -0.45168 -0.07310 150 ASP   B C   
2858 O O   . ASP   B 57  ? 1.61599 0.71445 1.06596 0.10189  -0.43643 -0.05365 150 ASP   B O   
2859 C CB  . ASP   B 57  ? 1.68529 0.75956 1.13968 0.18158  -0.48496 -0.10808 150 ASP   B CB  
2860 C CG  . ASP   B 57  ? 1.91362 0.92119 1.32414 0.14485  -0.48878 -0.08959 150 ASP   B CG  
2861 O OD1 . ASP   B 57  ? 2.02059 1.05392 1.44837 0.12237  -0.47022 -0.08639 150 ASP   B OD1 
2862 O OD2 . ASP   B 57  ? 2.04517 0.97427 1.40307 0.13772  -0.51068 -0.07837 150 ASP   B OD2 
2863 N N   . TRP   B 58  ? 1.63453 0.72840 1.08409 0.16069  -0.46801 -0.07520 151 TRP   B N   
2864 C CA  . TRP   B 58  ? 1.50922 0.57027 0.92730 0.13772  -0.46673 -0.05323 151 TRP   B CA  
2865 C C   . TRP   B 58  ? 1.56307 0.69492 1.02001 0.11328  -0.43059 -0.04106 151 TRP   B C   
2866 O O   . TRP   B 58  ? 1.55533 0.66931 0.99185 0.07780  -0.41758 -0.02005 151 TRP   B O   
2867 C CB  . TRP   B 58  ? 1.77272 0.80348 1.17001 0.16883  -0.49395 -0.06043 151 TRP   B CB  
2868 C CG  . TRP   B 58  ? 1.84539 0.85150 1.21386 0.14878  -0.49161 -0.03970 151 TRP   B CG  
2869 C CD1 . TRP   B 58  ? 1.92665 0.86171 1.23907 0.11680  -0.49699 -0.01739 151 TRP   B CD1 
2870 C CD2 . TRP   B 58  ? 1.74874 0.80077 1.14123 0.15860  -0.48328 -0.03996 151 TRP   B CD2 
2871 N NE1 . TRP   B 58  ? 1.97469 0.90926 1.27386 0.10663  -0.49196 -0.00378 151 TRP   B NE1 
2872 C CE2 . TRP   B 58  ? 1.88066 0.88579 1.22864 0.13250  -0.48422 -0.01744 151 TRP   B CE2 
2873 C CE3 . TRP   B 58  ? 1.75492 0.88328 1.20145 0.18548  -0.47476 -0.05732 151 TRP   B CE3 
2874 C CZ2 . TRP   B 58  ? 1.84630 0.87772 1.20206 0.13412  -0.47787 -0.01228 151 TRP   B CZ2 
2875 C CZ3 . TRP   B 58  ? 1.63398 0.78809 1.08937 0.18606  -0.46871 -0.05200 151 TRP   B CZ3 
2876 C CH2 . TRP   B 58  ? 1.73809 0.84354 1.14831 0.16137  -0.47076 -0.02989 151 TRP   B CH2 
2877 N N   . LEU   B 59  ? 1.55059 0.76289 1.06293 0.13123  -0.41392 -0.05461 152 LEU   B N   
2878 C CA  . LEU   B 59  ? 1.40027 0.67895 0.95023 0.11011  -0.38081 -0.04440 152 LEU   B CA  
2879 C C   . LEU   B 59  ? 1.42137 0.71278 0.97898 0.07619  -0.35872 -0.03300 152 LEU   B C   
2880 O O   . LEU   B 59  ? 1.39359 0.71063 0.96135 0.04886  -0.33592 -0.01796 152 LEU   B O   
2881 C CB  . LEU   B 59  ? 1.27443 0.63220 0.87945 0.13584  -0.36899 -0.06209 152 LEU   B CB  
2882 C CG  . LEU   B 59  ? 1.34581 0.70711 0.95388 0.16915  -0.38750 -0.07554 152 LEU   B CG  
2883 C CD1 . LEU   B 59  ? 1.34938 0.79373 1.01437 0.18973  -0.37250 -0.09354 152 LEU   B CD1 
2884 C CD2 . LEU   B 59  ? 1.26740 0.60771 0.85311 0.15663  -0.38856 -0.05949 152 LEU   B CD2 
2885 N N   . MET   B 60  ? 1.36104 0.63633 0.91481 0.07824  -0.36568 -0.04118 153 MET   B N   
2886 C CA  . MET   B 60  ? 1.39169 0.67468 0.95024 0.04608  -0.34801 -0.03128 153 MET   B CA  
2887 C C   . MET   B 60  ? 1.43853 0.66603 0.95398 0.01067  -0.34890 -0.01016 153 MET   B C   
2888 O O   . MET   B 60  ? 1.41685 0.67152 0.94482 -0.02017 -0.32543 0.00301  153 MET   B O   
2889 C CB  . MET   B 60  ? 1.45604 0.72410 1.01281 0.05631  -0.35945 -0.04510 153 MET   B CB  
2890 C CG  . MET   B 60  ? 1.43033 0.76032 1.03129 0.08491  -0.35306 -0.06555 153 MET   B CG  
2891 S SD  . MET   B 60  ? 1.51272 0.83106 1.11203 0.08674  -0.35972 -0.07821 153 MET   B SD  
2892 C CE  . MET   B 60  ? 1.38528 0.75856 1.02160 0.13016  -0.36171 -0.10568 153 MET   B CE  
2893 N N   . GLU   B 61  ? 1.55780 0.70645 1.02093 0.01446  -0.37625 -0.00726 154 GLU   B N   
2894 C CA  . GLU   B 61  ? 1.63861 0.72870 1.05438 -0.02086 -0.37800 0.01327  154 GLU   B CA  
2895 C C   . GLU   B 61  ? 1.57975 0.69459 0.99938 -0.03636 -0.36037 0.02743  154 GLU   B C   
2896 O O   . GLU   B 61  ? 1.55882 0.66989 0.96680 -0.07335 -0.34366 0.04371  154 GLU   B O   
2897 C CB  . GLU   B 61  ? 1.77277 0.76936 1.12817 -0.01015 -0.41345 0.01323  154 GLU   B CB  
2898 C CG  . GLU   B 61  ? 1.95580 0.88135 1.25548 -0.04982 -0.41754 0.03357  154 GLU   B CG  
2899 C CD  . GLU   B 61  ? 2.12588 0.95311 1.36348 -0.03852 -0.45491 0.03272  154 GLU   B CD  
2900 O OE1 . GLU   B 61  ? 2.06403 0.88077 1.30403 0.00283  -0.47831 0.01511  154 GLU   B OE1 
2901 O OE2 . GLU   B 61  ? 2.29171 1.07019 1.48429 -0.07038 -0.45739 0.04796  154 GLU   B OE2 
2902 N N   . VAL   B 62  ? 1.51446 0.65739 0.95165 -0.00867 -0.36349 0.02018  155 VAL   B N   
2903 C CA  . VAL   B 62  ? 1.40012 0.57037 0.84372 -0.02076 -0.34699 0.03164  155 VAL   B CA  
2904 C C   . VAL   B 62  ? 1.47264 0.71543 0.96271 -0.04292 -0.31230 0.03606  155 VAL   B C   
2905 O O   . VAL   B 62  ? 1.43687 0.68736 0.92097 -0.07086 -0.29493 0.05052  155 VAL   B O   
2906 C CB  . VAL   B 62  ? 1.47799 0.66939 0.93673 0.01544  -0.35813 0.02002  155 VAL   B CB  
2907 C CG1 . VAL   B 62  ? 1.43505 0.66299 0.90676 0.00373  -0.33916 0.02998  155 VAL   B CG1 
2908 C CG2 . VAL   B 62  ? 1.57284 0.68754 0.98102 0.03650  -0.39444 0.01679  155 VAL   B CG2 
2909 N N   . CYS   B 63  ? 1.43240 0.72819 0.96772 -0.03058 -0.30232 0.02319  156 CYS   B N   
2910 C CA  . CYS   B 63  ? 1.35491 0.71756 0.93388 -0.04866 -0.27198 0.02641  156 CYS   B CA  
2911 C C   . CYS   B 63  ? 1.33964 0.68453 0.90302 -0.08709 -0.26103 0.03914  156 CYS   B C   
2912 O O   . CYS   B 63  ? 1.26758 0.64913 0.84902 -0.11029 -0.23779 0.04803  156 CYS   B O   
2913 C CB  . CYS   B 63  ? 1.20749 0.62297 0.83135 -0.02707 -0.26639 0.01018  156 CYS   B CB  
2914 S SG  . CYS   B 63  ? 1.25443 0.71749 0.91215 0.01127  -0.26828 -0.00501 156 CYS   B SG  
2915 N N   . GLU   B 64  ? 1.33715 0.62725 0.86806 -0.09438 -0.27765 0.03902  157 GLU   B N   
2916 C CA  . GLU   B 64  ? 1.46998 0.74506 0.98771 -0.13250 -0.26756 0.04964  157 GLU   B CA  
2917 C C   . GLU   B 64  ? 1.49682 0.73810 0.97735 -0.16233 -0.26257 0.06719  157 GLU   B C   
2918 O O   . GLU   B 64  ? 1.52798 0.79090 1.01627 -0.19519 -0.24197 0.07611  157 GLU   B O   
2919 C CB  . GLU   B 64  ? 1.52850 0.74988 1.01871 -0.13309 -0.28812 0.04446  157 GLU   B CB  
2920 C CG  . GLU   B 64  ? 1.61225 0.82183 1.09275 -0.17302 -0.27821 0.05322  157 GLU   B CG  
2921 C CD  . GLU   B 64  ? 1.81305 0.96615 1.26465 -0.17399 -0.29995 0.04762  157 GLU   B CD  
2922 O OE1 . GLU   B 64  ? 1.82523 0.95380 1.26864 -0.14097 -0.32178 0.03525  157 GLU   B OE1 
2923 O OE2 . GLU   B 64  ? 1.88368 1.01785 1.32136 -0.20796 -0.29534 0.05454  157 GLU   B OE2 
2924 N N   . VAL   B 65  ? 1.60926 0.79873 1.04890 -0.15115 -0.28136 0.07154  158 VAL   B N   
2925 C CA  . VAL   B 65  ? 1.62745 0.77968 1.02517 -0.17925 -0.27786 0.08865  158 VAL   B CA  
2926 C C   . VAL   B 65  ? 1.53444 0.75197 0.96626 -0.19098 -0.24913 0.09349  158 VAL   B C   
2927 O O   . VAL   B 65  ? 1.56942 0.79142 0.99207 -0.22623 -0.23119 0.10492  158 VAL   B O   
2928 C CB  . VAL   B 65  ? 1.63579 0.72061 0.98346 -0.15979 -0.30621 0.09109  158 VAL   B CB  
2929 C CG1 . VAL   B 65  ? 1.76161 0.81369 1.06644 -0.18748 -0.30074 0.10896  158 VAL   B CG1 
2930 C CG2 . VAL   B 65  ? 1.65678 0.66762 0.96366 -0.15253 -0.33555 0.08757  158 VAL   B CG2 
2931 N N   . TYR   B 66  ? 1.47985 0.74970 0.95174 -0.16212 -0.24419 0.08393  159 TYR   B N   
2932 C CA  . TYR   B 66  ? 1.38759 0.72002 0.89446 -0.16936 -0.21851 0.08657  159 TYR   B CA  
2933 C C   . TYR   B 66  ? 1.33690 0.73909 0.89965 -0.17339 -0.19648 0.07969  159 TYR   B C   
2934 O O   . TYR   B 66  ? 1.26276 0.72113 0.86063 -0.17376 -0.17659 0.07916  159 TYR   B O   
2935 C CB  . TYR   B 66  ? 1.44491 0.79422 0.96275 -0.13845 -0.22520 0.08063  159 TYR   B CB  
2936 C CG  . TYR   B 66  ? 1.47072 0.75690 0.93402 -0.13661 -0.24465 0.08877  159 TYR   B CG  
2937 C CD1 . TYR   B 66  ? 1.58443 0.81170 1.01356 -0.11474 -0.27539 0.08410  159 TYR   B CD1 
2938 C CD2 . TYR   B 66  ? 1.49337 0.77729 0.93742 -0.15608 -0.23327 0.10055  159 TYR   B CD2 
2939 C CE1 . TYR   B 66  ? 1.62000 0.78574 0.99630 -0.11186 -0.29559 0.09173  159 TYR   B CE1 
2940 C CE2 . TYR   B 66  ? 1.65365 0.87716 1.04390 -0.15471 -0.25201 0.10861  159 TYR   B CE2 
2941 C CZ  . TYR   B 66  ? 1.68449 0.84791 1.04046 -0.13240 -0.28381 0.10458  159 TYR   B CZ  
2942 O OH  . TYR   B 66  ? 1.80397 0.90383 1.10378 -0.12971 -0.30479 0.11273  159 TYR   B OH  
2943 N N   . LYS   B 67  ? 1.38312 0.78033 0.95282 -0.17590 -0.20098 0.07420  160 LYS   B N   
2944 C CA  . LYS   B 67  ? 1.33387 0.79043 0.95086 -0.18212 -0.18244 0.06839  160 LYS   B CA  
2945 C C   . LYS   B 67  ? 1.18675 0.70465 0.85144 -0.15425 -0.17384 0.05822  160 LYS   B C   
2946 O O   . LYS   B 67  ? 1.07499 0.64898 0.77772 -0.16108 -0.15318 0.05760  160 LYS   B O   
2947 C CB  . LYS   B 67  ? 1.36712 0.84640 0.99005 -0.21846 -0.15997 0.07777  160 LYS   B CB  
2948 C CG  . LYS   B 67  ? 1.47939 0.90331 1.05811 -0.25092 -0.16573 0.08723  160 LYS   B CG  
2949 C CD  . LYS   B 67  ? 1.62063 1.07343 1.20747 -0.28728 -0.14173 0.09478  160 LYS   B CD  
2950 C CE  . LYS   B 67  ? 1.63216 1.03443 1.17830 -0.32265 -0.14600 0.10298  160 LYS   B CE  
2951 N NZ  . LYS   B 67  ? 1.66184 0.98405 1.14544 -0.32379 -0.16684 0.11230  160 LYS   B NZ  
2952 N N   . LEU   B 68  ? 1.16850 0.67531 0.83070 -0.12281 -0.19030 0.04958  161 LEU   B N   
2953 C CA  . LEU   B 68  ? 1.07177 0.63399 0.77653 -0.09725 -0.18312 0.03918  161 LEU   B CA  
2954 C C   . LEU   B 68  ? 0.98027 0.57259 0.71437 -0.08963 -0.17995 0.02918  161 LEU   B C   
2955 O O   . LEU   B 68  ? 1.11238 0.67345 0.82980 -0.09366 -0.19122 0.02655  161 LEU   B O   
2956 C CB  . LEU   B 68  ? 1.08322 0.62709 0.77679 -0.06697 -0.20159 0.03161  161 LEU   B CB  
2957 C CG  . LEU   B 68  ? 1.18306 0.69608 0.84603 -0.07034 -0.20771 0.04040  161 LEU   B CG  
2958 C CD1 . LEU   B 68  ? 1.12627 0.63050 0.78601 -0.03707 -0.22657 0.02997  161 LEU   B CD1 
2959 C CD2 . LEU   B 68  ? 1.02110 0.57645 0.70479 -0.08691 -0.18401 0.04832  161 LEU   B CD2 
2960 N N   . HIS   B 69  ? 0.94049 0.59182 0.71634 -0.07907 -0.16503 0.02369  162 HIS   B N   
2961 C CA  . HIS   B 69  ? 1.05246 0.73583 0.85567 -0.07283 -0.16021 0.01516  162 HIS   B CA  
2962 C C   . HIS   B 69  ? 0.97294 0.64260 0.77143 -0.04517 -0.17764 0.00153  162 HIS   B C   
2963 O O   . HIS   B 69  ? 0.98226 0.63437 0.76863 -0.02567 -0.19047 -0.00347 162 HIS   B O   
2964 C CB  . HIS   B 69  ? 0.91147 0.65738 0.75614 -0.07025 -0.13993 0.01429  162 HIS   B CB  
2965 C CG  . HIS   B 69  ? 0.97023 0.73696 0.82619 -0.09592 -0.12244 0.02405  162 HIS   B CG  
2966 N ND1 . HIS   B 69  ? 1.11262 0.87464 0.95926 -0.10889 -0.11532 0.03304  162 HIS   B ND1 
2967 C CD2 . HIS   B 69  ? 1.09224 0.88602 0.96841 -0.11010 -0.11122 0.02482  162 HIS   B CD2 
2968 C CE1 . HIS   B 69  ? 1.15730 0.94443 1.01922 -0.12979 -0.09957 0.03816  162 HIS   B CE1 
2969 N NE2 . HIS   B 69  ? 1.11877 0.92576 0.99962 -0.13050 -0.09738 0.03318  162 HIS   B NE2 
2970 N N   . ARG   B 70  ? 1.03602 0.71503 0.84445 -0.04306 -0.17855 -0.00570 163 ARG   B N   
2971 C CA  . ARG   B 70  ? 1.03514 0.70835 0.84247 -0.01653 -0.19275 -0.02077 163 ARG   B CA  
2972 C C   . ARG   B 70  ? 0.88533 0.60329 0.72026 0.00674  -0.18618 -0.02956 163 ARG   B C   
2973 O O   . ARG   B 70  ? 0.94422 0.65346 0.77404 0.03121  -0.19972 -0.04169 163 ARG   B O   
2974 C CB  . ARG   B 70  ? 0.96236 0.64392 0.77743 -0.02029 -0.19207 -0.02672 163 ARG   B CB  
2975 C CG  . ARG   B 70  ? 1.00750 0.64815 0.79807 -0.04499 -0.19840 -0.01953 163 ARG   B CG  
2976 C CD  . ARG   B 70  ? 1.06551 0.71664 0.86519 -0.04672 -0.19913 -0.02715 163 ARG   B CD  
2977 N NE  . ARG   B 70  ? 1.01974 0.63166 0.79657 -0.07128 -0.20620 -0.02158 163 ARG   B NE  
2978 C CZ  . ARG   B 70  ? 1.08219 0.63627 0.82417 -0.06993 -0.22676 -0.02505 163 ARG   B CZ  
2979 N NH1 . ARG   B 70  ? 1.11993 0.64819 0.84610 -0.04296 -0.24356 -0.03503 163 ARG   B NH1 
2980 N NH2 . ARG   B 70  ? 1.18622 0.70753 0.90891 -0.09634 -0.23112 -0.01915 163 ARG   B NH2 
2981 N N   . GLU   B 71  ? 0.83429 0.60066 0.69882 -0.00076 -0.16580 -0.02441 164 GLU   B N   
2982 C CA  . GLU   B 71  ? 0.81219 0.62113 0.70247 0.01704  -0.15793 -0.03137 164 GLU   B CA  
2983 C C   . GLU   B 71  ? 0.87324 0.66554 0.75215 0.02903  -0.16777 -0.03258 164 GLU   B C   
2984 O O   . GLU   B 71  ? 0.84246 0.65420 0.73347 0.05113  -0.17177 -0.04454 164 GLU   B O   
2985 C CB  . GLU   B 71  ? 0.84197 0.69623 0.76038 0.00354  -0.13586 -0.02331 164 GLU   B CB  
2986 C CG  . GLU   B 71  ? 1.00733 0.90305 0.95056 0.01661  -0.12618 -0.02790 164 GLU   B CG  
2987 C CD  . GLU   B 71  ? 0.90786 0.83197 0.86656 0.03444  -0.12529 -0.04146 164 GLU   B CD  
2988 O OE1 . GLU   B 71  ? 0.93174 0.84896 0.88507 0.03524  -0.12932 -0.04614 164 GLU   B OE1 
2989 O OE2 . GLU   B 71  ? 0.93582 0.89013 0.91168 0.04666  -0.12015 -0.04793 164 GLU   B OE2 
2990 N N   . THR   B 72  ? 0.92493 0.68183 0.77984 0.01437  -0.17208 -0.02098 165 THR   B N   
2991 C CA  . THR   B 72  ? 0.91938 0.65615 0.75928 0.02509  -0.18317 -0.02117 165 THR   B CA  
2992 C C   . THR   B 72  ? 0.89078 0.59216 0.70999 0.04900  -0.20767 -0.03385 165 THR   B C   
2993 O O   . THR   B 72  ? 0.87669 0.58720 0.70191 0.07078  -0.21613 -0.04359 165 THR   B O   
2994 C CB  . THR   B 72  ? 0.97331 0.67584 0.78645 0.00200  -0.18244 -0.00534 165 THR   B CB  
2995 O OG1 . THR   B 72  ? 0.93388 0.67342 0.76922 -0.01783 -0.15971 0.00392  165 THR   B OG1 
2996 C CG2 . THR   B 72  ? 0.92109 0.60172 0.71616 0.01313  -0.19465 -0.00497 165 THR   B CG2 
2997 N N   . PHE   B 73  ? 0.94601 0.60721 0.74146 0.04597  -0.22022 -0.03511 166 PHE   B N   
2998 C CA  . PHE   B 73  ? 0.99051 0.61562 0.76557 0.07055  -0.24505 -0.04871 166 PHE   B CA  
2999 C C   . PHE   B 73  ? 0.94697 0.61818 0.75340 0.09751  -0.24359 -0.06813 166 PHE   B C   
3000 O O   . PHE   B 73  ? 0.99044 0.66111 0.79750 0.12310  -0.25759 -0.08128 166 PHE   B O   
3001 C CB  . PHE   B 73  ? 0.98475 0.55849 0.72912 0.06053  -0.25791 -0.04679 166 PHE   B CB  
3002 C CG  . PHE   B 73  ? 1.05511 0.60066 0.78544 0.08823  -0.28145 -0.06432 166 PHE   B CG  
3003 C CD1 . PHE   B 73  ? 1.12643 0.62686 0.82864 0.10660  -0.30562 -0.06902 166 PHE   B CD1 
3004 C CD2 . PHE   B 73  ? 1.11120 0.67579 0.85605 0.09748  -0.28026 -0.07721 166 PHE   B CD2 
3005 C CE1 . PHE   B 73  ? 1.17646 0.65157 0.86688 0.13467  -0.32858 -0.08712 166 PHE   B CE1 
3006 C CE2 . PHE   B 73  ? 1.16547 0.70589 0.89804 0.12442  -0.30182 -0.09532 166 PHE   B CE2 
3007 C CZ  . PHE   B 73  ? 1.22476 0.72083 0.93108 0.14365  -0.32617 -0.10078 166 PHE   B CZ  
3008 N N   . TYR   B 74  ? 0.81397 0.52661 0.64633 0.09194  -0.22679 -0.07076 167 TYR   B N   
3009 C CA  . TYR   B 74  ? 0.87913 0.63460 0.73764 0.11476  -0.22400 -0.08916 167 TYR   B CA  
3010 C C   . TYR   B 74  ? 0.86460 0.66891 0.75217 0.12492  -0.21323 -0.09369 167 TYR   B C   
3011 O O   . TYR   B 74  ? 0.82801 0.66086 0.73239 0.14795  -0.21635 -0.11151 167 TYR   B O   
3012 C CB  . TYR   B 74  ? 0.76881 0.55233 0.64276 0.10430  -0.20913 -0.08923 167 TYR   B CB  
3013 C CG  . TYR   B 74  ? 0.91924 0.66435 0.77038 0.10693  -0.22405 -0.09569 167 TYR   B CG  
3014 C CD1 . TYR   B 74  ? 0.99650 0.74267 0.84715 0.13290  -0.23639 -0.11605 167 TYR   B CD1 
3015 C CD2 . TYR   B 74  ? 0.87330 0.58186 0.70365 0.08326  -0.22602 -0.08271 167 TYR   B CD2 
3016 C CE1 . TYR   B 74  ? 0.92294 0.63178 0.75151 0.13607  -0.25109 -0.12300 167 TYR   B CE1 
3017 C CE2 . TYR   B 74  ? 0.92612 0.59773 0.73496 0.08452  -0.24051 -0.08904 167 TYR   B CE2 
3018 C CZ  . TYR   B 74  ? 1.04178 0.71201 0.84897 0.11143  -0.25349 -0.10903 167 TYR   B CZ  
3019 O OH  . TYR   B 74  ? 0.99854 0.63026 0.78334 0.11340  -0.26877 -0.11632 167 TYR   B OH  
3020 N N   . LEU   B 75  ? 0.82491 0.64086 0.71929 0.10777  -0.20038 -0.07903 168 LEU   B N   
3021 C CA  . LEU   B 75  ? 0.78599 0.63874 0.70277 0.11718  -0.19418 -0.08323 168 LEU   B CA  
3022 C C   . LEU   B 75  ? 0.84954 0.67529 0.75093 0.13931  -0.21709 -0.09338 168 LEU   B C   
3023 O O   . LEU   B 75  ? 0.88393 0.74292 0.80639 0.15995  -0.21947 -0.10895 168 LEU   B O   
3024 C CB  . LEU   B 75  ? 0.78042 0.64385 0.70309 0.09448  -0.17815 -0.06570 168 LEU   B CB  
3025 C CG  . LEU   B 75  ? 0.80928 0.71497 0.75749 0.07776  -0.15395 -0.05849 168 LEU   B CG  
3026 C CD1 . LEU   B 75  ? 0.77036 0.67892 0.72025 0.05774  -0.14191 -0.04274 168 LEU   B CD1 
3027 C CD2 . LEU   B 75  ? 0.77357 0.73198 0.75298 0.09103  -0.14380 -0.07120 168 LEU   B CD2 
3028 N N   . ALA   B 76  ? 0.86861 0.63377 0.73247 0.13497  -0.23471 -0.08513 169 ALA   B N   
3029 C CA  . ALA   B 76  ? 0.99175 0.72297 0.83534 0.15699  -0.25999 -0.09404 169 ALA   B CA  
3030 C C   . ALA   B 76  ? 0.90588 0.63693 0.75249 0.18616  -0.27648 -0.11653 169 ALA   B C   
3031 O O   . ALA   B 76  ? 1.04673 0.78569 0.89995 0.21211  -0.29110 -0.13231 169 ALA   B O   
3032 C CB  . ALA   B 76  ? 1.00186 0.66212 0.79866 0.14321  -0.27525 -0.07868 169 ALA   B CB  
3033 N N   . GLN   B 77  ? 0.93263 0.65599 0.77505 0.18308  -0.27499 -0.11963 170 GLN   B N   
3034 C CA  . GLN   B 77  ? 0.99619 0.72339 0.84279 0.21074  -0.28872 -0.14256 170 GLN   B CA  
3035 C C   . GLN   B 77  ? 0.98467 0.78458 0.87458 0.22704  -0.27515 -0.16001 170 GLN   B C   
3036 O O   . GLN   B 77  ? 0.99078 0.80220 0.88930 0.25587  -0.28950 -0.18122 170 GLN   B O   
3037 C CB  . GLN   B 77  ? 0.99184 0.70014 0.82635 0.20101  -0.28712 -0.14148 170 GLN   B CB  
3038 C CG  . GLN   B 77  ? 1.06712 0.78873 0.90975 0.22763  -0.29639 -0.16606 170 GLN   B CG  
3039 C CD  . GLN   B 77  ? 1.02974 0.82159 0.91009 0.22653  -0.27167 -0.17407 170 GLN   B CD  
3040 O OE1 . GLN   B 77  ? 0.95953 0.77266 0.85008 0.20190  -0.25044 -0.15923 170 GLN   B OE1 
3041 N NE2 . GLN   B 77  ? 1.10408 0.93220 1.00438 0.25331  -0.27467 -0.19815 170 GLN   B NE2 
3042 N N   . ASP   B 78  ? 0.92099 0.77070 0.83822 0.20848  -0.24771 -0.15182 171 ASP   B N   
3043 C CA  . ASP   B 78  ? 0.91426 0.83241 0.87038 0.21917  -0.23249 -0.16662 171 ASP   B CA  
3044 C C   . ASP   B 78  ? 0.92223 0.86170 0.89381 0.23113  -0.23692 -0.17282 171 ASP   B C   
3045 O O   . ASP   B 78  ? 0.86127 0.84230 0.85750 0.25217  -0.23817 -0.19390 171 ASP   B O   
3046 C CB  . ASP   B 78  ? 0.89619 0.85392 0.87214 0.19465  -0.20388 -0.15394 171 ASP   B CB  
3047 C CG  . ASP   B 78  ? 0.88313 0.90844 0.89523 0.20166  -0.18678 -0.16740 171 ASP   B CG  
3048 O OD1 . ASP   B 78  ? 0.94099 0.98785 0.96109 0.21662  -0.18709 -0.18537 171 ASP   B OD1 
3049 O OD2 . ASP   B 78  ? 0.88325 0.93973 0.91466 0.19137  -0.17282 -0.16043 171 ASP   B OD2 
3050 N N   . PHE   B 79  ? 0.86561 0.77939 0.82354 0.21761  -0.23909 -0.15571 172 PHE   B N   
3051 C CA  . PHE   B 79  ? 0.91910 0.84794 0.88820 0.22925  -0.24610 -0.16148 172 PHE   B CA  
3052 C C   . PHE   B 79  ? 0.91741 0.81924 0.87308 0.26092  -0.27610 -0.18047 172 PHE   B C   
3053 O O   . PHE   B 79  ? 0.97719 0.91352 0.95573 0.28116  -0.28216 -0.19788 172 PHE   B O   
3054 C CB  . PHE   B 79  ? 0.78362 0.68429 0.73500 0.20805  -0.24359 -0.13903 172 PHE   B CB  
3055 C CG  . PHE   B 79  ? 0.79144 0.72291 0.75974 0.18001  -0.21533 -0.12266 172 PHE   B CG  
3056 C CD1 . PHE   B 79  ? 0.74357 0.72924 0.74370 0.17642  -0.19460 -0.12865 172 PHE   B CD1 
3057 C CD2 . PHE   B 79  ? 0.88237 0.78756 0.83309 0.15756  -0.21002 -0.10180 172 PHE   B CD2 
3058 C CE1 . PHE   B 79  ? 0.76607 0.77552 0.77933 0.15230  -0.17110 -0.11377 172 PHE   B CE1 
3059 C CE2 . PHE   B 79  ? 0.78053 0.71371 0.74746 0.13423  -0.18567 -0.08853 172 PHE   B CE2 
3060 C CZ  . PHE   B 79  ? 0.79603 0.77964 0.79389 0.13230  -0.16719 -0.09434 172 PHE   B CZ  
3061 N N   . PHE   B 80  ? 0.93251 0.77241 0.85128 0.26578  -0.29603 -0.17822 173 PHE   B N   
3062 C CA  . PHE   B 80  ? 1.06006 0.86541 0.96110 0.29718  -0.32765 -0.19598 173 PHE   B CA  
3063 C C   . PHE   B 80  ? 1.10374 0.95499 1.03402 0.32462  -0.32940 -0.22514 173 PHE   B C   
3064 O O   . PHE   B 80  ? 1.08571 0.95517 1.03007 0.35281  -0.34507 -0.24618 173 PHE   B O   
3065 C CB  . PHE   B 80  ? 1.10512 0.82899 0.95659 0.29221  -0.34748 -0.18501 173 PHE   B CB  
3066 C CG  . PHE   B 80  ? 1.15721 0.83672 0.98534 0.32501  -0.38222 -0.20301 173 PHE   B CG  
3067 C CD1 . PHE   B 80  ? 1.31230 0.95855 1.12085 0.33904  -0.40555 -0.20325 173 PHE   B CD1 
3068 C CD2 . PHE   B 80  ? 1.25182 0.92045 1.07564 0.34273  -0.39298 -0.22017 173 PHE   B CD2 
3069 C CE1 . PHE   B 80  ? 1.30906 0.91108 1.09439 0.37113  -0.44000 -0.22023 173 PHE   B CE1 
3070 C CE2 . PHE   B 80  ? 1.30438 0.92970 1.10600 0.37484  -0.42667 -0.23797 173 PHE   B CE2 
3071 C CZ  . PHE   B 80  ? 1.30684 0.89810 1.08915 0.38951  -0.45076 -0.23793 173 PHE   B CZ  
3072 N N   . ASP   B 81  ? 0.99818 0.87057 0.93814 0.31700  -0.31348 -0.22781 174 ASP   B N   
3073 C CA  . ASP   B 81  ? 1.01713 0.93123 0.98095 0.34195  -0.31427 -0.25600 174 ASP   B CA  
3074 C C   . ASP   B 81  ? 1.06252 1.05743 1.07300 0.34722  -0.29612 -0.26992 174 ASP   B C   
3075 O O   . ASP   B 81  ? 1.15163 1.18063 1.18329 0.37534  -0.30501 -0.29744 174 ASP   B O   
3076 C CB  . ASP   B 81  ? 1.00105 0.91596 0.96018 0.33022  -0.30113 -0.25393 174 ASP   B CB  
3077 C CG  . ASP   B 81  ? 1.11579 0.95328 1.03083 0.32896  -0.32195 -0.24625 174 ASP   B CG  
3078 O OD1 . ASP   B 81  ? 1.21846 1.00538 1.10814 0.34795  -0.35077 -0.25215 174 ASP   B OD1 
3079 O OD2 . ASP   B 81  ? 1.14779 0.97374 1.05259 0.30870  -0.31038 -0.23452 174 ASP   B OD2 
3080 N N   . ARG   B 82  ? 0.89369 0.92072 0.92106 0.32033  -0.27088 -0.25235 175 ARG   B N   
3081 C CA  . ARG   B 82  ? 0.89240 0.99403 0.96239 0.32148  -0.25262 -0.26420 175 ARG   B CA  
3082 C C   . ARG   B 82  ? 1.06385 1.17329 1.14459 0.33725  -0.26792 -0.27298 175 ARG   B C   
3083 O O   . ARG   B 82  ? 1.08861 1.25692 1.20454 0.35165  -0.26383 -0.29456 175 ARG   B O   
3084 C CB  . ARG   B 82  ? 0.80587 0.93542 0.88827 0.28791  -0.22196 -0.24286 175 ARG   B CB  
3085 C CG  . ARG   B 82  ? 0.88021 1.02456 0.96342 0.27554  -0.20361 -0.24040 175 ARG   B CG  
3086 C CD  . ARG   B 82  ? 0.78984 0.97547 0.89267 0.24813  -0.17372 -0.22580 175 ARG   B CD  
3087 N NE  . ARG   B 82  ? 0.82611 0.97865 0.91337 0.22425  -0.16927 -0.19867 175 ARG   B NE  
3088 C CZ  . ARG   B 82  ? 0.72833 0.89689 0.82832 0.21226  -0.16077 -0.18886 175 ARG   B CZ  
3089 N NH1 . ARG   B 82  ? 0.87565 1.09240 1.00465 0.22016  -0.15587 -0.20281 175 ARG   B NH1 
3090 N NH2 . ARG   B 82  ? 0.74954 0.88684 0.83354 0.19134  -0.15676 -0.16553 175 ARG   B NH2 
3091 N N   . TYR   B 83  ? 0.99271 1.04514 1.04344 0.33409  -0.28539 -0.25720 176 TYR   B N   
3092 C CA  . TYR   B 83  ? 0.96474 1.01870 1.02105 0.35101  -0.30351 -0.26583 176 TYR   B CA  
3093 C C   . TYR   B 83  ? 1.01908 1.06746 1.07599 0.39013  -0.33214 -0.29477 176 TYR   B C   
3094 O O   . TYR   B 83  ? 1.10793 1.19554 1.19180 0.41043  -0.34072 -0.31490 176 TYR   B O   
3095 C CB  . TYR   B 83  ? 1.01196 1.00198 1.03025 0.33685  -0.31515 -0.24092 176 TYR   B CB  
3096 C CG  . TYR   B 83  ? 1.03348 1.01236 1.04824 0.35612  -0.33889 -0.24888 176 TYR   B CG  
3097 C CD1 . TYR   B 83  ? 0.97899 1.00895 1.02555 0.35227  -0.32838 -0.25223 176 TYR   B CD1 
3098 C CD2 . TYR   B 83  ? 1.13500 1.04963 1.11262 0.37795  -0.37308 -0.25296 176 TYR   B CD2 
3099 C CE1 . TYR   B 83  ? 1.03546 1.05604 1.07883 0.37034  -0.35131 -0.26022 176 TYR   B CE1 
3100 C CE2 . TYR   B 83  ? 1.09702 0.99903 1.06886 0.39674  -0.39686 -0.26022 176 TYR   B CE2 
3101 C CZ  . TYR   B 83  ? 1.17201 1.12867 1.17769 0.39315  -0.38585 -0.26416 176 TYR   B CZ  
3102 O OH  . TYR   B 83  ? 1.17702 1.12203 1.17709 0.41232  -0.41068 -0.27212 176 TYR   B OH  
3103 N N   . MET   B 84  ? 1.12988 1.13031 1.15804 0.40170  -0.34805 -0.29843 177 MET   B N   
3104 C CA  . MET   B 84  ? 1.07063 1.06249 1.09781 0.44092  -0.37661 -0.32740 177 MET   B CA  
3105 C C   . MET   B 84  ? 1.12250 1.19673 1.19743 0.45783  -0.36334 -0.35774 177 MET   B C   
3106 O O   . MET   B 84  ? 1.07863 1.17376 1.16820 0.48665  -0.38060 -0.38465 177 MET   B O   
3107 C CB  . MET   B 84  ? 1.18166 1.10123 1.16561 0.44659  -0.39514 -0.32353 177 MET   B CB  
3108 C CG  . MET   B 84  ? 1.14300 0.97510 1.07560 0.43732  -0.41641 -0.29984 177 MET   B CG  
3109 S SD  . MET   B 84  ? 1.33192 1.14396 1.25725 0.46616  -0.44978 -0.31083 177 MET   B SD  
3110 C CE  . MET   B 84  ? 1.49784 1.19235 1.35023 0.45673  -0.47744 -0.28510 177 MET   B CE  
3111 N N   . ALA   B 85  ? 1.09156 1.21208 1.18705 0.43559  -0.33091 -0.35293 178 ALA   B N   
3112 C CA  . ALA   B 85  ? 0.97184 1.17284 1.11055 0.44684  -0.31457 -0.38009 178 ALA   B CA  
3113 C C   . ALA   B 85  ? 1.06515 1.33075 1.24490 0.45061  -0.30772 -0.39261 178 ALA   B C   
3114 O O   . ALA   B 85  ? 0.97450 1.30095 1.18370 0.45846  -0.29823 -0.41739 178 ALA   B O   
3115 C CB  . ALA   B 85  ? 1.03690 1.26644 1.18218 0.41866  -0.28143 -0.36830 178 ALA   B CB  
3116 N N   . THR   B 86  ? 0.99300 1.24174 1.16709 0.43547  -0.30884 -0.37284 179 THR   B N   
3117 C CA  . THR   B 86  ? 0.92749 1.23143 1.13787 0.43836  -0.30521 -0.38374 179 THR   B CA  
3118 C C   . THR   B 86  ? 1.00339 1.27545 1.19723 0.45860  -0.33506 -0.39528 179 THR   B C   
3119 O O   . THR   B 86  ? 1.00161 1.31764 1.22045 0.45944  -0.33194 -0.40885 179 THR   B O   
3120 C CB  . THR   B 86  ? 0.92546 1.22891 1.13458 0.40269  -0.28470 -0.35417 179 THR   B CB  
3121 O OG1 . THR   B 86  ? 0.91591 1.14239 1.08235 0.39737  -0.30313 -0.33075 179 THR   B OG1 
3122 C CG2 . THR   B 86  ? 0.93353 1.25514 1.14516 0.37132  -0.25143 -0.33727 179 THR   B CG2 
3123 N N   . GLN   B 87  ? 1.00595 1.20140 1.15674 0.47354  -0.36375 -0.39023 180 GLN   B N   
3124 C CA  . GLN   B 87  ? 1.04134 1.19699 1.16928 0.49184  -0.39381 -0.39900 180 GLN   B CA  
3125 C C   . GLN   B 87  ? 1.11079 1.26180 1.23124 0.51674  -0.41129 -0.42686 180 GLN   B C   
3126 O O   . GLN   B 87  ? 1.21760 1.38688 1.34485 0.51971  -0.40205 -0.43690 180 GLN   B O   
3127 C CB  . GLN   B 87  ? 1.03140 1.09827 1.10988 0.48839  -0.41543 -0.37244 180 GLN   B CB  
3128 C CG  . GLN   B 87  ? 1.07476 1.14288 1.15694 0.46408  -0.40109 -0.34427 180 GLN   B CG  
3129 C CD  . GLN   B 87  ? 1.02928 1.15116 1.14406 0.45850  -0.39182 -0.34994 180 GLN   B CD  
3130 O OE1 . GLN   B 87  ? 1.14592 1.25981 1.25513 0.47275  -0.40988 -0.36308 180 GLN   B OE1 
3131 N NE2 . GLN   B 87  ? 1.02003 1.19545 1.16742 0.43609  -0.36320 -0.34028 180 GLN   B NE2 
3132 N N   . GLU   B 88  ? 1.24895 1.37529 1.35442 0.53512  -0.43777 -0.43997 181 GLU   B N   
3133 C CA  . GLU   B 88  ? 1.35923 1.47748 1.45529 0.56092  -0.45955 -0.46743 181 GLU   B CA  
3134 C C   . GLU   B 88  ? 1.37772 1.41534 1.42676 0.57590  -0.49605 -0.46399 181 GLU   B C   
3135 O O   . GLU   B 88  ? 1.65017 1.67378 1.69324 0.57269  -0.50325 -0.45536 181 GLU   B O   
3136 C CB  . GLU   B 88  ? 1.35114 1.55225 1.49234 0.57000  -0.45052 -0.49826 181 GLU   B CB  
3137 C CG  . GLU   B 88  ? 1.36728 1.64909 1.55202 0.55388  -0.41430 -0.50382 181 GLU   B CG  
3138 C CD  . GLU   B 88  ? 1.33814 1.69894 1.56437 0.55973  -0.40556 -0.53320 181 GLU   B CD  
3139 O OE1 . GLU   B 88  ? 1.38712 1.74090 1.60964 0.57985  -0.42947 -0.55206 181 GLU   B OE1 
3140 O OE2 . GLU   B 88  ? 1.33320 1.76199 1.59432 0.54336  -0.37495 -0.53744 181 GLU   B OE2 
3141 N N   . ASN   B 89  ? 1.34878 1.33254 1.36281 0.59120  -0.51901 -0.47047 182 ASN   B N   
3142 C CA  . ASN   B 89  ? 1.45418 1.35776 1.41888 0.60608  -0.55564 -0.46970 182 ASN   B CA  
3143 C C   . ASN   B 89  ? 1.48113 1.31304 1.40525 0.58782  -0.56137 -0.43531 182 ASN   B C   
3144 O O   . ASN   B 89  ? 1.65046 1.49115 1.58155 0.57997  -0.55775 -0.42605 182 ASN   B O   
3145 C CB  . ASN   B 89  ? 1.34158 1.27304 1.32124 0.62675  -0.57212 -0.49608 182 ASN   B CB  
3146 C CG  . ASN   B 89  ? 1.53922 1.54971 1.56257 0.64229  -0.56419 -0.53055 182 ASN   B CG  
3147 O OD1 . ASN   B 89  ? 1.32237 1.31963 1.33344 0.66112  -0.58141 -0.54919 182 ASN   B OD1 
3148 N ND2 . ASN   B 89  ? 1.46433 1.55743 1.53789 0.63326  -0.53822 -0.53907 182 ASN   B ND2 
3149 N N   . VAL   B 90  ? 1.52515 1.28560 1.40550 0.57998  -0.57060 -0.41637 183 VAL   B N   
3150 C CA  . VAL   B 90  ? 1.51990 1.20765 1.35642 0.55982  -0.57593 -0.38278 183 VAL   B CA  
3151 C C   . VAL   B 90  ? 1.38890 0.98292 1.16355 0.56633  -0.60789 -0.37835 183 VAL   B C   
3152 O O   . VAL   B 90  ? 1.67519 1.25617 1.44073 0.57625  -0.61616 -0.38989 183 VAL   B O   
3153 C CB  . VAL   B 90  ? 1.55521 1.25340 1.40212 0.53381  -0.54783 -0.35758 183 VAL   B CB  
3154 C CG1 . VAL   B 90  ? 1.49796 1.11210 1.29190 0.51237  -0.55608 -0.32353 183 VAL   B CG1 
3155 C CG2 . VAL   B 90  ? 1.31639 1.09862 1.21769 0.52394  -0.51859 -0.35762 183 VAL   B CG2 
3156 N N   . VAL   B 91  ? 1.81576 1.34448 1.54648 0.55972  -0.62590 -0.36161 184 VAL   B N   
3157 C CA  . VAL   B 91  ? 1.97365 1.40884 1.64048 0.56241  -0.65684 -0.35534 184 VAL   B CA  
3158 C C   . VAL   B 91  ? 1.94463 1.32080 1.57417 0.53391  -0.64921 -0.32336 184 VAL   B C   
3159 O O   . VAL   B 91  ? 1.90336 1.30622 1.55344 0.51270  -0.62238 -0.30438 184 VAL   B O   
3160 C CB  . VAL   B 91  ? 1.97518 1.36731 1.60954 0.56785  -0.67983 -0.35347 184 VAL   B CB  
3161 C CG1 . VAL   B 91  ? 1.93241 1.29274 1.54436 0.53890  -0.66812 -0.31954 184 VAL   B CG1 
3162 C CG2 . VAL   B 91  ? 1.96005 1.27260 1.53780 0.58125  -0.71648 -0.36047 184 VAL   B CG2 
3163 N N   . LYS   B 92  ? 1.87453 1.17061 1.44871 0.53249  -0.67322 -0.31757 185 LYS   B N   
3164 C CA  . LYS   B 92  ? 1.90079 1.13851 1.43720 0.50376  -0.66703 -0.28861 185 LYS   B CA  
3165 C C   . LYS   B 92  ? 1.86679 1.07048 1.37736 0.47459  -0.65758 -0.25669 185 LYS   B C   
3166 O O   . LYS   B 92  ? 1.77717 0.97880 1.28865 0.44831  -0.63595 -0.23347 185 LYS   B O   
3167 C CB  . LYS   B 92  ? 2.05680 1.21594 1.53748 0.50773  -0.69668 -0.29022 185 LYS   B CB  
3168 C CG  . LYS   B 92  ? 1.94654 1.13290 1.44734 0.53354  -0.70602 -0.31866 185 LYS   B CG  
3169 C CD  . LYS   B 92  ? 2.22442 1.33027 1.66706 0.53976  -0.73995 -0.32084 185 LYS   B CD  
3170 C CE  . LYS   B 92  ? 2.32479 1.35390 1.71498 0.50546  -0.73885 -0.28794 185 LYS   B CE  
3171 N NZ  . LYS   B 92  ? 2.30182 1.25011 1.63218 0.50931  -0.77250 -0.28860 185 LYS   B NZ  
3172 N N   . THR   B 93  ? 1.83762 1.01412 1.32392 0.47859  -0.67381 -0.25552 186 THR   B N   
3173 C CA  . THR   B 93  ? 1.90309 1.04317 1.35894 0.45059  -0.66658 -0.22555 186 THR   B CA  
3174 C C   . THR   B 93  ? 1.84851 1.05743 1.35301 0.43900  -0.63552 -0.21564 186 THR   B C   
3175 O O   . THR   B 93  ? 1.79740 0.98268 1.28076 0.41088  -0.62343 -0.18763 186 THR   B O   
3176 C CB  . THR   B 93  ? 2.04846 1.14820 1.46954 0.46037  -0.69146 -0.22953 186 THR   B CB  
3177 O OG1 . THR   B 93  ? 2.02253 1.19077 1.49270 0.48722  -0.69156 -0.25484 186 THR   B OG1 
3178 C CG2 . THR   B 93  ? 2.04127 1.06944 1.41053 0.47166  -0.72447 -0.23881 186 THR   B CG2 
3179 N N   . LEU   B 94  ? 1.81274 1.10721 1.38055 0.45865  -0.62224 -0.23806 187 LEU   B N   
3180 C CA  . LEU   B 94  ? 1.73478 1.09919 1.35103 0.44785  -0.59305 -0.23011 187 LEU   B CA  
3181 C C   . LEU   B 94  ? 1.70994 1.09093 1.34220 0.43030  -0.57010 -0.21678 187 LEU   B C   
3182 O O   . LEU   B 94  ? 1.60188 1.02786 1.26399 0.41562  -0.54679 -0.20388 187 LEU   B O   
3183 C CB  . LEU   B 94  ? 1.69526 1.14692 1.37226 0.47333  -0.58735 -0.26026 187 LEU   B CB  
3184 C CG  . LEU   B 94  ? 1.62110 1.14855 1.34816 0.46451  -0.56155 -0.25591 187 LEU   B CG  
3185 C CD1 . LEU   B 94  ? 1.62013 1.11412 1.31798 0.44713  -0.56431 -0.23267 187 LEU   B CD1 
3186 C CD2 . LEU   B 94  ? 1.55513 1.16347 1.33741 0.48833  -0.55784 -0.28836 187 LEU   B CD2 
3187 N N   . LEU   B 95  ? 1.69195 1.03676 1.30392 0.43129  -0.57724 -0.21974 188 LEU   B N   
3188 C CA  . LEU   B 95  ? 1.55346 0.91210 1.18048 0.41604  -0.55650 -0.20912 188 LEU   B CA  
3189 C C   . LEU   B 95  ? 1.50104 0.82179 1.09767 0.37647  -0.54137 -0.17404 188 LEU   B C   
3190 O O   . LEU   B 95  ? 1.51112 0.88372 1.13857 0.34929  -0.50623 -0.16423 188 LEU   B O   
3191 C CB  . LEU   B 95  ? 1.65284 0.97684 1.26077 0.42467  -0.56906 -0.22103 188 LEU   B CB  
3192 C CG  . LEU   B 95  ? 1.73530 1.10708 1.37598 0.45828  -0.57767 -0.25709 188 LEU   B CG  
3193 C CD1 . LEU   B 95  ? 1.56496 0.89163 1.17708 0.46429  -0.59346 -0.26539 188 LEU   B CD1 
3194 C CD2 . LEU   B 95  ? 1.49556 0.96400 1.20320 0.46579  -0.55027 -0.27105 188 LEU   B CD2 
3195 N N   . GLN   B 96  ? 1.55291 0.79226 1.08983 0.36486  -0.56084 -0.15624 189 GLN   B N   
3196 C CA  . GLN   B 96  ? 1.56282 0.76836 1.06843 0.32230  -0.54341 -0.12426 189 GLN   B CA  
3197 C C   . GLN   B 96  ? 1.59646 0.86347 1.13424 0.30379  -0.51539 -0.11435 189 GLN   B C   
3198 O O   . GLN   B 96  ? 1.47468 0.76235 1.02053 0.26846  -0.48492 -0.09625 189 GLN   B O   
3199 C CB  . GLN   B 96  ? 1.66015 0.76972 1.09391 0.31204  -0.56870 -0.10931 189 GLN   B CB  
3200 C CG  . GLN   B 96  ? 1.76519 0.82951 1.15973 0.26855  -0.55400 -0.07644 189 GLN   B CG  
3201 C CD  . GLN   B 96  ? 1.99133 0.97098 1.31642 0.25205  -0.57333 -0.06427 189 GLN   B CD  
3202 O OE1 . GLN   B 96  ? 2.20101 1.15814 1.50676 0.27264  -0.59733 -0.07797 189 GLN   B OE1 
3203 N NE2 . GLN   B 96  ? 1.91526 0.85052 1.20316 0.21309  -0.56189 -0.03949 189 GLN   B NE2 
3204 N N   . LEU   B 97  ? 1.55550 0.85303 1.11288 0.32786  -0.52604 -0.12719 190 LEU   B N   
3205 C CA  . LEU   B 97  ? 1.51266 0.86806 1.10099 0.31196  -0.50121 -0.11964 190 LEU   B CA  
3206 C C   . LEU   B 97  ? 1.41114 0.85602 1.06293 0.30375  -0.46618 -0.12757 190 LEU   B C   
3207 O O   . LEU   B 97  ? 1.34102 0.81832 1.00838 0.27404  -0.43648 -0.11197 190 LEU   B O   
3208 C CB  . LEU   B 97  ? 1.40191 0.76820 0.99651 0.34112  -0.52356 -0.13367 190 LEU   B CB  
3209 C CG  . LEU   B 97  ? 1.30542 0.73620 0.93662 0.32973  -0.50095 -0.13064 190 LEU   B CG  
3210 C CD1 . LEU   B 97  ? 1.45767 0.85679 1.05444 0.29110  -0.48470 -0.10089 190 LEU   B CD1 
3211 C CD2 . LEU   B 97  ? 1.53959 0.98410 1.18081 0.36259  -0.52637 -0.14901 190 LEU   B CD2 
3212 N N   . ILE   B 98  ? 1.24433 0.72898 0.93163 0.32997  -0.46953 -0.15217 191 ILE   B N   
3213 C CA  . ILE   B 98  ? 1.36243 0.92913 1.10599 0.32247  -0.43733 -0.16004 191 ILE   B CA  
3214 C C   . ILE   B 98  ? 1.32348 0.87994 1.05865 0.29013  -0.41417 -0.14204 191 ILE   B C   
3215 O O   . ILE   B 98  ? 1.18261 0.79124 0.94943 0.26816  -0.38290 -0.13433 191 ILE   B O   
3216 C CB  . ILE   B 98  ? 1.35980 0.96799 1.13833 0.35802  -0.44735 -0.19157 191 ILE   B CB  
3217 C CG1 . ILE   B 98  ? 1.30725 0.93436 1.10010 0.38967  -0.46932 -0.21105 191 ILE   B CG1 
3218 C CG2 . ILE   B 98  ? 1.20141 0.88986 1.03230 0.34811  -0.41374 -0.19866 191 ILE   B CG2 
3219 C CD1 . ILE   B 98  ? 1.23947 0.91396 1.07007 0.42572  -0.47904 -0.24482 191 ILE   B CD1 
3220 N N   . GLY   B 99  ? 1.35413 0.84191 1.04585 0.28653  -0.43022 -0.13530 192 GLY   B N   
3221 C CA  . GLY   B 99  ? 1.28235 0.76023 0.96654 0.25635  -0.41037 -0.11992 192 GLY   B CA  
3222 C C   . GLY   B 99  ? 1.30347 0.77159 0.97268 0.21872  -0.39058 -0.09311 192 GLY   B C   
3223 O O   . GLY   B 99  ? 1.25423 0.76329 0.94877 0.19513  -0.36152 -0.08442 192 GLY   B O   
3224 N N   . ILE   B 100 ? 1.33639 0.74999 0.96312 0.21317  -0.40652 -0.08032 193 ILE   B N   
3225 C CA  . ILE   B 100 ? 1.42273 0.82485 1.03159 0.17702  -0.38800 -0.05578 193 ILE   B CA  
3226 C C   . ILE   B 100 ? 1.29179 0.76586 0.94492 0.17054  -0.36267 -0.05532 193 ILE   B C   
3227 O O   . ILE   B 100 ? 1.22823 0.72097 0.88817 0.14080  -0.33733 -0.03976 193 ILE   B O   
3228 C CB  . ILE   B 100 ? 1.45602 0.77868 1.00331 0.17235  -0.41201 -0.04241 193 ILE   B CB  
3229 C CG1 . ILE   B 100 ? 1.35309 0.65407 0.87399 0.13046  -0.39249 -0.01685 193 ILE   B CG1 
3230 C CG2 . ILE   B 100 ? 1.35654 0.68771 0.90613 0.19587  -0.42783 -0.05067 193 ILE   B CG2 
3231 C CD1 . ILE   B 100 ? 1.39054 0.67820 0.90548 0.10566  -0.37954 -0.00852 193 ILE   B CD1 
3232 N N   . SER   B 101 ? 1.30262 0.81910 0.98741 0.19792  -0.36913 -0.07329 194 SER   B N   
3233 C CA  . SER   B 101 ? 1.11131 0.69524 0.83841 0.19167  -0.34599 -0.07397 194 SER   B CA  
3234 C C   . SER   B 101 ? 1.07211 0.71901 0.84568 0.18306  -0.31794 -0.07846 194 SER   B C   
3235 O O   . SER   B 101 ? 1.02884 0.71616 0.82607 0.16330  -0.29259 -0.06959 194 SER   B O   
3236 C CB  . SER   B 101 ? 1.13623 0.74581 0.88238 0.22207  -0.36252 -0.09249 194 SER   B CB  
3237 O OG  . SER   B 101 ? 1.27170 0.82111 0.97245 0.23071  -0.39004 -0.08780 194 SER   B OG  
3238 N N   . SER   B 102 ? 1.07025 0.72455 0.85550 0.19834  -0.32296 -0.09261 195 SER   B N   
3239 C CA  . SER   B 102 ? 0.96828 0.67317 0.78922 0.18821  -0.29768 -0.09496 195 SER   B CA  
3240 C C   . SER   B 102 ? 1.00660 0.69282 0.81214 0.15463  -0.28011 -0.07367 195 SER   B C   
3241 O O   . SER   B 102 ? 0.91671 0.64793 0.75098 0.13793  -0.25440 -0.06816 195 SER   B O   
3242 C CB  . SER   B 102 ? 0.96435 0.67276 0.79325 0.21104  -0.30879 -0.11429 195 SER   B CB  
3243 O OG  . SER   B 102 ? 1.05098 0.78415 0.89887 0.24296  -0.32394 -0.13667 195 SER   B OG  
3244 N N   . LEU   B 103 ? 1.07181 0.69142 0.83159 0.14410  -0.29426 -0.06199 196 LEU   B N   
3245 C CA  . LEU   B 103 ? 1.00396 0.60635 0.74854 0.11061  -0.27817 -0.04246 196 LEU   B CA  
3246 C C   . LEU   B 103 ? 0.97192 0.58969 0.71902 0.08998  -0.26163 -0.02792 196 LEU   B C   
3247 O O   . LEU   B 103 ? 1.01526 0.65373 0.77387 0.06516  -0.23916 -0.01671 196 LEU   B O   
3248 C CB  . LEU   B 103 ? 1.13644 0.66210 0.82930 0.10307  -0.29815 -0.03435 196 LEU   B CB  
3249 C CG  . LEU   B 103 ? 1.13316 0.63754 0.80783 0.06738  -0.28366 -0.01594 196 LEU   B CG  
3250 C CD1 . LEU   B 103 ? 1.17376 0.72271 0.88329 0.05968  -0.26417 -0.01968 196 LEU   B CD1 
3251 C CD2 . LEU   B 103 ? 1.20137 0.62582 0.82171 0.06054  -0.30600 -0.00902 196 LEU   B CD2 
3252 N N   . PHE   B 104 ? 1.11042 0.71894 0.84707 0.10087  -0.27323 -0.02907 197 PHE   B N   
3253 C CA  . PHE   B 104 ? 1.01818 0.64264 0.75724 0.08329  -0.25825 -0.01717 197 PHE   B CA  
3254 C C   . PHE   B 104 ? 0.96546 0.66265 0.75611 0.08083  -0.23315 -0.02182 197 PHE   B C   
3255 O O   . PHE   B 104 ? 0.95765 0.67394 0.75709 0.05787  -0.21192 -0.01022 197 PHE   B O   
3256 C CB  . PHE   B 104 ? 1.13416 0.73255 0.85024 0.09829  -0.27880 -0.01934 197 PHE   B CB  
3257 C CG  . PHE   B 104 ? 1.16576 0.77526 0.87909 0.08119  -0.26573 -0.00787 197 PHE   B CG  
3258 C CD1 . PHE   B 104 ? 1.12245 0.70907 0.81094 0.05037  -0.25221 0.01041  197 PHE   B CD1 
3259 C CD2 . PHE   B 104 ? 1.22448 0.86819 0.96004 0.09580  -0.26725 -0.01661 197 PHE   B CD2 
3260 C CE1 . PHE   B 104 ? 1.31031 0.90796 0.99556 0.03556  -0.24002 0.01941  197 PHE   B CE1 
3261 C CE2 . PHE   B 104 ? 1.17673 0.82906 0.90835 0.08070  -0.25610 -0.00701 197 PHE   B CE2 
3262 C CZ  . PHE   B 104 ? 1.12502 0.75395 0.83089 0.05116  -0.24240 0.01086  197 PHE   B CZ  
3263 N N   . ILE   B 105 ? 1.00820 0.74612 0.83251 0.10399  -0.23541 -0.03929 198 ILE   B N   
3264 C CA  . ILE   B 105 ? 0.87123 0.67486 0.74178 0.10055  -0.21200 -0.04368 198 ILE   B CA  
3265 C C   . ILE   B 105 ? 0.86939 0.68548 0.75003 0.08218  -0.19339 -0.03642 198 ILE   B C   
3266 O O   . ILE   B 105 ? 0.78195 0.63065 0.68325 0.06551  -0.17181 -0.02895 198 ILE   B O   
3267 C CB  . ILE   B 105 ? 0.92249 0.76550 0.82402 0.12762  -0.21845 -0.06488 198 ILE   B CB  
3268 C CG1 . ILE   B 105 ? 0.87377 0.70628 0.76715 0.14722  -0.23896 -0.07369 198 ILE   B CG1 
3269 C CG2 . ILE   B 105 ? 0.68344 0.59102 0.62886 0.12132  -0.19389 -0.06828 198 ILE   B CG2 
3270 C CD1 . ILE   B 105 ? 0.79874 0.66372 0.71845 0.17644  -0.25014 -0.09730 198 ILE   B CD1 
3271 N N   . ALA   B 106 ? 0.82813 0.61704 0.69365 0.08569  -0.20287 -0.03916 199 ALA   B N   
3272 C CA  . ALA   B 106 ? 0.88453 0.68575 0.75999 0.07016  -0.18758 -0.03412 199 ALA   B CA  
3273 C C   . ALA   B 106 ? 0.79351 0.57822 0.65415 0.04099  -0.17526 -0.01589 199 ALA   B C   
3274 O O   . ALA   B 106 ? 0.75343 0.57045 0.63605 0.02626  -0.15543 -0.01071 199 ALA   B O   
3275 C CB  . ALA   B 106 ? 0.88474 0.65598 0.74396 0.08056  -0.20283 -0.04192 199 ALA   B CB  
3276 N N   . ALA   B 107 ? 0.85416 0.58897 0.67681 0.03232  -0.18696 -0.00656 200 ALA   B N   
3277 C CA  . ALA   B 107 ? 0.90882 0.62937 0.71620 0.00322  -0.17451 0.00950  200 ALA   B CA  
3278 C C   . ALA   B 107 ? 0.85661 0.61863 0.68815 -0.00651 -0.15467 0.01437  200 ALA   B C   
3279 O O   . ALA   B 107 ? 0.88303 0.66349 0.72569 -0.02670 -0.13663 0.02217  200 ALA   B O   
3280 C CB  . ALA   B 107 ? 0.96832 0.62540 0.72612 -0.00460 -0.19125 0.01837  200 ALA   B CB  
3281 N N   . LYS   B 108 ? 0.97099 0.74849 0.81157 0.00819  -0.15857 0.00874  201 LYS   B N   
3282 C CA  . LYS   B 108 ? 0.82828 0.64332 0.69125 -0.00009 -0.14100 0.01224  201 LYS   B CA  
3283 C C   . LYS   B 108 ? 0.87731 0.74474 0.78193 -0.00033 -0.12288 0.00782  201 LYS   B C   
3284 O O   . LYS   B 108 ? 0.79108 0.68544 0.71265 -0.01296 -0.10568 0.01314  201 LYS   B O   
3285 C CB  . LYS   B 108 ? 0.88543 0.70420 0.74832 0.01591  -0.15116 0.00604  201 LYS   B CB  
3286 C CG  . LYS   B 108 ? 0.94883 0.71829 0.76865 0.01149  -0.16539 0.01374  201 LYS   B CG  
3287 C CD  . LYS   B 108 ? 0.96084 0.74052 0.78418 0.02521  -0.17314 0.00795  201 LYS   B CD  
3288 C CE  . LYS   B 108 ? 1.00864 0.80060 0.84790 0.05408  -0.18988 -0.00872 201 LYS   B CE  
3289 N NZ  . LYS   B 108 ? 0.86373 0.66658 0.70732 0.06760  -0.19927 -0.01569 201 LYS   B NZ  
3290 N N   . LEU   B 109 ? 0.86671 0.74738 0.78608 0.01364  -0.12693 -0.00212 202 LEU   B N   
3291 C CA  . LEU   B 109 ? 0.80600 0.73272 0.76014 0.01323  -0.11077 -0.00584 202 LEU   B CA  
3292 C C   . LEU   B 109 ? 0.83119 0.75744 0.78613 -0.00443 -0.09989 0.00210  202 LEU   B C   
3293 O O   . LEU   B 109 ? 0.79920 0.75733 0.77666 -0.01338 -0.08353 0.00536  202 LEU   B O   
3294 C CB  . LEU   B 109 ? 0.72555 0.66921 0.69395 0.03449  -0.11829 -0.02051 202 LEU   B CB  
3295 C CG  . LEU   B 109 ? 0.88745 0.85764 0.87347 0.05133  -0.12170 -0.03165 202 LEU   B CG  
3296 C CD1 . LEU   B 109 ? 0.70608 0.68772 0.70112 0.07265  -0.13154 -0.04791 202 LEU   B CD1 
3297 C CD2 . LEU   B 109 ? 0.84817 0.86225 0.86353 0.04276  -0.10215 -0.02939 202 LEU   B CD2 
3298 N N   . GLU   B 110 ? 0.87895 0.76859 0.80932 -0.00956 -0.10979 0.00476  203 GLU   B N   
3299 C CA  . GLU   B 110 ? 0.85221 0.74349 0.78559 -0.02381 -0.10218 0.00910  203 GLU   B CA  
3300 C C   . GLU   B 110 ? 1.00295 0.87757 0.92170 -0.04812 -0.09516 0.02110  203 GLU   B C   
3301 O O   . GLU   B 110 ? 0.91942 0.81775 0.85535 -0.06132 -0.08119 0.02482  203 GLU   B O   
3302 C CB  . GLU   B 110 ? 0.84132 0.70593 0.75939 -0.01525 -0.11698 0.00268  203 GLU   B CB  
3303 C CG  . GLU   B 110 ? 0.99336 0.86533 0.91873 -0.02658 -0.11043 0.00419  203 GLU   B CG  
3304 C CD  . GLU   B 110 ? 1.11553 1.03520 1.07382 -0.02107 -0.09713 -0.00038 203 GLU   B CD  
3305 O OE1 . GLU   B 110 ? 1.04016 0.98315 1.01314 -0.00500 -0.09622 -0.00797 203 GLU   B OE1 
3306 O OE2 . GLU   B 110 ? 1.26642 1.20000 1.23508 -0.03338 -0.08797 0.00343  203 GLU   B OE2 
3307 N N   . GLU   B 111 ? 0.90677 0.74166 0.79351 -0.05450 -0.10468 0.02667  204 GLU   B N   
3308 C CA  . GLU   B 111 ? 0.96898 0.78665 0.83832 -0.07991 -0.09760 0.03739  204 GLU   B CA  
3309 C C   . GLU   B 111 ? 1.02776 0.87648 0.91371 -0.08981 -0.08032 0.04189  204 GLU   B C   
3310 O O   . GLU   B 111 ? 0.98724 0.85257 0.88366 -0.07810 -0.07899 0.03910  204 GLU   B O   
3311 C CB  . GLU   B 111 ? 0.86256 0.62401 0.68718 -0.08499 -0.11336 0.04280  204 GLU   B CB  
3312 C CG  . GLU   B 111 ? 0.97253 0.69605 0.77641 -0.07352 -0.13340 0.03766  204 GLU   B CG  
3313 C CD  . GLU   B 111 ? 1.13000 0.85108 0.93682 -0.08659 -0.13051 0.03801  204 GLU   B CD  
3314 O OE1 . GLU   B 111 ? 1.09697 0.83370 0.91172 -0.10936 -0.11534 0.04454  204 GLU   B OE1 
3315 O OE2 . GLU   B 111 ? 1.04332 0.74825 0.84534 -0.07350 -0.14387 0.03051  204 GLU   B OE2 
3316 N N   . ILE   B 112 ? 0.91657 0.77420 0.80573 -0.11161 -0.06731 0.04770  205 ILE   B N   
3317 C CA  . ILE   B 112 ? 1.04614 0.93021 0.94810 -0.12192 -0.05134 0.05104  205 ILE   B CA  
3318 C C   . ILE   B 112 ? 1.05465 0.90845 0.92383 -0.12968 -0.05497 0.05713  205 ILE   B C   
3319 O O   . ILE   B 112 ? 1.03905 0.90588 0.91328 -0.12384 -0.05102 0.05654  205 ILE   B O   
3320 C CB  . ILE   B 112 ? 0.97552 0.88221 0.89335 -0.14135 -0.03686 0.05295  205 ILE   B CB  
3321 C CG1 . ILE   B 112 ? 0.91538 0.85294 0.86518 -0.13168 -0.03419 0.04693  205 ILE   B CG1 
3322 C CG2 . ILE   B 112 ? 0.92928 0.86077 0.85753 -0.15182 -0.02112 0.05499  205 ILE   B CG2 
3323 C CD1 . ILE   B 112 ? 0.80913 0.77168 0.77765 -0.14772 -0.02230 0.04701  205 ILE   B CD1 
3324 N N   . TYR   B 113 ? 0.96605 0.77669 0.79872 -0.14370 -0.06316 0.06322  206 TYR   B N   
3325 C CA  . TYR   B 113 ? 1.10104 0.87359 0.89375 -0.15208 -0.06926 0.07027  206 TYR   B CA  
3326 C C   . TYR   B 113 ? 1.05455 0.77574 0.81346 -0.14043 -0.09294 0.07051  206 TYR   B C   
3327 O O   . TYR   B 113 ? 1.13731 0.81796 0.86476 -0.15502 -0.10033 0.07615  206 TYR   B O   
3328 C CB  . TYR   B 113 ? 1.05174 0.81562 0.82573 -0.18303 -0.05677 0.07830  206 TYR   B CB  
3329 C CG  . TYR   B 113 ? 1.10402 0.91969 0.91255 -0.19344 -0.03426 0.07594  206 TYR   B CG  
3330 C CD1 . TYR   B 113 ? 0.98001 0.81744 0.79681 -0.19005 -0.02506 0.07497  206 TYR   B CD1 
3331 C CD2 . TYR   B 113 ? 1.09408 0.93627 0.92679 -0.20569 -0.02356 0.07358  206 TYR   B CD2 
3332 C CE1 . TYR   B 113 ? 1.11987 1.00261 0.96762 -0.19765 -0.00595 0.07148  206 TYR   B CE1 
3333 C CE2 . TYR   B 113 ? 1.16160 1.05081 1.02641 -0.21280 -0.00497 0.06992  206 TYR   B CE2 
3334 C CZ  . TYR   B 113 ? 1.25325 1.16177 1.12514 -0.20832 0.00370  0.06877  206 TYR   B CZ  
3335 O OH  . TYR   B 113 ? 1.20391 1.15723 1.10714 -0.21355 0.02080  0.06386  206 TYR   B OH  
3336 N N   . PRO   B 114 ? 1.10124 0.82249 0.86554 -0.11433 -0.10587 0.06368  207 PRO   B N   
3337 C CA  . PRO   B 114 ? 1.10635 0.78206 0.84251 -0.09868 -0.13020 0.06098  207 PRO   B CA  
3338 C C   . PRO   B 114 ? 1.11575 0.73545 0.79982 -0.10803 -0.14286 0.07014  207 PRO   B C   
3339 O O   . PRO   B 114 ? 1.28709 0.90913 0.95974 -0.12203 -0.13292 0.07696  207 PRO   B O   
3340 C CB  . PRO   B 114 ? 1.05760 0.76133 0.82082 -0.06912 -0.13689 0.04940  207 PRO   B CB  
3341 C CG  . PRO   B 114 ? 1.04938 0.79213 0.83460 -0.07336 -0.12028 0.05053  207 PRO   B CG  
3342 C CD  . PRO   B 114 ? 1.03056 0.79485 0.82802 -0.09799 -0.09911 0.05695  207 PRO   B CD  
3343 N N   . PRO   B 115 ? 1.27381 0.84014 0.92281 -0.10067 -0.16540 0.07043  208 PRO   B N   
3344 C CA  . PRO   B 115 ? 1.24943 0.75593 0.84372 -0.10696 -0.18098 0.07942  208 PRO   B CA  
3345 C C   . PRO   B 115 ? 1.37221 0.88427 0.96578 -0.08653 -0.18986 0.07530  208 PRO   B C   
3346 O O   . PRO   B 115 ? 1.14785 0.70000 0.77926 -0.06245 -0.19084 0.06334  208 PRO   B O   
3347 C CB  . PRO   B 115 ? 1.26954 0.72089 0.83314 -0.09743 -0.20569 0.07755  208 PRO   B CB  
3348 C CG  . PRO   B 115 ? 1.22853 0.70991 0.82669 -0.09773 -0.19714 0.07084  208 PRO   B CG  
3349 C CD  . PRO   B 115 ? 1.24623 0.80059 0.90034 -0.08799 -0.17791 0.06290  208 PRO   B CD  
3350 N N   . LYS   B 116 ? 1.38461 0.85548 0.93292 -0.09777 -0.19635 0.08529  209 LYS   B N   
3351 C CA  . LYS   B 116 ? 1.34483 0.81620 0.88676 -0.08069 -0.20615 0.08221  209 LYS   B CA  
3352 C C   . LYS   B 116 ? 1.38841 0.82628 0.91564 -0.04925 -0.23736 0.07315  209 LYS   B C   
3353 O O   . LYS   B 116 ? 1.46273 0.86634 0.97491 -0.04284 -0.25267 0.07114  209 LYS   B O   
3354 C CB  . LYS   B 116 ? 1.45098 0.88738 0.94547 -0.10351 -0.20329 0.09589  209 LYS   B CB  
3355 C CG  . LYS   B 116 ? 1.31367 0.79254 0.82755 -0.13011 -0.17218 0.10127  209 LYS   B CG  
3356 C CD  . LYS   B 116 ? 1.37873 0.92410 0.94664 -0.11513 -0.15867 0.09076  209 LYS   B CD  
3357 C CE  . LYS   B 116 ? 1.36369 0.94869 0.94939 -0.13891 -0.12985 0.09470  209 LYS   B CE  
3358 N NZ  . LYS   B 116 ? 1.23406 0.83737 0.83836 -0.15823 -0.11300 0.09684  209 LYS   B NZ  
3359 N N   . LEU   B 117 ? 1.41153 0.86042 0.94391 -0.02882 -0.24754 0.06639  210 LEU   B N   
3360 C CA  . LEU   B 117 ? 1.37800 0.80628 0.90492 0.00458  -0.27698 0.05427  210 LEU   B CA  
3361 C C   . LEU   B 117 ? 1.51265 0.85730 0.97478 0.00444  -0.30435 0.06221  210 LEU   B C   
3362 O O   . LEU   B 117 ? 1.59523 0.91284 1.05045 0.02490  -0.32616 0.05379  210 LEU   B O   
3363 C CB  . LEU   B 117 ? 1.38702 0.84449 0.93108 0.02336  -0.28215 0.04572  210 LEU   B CB  
3364 C CG  . LEU   B 117 ? 1.40755 0.83833 0.93806 0.05718  -0.31573 0.03350  210 LEU   B CG  
3365 C CD1 . LEU   B 117 ? 1.29330 0.75225 0.86283 0.08220  -0.32262 0.01610  210 LEU   B CD1 
3366 C CD2 . LEU   B 117 ? 1.35932 0.81497 0.90058 0.06998  -0.32025 0.02724  210 LEU   B CD2 
3367 N N   . HIS   B 118 ? 1.57018 0.87121 0.98216 -0.01857 -0.30400 0.07812  211 HIS   B N   
3368 C CA  . HIS   B 118 ? 1.78904 1.00431 1.13288 -0.01946 -0.33174 0.08706  211 HIS   B CA  
3369 C C   . HIS   B 118 ? 1.67580 0.85363 1.00147 -0.03254 -0.33457 0.09192  211 HIS   B C   
3370 O O   . HIS   B 118 ? 1.72770 0.83839 1.00897 -0.02209 -0.36320 0.09299  211 HIS   B O   
3371 C CB  . HIS   B 118 ? 1.80782 0.98625 1.09967 -0.04528 -0.32759 0.10407  211 HIS   B CB  
3372 C CG  . HIS   B 118 ? 1.83400 0.99958 1.10464 -0.08702 -0.30430 0.11995  211 HIS   B CG  
3373 N ND1 . HIS   B 118 ? 1.72096 0.95030 1.03534 -0.10767 -0.26983 0.12052  211 HIS   B ND1 
3374 C CD2 . HIS   B 118 ? 1.88263 0.97962 1.09319 -0.11244 -0.31089 0.13504  211 HIS   B CD2 
3375 C CE1 . HIS   B 118 ? 1.83222 1.03722 1.11751 -0.14327 -0.25578 0.13401  211 HIS   B CE1 
3376 N NE2 . HIS   B 118 ? 1.97743 1.10242 1.19931 -0.14837 -0.27937 0.14347  211 HIS   B NE2 
3377 N N   . GLN   B 119 ? 1.65585 0.87453 1.01462 -0.05447 -0.30685 0.09418  212 GLN   B N   
3378 C CA  . GLN   B 119 ? 1.79325 0.98229 1.14035 -0.06624 -0.30936 0.09682  212 GLN   B CA  
3379 C C   . GLN   B 119 ? 1.61573 0.80862 0.98693 -0.03176 -0.32904 0.07961  212 GLN   B C   
3380 O O   . GLN   B 119 ? 1.65044 0.78838 0.98997 -0.02933 -0.34850 0.07997  212 GLN   B O   
3381 C CB  . GLN   B 119 ? 1.59935 0.83777 0.98093 -0.09561 -0.27572 0.10125  212 GLN   B CB  
3382 C CG  . GLN   B 119 ? 1.77193 0.99483 1.12086 -0.13483 -0.25757 0.11830  212 GLN   B CG  
3383 C CD  . GLN   B 119 ? 1.67508 0.95056 1.06204 -0.16121 -0.22594 0.11998  212 GLN   B CD  
3384 O OE1 . GLN   B 119 ? 1.58526 0.93009 1.02792 -0.15307 -0.20749 0.11142  212 GLN   B OE1 
3385 N NE2 . GLN   B 119 ? 1.81548 1.05736 1.17196 -0.19326 -0.22037 0.13066  212 GLN   B NE2 
3386 N N   . PHE   B 120 ? 1.57678 0.83403 1.00316 -0.00562 -0.32400 0.06380  213 PHE   B N   
3387 C CA  . PHE   B 120 ? 1.47600 0.74045 0.92482 0.02913  -0.34296 0.04534  213 PHE   B CA  
3388 C C   . PHE   B 120 ? 1.51866 0.72242 0.92503 0.05541  -0.37995 0.04053  213 PHE   B C   
3389 O O   . PHE   B 120 ? 1.52160 0.69568 0.91942 0.07693  -0.40243 0.02989  213 PHE   B O   
3390 C CB  . PHE   B 120 ? 1.42816 0.77695 0.94381 0.04781  -0.32734 0.03001  213 PHE   B CB  
3391 C CG  . PHE   B 120 ? 1.34802 0.75156 0.90751 0.03156  -0.29827 0.02988  213 PHE   B CG  
3392 C CD1 . PHE   B 120 ? 1.36392 0.80116 0.93813 0.00416  -0.27023 0.04095  213 PHE   B CD1 
3393 C CD2 . PHE   B 120 ? 1.31938 0.73978 0.90403 0.04471  -0.30003 0.01786  213 PHE   B CD2 
3394 C CE1 . PHE   B 120 ? 1.29198 0.77746 0.90536 -0.00891 -0.24594 0.04030  213 PHE   B CE1 
3395 C CE2 . PHE   B 120 ? 1.24933 0.71743 0.87130 0.03043  -0.27510 0.01798  213 PHE   B CE2 
3396 C CZ  . PHE   B 120 ? 1.26216 0.76218 0.89857 0.00402  -0.24874 0.02936  213 PHE   B CZ  
3397 N N   . ALA   B 121 ? 1.66337 0.84691 1.04178 0.05520  -0.38796 0.04737  214 ALA   B N   
3398 C CA  . ALA   B 121 ? 1.69335 0.80949 1.02257 0.07766  -0.42534 0.04523  214 ALA   B CA  
3399 C C   . ALA   B 121 ? 1.69165 0.71642 0.94962 0.05642  -0.44051 0.06208  214 ALA   B C   
3400 O O   . ALA   B 121 ? 1.75581 0.71525 0.97191 0.07717  -0.47504 0.05859  214 ALA   B O   
3401 C CB  . ALA   B 121 ? 1.55826 0.68156 0.87867 0.08417  -0.43003 0.04706  214 ALA   B CB  
3402 N N   . TYR   B 122 ? 1.69763 0.71675 0.94144 0.01547  -0.41586 0.07941  215 TYR   B N   
3403 C CA  . TYR   B 122 ? 1.67639 0.60995 0.85073 -0.01081 -0.42719 0.09691  215 TYR   B CA  
3404 C C   . TYR   B 122 ? 1.83452 0.73245 1.00163 -0.00316 -0.44285 0.09048  215 TYR   B C   
3405 O O   . TYR   B 122 ? 1.83861 0.66587 0.95306 -0.00510 -0.46588 0.09307  215 TYR   B O   
3406 C CB  . TYR   B 122 ? 1.77333 0.72141 0.94072 -0.05780 -0.39374 0.11501  215 TYR   B CB  
3407 C CG  . TYR   B 122 ? 1.85030 0.72409 0.95692 -0.09198 -0.39775 0.13214  215 TYR   B CG  
3408 C CD1 . TYR   B 122 ? 1.94678 0.76209 0.99446 -0.10046 -0.41388 0.13723  215 TYR   B CD1 
3409 C CD2 . TYR   B 122 ? 1.88759 0.77813 1.01300 -0.11706 -0.37836 0.13446  215 TYR   B CD2 
3410 C CE1 . TYR   B 122 ? 1.86357 0.63629 0.86988 -0.13303 -0.41141 0.14560  215 TYR   B CE1 
3411 C CE2 . TYR   B 122 ? 2.02766 0.86851 1.10834 -0.14980 -0.37801 0.14501  215 TYR   B CE2 
3412 C CZ  . TYR   B 122 ? 2.03334 0.82101 1.05725 -0.15750 -0.39328 0.14936  215 TYR   B CZ  
3413 O OH  . TYR   B 122 ? 2.03551 0.78534 1.02021 -0.18997 -0.39092 0.15693  215 TYR   B OH  
3414 N N   . VAL   B 123 ? 1.78573 0.74549 1.01215 0.00410  -0.42670 0.07741  216 VAL   B N   
3415 C CA  . VAL   B 123 ? 1.73069 0.66034 0.95204 0.01045  -0.43990 0.07032  216 VAL   B CA  
3416 C C   . VAL   B 123 ? 1.82118 0.71820 1.03321 0.05527  -0.47700 0.05261  216 VAL   B C   
3417 O O   . VAL   B 123 ? 2.04997 0.89921 1.23948 0.06245  -0.49640 0.04747  216 VAL   B O   
3418 C CB  . VAL   B 123 ? 1.79681 0.80274 1.08254 0.00511  -0.41182 0.06133  216 VAL   B CB  
3419 C CG1 . VAL   B 123 ? 1.75705 0.79002 1.04964 -0.03875 -0.37803 0.07765  216 VAL   B CG1 
3420 C CG2 . VAL   B 123 ? 1.73848 0.82491 1.08801 0.03670  -0.40402 0.04278  216 VAL   B CG2 
3421 N N   . THR   B 124 ? 1.77005 0.69442 1.00052 0.08585  -0.48750 0.04136  217 THR   B N   
3422 C CA  . THR   B 124 ? 1.90885 0.81232 1.13615 0.12984  -0.52186 0.02108  217 THR   B CA  
3423 C C   . THR   B 124 ? 1.98311 0.81723 1.14977 0.12665  -0.54595 0.02176  217 THR   B C   
3424 O O   . THR   B 124 ? 2.00298 0.82626 1.16799 0.15982  -0.57205 0.00155  217 THR   B O   
3425 C CB  . THR   B 124 ? 1.89929 0.86855 1.17416 0.16072  -0.52157 0.00566  217 THR   B CB  
3426 O OG1 . THR   B 124 ? 1.91665 0.87632 1.16715 0.14751  -0.51874 0.01969  217 THR   B OG1 
3427 C CG2 . THR   B 124 ? 1.72176 0.79005 1.07165 0.15730  -0.48676 -0.00401 217 THR   B CG2 
3428 N N   . ASP   B 125 ? 2.22803 1.01741 1.34555 0.08746  -0.53754 0.04335  218 ASP   B N   
3429 C CA  . ASP   B 125 ? 2.33430 1.05473 1.38906 0.08041  -0.55939 0.04635  218 ASP   B CA  
3430 C C   . ASP   B 125 ? 2.34905 1.06972 1.39957 0.10879  -0.57849 0.03512  218 ASP   B C   
3431 O O   . ASP   B 125 ? 2.44298 1.11906 1.46134 0.12712  -0.60730 0.02364  218 ASP   B O   
3432 C CB  . ASP   B 125 ? 2.60474 1.27984 1.63572 0.08900  -0.58175 0.03610  218 ASP   B CB  
3433 C CG  . ASP   B 125 ? 2.67961 1.27778 1.63849 0.06794  -0.59838 0.04612  218 ASP   B CG  
3434 O OD1 . ASP   B 125 ? 2.81077 1.39125 1.73837 0.04643  -0.59165 0.06045  218 ASP   B OD1 
3435 O OD2 . ASP   B 125 ? 2.66080 1.21605 1.59316 0.07283  -0.61841 0.03947  218 ASP   B OD2 
3436 N N   . GLY   B 126 ? 2.07226 0.84410 1.15567 0.11253  -0.56296 0.03784  219 GLY   B N   
3437 C CA  . GLY   B 126 ? 2.27209 1.05046 1.35515 0.13612  -0.57779 0.02820  219 GLY   B CA  
3438 C C   . GLY   B 126 ? 2.20194 1.02139 1.33181 0.18347  -0.59544 -0.00009 219 GLY   B C   
3439 O O   . GLY   B 126 ? 2.26077 1.09728 1.40013 0.20408  -0.60551 -0.01008 219 GLY   B O   
3440 N N   . ALA   B 127 ? 2.11302 0.95178 1.27362 0.20091  -0.59876 -0.01460 220 ALA   B N   
3441 C CA  . ALA   B 127 ? 2.08963 0.97418 1.29759 0.24479  -0.61305 -0.04395 220 ALA   B CA  
3442 C C   . ALA   B 127 ? 2.04214 1.01112 1.31343 0.25741  -0.59447 -0.04979 220 ALA   B C   
3443 O O   . ALA   B 127 ? 2.06235 1.07668 1.37438 0.29173  -0.60434 -0.07462 220 ALA   B O   
3444 C CB  . ALA   B 127 ? 2.08906 0.97359 1.31164 0.25787  -0.61945 -0.05796 220 ALA   B CB  
3445 N N   . CYS   B 128 ? 1.96246 0.95556 1.24296 0.22982  -0.56795 -0.02860 221 CYS   B N   
3446 C CA  . CYS   B 128 ? 1.95909 1.03146 1.29596 0.23853  -0.55060 -0.03221 221 CYS   B CA  
3447 C C   . CYS   B 128 ? 1.93524 1.00372 1.25017 0.20871  -0.53444 -0.00844 221 CYS   B C   
3448 O O   . CYS   B 128 ? 1.88929 0.93196 1.17677 0.17118  -0.51540 0.01252  221 CYS   B O   
3449 C CB  . CYS   B 128 ? 1.79962 0.93335 1.19057 0.23381  -0.52483 -0.03770 221 CYS   B CB  
3450 S SG  . CYS   B 128 ? 1.82442 0.96190 1.23862 0.27108  -0.54525 -0.06439 221 CYS   B SG  
3451 N N   . SER   B 129 ? 1.82440 0.92744 1.15714 0.22194  -0.53703 -0.01530 222 SER   B N   
3452 C CA  . SER   B 129 ? 1.73653 0.84761 1.05583 0.19426  -0.51812 0.00226  222 SER   B CA  
3453 C C   . SER   B 129 ? 1.70066 0.90234 1.08550 0.17709  -0.47697 0.00027  222 SER   B C   
3454 O O   . SER   B 129 ? 1.66450 0.92425 1.10507 0.18964  -0.46564 -0.01537 222 SER   B O   
3455 C CB  . SER   B 129 ? 1.88415 0.99012 1.19232 0.21396  -0.53819 -0.00590 222 SER   B CB  
3456 O OG  . SER   B 129 ? 1.84757 1.02679 1.21806 0.24465  -0.54051 -0.02888 222 SER   B OG  
3457 N N   . GLY   B 130 ? 1.69125 0.90284 1.06656 0.14791  -0.45487 0.01625  223 GLY   B N   
3458 C CA  . GLY   B 130 ? 1.47230 0.76452 0.90553 0.13214  -0.41793 0.01488  223 GLY   B CA  
3459 C C   . GLY   B 130 ? 1.55588 0.91795 1.04708 0.15936  -0.41840 -0.00624 223 GLY   B C   
3460 O O   . GLY   B 130 ? 1.42704 0.85632 0.97575 0.15930  -0.39588 -0.01560 223 GLY   B O   
3461 N N   . ASP   B 131 ? 1.51492 0.86140 0.99067 0.18236  -0.44471 -0.01423 224 ASP   B N   
3462 C CA  . ASP   B 131 ? 1.57434 0.98751 1.10498 0.20796  -0.44709 -0.03581 224 ASP   B CA  
3463 C C   . ASP   B 131 ? 1.43339 0.87446 1.00232 0.23790  -0.45854 -0.05816 224 ASP   B C   
3464 O O   . ASP   B 131 ? 1.40160 0.91638 1.03073 0.24908  -0.44595 -0.07510 224 ASP   B O   
3465 C CB  . ASP   B 131 ? 1.62148 1.00907 1.12383 0.22494  -0.47439 -0.03925 224 ASP   B CB  
3466 C CG  . ASP   B 131 ? 1.73107 1.12081 1.21632 0.19850  -0.45722 -0.02360 224 ASP   B CG  
3467 O OD1 . ASP   B 131 ? 1.71763 1.13756 1.22109 0.16937  -0.42319 -0.01270 224 ASP   B OD1 
3468 O OD2 . ASP   B 131 ? 1.94144 1.30272 1.39465 0.20781  -0.47851 -0.02310 224 ASP   B OD2 
3469 N N   . GLU   B 132 ? 1.42626 0.80913 0.96015 0.25068  -0.48226 -0.05913 225 GLU   B N   
3470 C CA  . GLU   B 132 ? 1.54926 0.95788 1.11801 0.27845  -0.49177 -0.08108 225 GLU   B CA  
3471 C C   . GLU   B 132 ? 1.36670 0.83040 0.98107 0.26112  -0.45728 -0.08124 225 GLU   B C   
3472 O O   . GLU   B 132 ? 1.37006 0.89402 1.03671 0.27911  -0.45133 -0.10150 225 GLU   B O   
3473 C CB  . GLU   B 132 ? 1.56606 0.89327 1.08231 0.29393  -0.52480 -0.08079 225 GLU   B CB  
3474 C CG  . GLU   B 132 ? 1.72649 1.01568 1.21523 0.31931  -0.55749 -0.09277 225 GLU   B CG  
3475 C CD  . GLU   B 132 ? 1.92253 1.13418 1.36145 0.32358  -0.57878 -0.09429 225 GLU   B CD  
3476 O OE1 . GLU   B 132 ? 1.94207 1.09805 1.33656 0.29732  -0.57434 -0.07259 225 GLU   B OE1 
3477 O OE2 . GLU   B 132 ? 1.94163 1.14912 1.38573 0.35215  -0.59994 -0.11807 225 GLU   B OE2 
3478 N N   . ILE   B 133 ? 1.36020 0.80507 0.95505 0.22593  -0.43436 -0.05934 226 ILE   B N   
3479 C CA  . ILE   B 133 ? 1.30494 0.79829 0.93965 0.20892  -0.40301 -0.05836 226 ILE   B CA  
3480 C C   . ILE   B 133 ? 1.29330 0.86828 0.98459 0.20423  -0.37691 -0.06472 226 ILE   B C   
3481 O O   . ILE   B 133 ? 1.18175 0.81359 0.92090 0.20967  -0.36144 -0.07700 226 ILE   B O   
3482 C CB  . ILE   B 133 ? 1.27881 0.73150 0.87816 0.17279  -0.38700 -0.03439 226 ILE   B CB  
3483 C CG1 . ILE   B 133 ? 1.38954 0.76272 0.93580 0.17647  -0.41220 -0.02959 226 ILE   B CG1 
3484 C CG2 . ILE   B 133 ? 1.17848 0.68557 0.82077 0.15439  -0.35398 -0.03281 226 ILE   B CG2 
3485 C CD1 . ILE   B 133 ? 1.48459 0.81816 0.99640 0.13963  -0.39722 -0.00746 226 ILE   B CD1 
3486 N N   . LEU   B 134 ? 1.29852 0.87855 0.98296 0.19361  -0.37204 -0.05658 227 LEU   B N   
3487 C CA  . LEU   B 134 ? 1.14275 0.79510 0.87763 0.18840  -0.34894 -0.06236 227 LEU   B CA  
3488 C C   . LEU   B 134 ? 1.14265 0.84535 0.92120 0.21917  -0.36010 -0.08781 227 LEU   B C   
3489 O O   . LEU   B 134 ? 1.17099 0.94009 1.00031 0.21687  -0.33896 -0.09680 227 LEU   B O   
3490 C CB  . LEU   B 134 ? 1.18737 0.82884 0.90117 0.17194  -0.34433 -0.04941 227 LEU   B CB  
3491 C CG  . LEU   B 134 ? 1.31961 0.91813 0.99192 0.13933  -0.33062 -0.02535 227 LEU   B CG  
3492 C CD1 . LEU   B 134 ? 1.34167 0.94318 1.00178 0.12403  -0.32214 -0.01592 227 LEU   B CD1 
3493 C CD2 . LEU   B 134 ? 1.14687 0.77402 0.84508 0.11892  -0.30197 -0.01933 227 LEU   B CD2 
3494 N N   . THR   B 135 ? 1.12641 0.79894 0.88572 0.24770  -0.39333 -0.10014 228 THR   B N   
3495 C CA  . THR   B 135 ? 1.18217 0.90508 0.98503 0.27869  -0.40511 -0.12729 228 THR   B CA  
3496 C C   . THR   B 135 ? 1.23174 0.98372 1.06484 0.28785  -0.39716 -0.14020 228 THR   B C   
3497 O O   . THR   B 135 ? 1.24423 1.06459 1.12950 0.29769  -0.38593 -0.15846 228 THR   B O   
3498 C CB  . THR   B 135 ? 1.26873 0.94867 1.04142 0.30911  -0.44534 -0.13823 228 THR   B CB  
3499 O OG1 . THR   B 135 ? 1.37328 1.02568 1.11507 0.29953  -0.45237 -0.12568 228 THR   B OG1 
3500 C CG2 . THR   B 135 ? 1.02029 0.75886 0.84222 0.34204  -0.45773 -0.16899 228 THR   B CG2 
3501 N N   . MET   B 136 ? 1.27790 0.97881 1.07771 0.28298  -0.40200 -0.13090 229 MET   B N   
3502 C CA  . MET   B 136 ? 1.05556 0.77803 0.87880 0.29297  -0.39703 -0.14369 229 MET   B CA  
3503 C C   . MET   B 136 ? 1.13733 0.91388 0.99751 0.26813  -0.35948 -0.13734 229 MET   B C   
3504 O O   . MET   B 136 ? 1.00678 0.83522 0.90716 0.27790  -0.34913 -0.15361 229 MET   B O   
3505 C CB  . MET   B 136 ? 1.24886 0.89599 1.02263 0.29475  -0.41553 -0.13577 229 MET   B CB  
3506 C CG  . MET   B 136 ? 1.23736 0.89791 1.02919 0.31092  -0.41746 -0.15213 229 MET   B CG  
3507 S SD  . MET   B 136 ? 1.42737 1.11593 1.24615 0.35933  -0.44636 -0.18793 229 MET   B SD  
3508 C CE  . MET   B 136 ? 0.98401 0.78158 0.87752 0.35707  -0.41293 -0.20479 229 MET   B CE  
3509 N N   . GLU   B 137 ? 1.02860 0.79393 0.87483 0.23629  -0.33908 -0.11443 230 GLU   B N   
3510 C CA  . GLU   B 137 ? 1.03166 0.84364 0.91012 0.21367  -0.30565 -0.10791 230 GLU   B CA  
3511 C C   . GLU   B 137 ? 1.02035 0.90683 0.95071 0.21770  -0.29018 -0.12113 230 GLU   B C   
3512 O O   . GLU   B 137 ? 0.90483 0.83765 0.86889 0.21103  -0.26882 -0.12537 230 GLU   B O   
3513 C CB  . GLU   B 137 ? 1.06727 0.85303 0.92097 0.18077  -0.28878 -0.08267 230 GLU   B CB  
3514 C CG  . GLU   B 137 ? 1.13429 0.92763 0.98588 0.17107  -0.28449 -0.07530 230 GLU   B CG  
3515 C CD  . GLU   B 137 ? 1.14140 0.94455 0.99459 0.13905  -0.25669 -0.05682 230 GLU   B CD  
3516 O OE1 . GLU   B 137 ? 1.11098 0.91630 0.96817 0.12456  -0.24125 -0.04973 230 GLU   B OE1 
3517 O OE2 . GLU   B 137 ? 1.14299 0.95257 0.99399 0.12931  -0.25102 -0.05055 230 GLU   B OE2 
3518 N N   . LEU   B 138 ? 0.98003 0.87775 0.91595 0.22771  -0.30110 -0.12781 231 LEU   B N   
3519 C CA  . LEU   B 138 ? 0.94916 0.91719 0.93435 0.23088  -0.28793 -0.14172 231 LEU   B CA  
3520 C C   . LEU   B 138 ? 0.93780 0.94633 0.95589 0.25731  -0.29610 -0.16797 231 LEU   B C   
3521 O O   . LEU   B 138 ? 0.89961 0.96913 0.95988 0.25335  -0.27603 -0.17773 231 LEU   B O   
3522 C CB  . LEU   B 138 ? 0.90656 0.87425 0.88754 0.23338  -0.29841 -0.14200 231 LEU   B CB  
3523 C CG  . LEU   B 138 ? 1.04857 1.00986 1.01886 0.20440  -0.27954 -0.12128 231 LEU   B CG  
3524 C CD1 . LEU   B 138 ? 1.02528 0.97338 0.98090 0.20987  -0.29562 -0.12188 231 LEU   B CD1 
3525 C CD2 . LEU   B 138 ? 0.96023 0.98201 0.97413 0.18742  -0.24896 -0.12168 231 LEU   B CD2 
3526 N N   . MET   B 139 ? 1.01042 0.98528 1.00859 0.28429  -0.32558 -0.18018 232 MET   B N   
3527 C CA  . MET   B 139 ? 0.94943 0.96268 0.97833 0.31153  -0.33427 -0.20739 232 MET   B CA  
3528 C C   . MET   B 139 ? 0.86848 0.89744 0.90874 0.30412  -0.31568 -0.20780 232 MET   B C   
3529 O O   . MET   B 139 ? 0.83972 0.92706 0.91954 0.31330  -0.30540 -0.22700 232 MET   B O   
3530 C CB  . MET   B 139 ? 1.00191 0.96827 1.00268 0.34353  -0.37244 -0.22008 232 MET   B CB  
3531 C CG  . MET   B 139 ? 0.98866 0.95164 0.98610 0.35811  -0.39422 -0.22689 232 MET   B CG  
3532 S SD  . MET   B 139 ? 1.44570 1.35259 1.40987 0.39937  -0.44213 -0.24376 232 MET   B SD  
3533 C CE  . MET   B 139 ? 1.11529 0.91911 1.00603 0.38113  -0.45099 -0.21294 232 MET   B CE  
3534 N N   . ILE   B 140 ? 0.94822 0.92712 0.95391 0.28671  -0.31091 -0.18737 233 ILE   B N   
3535 C CA  . ILE   B 140 ? 0.82940 0.82031 0.84333 0.27869  -0.29418 -0.18679 233 ILE   B CA  
3536 C C   . ILE   B 140 ? 0.79891 0.85010 0.84968 0.25651  -0.26064 -0.18229 233 ILE   B C   
3537 O O   . ILE   B 140 ? 0.81643 0.91460 0.89709 0.26079  -0.24774 -0.19591 233 ILE   B O   
3538 C CB  . ILE   B 140 ? 0.93188 0.85488 0.90032 0.26354  -0.29790 -0.16597 233 ILE   B CB  
3539 C CG1 . ILE   B 140 ? 1.04560 0.90685 0.97632 0.28698  -0.33209 -0.17273 233 ILE   B CG1 
3540 C CG2 . ILE   B 140 ? 0.88709 0.82662 0.86599 0.25040  -0.27739 -0.16278 233 ILE   B CG2 
3541 C CD1 . ILE   B 140 ? 1.09996 0.89136 0.98354 0.27050  -0.33712 -0.15280 233 ILE   B CD1 
3542 N N   . MET   B 141 ? 0.89045 0.93974 0.93768 0.23260  -0.24650 -0.16348 234 MET   B N   
3543 C CA  . MET   B 141 ? 0.77640 0.87400 0.85329 0.21052  -0.21617 -0.15705 234 MET   B CA  
3544 C C   . MET   B 141 ? 0.77665 0.94104 0.89738 0.21972  -0.20909 -0.17687 234 MET   B C   
3545 O O   . MET   B 141 ? 0.73483 0.94445 0.88266 0.21015  -0.18747 -0.18046 234 MET   B O   
3546 C CB  . MET   B 141 ? 0.78662 0.86458 0.84872 0.18546  -0.20523 -0.13444 234 MET   B CB  
3547 C CG  . MET   B 141 ? 0.88412 0.90586 0.90780 0.17054  -0.20594 -0.11452 234 MET   B CG  
3548 S SD  . MET   B 141 ? 0.95423 0.96112 0.96440 0.14044  -0.18962 -0.09032 234 MET   B SD  
3549 C CE  . MET   B 141 ? 0.86290 0.85180 0.85833 0.15163  -0.20998 -0.09356 234 MET   B CE  
3550 N N   . LYS   B 142 ? 0.65926 0.83068 0.78659 0.23765  -0.22746 -0.19027 235 LYS   B N   
3551 C CA  . LYS   B 142 ? 0.69568 0.93363 0.86678 0.24589  -0.22165 -0.21106 235 LYS   B CA  
3552 C C   . LYS   B 142 ? 0.72313 0.99603 0.91630 0.26575  -0.22347 -0.23469 235 LYS   B C   
3553 O O   . LYS   B 142 ? 0.77214 1.10606 1.00184 0.26081  -0.20486 -0.24670 235 LYS   B O   
3554 C CB  . LYS   B 142 ? 0.77344 1.00924 0.94562 0.26088  -0.24309 -0.22023 235 LYS   B CB  
3555 C CG  . LYS   B 142 ? 0.78676 1.00730 0.94763 0.23979  -0.23641 -0.20122 235 LYS   B CG  
3556 C CD  . LYS   B 142 ? 0.84202 1.04146 0.98970 0.25655  -0.26328 -0.20744 235 LYS   B CD  
3557 C CE  . LYS   B 142 ? 0.95887 1.21592 1.14742 0.27726  -0.27248 -0.23577 235 LYS   B CE  
3558 N NZ  . LYS   B 142 ? 0.89387 1.13100 1.06970 0.29372  -0.29986 -0.24187 235 LYS   B NZ  
3559 N N   . ALA   B 143 ? 0.75099 0.98529 0.92107 0.28771  -0.24561 -0.24211 236 ALA   B N   
3560 C CA  . ALA   B 143 ? 0.80032 1.06602 0.98962 0.30849  -0.24830 -0.26620 236 ALA   B CA  
3561 C C   . ALA   B 143 ? 0.76381 1.04675 0.95827 0.29056  -0.22246 -0.25926 236 ALA   B C   
3562 O O   . ALA   B 143 ? 0.84264 1.17735 1.06562 0.29750  -0.21170 -0.27827 236 ALA   B O   
3563 C CB  . ALA   B 143 ? 0.75773 0.97076 0.91720 0.33699  -0.28046 -0.27542 236 ALA   B CB  
3564 N N   . LEU   B 144 ? 0.79507 1.03696 0.96221 0.26760  -0.21242 -0.23316 237 LEU   B N   
3565 C CA  . LEU   B 144 ? 0.75889 1.01321 0.92826 0.24958  -0.18923 -0.22451 237 LEU   B CA  
3566 C C   . LEU   B 144 ? 0.75625 1.05908 0.95233 0.22517  -0.16071 -0.21711 237 LEU   B C   
3567 O O   . LEU   B 144 ? 0.75350 1.06100 0.94744 0.20697  -0.14136 -0.20563 237 LEU   B O   
3568 C CB  . LEU   B 144 ? 0.69756 0.88891 0.82792 0.23569  -0.19181 -0.20109 237 LEU   B CB  
3569 C CG  . LEU   B 144 ? 0.81699 0.95301 0.91532 0.25541  -0.21838 -0.20585 237 LEU   B CG  
3570 C CD1 . LEU   B 144 ? 0.70344 0.78269 0.76586 0.23604  -0.21729 -0.18183 237 LEU   B CD1 
3571 C CD2 . LEU   B 144 ? 0.80560 0.96559 0.91658 0.27653  -0.22221 -0.22932 237 LEU   B CD2 
3572 N N   . LYS   B 145 ? 0.71226 1.04863 0.93174 0.22445  -0.15904 -0.22349 238 LYS   B N   
3573 C CA  . LYS   B 145 ? 0.64678 1.02483 0.88973 0.20056  -0.13392 -0.21641 238 LYS   B CA  
3574 C C   . LYS   B 145 ? 0.68504 1.02949 0.90697 0.17425  -0.12057 -0.18801 238 LYS   B C   
3575 O O   . LYS   B 145 ? 0.74943 1.11860 0.98302 0.15369  -0.09806 -0.17959 238 LYS   B O   
3576 C CB  . LYS   B 145 ? 0.75221 1.18690 1.02230 0.19781  -0.11473 -0.23086 238 LYS   B CB  
3577 C CG  . LYS   B 145 ? 0.76273 1.24432 1.06121 0.22182  -0.12392 -0.26188 238 LYS   B CG  
3578 C CD  . LYS   B 145 ? 0.87408 1.39162 1.19970 0.22080  -0.12520 -0.27078 238 LYS   B CD  
3579 C CE  . LYS   B 145 ? 1.02330 1.59604 1.38229 0.24397  -0.13280 -0.30398 238 LYS   B CE  
3580 N NZ  . LYS   B 145 ? 0.95065 1.56261 1.33896 0.24223  -0.13436 -0.31426 238 LYS   B NZ  
3581 N N   . TRP   B 146 ? 0.64050 0.92811 0.83045 0.17479  -0.13481 -0.17375 239 TRP   B N   
3582 C CA  . TRP   B 146 ? 0.69185 0.94648 0.86128 0.15174  -0.12425 -0.14863 239 TRP   B CA  
3583 C C   . TRP   B 146 ? 0.75526 1.01249 0.92189 0.13954  -0.10799 -0.14091 239 TRP   B C   
3584 O O   . TRP   B 146 ? 0.64869 0.89939 0.81082 0.11868  -0.09311 -0.12353 239 TRP   B O   
3585 C CB  . TRP   B 146 ? 0.63818 0.91036 0.82042 0.13435  -0.11197 -0.13950 239 TRP   B CB  
3586 C CG  . TRP   B 146 ? 0.62724 0.89283 0.80872 0.14478  -0.12865 -0.14535 239 TRP   B CG  
3587 C CD1 . TRP   B 146 ? 0.57573 0.87974 0.78295 0.15810  -0.13516 -0.16469 239 TRP   B CD1 
3588 C CD2 . TRP   B 146 ? 0.74117 0.95969 0.89387 0.14243  -0.14128 -0.13239 239 TRP   B CD2 
3589 N NE1 . TRP   B 146 ? 0.60427 0.88653 0.80017 0.16547  -0.15257 -0.16445 239 TRP   B NE1 
3590 C CE2 . TRP   B 146 ? 0.64495 0.87349 0.80564 0.15570  -0.15626 -0.14427 239 TRP   B CE2 
3591 C CE3 . TRP   B 146 ? 0.59491 0.76554 0.71575 0.12960  -0.14100 -0.11257 239 TRP   B CE3 
3592 C CZ2 . TRP   B 146 ? 0.67802 0.86700 0.81250 0.15677  -0.17130 -0.13594 239 TRP   B CZ2 
3593 C CZ3 . TRP   B 146 ? 0.73151 0.86511 0.82729 0.12927  -0.15421 -0.10460 239 TRP   B CZ3 
3594 C CH2 . TRP   B 146 ? 0.76891 0.91016 0.86991 0.14292  -0.16940 -0.11575 239 TRP   B CH2 
3595 N N   . ARG   B 147 ? 0.70333 0.96997 0.87213 0.15358  -0.11172 -0.15476 240 ARG   B N   
3596 C CA  . ARG   B 147 ? 0.72122 0.98489 0.88269 0.14473  -0.10003 -0.14866 240 ARG   B CA  
3597 C C   . ARG   B 147 ? 0.62015 0.82637 0.74862 0.14583  -0.11387 -0.13781 240 ARG   B C   
3598 O O   . ARG   B 147 ? 0.72601 0.91249 0.84184 0.16255  -0.12888 -0.14815 240 ARG   B O   
3599 C CB  . ARG   B 147 ? 0.75295 1.05474 0.93092 0.15840  -0.09674 -0.16949 240 ARG   B CB  
3600 C CG  . ARG   B 147 ? 0.71118 1.07239 0.92032 0.15064  -0.07783 -0.17818 240 ARG   B CG  
3601 C CD  . ARG   B 147 ? 0.90705 1.27361 1.11602 0.12362  -0.05611 -0.15873 240 ARG   B CD  
3602 N NE  . ARG   B 147 ? 1.03835 1.45729 1.27078 0.11448  -0.03694 -0.16681 240 ARG   B NE  
3603 C CZ  . ARG   B 147 ? 1.06353 1.51628 1.31864 0.10884  -0.03045 -0.17231 240 ARG   B CZ  
3604 N NH1 . ARG   B 147 ? 1.02885 1.47032 1.28731 0.11311  -0.04219 -0.17145 240 ARG   B NH1 
3605 N NH2 . ARG   B 147 ? 1.02563 1.52396 1.29898 0.09756  -0.01183 -0.17891 240 ARG   B NH2 
3606 N N   . LEU   B 148 ? 0.70281 0.88197 0.81705 0.12693  -0.10858 -0.11724 241 LEU   B N   
3607 C CA  . LEU   B 148 ? 0.70802 0.83307 0.79082 0.12361  -0.12059 -0.10556 241 LEU   B CA  
3608 C C   . LEU   B 148 ? 0.76901 0.88468 0.84421 0.10506  -0.10757 -0.09124 241 LEU   B C   
3609 O O   . LEU   B 148 ? 0.75321 0.83043 0.80641 0.09454  -0.11196 -0.07801 241 LEU   B O   
3610 C CB  . LEU   B 148 ? 0.75320 0.85056 0.82197 0.11813  -0.12842 -0.09512 241 LEU   B CB  
3611 C CG  . LEU   B 148 ? 0.77520 0.87923 0.84981 0.13622  -0.14339 -0.10825 241 LEU   B CG  
3612 C CD1 . LEU   B 148 ? 0.68079 0.75646 0.73826 0.12774  -0.14914 -0.09581 241 LEU   B CD1 
3613 C CD2 . LEU   B 148 ? 0.72743 0.81031 0.78942 0.16073  -0.16589 -0.12365 241 LEU   B CD2 
3614 N N   . SER   B 149 ? 0.70395 0.85394 0.79591 0.10048  -0.09212 -0.09404 242 SER   B N   
3615 C CA  . SER   B 149 ? 0.66316 0.80746 0.74946 0.08444  -0.08075 -0.08167 242 SER   B CA  
3616 C C   . SER   B 149 ? 0.75148 0.90569 0.83718 0.09267  -0.08043 -0.09207 242 SER   B C   
3617 O O   . SER   B 149 ? 0.79556 0.97986 0.89320 0.08626  -0.06557 -0.09223 242 SER   B O   
3618 C CB  . SER   B 149 ? 0.74276 0.91476 0.84569 0.06774  -0.06156 -0.07159 242 SER   B CB  
3619 O OG  . SER   B 149 ? 0.93348 1.09733 1.03693 0.06079  -0.06177 -0.06341 242 SER   B OG  
3620 N N   . PRO   B 150 ? 0.84889 0.97568 0.91815 0.10652  -0.09710 -0.10073 243 PRO   B N   
3621 C CA  . PRO   B 150 ? 0.65912 0.79331 0.72588 0.11532  -0.09785 -0.11196 243 PRO   B CA  
3622 C C   . PRO   B 150 ? 0.86736 0.97663 0.91806 0.10171  -0.09614 -0.10002 243 PRO   B C   
3623 O O   . PRO   B 150 ? 0.89467 0.97833 0.93539 0.08693  -0.09648 -0.08460 243 PRO   B O   
3624 C CB  . PRO   B 150 ? 0.79851 0.91014 0.85400 0.13807  -0.11945 -0.12767 243 PRO   B CB  
3625 C CG  . PRO   B 150 ? 0.67101 0.73833 0.70751 0.13276  -0.13202 -0.11550 243 PRO   B CG  
3626 C CD  . PRO   B 150 ? 0.78208 0.86677 0.83142 0.11547  -0.11740 -0.10132 243 PRO   B CD  
3627 N N   . LEU   B 151 ? 0.79027 0.90981 0.83916 0.10690  -0.09418 -0.10868 244 LEU   B N   
3628 C CA  . LEU   B 151 ? 0.85250 0.94889 0.88580 0.09746  -0.09584 -0.10144 244 LEU   B CA  
3629 C C   . LEU   B 151 ? 0.87704 0.93442 0.88940 0.11071  -0.11650 -0.11093 244 LEU   B C   
3630 O O   . LEU   B 151 ? 0.96288 1.02785 0.97404 0.12826  -0.12278 -0.12826 244 LEU   B O   
3631 C CB  . LEU   B 151 ? 0.65568 0.78305 0.69573 0.09464  -0.08252 -0.10471 244 LEU   B CB  
3632 C CG  . LEU   B 151 ? 0.80396 0.96488 0.86065 0.08084  -0.06314 -0.09470 244 LEU   B CG  
3633 C CD1 . LEU   B 151 ? 0.73338 0.91741 0.78967 0.07755  -0.05209 -0.09696 244 LEU   B CD1 
3634 C CD2 . LEU   B 151 ? 0.71707 0.86060 0.77291 0.06318  -0.06017 -0.07570 244 LEU   B CD2 
3635 N N   . THR   B 152 ? 0.77220 0.78702 0.76684 0.10176  -0.12699 -0.09998 245 THR   B N   
3636 C CA  . THR   B 152 ? 0.88011 0.84959 0.85062 0.11216  -0.14830 -0.10684 245 THR   B CA  
3637 C C   . THR   B 152 ? 0.86943 0.82746 0.82857 0.11250  -0.15243 -0.11242 245 THR   B C   
3638 O O   . THR   B 152 ? 0.83189 0.81408 0.79995 0.10262  -0.13919 -0.10867 245 THR   B O   
3639 C CB  . THR   B 152 ? 0.85367 0.77985 0.80530 0.09788  -0.15640 -0.09172 245 THR   B CB  
3640 O OG1 . THR   B 152 ? 0.85922 0.78512 0.81145 0.07421  -0.14511 -0.07653 245 THR   B OG1 
3641 C CG2 . THR   B 152 ? 0.81422 0.74905 0.77402 0.09887  -0.15406 -0.08724 245 THR   B CG2 
3642 N N   . ILE   B 153 ? 0.79672 0.71444 0.73385 0.12458  -0.17264 -0.12177 246 ILE   B N   
3643 C CA  . ILE   B 153 ? 0.84243 0.74198 0.76526 0.12479  -0.17958 -0.12768 246 ILE   B CA  
3644 C C   . ILE   B 153 ? 0.86962 0.75209 0.78516 0.09837  -0.17455 -0.11019 246 ILE   B C   
3645 O O   . ILE   B 153 ? 0.91871 0.81129 0.83549 0.09194  -0.16956 -0.11087 246 ILE   B O   
3646 C CB  . ILE   B 153 ? 0.85943 0.71279 0.75778 0.14307  -0.20446 -0.14104 246 ILE   B CB  
3647 C CG1 . ILE   B 153 ? 0.86940 0.74475 0.77881 0.17134  -0.21010 -0.16063 246 ILE   B CG1 
3648 C CG2 . ILE   B 153 ? 0.88951 0.72360 0.77269 0.14392  -0.21235 -0.14879 246 ILE   B CG2 
3649 C CD1 . ILE   B 153 ? 0.95533 0.78516 0.84122 0.19326  -0.23667 -0.17577 246 ILE   B CD1 
3650 N N   . VAL   B 154 ? 0.83924 0.69765 0.74735 0.08265  -0.17572 -0.09515 247 VAL   B N   
3651 C CA  . VAL   B 154 ? 0.82263 0.66677 0.72522 0.05712  -0.17122 -0.08039 247 VAL   B CA  
3652 C C   . VAL   B 154 ? 0.72871 0.61854 0.65674 0.04435  -0.15000 -0.07121 247 VAL   B C   
3653 O O   . VAL   B 154 ? 0.89697 0.78928 0.82700 0.02834  -0.14518 -0.06448 247 VAL   B O   
3654 C CB  . VAL   B 154 ? 0.89570 0.69812 0.77900 0.04349  -0.17918 -0.06841 247 VAL   B CB  
3655 C CG1 . VAL   B 154 ? 0.89368 0.71672 0.79037 0.04157  -0.16871 -0.06032 247 VAL   B CG1 
3656 C CG2 . VAL   B 154 ? 0.90635 0.69122 0.78167 0.01694  -0.17677 -0.05661 247 VAL   B CG2 
3657 N N   . SER   B 155 ? 0.71141 0.63713 0.65895 0.05132  -0.13815 -0.07147 248 SER   B N   
3658 C CA  . SER   B 155 ? 0.77222 0.73716 0.74126 0.04033  -0.11948 -0.06302 248 SER   B CA  
3659 C C   . SER   B 155 ? 0.78355 0.76986 0.75705 0.04356  -0.11494 -0.06946 248 SER   B C   
3660 O O   . SER   B 155 ? 0.79396 0.79470 0.77530 0.03044  -0.10609 -0.06117 248 SER   B O   
3661 C CB  . SER   B 155 ? 0.76003 0.75536 0.74661 0.04677  -0.10901 -0.06285 248 SER   B CB  
3662 O OG  . SER   B 155 ? 0.82909 0.84558 0.82143 0.06599  -0.10952 -0.07793 248 SER   B OG  
3663 N N   . TRP   B 156 ? 0.78653 0.77517 0.75427 0.06168  -0.12154 -0.08502 249 TRP   B N   
3664 C CA  . TRP   B 156 ? 0.78693 0.79298 0.75431 0.06479  -0.11802 -0.09194 249 TRP   B CA  
3665 C C   . TRP   B 156 ? 0.78599 0.76557 0.74000 0.05321  -0.12666 -0.08835 249 TRP   B C   
3666 O O   . TRP   B 156 ? 0.80507 0.80069 0.76276 0.04583  -0.12046 -0.08533 249 TRP   B O   
3667 C CB  . TRP   B 156 ? 0.77593 0.78953 0.73878 0.08710  -0.12373 -0.11149 249 TRP   B CB  
3668 C CG  . TRP   B 156 ? 0.78436 0.83836 0.76479 0.09647  -0.11109 -0.11724 249 TRP   B CG  
3669 C CD1 . TRP   B 156 ? 0.75381 0.81276 0.74052 0.11067  -0.11499 -0.12634 249 TRP   B CD1 
3670 C CD2 . TRP   B 156 ? 0.70928 0.80397 0.70258 0.09122  -0.09306 -0.11452 249 TRP   B CD2 
3671 N NE1 . TRP   B 156 ? 0.76381 0.86737 0.76908 0.11351  -0.09950 -0.13020 249 TRP   B NE1 
3672 C CE2 . TRP   B 156 ? 0.73533 0.85958 0.74331 0.10086  -0.08553 -0.12238 249 TRP   B CE2 
3673 C CE3 . TRP   B 156 ? 0.80473 0.91219 0.79717 0.07911  -0.08355 -0.10626 249 TRP   B CE3 
3674 C CZ2 . TRP   B 156 ? 0.79195 0.95680 0.81257 0.09642  -0.06764 -0.12154 249 TRP   B CZ2 
3675 C CZ3 . TRP   B 156 ? 0.83269 0.97696 0.83505 0.07625  -0.06705 -0.10475 249 TRP   B CZ3 
3676 C CH2 . TRP   B 156 ? 0.84416 1.01620 0.85994 0.08372  -0.05862 -0.11202 249 TRP   B CH2 
3677 N N   . LEU   B 157 ? 0.83255 0.77031 0.76979 0.05080  -0.14177 -0.08866 250 LEU   B N   
3678 C CA  . LEU   B 157 ? 0.84124 0.75336 0.76636 0.03693  -0.15009 -0.08541 250 LEU   B CA  
3679 C C   . LEU   B 157 ? 0.84888 0.77533 0.78749 0.01500  -0.13920 -0.07011 250 LEU   B C   
3680 O O   . LEU   B 157 ? 0.82937 0.75784 0.76819 0.00509  -0.14022 -0.06893 250 LEU   B O   
3681 C CB  . LEU   B 157 ? 0.86074 0.72187 0.76302 0.03575  -0.16788 -0.08710 250 LEU   B CB  
3682 C CG  . LEU   B 157 ? 0.87762 0.70838 0.76569 0.01888  -0.17753 -0.08433 250 LEU   B CG  
3683 C CD1 . LEU   B 157 ? 0.83537 0.67516 0.72068 0.02647  -0.18133 -0.09601 250 LEU   B CD1 
3684 C CD2 . LEU   B 157 ? 1.01679 0.79242 0.87820 0.01683  -0.19534 -0.08514 250 LEU   B CD2 
3685 N N   . ASN   B 158 ? 0.85164 0.78934 0.80223 0.00815  -0.12944 -0.05962 251 ASN   B N   
3686 C CA  . ASN   B 158 ? 0.90463 0.85985 0.87029 -0.01024 -0.11859 -0.04706 251 ASN   B CA  
3687 C C   . ASN   B 158 ? 0.92078 0.91256 0.90114 -0.00771 -0.10834 -0.04710 251 ASN   B C   
3688 O O   . ASN   B 158 ? 0.92871 0.92962 0.91639 -0.01960 -0.10608 -0.04208 251 ASN   B O   
3689 C CB  . ASN   B 158 ? 0.85672 0.81629 0.83066 -0.01585 -0.11047 -0.03758 251 ASN   B CB  
3690 C CG  . ASN   B 158 ? 1.06603 1.01179 1.03927 -0.03743 -0.10958 -0.02733 251 ASN   B CG  
3691 O OD1 . ASN   B 158 ? 1.24859 1.16009 1.20422 -0.04398 -0.11832 -0.02561 251 ASN   B OD1 
3692 N ND2 . ASN   B 158 ? 0.96904 0.94116 0.96045 -0.04877 -0.09928 -0.02098 251 ASN   B ND2 
3693 N N   . VAL   B 159 ? 0.93219 0.94504 0.91613 0.00734  -0.10254 -0.05314 252 VAL   B N   
3694 C CA  . VAL   B 159 ? 0.76375 0.80645 0.75543 0.00931  -0.09351 -0.05293 252 VAL   B CA  
3695 C C   . VAL   B 159 ? 0.90929 0.94436 0.88911 0.01049  -0.10229 -0.06003 252 VAL   B C   
3696 O O   . VAL   B 159 ? 0.94517 0.99231 0.92930 0.00324  -0.10000 -0.05555 252 VAL   B O   
3697 C CB  . VAL   B 159 ? 0.80926 0.87546 0.80492 0.02295  -0.08475 -0.05876 252 VAL   B CB  
3698 C CG1 . VAL   B 159 ? 0.99253 1.08640 0.99266 0.02156  -0.07421 -0.05577 252 VAL   B CG1 
3699 C CG2 . VAL   B 159 ? 0.74746 0.81872 0.75409 0.02249  -0.07851 -0.05356 252 VAL   B CG2 
3700 N N   . TYR   B 160 ? 0.86528 0.87899 0.82931 0.02061  -0.11384 -0.07200 253 TYR   B N   
3701 C CA  . TYR   B 160 ? 0.82789 0.83340 0.77882 0.02325  -0.12294 -0.08071 253 TYR   B CA  
3702 C C   . TYR   B 160 ? 0.97468 0.96447 0.92540 0.00625  -0.13033 -0.07471 253 TYR   B C   
3703 O O   . TYR   B 160 ? 0.91460 0.90948 0.86181 0.00393  -0.13407 -0.07754 253 TYR   B O   
3704 C CB  . TYR   B 160 ? 0.91611 0.89879 0.84991 0.03859  -0.13509 -0.09601 253 TYR   B CB  
3705 C CG  . TYR   B 160 ? 0.84684 0.84960 0.78289 0.05684  -0.12863 -0.10580 253 TYR   B CG  
3706 C CD1 . TYR   B 160 ? 0.79623 0.83647 0.74510 0.05760  -0.11229 -0.10181 253 TYR   B CD1 
3707 C CD2 . TYR   B 160 ? 0.80022 0.78443 0.72551 0.07312  -0.13950 -0.11992 253 TYR   B CD2 
3708 C CE1 . TYR   B 160 ? 0.91862 0.98093 0.87135 0.07203  -0.10534 -0.11179 253 TYR   B CE1 
3709 C CE2 . TYR   B 160 ? 0.73775 0.74537 0.66848 0.09024  -0.13367 -0.13116 253 TYR   B CE2 
3710 C CZ  . TYR   B 160 ? 0.85669 0.90522 0.80205 0.08863  -0.11578 -0.12717 253 TYR   B CZ  
3711 O OH  . TYR   B 160 ? 0.85105 0.92653 0.80355 0.10353  -0.10892 -0.13935 253 TYR   B OH  
3712 N N   . MET   B 161 ? 0.95319 0.92517 0.90728 -0.00646 -0.13242 -0.06699 254 MET   B N   
3713 C CA  . MET   B 161 ? 0.99786 0.95836 0.95373 -0.02498 -0.13815 -0.06234 254 MET   B CA  
3714 C C   . MET   B 161 ? 1.05225 1.04435 1.02859 -0.03475 -0.12820 -0.05357 254 MET   B C   
3715 O O   . MET   B 161 ? 1.04825 1.04392 1.02818 -0.04406 -0.13328 -0.05433 254 MET   B O   
3716 C CB  . MET   B 161 ? 0.90336 0.83470 0.85354 -0.03725 -0.14237 -0.05700 254 MET   B CB  
3717 C CG  . MET   B 161 ? 0.79769 0.68727 0.72308 -0.03103 -0.15788 -0.06591 254 MET   B CG  
3718 S SD  . MET   B 161 ? 1.04727 0.91931 0.95912 -0.03432 -0.17261 -0.07640 254 MET   B SD  
3719 C CE  . MET   B 161 ? 1.06978 0.94922 0.99629 -0.06365 -0.16950 -0.06617 254 MET   B CE  
3720 N N   . GLN   B 162 ? 0.95249 0.96721 0.94247 -0.03213 -0.11525 -0.04613 255 GLN   B N   
3721 C CA  . GLN   B 162 ? 1.00019 1.04248 1.00834 -0.03885 -0.10717 -0.03856 255 GLN   B CA  
3722 C C   . GLN   B 162 ? 1.14217 1.19980 1.14658 -0.03070 -0.10878 -0.04255 255 GLN   B C   
3723 O O   . GLN   B 162 ? 1.07919 1.14834 1.09199 -0.03720 -0.11136 -0.04058 255 GLN   B O   
3724 C CB  . GLN   B 162 ? 0.98050 1.03927 1.00118 -0.03715 -0.09400 -0.03040 255 GLN   B CB  
3725 C CG  . GLN   B 162 ? 1.02321 1.10667 1.06218 -0.04320 -0.08676 -0.02284 255 GLN   B CG  
3726 C CD  . GLN   B 162 ? 1.03142 1.11495 1.08261 -0.05917 -0.08951 -0.02034 255 GLN   B CD  
3727 O OE1 . GLN   B 162 ? 1.00381 1.06895 1.05073 -0.06891 -0.09254 -0.02063 255 GLN   B OE1 
3728 N NE2 . GLN   B 162 ? 1.16735 1.27159 1.23307 -0.06221 -0.08882 -0.01837 255 GLN   B NE2 
3729 N N   . VAL   B 163 ? 0.98117 1.04004 0.97249 -0.01637 -0.10755 -0.04888 256 VAL   B N   
3730 C CA  . VAL   B 163 ? 1.14799 1.21986 1.13092 -0.00935 -0.10824 -0.05237 256 VAL   B CA  
3731 C C   . VAL   B 163 ? 1.06970 1.12763 1.04182 -0.01160 -0.12237 -0.06046 256 VAL   B C   
3732 O O   . VAL   B 163 ? 1.08781 1.15591 1.05773 -0.01191 -0.12583 -0.06054 256 VAL   B O   
3733 C CB  . VAL   B 163 ? 1.02349 1.10316 0.99500 0.00485  -0.10142 -0.05830 256 VAL   B CB  
3734 C CG1 . VAL   B 163 ? 1.04830 1.14097 1.00730 0.01015  -0.10051 -0.06078 256 VAL   B CG1 
3735 C CG2 . VAL   B 163 ? 0.93545 1.02932 0.91927 0.00533  -0.08809 -0.05086 256 VAL   B CG2 
3736 N N   . ALA   B 164 ? 0.99740 1.02979 0.96118 -0.01338 -0.13196 -0.06736 257 ALA   B N   
3737 C CA  . ALA   B 164 ? 1.15865 1.17509 1.11186 -0.01716 -0.14628 -0.07559 257 ALA   B CA  
3738 C C   . ALA   B 164 ? 1.26344 1.28834 1.23221 -0.03302 -0.14986 -0.07009 257 ALA   B C   
3739 O O   . ALA   B 164 ? 1.16880 1.19505 1.13332 -0.03468 -0.15941 -0.07552 257 ALA   B O   
3740 C CB  . ALA   B 164 ? 1.03559 1.01800 0.97542 -0.01734 -0.15645 -0.08308 257 ALA   B CB  
3741 N N   . TYR   B 165 ? 1.15659 1.18923 1.14397 -0.04431 -0.14258 -0.06064 258 TYR   B N   
3742 C CA  . TYR   B 165 ? 1.13308 1.17958 1.13963 -0.05918 -0.14434 -0.05683 258 TYR   B CA  
3743 C C   . TYR   B 165 ? 1.23525 1.31125 1.25962 -0.05663 -0.13409 -0.04836 258 TYR   B C   
3744 O O   . TYR   B 165 ? 1.39974 1.48883 1.44433 -0.06731 -0.12931 -0.04296 258 TYR   B O   
3745 C CB  . TYR   B 165 ? 1.11879 1.15031 1.13173 -0.07659 -0.14482 -0.05441 258 TYR   B CB  
3746 C CG  . TYR   B 165 ? 1.24444 1.24545 1.24079 -0.08384 -0.15844 -0.06273 258 TYR   B CG  
3747 C CD1 . TYR   B 165 ? 1.17579 1.14545 1.14922 -0.07528 -0.16347 -0.06738 258 TYR   B CD1 
3748 C CD2 . TYR   B 165 ? 1.24028 1.24367 1.24410 -0.09881 -0.16734 -0.06701 258 TYR   B CD2 
3749 C CE1 . TYR   B 165 ? 1.25586 1.19298 1.21167 -0.08131 -0.17750 -0.07532 258 TYR   B CE1 
3750 C CE2 . TYR   B 165 ? 1.25173 1.22461 1.23904 -0.10699 -0.18039 -0.07468 258 TYR   B CE2 
3751 C CZ  . TYR   B 165 ? 1.14262 1.08027 1.10464 -0.09810 -0.18568 -0.07844 258 TYR   B CZ  
3752 O OH  . TYR   B 165 ? 1.33581 1.23861 1.27913 -0.10576 -0.20012 -0.08633 258 TYR   B OH  
3753 N N   . LEU   B 166 ? 1.19789 1.28362 1.21337 -0.04276 -0.13063 -0.04759 259 LEU   B N   
3754 C CA  . LEU   B 166 ? 1.29242 1.40077 1.31978 -0.03971 -0.12356 -0.03975 259 LEU   B CA  
3755 C C   . LEU   B 166 ? 1.40428 1.52469 1.43851 -0.04197 -0.13382 -0.04205 259 LEU   B C   
3756 O O   . LEU   B 166 ? 1.27279 1.38736 1.29177 -0.03736 -0.14394 -0.04883 259 LEU   B O   
3757 C CB  . LEU   B 166 ? 1.26045 1.37216 1.27234 -0.02651 -0.11596 -0.03753 259 LEU   B CB  
3758 C CG  . LEU   B 166 ? 1.22511 1.33866 1.24060 -0.02402 -0.10254 -0.03195 259 LEU   B CG  
3759 C CD1 . LEU   B 166 ? 1.24751 1.36672 1.24693 -0.01309 -0.09552 -0.03195 259 LEU   B CD1 
3760 C CD2 . LEU   B 166 ? 1.19055 1.31718 1.22762 -0.03071 -0.09545 -0.02272 259 LEU   B CD2 
3761 N N   . ASN   B 167 ? 1.63481 1.77288 1.69220 -0.04816 -0.13196 -0.03759 260 ASN   B N   
3762 C CA  . ASN   B 167 ? 1.91989 2.07301 1.98705 -0.04806 -0.14255 -0.04049 260 ASN   B CA  
3763 C C   . ASN   B 167 ? 2.13941 2.29622 2.19207 -0.03431 -0.14352 -0.03612 260 ASN   B C   
3764 O O   . ASN   B 167 ? 2.06084 2.21135 2.09841 -0.02723 -0.13399 -0.03057 260 ASN   B O   
3765 C CB  . ASN   B 167 ? 1.92502 2.09868 2.02315 -0.05740 -0.14010 -0.03897 260 ASN   B CB  
3766 C CG  . ASN   B 167 ? 1.80753 1.97611 1.91638 -0.07308 -0.13478 -0.04040 260 ASN   B CG  
3767 O OD1 . ASN   B 167 ? 1.70563 1.87147 1.81855 -0.08468 -0.14260 -0.04748 260 ASN   B OD1 
3768 N ND2 . ASN   B 167 ? 1.73247 1.89820 1.84402 -0.07451 -0.12182 -0.03352 260 ASN   B ND2 
3769 N N   . ASP   B 168 ? 2.74416 2.91103 2.80054 -0.03122 -0.15577 -0.03895 261 ASP   B N   
3770 C CA  . ASP   B 168 ? 2.86618 3.03326 2.90635 -0.01923 -0.15834 -0.03347 261 ASP   B CA  
3771 C C   . ASP   B 168 ? 2.73879 2.91246 2.78879 -0.01650 -0.14753 -0.02335 261 ASP   B C   
3772 O O   . ASP   B 168 ? 2.53516 2.70153 2.56536 -0.00890 -0.14338 -0.01605 261 ASP   B O   
3773 C CB  . ASP   B 168 ? 2.96950 3.14506 3.01277 -0.01571 -0.17612 -0.03896 261 ASP   B CB  
3774 C CG  . ASP   B 168 ? 2.93287 3.12902 3.01190 -0.02430 -0.18175 -0.04490 261 ASP   B CG  
3775 O OD1 . ASP   B 168 ? 2.91861 3.12057 3.01721 -0.03417 -0.17097 -0.04399 261 ASP   B OD1 
3776 O OD2 . ASP   B 168 ? 2.95872 3.16643 3.04601 -0.02145 -0.19703 -0.05114 261 ASP   B OD2 
3777 N N   . LEU   B 169 ? 2.30276 2.48950 2.38162 -0.02361 -0.14260 -0.02308 262 LEU   B N   
3778 C CA  . LEU   B 169 ? 2.08319 2.27459 2.17197 -0.02201 -0.13110 -0.01469 262 LEU   B CA  
3779 C C   . LEU   B 169 ? 2.01101 2.19197 2.09209 -0.02598 -0.11649 -0.01109 262 LEU   B C   
3780 O O   . LEU   B 169 ? 1.98586 2.16723 2.07886 -0.03512 -0.11205 -0.01413 262 LEU   B O   
3781 C CB  . LEU   B 169 ? 1.89991 2.11183 2.02236 -0.02728 -0.13193 -0.01773 262 LEU   B CB  
3782 C CG  . LEU   B 169 ? 1.77486 1.99701 1.91718 -0.04079 -0.13375 -0.02651 262 LEU   B CG  
3783 C CD1 . LEU   B 169 ? 1.44882 1.68432 1.61581 -0.04957 -0.12226 -0.02544 262 LEU   B CD1 
3784 C CD2 . LEU   B 169 ? 1.77485 2.01229 1.92992 -0.04054 -0.14988 -0.03580 262 LEU   B CD2 
3785 N N   . HIS   B 170 ? 2.00149 2.17289 2.06159 -0.01955 -0.10944 -0.00489 263 HIS   B N   
3786 C CA  . HIS   B 170 ? 1.90330 2.06688 1.95482 -0.02107 -0.09725 -0.00350 263 HIS   B CA  
3787 C C   . HIS   B 170 ? 1.92186 2.09136 1.99246 -0.02567 -0.08637 0.00148  263 HIS   B C   
3788 O O   . HIS   B 170 ? 1.93151 2.10371 2.00321 -0.02271 -0.08041 0.00853  263 HIS   B O   
3789 C CB  . HIS   B 170 ? 1.78807 1.94476 1.81322 -0.01417 -0.09238 0.00017  263 HIS   B CB  
3790 C CG  . HIS   B 170 ? 1.82566 1.97572 1.82823 -0.00975 -0.10149 -0.00570 263 HIS   B CG  
3791 N ND1 . HIS   B 170 ? 1.88267 2.02981 1.88739 -0.01178 -0.11203 -0.01493 263 HIS   B ND1 
3792 C CD2 . HIS   B 170 ? 1.68799 1.83298 1.66354 -0.00431 -0.10154 -0.00392 263 HIS   B CD2 
3793 C CE1 . HIS   B 170 ? 1.84337 1.98428 1.82420 -0.00640 -0.11877 -0.01923 263 HIS   B CE1 
3794 N NE2 . HIS   B 170 ? 1.70914 1.84913 1.67131 -0.00186 -0.11218 -0.01259 263 HIS   B NE2 
3795 N N   . GLU   B 171 ? 1.93989 2.10908 2.02320 -0.03358 -0.08425 -0.00212 264 GLU   B N   
3796 C CA  . GLU   B 171 ? 1.83847 2.01076 1.93574 -0.03861 -0.07370 0.00177  264 GLU   B CA  
3797 C C   . GLU   B 171 ? 1.70735 1.86653 1.79637 -0.04194 -0.07063 -0.00132 264 GLU   B C   
3798 O O   . GLU   B 171 ? 1.63441 1.78744 1.72653 -0.04973 -0.07565 -0.00594 264 GLU   B O   
3799 C CB  . GLU   B 171 ? 1.81020 1.99613 1.93213 -0.04613 -0.07503 0.00057  264 GLU   B CB  
3800 C CG  . GLU   B 171 ? 1.75738 1.94624 1.89159 -0.05209 -0.06401 0.00394  264 GLU   B CG  
3801 C CD  . GLU   B 171 ? 1.86447 2.05336 1.99551 -0.04518 -0.05552 0.01084  264 GLU   B CD  
3802 O OE1 . GLU   B 171 ? 1.82310 2.01541 1.95174 -0.03793 -0.05840 0.01373  264 GLU   B OE1 
3803 O OE2 . GLU   B 171 ? 1.80476 1.98856 1.93430 -0.04738 -0.04684 0.01334  264 GLU   B OE2 
3804 N N   . VAL   B 172 ? 1.44339 1.59772 1.52147 -0.03625 -0.06308 0.00079  265 VAL   B N   
3805 C CA  . VAL   B 172 ? 1.30825 1.44932 1.37584 -0.03516 -0.06276 -0.00391 265 VAL   B CA  
3806 C C   . VAL   B 172 ? 1.15216 1.28897 1.22847 -0.04070 -0.05676 -0.00135 265 VAL   B C   
3807 O O   . VAL   B 172 ? 1.09564 1.21777 1.16305 -0.04003 -0.05899 -0.00528 265 VAL   B O   
3808 C CB  . VAL   B 172 ? 1.27787 1.41957 1.32966 -0.02507 -0.05858 -0.00585 265 VAL   B CB  
3809 C CG1 . VAL   B 172 ? 1.18381 1.33342 1.24137 -0.02376 -0.04689 -0.00055 265 VAL   B CG1 
3810 C CG2 . VAL   B 172 ? 1.20364 1.33191 1.24158 -0.02024 -0.06414 -0.01516 265 VAL   B CG2 
3811 N N   . LEU   B 173 ? 1.08315 1.23063 1.17490 -0.04543 -0.05028 0.00453  266 LEU   B N   
3812 C CA  . LEU   B 173 ? 1.10609 1.24956 1.20363 -0.05061 -0.04415 0.00708  266 LEU   B CA  
3813 C C   . LEU   B 173 ? 0.99458 1.13263 1.09850 -0.06321 -0.04708 0.00615  266 LEU   B C   
3814 O O   . LEU   B 173 ? 0.91990 1.04578 1.01953 -0.06838 -0.04507 0.00711  266 LEU   B O   
3815 C CB  . LEU   B 173 ? 1.05232 1.20910 1.16143 -0.04945 -0.03485 0.01305  266 LEU   B CB  
3816 C CG  . LEU   B 173 ? 0.96979 1.12985 1.07153 -0.04076 -0.02931 0.01478  266 LEU   B CG  
3817 C CD1 . LEU   B 173 ? 0.92354 1.09237 1.03593 -0.04177 -0.02078 0.02050  266 LEU   B CD1 
3818 C CD2 . LEU   B 173 ? 0.95728 1.10782 1.04782 -0.03623 -0.02954 0.01013  266 LEU   B CD2 
3819 N N   . LEU   B 174 ? 1.01023 1.15714 1.12338 -0.06899 -0.05201 0.00401  267 LEU   B N   
3820 C CA  . LEU   B 174 ? 1.01143 1.15652 1.13146 -0.08372 -0.05379 0.00213  267 LEU   B CA  
3821 C C   . LEU   B 174 ? 1.11126 1.23526 1.21530 -0.08777 -0.06368 -0.00277 267 LEU   B C   
3822 O O   . LEU   B 174 ? 1.10031 1.22456 1.19955 -0.08223 -0.07166 -0.00714 267 LEU   B O   
3823 C CB  . LEU   B 174 ? 0.94321 1.11219 1.08446 -0.08832 -0.05454 0.00016  267 LEU   B CB  
3824 C CG  . LEU   B 174 ? 1.01292 1.19307 1.16995 -0.10385 -0.04921 -0.00082 267 LEU   B CG  
3825 C CD1 . LEU   B 174 ? 1.13197 1.34196 1.31398 -0.10203 -0.04792 -0.00354 267 LEU   B CD1 
3826 C CD2 . LEU   B 174 ? 0.99259 1.16157 1.14397 -0.11905 -0.05513 -0.00503 267 LEU   B CD2 
3827 N N   . PRO   B 175 ? 1.03306 1.13608 1.12623 -0.09727 -0.06441 -0.00229 268 PRO   B N   
3828 C CA  . PRO   B 175 ? 0.98939 1.06560 1.06313 -0.09932 -0.07530 -0.00703 268 PRO   B CA  
3829 C C   . PRO   B 175 ? 1.01880 1.09874 1.09854 -0.11178 -0.08249 -0.01173 268 PRO   B C   
3830 O O   . PRO   B 175 ? 1.05152 1.14872 1.14844 -0.12550 -0.07816 -0.01105 268 PRO   B O   
3831 C CB  . PRO   B 175 ? 1.03466 1.08536 1.09420 -0.10734 -0.07420 -0.00362 268 PRO   B CB  
3832 C CG  . PRO   B 175 ? 0.98418 1.05338 1.05996 -0.11773 -0.06266 0.00189  268 PRO   B CG  
3833 C CD  . PRO   B 175 ? 0.97308 1.07262 1.06788 -0.10603 -0.05613 0.00275  268 PRO   B CD  
3834 N N   . GLN   B 176 ? 0.94517 1.01044 1.01129 -0.10688 -0.09364 -0.01786 269 GLN   B N   
3835 C CA  . GLN   B 176 ? 1.06031 1.12702 1.13047 -0.11853 -0.10243 -0.02361 269 GLN   B CA  
3836 C C   . GLN   B 176 ? 1.06715 1.10607 1.11404 -0.11182 -0.11513 -0.03034 269 GLN   B C   
3837 O O   . GLN   B 176 ? 1.15277 1.19779 1.19520 -0.09677 -0.11916 -0.03446 269 GLN   B O   
3838 C CB  . GLN   B 176 ? 0.92550 1.02616 1.01752 -0.11500 -0.10212 -0.02563 269 GLN   B CB  
3839 C CG  . GLN   B 176 ? 1.17067 1.28020 1.27312 -0.12839 -0.11084 -0.03252 269 GLN   B CG  
3840 C CD  . GLN   B 176 ? 1.37984 1.47586 1.46682 -0.12101 -0.12448 -0.03981 269 GLN   B CD  
3841 O OE1 . GLN   B 176 ? 1.38494 1.48128 1.46217 -0.10328 -0.12634 -0.04025 269 GLN   B OE1 
3842 N NE2 . GLN   B 176 ? 1.18201 1.26594 1.26551 -0.13577 -0.13376 -0.04591 269 GLN   B NE2 
3843 N N   . TYR   B 177 ? 1.02388 1.03086 1.05404 -0.12328 -0.12152 -0.03156 270 TYR   B N   
3844 C CA  . TYR   B 177 ? 1.10046 1.07671 1.10764 -0.11850 -0.13539 -0.03923 270 TYR   B CA  
3845 C C   . TYR   B 177 ? 1.01514 0.95717 1.00723 -0.13838 -0.14179 -0.03857 270 TYR   B C   
3846 O O   . TYR   B 177 ? 1.15576 1.09329 1.14902 -0.15120 -0.13417 -0.03110 270 TYR   B O   
3847 C CB  . TYR   B 177 ? 1.10124 1.06386 1.09166 -0.09603 -0.13672 -0.04168 270 TYR   B CB  
3848 C CG  . TYR   B 177 ? 1.07528 1.02767 1.06095 -0.09287 -0.12964 -0.03520 270 TYR   B CG  
3849 C CD1 . TYR   B 177 ? 0.96014 0.87357 0.92484 -0.09896 -0.13678 -0.03451 270 TYR   B CD1 
3850 C CD2 . TYR   B 177 ? 0.91418 0.89334 0.91420 -0.08353 -0.11718 -0.02996 270 TYR   B CD2 
3851 C CE1 . TYR   B 177 ? 0.90621 0.80936 0.86494 -0.09491 -0.13207 -0.02898 270 TYR   B CE1 
3852 C CE2 . TYR   B 177 ? 1.04526 1.01606 1.04129 -0.08034 -0.11169 -0.02498 270 TYR   B CE2 
3853 C CZ  . TYR   B 177 ? 1.00524 0.93886 0.98086 -0.08549 -0.11939 -0.02466 270 TYR   B CZ  
3854 O OH  . TYR   B 177 ? 1.04373 0.96846 1.01410 -0.08135 -0.11547 -0.01998 270 TYR   B OH  
3855 N N   . PRO   B 178 ? 1.04715 0.96319 1.02302 -0.14250 -0.15575 -0.04609 271 PRO   B N   
3856 C CA  . PRO   B 178 ? 1.03301 0.91106 0.99064 -0.16370 -0.16292 -0.04493 271 PRO   B CA  
3857 C C   . PRO   B 178 ? 1.03788 0.87857 0.97105 -0.15848 -0.16422 -0.03988 271 PRO   B C   
3858 O O   . PRO   B 178 ? 0.98264 0.80778 0.90145 -0.13601 -0.17011 -0.04420 271 PRO   B O   
3859 C CB  . PRO   B 178 ? 0.82565 0.68197 0.76882 -0.16288 -0.17934 -0.05564 271 PRO   B CB  
3860 C CG  . PRO   B 178 ? 1.13470 1.03043 1.09766 -0.14970 -0.17803 -0.06127 271 PRO   B CG  
3861 C CD  . PRO   B 178 ? 1.08199 1.00370 1.05589 -0.13094 -0.16554 -0.05594 271 PRO   B CD  
3862 N N   . GLN   B 179 ? 1.01238 0.83953 0.94043 -0.17965 -0.15896 -0.03142 272 GLN   B N   
3863 C CA  . GLN   B 179 ? 0.99716 0.78379 0.89816 -0.17703 -0.16231 -0.02588 272 GLN   B CA  
3864 C C   . GLN   B 179 ? 1.01419 0.74451 0.88052 -0.17658 -0.18158 -0.03128 272 GLN   B C   
3865 O O   . GLN   B 179 ? 1.01574 0.71226 0.85883 -0.16095 -0.18985 -0.03167 272 GLN   B O   
3866 C CB  . GLN   B 179 ? 1.03385 0.82019 0.93536 -0.20199 -0.15131 -0.01513 272 GLN   B CB  
3867 C CG  . GLN   B 179 ? 1.07284 0.91387 1.00890 -0.20346 -0.13298 -0.01121 272 GLN   B CG  
3868 C CD  . GLN   B 179 ? 1.25038 1.09629 1.18921 -0.23173 -0.12171 -0.00348 272 GLN   B CD  
3869 O OE1 . GLN   B 179 ? 1.28702 1.12199 1.22050 -0.25727 -0.12400 -0.00403 272 GLN   B OE1 
3870 N NE2 . GLN   B 179 ? 1.22872 1.09176 1.17540 -0.22835 -0.10906 0.00314  272 GLN   B NE2 
3871 N N   . GLN   B 180 ? 0.98648 0.70573 0.84914 -0.19283 -0.19005 -0.03643 273 GLN   B N   
3872 C CA  . GLN   B 180 ? 1.15020 0.81146 0.97801 -0.19513 -0.20946 -0.04166 273 GLN   B CA  
3873 C C   . GLN   B 180 ? 1.11367 0.76245 0.93046 -0.16178 -0.22130 -0.05274 273 GLN   B C   
3874 O O   . GLN   B 180 ? 1.21420 0.81572 1.00116 -0.15054 -0.23455 -0.05502 273 GLN   B O   
3875 C CB  . GLN   B 180 ? 1.30938 0.96814 1.13992 -0.21946 -0.21538 -0.04631 273 GLN   B CB  
3876 C CG  . GLN   B 180 ? 1.48118 1.07617 1.27423 -0.22636 -0.23605 -0.05141 273 GLN   B CG  
3877 C CD  . GLN   B 180 ? 1.56146 1.11647 1.33129 -0.26023 -0.23699 -0.04137 273 GLN   B CD  
3878 O OE1 . GLN   B 180 ? 1.44467 0.98576 1.20257 -0.26426 -0.23045 -0.03065 273 GLN   B OE1 
3879 N NE2 . GLN   B 180 ? 1.53380 1.07000 1.29585 -0.28612 -0.24505 -0.04485 273 GLN   B NE2 
3880 N N   . ILE   B 181 ? 1.12732 0.81806 0.96689 -0.14528 -0.21705 -0.06040 274 ILE   B N   
3881 C CA  . ILE   B 181 ? 1.12659 0.81050 0.95630 -0.11508 -0.22642 -0.07241 274 ILE   B CA  
3882 C C   . ILE   B 181 ? 1.09117 0.78680 0.92391 -0.09199 -0.21925 -0.07059 274 ILE   B C   
3883 O O   . ILE   B 181 ? 1.07322 0.75360 0.89240 -0.06764 -0.22846 -0.08077 274 ILE   B O   
3884 C CB  . ILE   B 181 ? 1.12468 0.84641 0.97279 -0.10727 -0.22479 -0.08119 274 ILE   B CB  
3885 C CG1 . ILE   B 181 ? 1.01521 0.78659 0.88683 -0.08886 -0.20956 -0.07954 274 ILE   B CG1 
3886 C CG2 . ILE   B 181 ? 1.18429 0.92171 1.04741 -0.13438 -0.22286 -0.07839 274 ILE   B CG2 
3887 C CD1 . ILE   B 181 ? 1.08328 0.85954 0.94736 -0.06058 -0.21423 -0.09205 274 ILE   B CD1 
3888 N N   . PHE   B 182 ? 0.96390 0.68726 0.81473 -0.09889 -0.20337 -0.05916 275 PHE   B N   
3889 C CA  . PHE   B 182 ? 0.97399 0.70798 0.82806 -0.07915 -0.19700 -0.05742 275 PHE   B CA  
3890 C C   . PHE   B 182 ? 1.02873 0.71092 0.85263 -0.07380 -0.21027 -0.05737 275 PHE   B C   
3891 O O   . PHE   B 182 ? 0.97105 0.64724 0.78815 -0.04865 -0.21615 -0.06528 275 PHE   B O   
3892 C CB  . PHE   B 182 ? 0.91777 0.69024 0.79668 -0.08946 -0.17803 -0.04546 275 PHE   B CB  
3893 C CG  . PHE   B 182 ? 0.91431 0.69498 0.79585 -0.07330 -0.17175 -0.04264 275 PHE   B CG  
3894 C CD1 . PHE   B 182 ? 0.93450 0.75054 0.83239 -0.05201 -0.16448 -0.04807 275 PHE   B CD1 
3895 C CD2 . PHE   B 182 ? 0.96593 0.71882 0.83242 -0.08064 -0.17321 -0.03463 275 PHE   B CD2 
3896 C CE1 . PHE   B 182 ? 0.86936 0.69525 0.77160 -0.03854 -0.15883 -0.04648 275 PHE   B CE1 
3897 C CE2 . PHE   B 182 ? 0.99137 0.75275 0.86097 -0.06552 -0.16870 -0.03296 275 PHE   B CE2 
3898 C CZ  . PHE   B 182 ? 0.97822 0.77739 0.86732 -0.04456 -0.16149 -0.03933 275 PHE   B CZ  
3899 N N   . ILE   B 183 ? 1.01079 0.65504 0.81550 -0.09752 -0.21552 -0.04890 276 ILE   B N   
3900 C CA  . ILE   B 183 ? 1.06111 0.64993 0.83226 -0.09378 -0.22981 -0.04719 276 ILE   B CA  
3901 C C   . ILE   B 183 ? 1.14625 0.69118 0.89118 -0.07801 -0.25185 -0.06069 276 ILE   B C   
3902 O O   . ILE   B 183 ? 1.20349 0.70790 0.92348 -0.06231 -0.26628 -0.06416 276 ILE   B O   
3903 C CB  . ILE   B 183 ? 1.10807 0.66641 0.86193 -0.12651 -0.22834 -0.03324 276 ILE   B CB  
3904 C CG1 . ILE   B 183 ? 1.18361 0.72008 0.92733 -0.15105 -0.23546 -0.03459 276 ILE   B CG1 
3905 C CG2 . ILE   B 183 ? 1.00779 0.61280 0.78900 -0.14059 -0.20611 -0.02205 276 ILE   B CG2 
3906 C CD1 . ILE   B 183 ? 1.27431 0.73585 0.97289 -0.15959 -0.25638 -0.03414 276 ILE   B CD1 
3907 N N   . GLN   B 184 ? 1.13228 0.68380 0.88181 -0.08038 -0.25602 -0.06948 277 GLN   B N   
3908 C CA  . GLN   B 184 ? 1.23919 0.75165 0.96481 -0.06321 -0.27683 -0.08438 277 GLN   B CA  
3909 C C   . GLN   B 184 ? 1.11091 0.64668 0.84543 -0.02662 -0.27775 -0.09807 277 GLN   B C   
3910 O O   . GLN   B 184 ? 1.22041 0.71886 0.93232 -0.00566 -0.29504 -0.10877 277 GLN   B O   
3911 C CB  . GLN   B 184 ? 1.30233 0.81777 1.03081 -0.07650 -0.28075 -0.09060 277 GLN   B CB  
3912 C CG  . GLN   B 184 ? 1.38064 0.86942 1.09839 -0.11375 -0.28234 -0.08008 277 GLN   B CG  
3913 C CD  . GLN   B 184 ? 1.57151 1.07072 1.29714 -0.12707 -0.28571 -0.08721 277 GLN   B CD  
3914 O OE1 . GLN   B 184 ? 1.61184 1.13176 1.34602 -0.10742 -0.28886 -0.10013 277 GLN   B OE1 
3915 N NE2 . GLN   B 184 ? 1.50841 0.99449 1.23080 -0.16137 -0.28494 -0.07939 277 GLN   B NE2 
3916 N N   . ILE   B 185 ? 1.02559 0.62280 0.79242 -0.01873 -0.25959 -0.09853 278 ILE   B N   
3917 C CA  . ILE   B 185 ? 1.05723 0.68227 0.83422 0.01269  -0.25733 -0.11107 278 ILE   B CA  
3918 C C   . ILE   B 185 ? 1.05294 0.67014 0.82684 0.02520  -0.25780 -0.10792 278 ILE   B C   
3919 O O   . ILE   B 185 ? 1.04605 0.65789 0.81414 0.05232  -0.26688 -0.12148 278 ILE   B O   
3920 C CB  . ILE   B 185 ? 1.01568 0.70471 0.82436 0.01418  -0.23752 -0.11047 278 ILE   B CB  
3921 C CG1 . ILE   B 185 ? 1.10749 0.80231 0.91770 0.00155  -0.23915 -0.11334 278 ILE   B CG1 
3922 C CG2 . ILE   B 185 ? 0.98038 0.69916 0.79785 0.04374  -0.23399 -0.12421 278 ILE   B CG2 
3923 C CD1 . ILE   B 185 ? 0.98010 0.73166 0.81687 0.00190  -0.22207 -0.11153 278 ILE   B CD1 
3924 N N   . ALA   B 186 ? 1.07375 0.69190 0.85200 0.00625  -0.24840 -0.09126 279 ALA   B N   
3925 C CA  . ALA   B 186 ? 1.02230 0.62832 0.79427 0.01630  -0.25066 -0.08751 279 ALA   B CA  
3926 C C   . ALA   B 186 ? 1.13387 0.67391 0.86869 0.02605  -0.27568 -0.09348 279 ALA   B C   
3927 O O   . ALA   B 186 ? 1.10432 0.63533 0.83330 0.04889  -0.28428 -0.10026 279 ALA   B O   
3928 C CB  . ALA   B 186 ? 0.98136 0.59634 0.76073 -0.00848 -0.23660 -0.06857 279 ALA   B CB  
3929 N N   . GLU   B 187 ? 1.09383 0.58648 0.80296 0.00919  -0.28864 -0.09167 280 GLU   B N   
3930 C CA  . GLU   B 187 ? 1.22669 0.64931 0.89610 0.01788  -0.31470 -0.09733 280 GLU   B CA  
3931 C C   . GLU   B 187 ? 1.26373 0.68600 0.93166 0.05497  -0.32870 -0.11971 280 GLU   B C   
3932 O O   . GLU   B 187 ? 1.24512 0.63134 0.89276 0.07598  -0.34658 -0.12687 280 GLU   B O   
3933 C CB  . GLU   B 187 ? 1.41775 0.79353 1.06192 -0.00913 -0.32469 -0.09239 280 GLU   B CB  
3934 C CG  . GLU   B 187 ? 1.53647 0.83468 1.13655 -0.00021 -0.35383 -0.09989 280 GLU   B CG  
3935 C CD  . GLU   B 187 ? 1.92318 1.17885 1.50054 -0.02805 -0.36296 -0.09666 280 GLU   B CD  
3936 O OE1 . GLU   B 187 ? 1.93341 1.21789 1.52821 -0.05779 -0.34623 -0.08610 280 GLU   B OE1 
3937 O OE2 . GLU   B 187 ? 2.12725 1.32107 1.66992 -0.01995 -0.38751 -0.10564 280 GLU   B OE2 
3938 N N   . LEU   B 188 ? 1.21849 0.68126 0.90715 0.06409  -0.32124 -0.13185 281 LEU   B N   
3939 C CA  . LEU   B 188 ? 1.20228 0.67319 0.89225 0.09902  -0.33143 -0.15479 281 LEU   B CA  
3940 C C   . LEU   B 188 ? 1.18494 0.69611 0.89635 0.12253  -0.32329 -0.16015 281 LEU   B C   
3941 O O   . LEU   B 188 ? 1.18074 0.67815 0.88399 0.15184  -0.33855 -0.17680 281 LEU   B O   
3942 C CB  . LEU   B 188 ? 1.09630 0.60483 0.80237 0.10067  -0.32276 -0.16522 281 LEU   B CB  
3943 C CG  . LEU   B 188 ? 1.17258 0.70194 0.88383 0.13527  -0.32822 -0.19002 281 LEU   B CG  
3944 C CD1 . LEU   B 188 ? 1.27538 0.74234 0.95386 0.15551  -0.35721 -0.20531 281 LEU   B CD1 
3945 C CD2 . LEU   B 188 ? 1.16107 0.72578 0.88427 0.13273  -0.31849 -0.19774 281 LEU   B CD2 
3946 N N   . LEU   B 189 ? 1.08087 0.64221 0.82039 0.11038  -0.30009 -0.14730 282 LEU   B N   
3947 C CA  . LEU   B 189 ? 1.09642 0.69795 0.85772 0.12966  -0.29138 -0.15187 282 LEU   B CA  
3948 C C   . LEU   B 189 ? 1.12834 0.68907 0.87058 0.13620  -0.30624 -0.14756 282 LEU   B C   
3949 O O   . LEU   B 189 ? 1.10553 0.67797 0.85439 0.16286  -0.31262 -0.16048 282 LEU   B O   
3950 C CB  . LEU   B 189 ? 1.00008 0.66040 0.79352 0.11333  -0.26394 -0.13863 282 LEU   B CB  
3951 C CG  . LEU   B 189 ? 1.03459 0.74377 0.84911 0.11394  -0.24886 -0.14525 282 LEU   B CG  
3952 C CD1 . LEU   B 189 ? 0.96505 0.72001 0.80543 0.09451  -0.22490 -0.12936 282 LEU   B CD1 
3953 C CD2 . LEU   B 189 ? 1.02134 0.76166 0.84678 0.14434  -0.24934 -0.16688 282 LEU   B CD2 
3954 N N   . ASP   B 190 ? 1.14235 0.65563 0.86016 0.11185  -0.31217 -0.13004 283 ASP   B N   
3955 C CA  . ASP   B 190 ? 1.21328 0.68082 0.90632 0.11654  -0.32788 -0.12456 283 ASP   B CA  
3956 C C   . ASP   B 190 ? 1.29321 0.71055 0.95856 0.14487  -0.35723 -0.14245 283 ASP   B C   
3957 O O   . ASP   B 190 ? 1.37960 0.77459 1.03290 0.16302  -0.37178 -0.14599 283 ASP   B O   
3958 C CB  . ASP   B 190 ? 1.16335 0.58770 0.83134 0.08172  -0.32762 -0.10232 283 ASP   B CB  
3959 C CG  . ASP   B 190 ? 1.28370 0.75607 0.97854 0.05736  -0.30050 -0.08549 283 ASP   B CG  
3960 O OD1 . ASP   B 190 ? 1.18201 0.70998 0.90877 0.06929  -0.28548 -0.08854 283 ASP   B OD1 
3961 O OD2 . ASP   B 190 ? 1.34010 0.79474 1.02412 0.02596  -0.29437 -0.06999 283 ASP   B OD2 
3962 N N   . LEU   B 191 ? 1.25149 0.64968 0.90591 0.15016  -0.36760 -0.15475 284 LEU   B N   
3963 C CA  . LEU   B 191 ? 1.35591 0.70853 0.98562 0.18009  -0.39605 -0.17464 284 LEU   B CA  
3964 C C   . LEU   B 191 ? 1.39036 0.79669 1.04958 0.21675  -0.39366 -0.19847 284 LEU   B C   
3965 O O   . LEU   B 191 ? 1.46968 0.85741 1.12034 0.24555  -0.41267 -0.21217 284 LEU   B O   
3966 C CB  . LEU   B 191 ? 1.55299 0.86470 1.15950 0.17208  -0.40838 -0.18027 284 LEU   B CB  
3967 C CG  . LEU   B 191 ? 1.75879 0.98970 1.32159 0.18873  -0.44293 -0.19167 284 LEU   B CG  
3968 C CD1 . LEU   B 191 ? 1.67236 0.86274 1.21238 0.16859  -0.45059 -0.19052 284 LEU   B CD1 
3969 C CD2 . LEU   B 191 ? 1.78223 1.02668 1.35319 0.23393  -0.45746 -0.22055 284 LEU   B CD2 
3970 N N   . CYS   B 192 ? 1.27859 0.75226 0.97213 0.21571  -0.37062 -0.20408 285 CYS   B N   
3971 C CA  . CYS   B 192 ? 1.30943 0.83800 1.03073 0.24708  -0.36566 -0.22746 285 CYS   B CA  
3972 C C   . CYS   B 192 ? 1.30666 0.86821 1.04876 0.25956  -0.36007 -0.22742 285 CYS   B C   
3973 O O   . CYS   B 192 ? 1.32543 0.91244 1.08147 0.29086  -0.36649 -0.24956 285 CYS   B O   
3974 C CB  . CYS   B 192 ? 1.37376 0.96465 1.12304 0.23810  -0.34043 -0.22970 285 CYS   B CB  
3975 S SG  . CYS   B 192 ? 1.40597 0.96742 1.13467 0.22685  -0.34704 -0.23377 285 CYS   B SG  
3976 N N   . VAL   B 193 ? 1.30698 0.87093 1.05258 0.23572  -0.34814 -0.20422 286 VAL   B N   
3977 C CA  . VAL   B 193 ? 1.26153 0.85748 1.02706 0.24563  -0.34244 -0.20360 286 VAL   B CA  
3978 C C   . VAL   B 193 ? 1.18639 0.73169 0.92715 0.26895  -0.37169 -0.21195 286 VAL   B C   
3979 O O   . VAL   B 193 ? 1.29802 0.87181 1.05664 0.28839  -0.37320 -0.22099 286 VAL   B O   
3980 C CB  . VAL   B 193 ? 1.12718 0.73867 0.90191 0.21369  -0.32173 -0.17717 286 VAL   B CB  
3981 C CG1 . VAL   B 193 ? 1.18090 0.72319 0.91808 0.19500  -0.33614 -0.15844 286 VAL   B CG1 
3982 C CG2 . VAL   B 193 ? 1.01209 0.67856 0.81858 0.22241  -0.30804 -0.17902 286 VAL   B CG2 
3983 N N   . LEU   B 194 ? 1.26196 0.73129 0.96096 0.26774  -0.39626 -0.20975 287 LEU   B N   
3984 C CA  . LEU   B 194 ? 1.35950 0.77326 1.02990 0.29215  -0.42761 -0.21855 287 LEU   B CA  
3985 C C   . LEU   B 194 ? 1.45744 0.89191 1.14154 0.33454  -0.44230 -0.25123 287 LEU   B C   
3986 O O   . LEU   B 194 ? 1.54693 0.96182 1.22314 0.36154  -0.46416 -0.26289 287 LEU   B O   
3987 C CB  . LEU   B 194 ? 1.36058 0.68333 0.97914 0.27738  -0.45012 -0.20697 287 LEU   B CB  
3988 C CG  . LEU   B 194 ? 1.40234 0.70123 1.00431 0.23394  -0.43671 -0.17601 287 LEU   B CG  
3989 C CD1 . LEU   B 194 ? 1.56196 0.76848 1.11017 0.21952  -0.46052 -0.16645 287 LEU   B CD1 
3990 C CD2 . LEU   B 194 ? 1.34283 0.65892 0.95289 0.22714  -0.42788 -0.16173 287 LEU   B CD2 
3991 N N   . ASP   B 195 ? 1.37930 0.85374 1.08331 0.34148  -0.43124 -0.26711 288 ASP   B N   
3992 C CA  . ASP   B 195 ? 1.48847 0.99390 1.20995 0.38052  -0.44070 -0.30010 288 ASP   B CA  
3993 C C   . ASP   B 195 ? 1.36897 0.96395 1.13904 0.38825  -0.41637 -0.30848 288 ASP   B C   
3994 O O   . ASP   B 195 ? 1.37396 1.02015 1.16827 0.36463  -0.38647 -0.29636 288 ASP   B O   
3995 C CB  . ASP   B 195 ? 1.46688 0.97193 1.18354 0.38347  -0.44005 -0.31394 288 ASP   B CB  
3996 C CG  . ASP   B 195 ? 1.52469 1.04305 1.24847 0.42608  -0.45681 -0.35007 288 ASP   B CG  
3997 O OD1 . ASP   B 195 ? 1.52351 1.09872 1.27951 0.44890  -0.45125 -0.36721 288 ASP   B OD1 
3998 O OD2 . ASP   B 195 ? 1.68828 1.16120 1.38599 0.43673  -0.47573 -0.36254 288 ASP   B OD2 
3999 N N   . VAL   B 196 ? 1.35299 0.96590 1.13680 0.42138  -0.43019 -0.32988 289 VAL   B N   
4000 C CA  . VAL   B 196 ? 1.38451 1.08002 1.21387 0.42772  -0.40898 -0.33811 289 VAL   B CA  
4001 C C   . VAL   B 196 ? 1.28818 1.05585 1.14984 0.43169  -0.38532 -0.35573 289 VAL   B C   
4002 O O   . VAL   B 196 ? 1.27533 1.11305 1.17277 0.42309  -0.35910 -0.35471 289 VAL   B O   
4003 C CB  . VAL   B 196 ? 1.37789 1.07411 1.21417 0.46342  -0.43236 -0.35890 289 VAL   B CB  
4004 C CG1 . VAL   B 196 ? 1.21835 0.98622 1.09580 0.46042  -0.41189 -0.35817 289 VAL   B CG1 
4005 C CG2 . VAL   B 196 ? 1.48948 1.09525 1.28032 0.46603  -0.46446 -0.34630 289 VAL   B CG2 
4006 N N   . ASP   B 197 ? 1.34671 1.09745 1.19442 0.44345  -0.39387 -0.37171 290 ASP   B N   
4007 C CA  . ASP   B 197 ? 1.33712 1.15356 1.21074 0.44787  -0.37232 -0.38955 290 ASP   B CA  
4008 C C   . ASP   B 197 ? 1.30302 1.14974 1.18538 0.41082  -0.34078 -0.36628 290 ASP   B C   
4009 O O   . ASP   B 197 ? 1.24749 1.15071 1.14992 0.41066  -0.32020 -0.37774 290 ASP   B O   
4010 C CB  . ASP   B 197 ? 1.38188 1.16687 1.23439 0.47071  -0.39174 -0.41312 290 ASP   B CB  
4011 C CG  . ASP   B 197 ? 1.47358 1.25139 1.32802 0.51430  -0.41909 -0.44499 290 ASP   B CG  
4012 O OD1 . ASP   B 197 ? 1.44448 1.28564 1.33367 0.52664  -0.41071 -0.45689 290 ASP   B OD1 
4013 O OD2 . ASP   B 197 ? 1.51102 1.23190 1.33443 0.52341  -0.44609 -0.44708 290 ASP   B OD2 
4014 N N   . CYS   B 198 ? 1.32133 1.13295 1.18862 0.38005  -0.33665 -0.33491 291 CYS   B N   
4015 C CA  . CYS   B 198 ? 1.21122 1.05290 1.08884 0.34687  -0.30821 -0.31363 291 CYS   B CA  
4016 C C   . CYS   B 198 ? 1.20775 1.12458 1.12346 0.34098  -0.28125 -0.31236 291 CYS   B C   
4017 O O   . CYS   B 198 ? 1.12895 1.08491 1.05736 0.32218  -0.25690 -0.30438 291 CYS   B O   
4018 C CB  . CYS   B 198 ? 1.13664 0.92555 0.99130 0.31683  -0.31092 -0.28265 291 CYS   B CB  
4019 S SG  . CYS   B 198 ? 1.29270 1.07333 1.15221 0.30955  -0.31260 -0.26498 291 CYS   B SG  
4020 N N   . LEU   B 199 ? 1.20321 1.13953 1.13616 0.35656  -0.28612 -0.32045 292 LEU   B N   
4021 C CA  . LEU   B 199 ? 1.14960 1.15565 1.11866 0.34977  -0.26153 -0.31972 292 LEU   B CA  
4022 C C   . LEU   B 199 ? 1.20334 1.27517 1.19612 0.36002  -0.24396 -0.34222 292 LEU   B C   
4023 O O   . LEU   B 199 ? 1.14724 1.27736 1.16685 0.34772  -0.21923 -0.33907 292 LEU   B O   
4024 C CB  . LEU   B 199 ? 1.15665 1.16760 1.13842 0.36624  -0.27377 -0.32628 292 LEU   B CB  
4025 C CG  . LEU   B 199 ? 1.19085 1.14300 1.14964 0.35368  -0.28794 -0.30253 292 LEU   B CG  
4026 C CD1 . LEU   B 199 ? 1.14708 1.10905 1.11916 0.37172  -0.30015 -0.31102 292 LEU   B CD1 
4027 C CD2 . LEU   B 199 ? 1.09300 1.04918 1.05251 0.31639  -0.26512 -0.27213 292 LEU   B CD2 
4028 N N   . GLU   B 200 ? 1.10420 1.16703 1.08611 0.38168  -0.25615 -0.36521 293 GLU   B N   
4029 C CA  . GLU   B 200 ? 1.16339 1.28638 1.16280 0.38835  -0.23777 -0.38565 293 GLU   B CA  
4030 C C   . GLU   B 200 ? 1.09415 1.23833 1.09307 0.35626  -0.21073 -0.36490 293 GLU   B C   
4031 O O   . GLU   B 200 ? 1.13147 1.33763 1.15179 0.34984  -0.18637 -0.37070 293 GLU   B O   
4032 C CB  . GLU   B 200 ? 1.13492 1.23392 1.11627 0.41483  -0.25705 -0.41140 293 GLU   B CB  
4033 C CG  . GLU   B 200 ? 1.28163 1.43467 1.27293 0.41867  -0.23799 -0.43076 293 GLU   B CG  
4034 C CD  . GLU   B 200 ? 1.16758 1.28789 1.13548 0.44107  -0.25737 -0.45280 293 GLU   B CD  
4035 O OE1 . GLU   B 200 ? 1.23036 1.29101 1.17847 0.45904  -0.28740 -0.45801 293 GLU   B OE1 
4036 O OE2 . GLU   B 200 ? 1.18149 1.33316 1.14838 0.44033  -0.24316 -0.46473 293 GLU   B OE2 
4037 N N   . PHE   B 201 ? 1.00605 1.09921 0.98016 0.33536  -0.21507 -0.34081 294 PHE   B N   
4038 C CA  . PHE   B 201 ? 1.07776 1.18373 1.04900 0.30638  -0.19363 -0.32064 294 PHE   B CA  
4039 C C   . PHE   B 201 ? 0.97317 1.08180 0.95440 0.28086  -0.18118 -0.29267 294 PHE   B C   
4040 O O   . PHE   B 201 ? 0.93002 1.00189 0.90539 0.27964  -0.19488 -0.28182 294 PHE   B O   
4041 C CB  . PHE   B 201 ? 1.07376 1.12645 1.01414 0.29887  -0.20606 -0.31337 294 PHE   B CB  
4042 C CG  . PHE   B 201 ? 1.00352 1.03291 0.92772 0.32591  -0.22655 -0.33965 294 PHE   B CG  
4043 C CD1 . PHE   B 201 ? 1.07128 1.14037 0.99994 0.33882  -0.21748 -0.36221 294 PHE   B CD1 
4044 C CD2 . PHE   B 201 ? 1.09311 1.05887 0.99530 0.33814  -0.25519 -0.34204 294 PHE   B CD2 
4045 C CE1 . PHE   B 201 ? 1.18592 1.23372 1.09969 0.36512  -0.23678 -0.38812 294 PHE   B CE1 
4046 C CE2 . PHE   B 201 ? 1.12085 1.06126 1.00665 0.36412  -0.27576 -0.36692 294 PHE   B CE2 
4047 C CZ  . PHE   B 201 ? 1.17452 1.15698 1.06725 0.37846  -0.26663 -0.39070 294 PHE   B CZ  
4048 N N   . PRO   B 202 ? 0.93610 1.08580 0.93023 0.26059  -0.15594 -0.28104 295 PRO   B N   
4049 C CA  . PRO   B 202 ? 0.81987 0.97147 0.82298 0.23661  -0.14412 -0.25512 295 PRO   B CA  
4050 C C   . PRO   B 202 ? 0.99987 1.09503 0.98152 0.22004  -0.15484 -0.23311 295 PRO   B C   
4051 O O   . PRO   B 202 ? 0.85874 0.91952 0.81901 0.22034  -0.16600 -0.23440 295 PRO   B O   
4052 C CB  . PRO   B 202 ? 0.83320 1.03224 0.84705 0.21977  -0.11768 -0.24918 295 PRO   B CB  
4053 C CG  . PRO   B 202 ? 0.82262 1.05922 0.84120 0.23793  -0.11305 -0.27590 295 PRO   B CG  
4054 C CD  . PRO   B 202 ? 0.77918 0.97575 0.77898 0.25954  -0.13725 -0.29219 295 PRO   B CD  
4055 N N   . TYR   B 203 ? 0.86350 0.95095 0.85155 0.20458  -0.15091 -0.21349 296 TYR   B N   
4056 C CA  . TYR   B 203 ? 0.87807 0.91661 0.84807 0.18710  -0.15925 -0.19295 296 TYR   B CA  
4057 C C   . TYR   B 203 ? 0.76667 0.80400 0.72886 0.16852  -0.14988 -0.18172 296 TYR   B C   
4058 O O   . TYR   B 203 ? 0.83212 0.82782 0.77477 0.16089  -0.16158 -0.17525 296 TYR   B O   
4059 C CB  . TYR   B 203 ? 0.83322 0.87220 0.81352 0.17359  -0.15337 -0.17537 296 TYR   B CB  
4060 C CG  . TYR   B 203 ? 0.91155 0.93622 0.89242 0.19000  -0.16822 -0.18305 296 TYR   B CG  
4061 C CD1 . TYR   B 203 ? 0.84995 0.85331 0.81953 0.21505  -0.18871 -0.20295 296 TYR   B CD1 
4062 C CD2 . TYR   B 203 ? 0.77841 0.80919 0.76985 0.18146  -0.16319 -0.17103 296 TYR   B CD2 
4063 C CE1 . TYR   B 203 ? 0.89259 0.88074 0.86124 0.23174  -0.20468 -0.21031 296 TYR   B CE1 
4064 C CE2 . TYR   B 203 ? 0.93888 0.95550 0.92909 0.19689  -0.17823 -0.17801 296 TYR   B CE2 
4065 C CZ  . TYR   B 203 ? 0.93354 0.92859 0.91223 0.22229  -0.19942 -0.19746 296 TYR   B CZ  
4066 O OH  . TYR   B 203 ? 0.99438 0.97344 0.97054 0.23933  -0.21667 -0.20478 296 TYR   B OH  
4067 N N   . GLY   B 204 ? 0.74222 0.82389 0.71842 0.16049  -0.12958 -0.17940 297 GLY   B N   
4068 C CA  . GLY   B 204 ? 0.80978 0.89143 0.77764 0.14531  -0.12228 -0.17013 297 GLY   B CA  
4069 C C   . GLY   B 204 ? 0.88312 0.94975 0.83292 0.15642  -0.13303 -0.18526 297 GLY   B C   
4070 O O   . GLY   B 204 ? 0.83276 0.87934 0.76939 0.14494  -0.13638 -0.17772 297 GLY   B O   
4071 N N   . ILE   B 205 ? 0.90174 0.97903 0.85148 0.17939  -0.13912 -0.20803 298 ILE   B N   
4072 C CA  . ILE   B 205 ? 0.83756 0.89896 0.76912 0.19252  -0.15077 -0.22505 298 ILE   B CA  
4073 C C   . ILE   B 205 ? 0.91468 0.91554 0.82567 0.19475  -0.17477 -0.22378 298 ILE   B C   
4074 O O   . ILE   B 205 ? 0.91131 0.88547 0.80393 0.19067  -0.18363 -0.22479 298 ILE   B O   
4075 C CB  . ILE   B 205 ? 0.89827 0.99309 0.83781 0.21760  -0.14944 -0.25194 298 ILE   B CB  
4076 C CG1 . ILE   B 205 ? 0.93167 1.08598 0.88768 0.21105  -0.12396 -0.25280 298 ILE   B CG1 
4077 C CG2 . ILE   B 205 ? 0.86428 0.93866 0.78384 0.23397  -0.16390 -0.27177 298 ILE   B CG2 
4078 C CD1 . ILE   B 205 ? 1.00198 1.16521 0.94442 0.19915  -0.11395 -0.24858 298 ILE   B CD1 
4079 N N   . LEU   B 206 ? 0.88193 0.85857 0.79379 0.20019  -0.18612 -0.22133 299 LEU   B N   
4080 C CA  . LEU   B 206 ? 0.96901 0.88346 0.85731 0.20066  -0.20934 -0.21895 299 LEU   B CA  
4081 C C   . LEU   B 206 ? 0.97050 0.85819 0.84858 0.17275  -0.20802 -0.19727 299 LEU   B C   
4082 O O   . LEU   B 206 ? 0.97654 0.82292 0.83311 0.16910  -0.22280 -0.19869 299 LEU   B O   
4083 C CB  . LEU   B 206 ? 0.86725 0.76202 0.75668 0.20958  -0.22029 -0.21774 299 LEU   B CB  
4084 C CG  . LEU   B 206 ? 0.92606 0.83179 0.82064 0.24142  -0.23113 -0.24276 299 LEU   B CG  
4085 C CD1 . LEU   B 206 ? 1.06497 0.96373 0.96640 0.24689  -0.23729 -0.23820 299 LEU   B CD1 
4086 C CD2 . LEU   B 206 ? 1.02873 0.88813 0.89742 0.25942  -0.25558 -0.25975 299 LEU   B CD2 
4087 N N   . ALA   B 207 ? 0.81166 0.72321 0.70570 0.15286  -0.19081 -0.17819 300 ALA   B N   
4088 C CA  . ALA   B 207 ? 0.91669 0.80966 0.80537 0.12696  -0.18857 -0.15918 300 ALA   B CA  
4089 C C   . ALA   B 207 ? 0.85187 0.75373 0.73538 0.12149  -0.18579 -0.16253 300 ALA   B C   
4090 O O   . ALA   B 207 ? 0.88331 0.75424 0.75338 0.10801  -0.19490 -0.15693 300 ALA   B O   
4091 C CB  . ALA   B 207 ? 0.73468 0.65476 0.64323 0.11018  -0.17092 -0.14068 300 ALA   B CB  
4092 N N   . ALA   B 208 ? 0.82177 0.76582 0.71476 0.13073  -0.17332 -0.17180 301 ALA   B N   
4093 C CA  . ALA   B 208 ? 0.97094 0.92296 0.85571 0.12717  -0.17156 -0.17592 301 ALA   B CA  
4094 C C   . ALA   B 208 ? 0.91493 0.83183 0.77740 0.14000  -0.19118 -0.19301 301 ALA   B C   
4095 O O   . ALA   B 208 ? 0.91247 0.81289 0.76252 0.13098  -0.19761 -0.19230 301 ALA   B O   
4096 C CB  . ALA   B 208 ? 0.88989 0.89269 0.78538 0.13376  -0.15352 -0.18209 301 ALA   B CB  
4097 N N   . SER   B 209 ? 0.91242 0.81688 0.76967 0.16178  -0.20213 -0.20942 302 SER   B N   
4098 C CA  . SER   B 209 ? 0.92105 0.78883 0.75583 0.17649  -0.22253 -0.22739 302 SER   B CA  
4099 C C   . SER   B 209 ? 1.02232 0.83139 0.83842 0.16200  -0.24056 -0.21726 302 SER   B C   
4100 O O   . SER   B 209 ? 1.06322 0.84184 0.86006 0.16123  -0.25424 -0.22473 302 SER   B O   
4101 C CB  . SER   B 209 ? 1.07375 0.94393 0.90923 0.20543  -0.23081 -0.24854 302 SER   B CB  
4102 O OG  . SER   B 209 ? 1.02094 0.94915 0.87462 0.21673  -0.21273 -0.25930 302 SER   B OG  
4103 N N   . ALA   B 210 ? 1.01965 0.81184 0.83982 0.14924  -0.24062 -0.20061 303 ALA   B N   
4104 C CA  . ALA   B 210 ? 1.05202 0.79107 0.85388 0.13060  -0.25476 -0.18899 303 ALA   B CA  
4105 C C   . ALA   B 210 ? 0.95613 0.70275 0.76140 0.10526  -0.24736 -0.17666 303 ALA   B C   
4106 O O   . ALA   B 210 ? 1.03703 0.74514 0.82450 0.09354  -0.26094 -0.17631 303 ALA   B O   
4107 C CB  . ALA   B 210 ? 0.96388 0.68701 0.76821 0.12212  -0.25445 -0.17407 303 ALA   B CB  
4108 N N   . LEU   B 211 ? 0.95517 0.75042 0.78304 0.09655  -0.22690 -0.16701 304 LEU   B N   
4109 C CA  . LEU   B 211 ? 1.07837 0.88527 0.91138 0.07591  -0.22092 -0.15736 304 LEU   B CA  
4110 C C   . LEU   B 211 ? 0.90998 0.71232 0.72910 0.08316  -0.22971 -0.17222 304 LEU   B C   
4111 O O   . LEU   B 211 ? 1.03597 0.82178 0.84834 0.06727  -0.23678 -0.16895 304 LEU   B O   
4112 C CB  . LEU   B 211 ? 1.05771 0.91555 0.91513 0.06953  -0.19913 -0.14599 304 LEU   B CB  
4113 C CG  . LEU   B 211 ? 1.07304 0.94997 0.93722 0.05357  -0.19310 -0.13852 304 LEU   B CG  
4114 C CD1 . LEU   B 211 ? 0.90668 0.76903 0.77722 0.02879  -0.19418 -0.12305 304 LEU   B CD1 
4115 C CD2 . LEU   B 211 ? 1.20037 1.12534 1.08068 0.05699  -0.17456 -0.13427 304 LEU   B CD2 
4116 N N   . TYR   B 212 ? 1.03949 0.85799 0.85451 0.10687  -0.22937 -0.18979 305 TYR   B N   
4117 C CA  . TYR   B 212 ? 1.05551 0.87104 0.85540 0.11543  -0.23722 -0.20560 305 TYR   B CA  
4118 C C   . TYR   B 212 ? 1.05393 0.81307 0.83020 0.11364  -0.26065 -0.21325 305 TYR   B C   
4119 O O   . TYR   B 212 ? 1.11157 0.85943 0.87718 0.10558  -0.26832 -0.21695 305 TYR   B O   
4120 C CB  . TYR   B 212 ? 1.00183 0.84557 0.80128 0.14182  -0.23190 -0.22490 305 TYR   B CB  
4121 C CG  . TYR   B 212 ? 1.05786 0.88939 0.83672 0.15524  -0.24379 -0.24557 305 TYR   B CG  
4122 C CD1 . TYR   B 212 ? 1.07262 0.92466 0.84705 0.14868  -0.23811 -0.24634 305 TYR   B CD1 
4123 C CD2 . TYR   B 212 ? 1.05341 0.85107 0.81567 0.17540  -0.26195 -0.26492 305 TYR   B CD2 
4124 C CE1 . TYR   B 212 ? 1.11194 0.95265 0.86595 0.16088  -0.24913 -0.26584 305 TYR   B CE1 
4125 C CE2 . TYR   B 212 ? 1.25557 1.04135 0.99840 0.18847  -0.27325 -0.28518 305 TYR   B CE2 
4126 C CZ  . TYR   B 212 ? 1.12541 0.93358 0.86420 0.18066  -0.26623 -0.28557 305 TYR   B CZ  
4127 O OH  . TYR   B 212 ? 1.33172 1.12804 1.04966 0.19367  -0.27757 -0.30633 305 TYR   B OH  
4128 N N   . HIS   B 213 ? 1.07135 0.79230 0.83749 0.12078  -0.27338 -0.21573 306 HIS   B N   
4129 C CA  . HIS   B 213 ? 1.15083 0.81175 0.89038 0.11923  -0.29713 -0.22301 306 HIS   B CA  
4130 C C   . HIS   B 213 ? 1.04244 0.67864 0.77853 0.08736  -0.30087 -0.20663 306 HIS   B C   
4131 O O   . HIS   B 213 ? 1.16243 0.75423 0.87690 0.08093  -0.31891 -0.21269 306 HIS   B O   
4132 C CB  . HIS   B 213 ? 1.13244 0.75514 0.85941 0.13439  -0.31089 -0.22803 306 HIS   B CB  
4133 C CG  . HIS   B 213 ? 1.24235 0.87691 0.96685 0.16872  -0.31556 -0.25160 306 HIS   B CG  
4134 N ND1 . HIS   B 213 ? 1.09470 0.77109 0.83929 0.18494  -0.30221 -0.25466 306 HIS   B ND1 
4135 C CD2 . HIS   B 213 ? 1.20967 0.82249 0.91530 0.18993  -0.33185 -0.27480 306 HIS   B CD2 
4136 C CE1 . HIS   B 213 ? 1.30263 0.98522 1.04238 0.21448  -0.30953 -0.27918 306 HIS   B CE1 
4137 N NE2 . HIS   B 213 ? 1.29755 0.94162 1.01334 0.21894  -0.32757 -0.29203 306 HIS   B NE2 
4138 N N   . PHE   B 214 ? 1.06442 0.72918 0.82174 0.06716  -0.28443 -0.18730 307 PHE   B N   
4139 C CA  . PHE   B 214 ? 1.16475 0.81745 0.92439 0.03648  -0.28510 -0.17318 307 PHE   B CA  
4140 C C   . PHE   B 214 ? 1.14471 0.83926 0.92093 0.02681  -0.27465 -0.17077 307 PHE   B C   
4141 O O   . PHE   B 214 ? 1.26889 0.96015 1.05050 0.00250  -0.27560 -0.16183 307 PHE   B O   
4142 C CB  . PHE   B 214 ? 1.07653 0.72883 0.84725 0.01945  -0.27570 -0.15403 307 PHE   B CB  
4143 C CG  . PHE   B 214 ? 1.09809 0.69755 0.84639 0.02179  -0.28973 -0.15334 307 PHE   B CG  
4144 C CD1 . PHE   B 214 ? 1.07809 0.67786 0.82485 0.04535  -0.29004 -0.15850 307 PHE   B CD1 
4145 C CD2 . PHE   B 214 ? 1.15710 0.70559 0.88459 -0.00007 -0.30343 -0.14784 307 PHE   B CD2 
4146 C CE1 . PHE   B 214 ? 1.18515 0.73331 0.90882 0.04919  -0.30534 -0.15800 307 PHE   B CE1 
4147 C CE2 . PHE   B 214 ? 1.21690 0.71107 0.91859 0.00158  -0.31774 -0.14611 307 PHE   B CE2 
4148 C CZ  . PHE   B 214 ? 1.20178 0.69470 0.90091 0.02733  -0.31952 -0.15113 307 PHE   B CZ  
4149 N N   . SER   B 215 ? 1.18743 0.92109 0.97095 0.04484  -0.26518 -0.17896 308 SER   B N   
4150 C CA  . SER   B 215 ? 0.97091 0.74085 0.76556 0.03784  -0.25706 -0.17681 308 SER   B CA  
4151 C C   . SER   B 215 ? 1.05499 0.83569 0.83614 0.05838  -0.26048 -0.19503 308 SER   B C   
4152 O O   . SER   B 215 ? 0.98842 0.73764 0.74916 0.06308  -0.27725 -0.20903 308 SER   B O   
4153 C CB  . SER   B 215 ? 0.99662 0.81217 0.81656 0.03293  -0.23615 -0.16180 308 SER   B CB  
4154 O OG  . SER   B 215 ? 1.04625 0.88266 0.86964 0.05268  -0.22569 -0.16586 308 SER   B OG  
4155 N N   . SER   B 216 ? 0.99740 0.82142 0.78809 0.06978  -0.24453 -0.19525 309 SER   B N   
4156 C CA  . SER   B 216 ? 1.10996 0.94988 0.88713 0.08738  -0.24449 -0.21173 309 SER   B CA  
4157 C C   . SER   B 216 ? 1.04685 0.92968 0.83459 0.10005  -0.22484 -0.21100 309 SER   B C   
4158 O O   . SER   B 216 ? 0.99292 0.89402 0.79948 0.09337  -0.21189 -0.19650 309 SER   B O   
4159 C CB  . SER   B 216 ? 1.05767 0.90619 0.82995 0.07663  -0.24817 -0.21106 309 SER   B CB  
4160 O OG  . SER   B 216 ? 1.07254 0.95392 0.86381 0.06337  -0.23425 -0.19370 309 SER   B OG  
4161 N N   . SER   B 217 ? 1.10410 1.00338 0.87875 0.11749  -0.22240 -0.22755 310 SER   B N   
4162 C CA  . SER   B 217 ? 1.06954 1.01163 0.85218 0.12766  -0.20281 -0.22859 310 SER   B CA  
4163 C C   . SER   B 217 ? 1.07381 1.04744 0.86536 0.11301  -0.18788 -0.21137 310 SER   B C   
4164 O O   . SER   B 217 ? 0.98784 0.99213 0.79204 0.11311  -0.17058 -0.20367 310 SER   B O   
4165 C CB  . SER   B 217 ? 1.30548 1.25831 1.07024 0.14869  -0.20338 -0.25219 310 SER   B CB  
4166 O OG  . SER   B 217 ? 1.26348 1.20986 1.00891 0.14583  -0.21114 -0.25818 310 SER   B OG  
4167 N N   . GLU   B 218 ? 1.06694 1.03262 0.85182 0.10064  -0.19539 -0.20571 311 GLU   B N   
4168 C CA  . GLU   B 218 ? 1.04181 1.03313 0.83401 0.08808  -0.18444 -0.18950 311 GLU   B CA  
4169 C C   . GLU   B 218 ? 0.94771 0.94215 0.76488 0.07382  -0.17806 -0.17013 311 GLU   B C   
4170 O O   . GLU   B 218 ? 1.02488 1.04572 0.85272 0.07014  -0.16289 -0.15822 311 GLU   B O   
4171 C CB  . GLU   B 218 ? 1.15045 1.13240 0.92988 0.08041  -0.19685 -0.19044 311 GLU   B CB  
4172 C CG  . GLU   B 218 ? 1.09409 1.07712 0.84615 0.09357  -0.20147 -0.20845 311 GLU   B CG  
4173 C CD  . GLU   B 218 ? 1.30880 1.26094 1.04822 0.10462  -0.21708 -0.22791 311 GLU   B CD  
4174 O OE1 . GLU   B 218 ? 1.30586 1.23075 1.05527 0.09944  -0.22667 -0.22574 311 GLU   B OE1 
4175 O OE2 . GLU   B 218 ? 1.43926 1.39273 1.15677 0.11836  -0.22006 -0.24559 311 GLU   B OE2 
4176 N N   . LEU   B 219 ? 1.03372 1.00027 0.85869 0.06483  -0.18937 -0.16696 312 LEU   B N   
4177 C CA  . LEU   B 219 ? 0.87412 0.84326 0.72142 0.05133  -0.18295 -0.15008 312 LEU   B CA  
4178 C C   . LEU   B 219 ? 0.90585 0.88682 0.76251 0.06007  -0.17050 -0.14823 312 LEU   B C   
4179 O O   . LEU   B 219 ? 0.87931 0.87995 0.75289 0.05304  -0.15781 -0.13444 312 LEU   B O   
4180 C CB  . LEU   B 219 ? 1.04368 0.97883 0.89301 0.03850  -0.19732 -0.14847 312 LEU   B CB  
4181 C CG  . LEU   B 219 ? 0.89688 0.83240 0.76724 0.02067  -0.19250 -0.13194 312 LEU   B CG  
4182 C CD1 . LEU   B 219 ? 0.94654 0.86977 0.82077 0.02448  -0.18855 -0.12920 312 LEU   B CD1 
4183 C CD2 . LEU   B 219 ? 1.00427 0.97514 0.89156 0.01454  -0.17927 -0.11913 312 LEU   B CD2 
4184 N N   . MET   B 220 ? 0.95543 0.92488 0.80181 0.07618  -0.17497 -0.16315 313 MET   B N   
4185 C CA  . MET   B 220 ? 0.98554 0.96882 0.84182 0.08641  -0.16473 -0.16423 313 MET   B CA  
4186 C C   . MET   B 220 ? 0.96943 0.99473 0.83273 0.08844  -0.14548 -0.16011 313 MET   B C   
4187 O O   . MET   B 220 ? 0.93401 0.97666 0.81382 0.08453  -0.13331 -0.14970 313 MET   B O   
4188 C CB  . MET   B 220 ? 1.02141 0.98779 0.86470 0.10648  -0.17491 -0.18461 313 MET   B CB  
4189 C CG  . MET   B 220 ? 1.06311 1.04670 0.91734 0.12036  -0.16646 -0.18997 313 MET   B CG  
4190 S SD  . MET   B 220 ? 1.03545 1.07146 0.89278 0.13238  -0.14668 -0.20005 313 MET   B SD  
4191 C CE  . MET   B 220 ? 1.16620 1.19530 0.99763 0.14167  -0.15583 -0.21824 313 MET   B CE  
4192 N N   . GLN   B 221 ? 1.00924 1.04954 0.85787 0.09346  -0.14270 -0.16803 314 GLN   B N   
4193 C CA  . GLN   B 221 ? 1.05031 1.12743 0.89993 0.09437  -0.12437 -0.16496 314 GLN   B CA  
4194 C C   . GLN   B 221 ? 0.91091 0.99908 0.77101 0.07773  -0.11598 -0.14386 314 GLN   B C   
4195 O O   . GLN   B 221 ? 0.97290 1.08570 0.84113 0.07506  -0.10035 -0.13617 314 GLN   B O   
4196 C CB  . GLN   B 221 ? 0.99208 1.07891 0.81842 0.10286  -0.12424 -0.17884 314 GLN   B CB  
4197 C CG  . GLN   B 221 ? 0.96402 1.08785 0.78626 0.10470  -0.10461 -0.17944 314 GLN   B CG  
4198 C CD  . GLN   B 221 ? 1.06822 1.20127 0.86515 0.11462  -0.10415 -0.19647 314 GLN   B CD  
4199 O OE1 . GLN   B 221 ? 1.13645 1.24729 0.91808 0.11918  -0.11942 -0.20597 314 GLN   B OE1 
4200 N NE2 . GLN   B 221 ? 1.16699 1.33324 0.95857 0.11704  -0.08625 -0.20102 314 GLN   B NE2 
4201 N N   . LYS   B 222 ? 0.93840 1.00918 0.79910 0.06655  -0.12663 -0.13532 315 LYS   B N   
4202 C CA  . LYS   B 222 ? 0.94995 1.03141 0.82138 0.05303  -0.12069 -0.11735 315 LYS   B CA  
4203 C C   . LYS   B 222 ? 1.02029 1.10518 0.91495 0.04634  -0.11311 -0.10547 315 LYS   B C   
4204 O O   . LYS   B 222 ? 1.11474 1.21587 1.01861 0.03942  -0.10268 -0.09258 315 LYS   B O   
4205 C CB  . LYS   B 222 ? 1.03831 1.10408 0.90779 0.04385  -0.13505 -0.11409 315 LYS   B CB  
4206 C CG  . LYS   B 222 ? 1.17797 1.25686 1.05537 0.03359  -0.13135 -0.09892 315 LYS   B CG  
4207 C CD  . LYS   B 222 ? 1.27553 1.34259 1.15715 0.02460  -0.14645 -0.09753 315 LYS   B CD  
4208 C CE  . LYS   B 222 ? 1.32819 1.38129 1.22967 0.01496  -0.15141 -0.09482 315 LYS   B CE  
4209 N NZ  . LYS   B 222 ? 1.27048 1.31811 1.18018 0.00353  -0.16415 -0.09362 315 LYS   B NZ  
4210 N N   . VAL   B 223 ? 0.98854 1.05601 0.89049 0.04845  -0.11898 -0.10963 316 VAL   B N   
4211 C CA  . VAL   B 223 ? 1.06292 1.13009 0.98430 0.04141  -0.11355 -0.09867 316 VAL   B CA  
4212 C C   . VAL   B 223 ? 0.92864 1.00636 0.85527 0.05179  -0.10493 -0.10381 316 VAL   B C   
4213 O O   . VAL   B 223 ? 0.83794 0.92188 0.78015 0.04660  -0.09752 -0.09419 316 VAL   B O   
4214 C CB  . VAL   B 223 ? 1.06488 1.10294 0.99012 0.03258  -0.12637 -0.09661 316 VAL   B CB  
4215 C CG1 . VAL   B 223 ? 0.96966 0.99809 0.88861 0.02428  -0.13730 -0.09707 316 VAL   B CG1 
4216 C CG2 . VAL   B 223 ? 0.81937 0.83357 0.73486 0.04310  -0.13569 -0.10884 316 VAL   B CG2 
4217 N N   . SER   B 224 ? 0.95712 1.03883 0.87231 0.06670  -0.10600 -0.11985 317 SER   B N   
4218 C CA  . SER   B 224 ? 0.97366 1.07078 0.89636 0.07793  -0.09832 -0.12744 317 SER   B CA  
4219 C C   . SER   B 224 ? 1.06368 1.19649 0.98447 0.08222  -0.08255 -0.13190 317 SER   B C   
4220 O O   . SER   B 224 ? 0.98979 1.14394 0.92296 0.08574  -0.07186 -0.13343 317 SER   B O   
4221 C CB  . SER   B 224 ? 0.94355 1.01991 0.85748 0.09380  -0.11197 -0.14521 317 SER   B CB  
4222 O OG  . SER   B 224 ? 1.02007 1.09715 0.91632 0.10354  -0.11670 -0.16019 317 SER   B OG  
4223 N N   . GLY   B 225 ? 0.99270 1.13237 0.89725 0.08091  -0.08089 -0.13407 318 GLY   B N   
4224 C CA  . GLY   B 225 ? 1.08517 1.25628 0.98254 0.08278  -0.06555 -0.13820 318 GLY   B CA  
4225 C C   . GLY   B 225 ? 1.17617 1.36259 1.06758 0.09942  -0.06357 -0.16046 318 GLY   B C   
4226 O O   . GLY   B 225 ? 1.34002 1.55531 1.22383 0.10003  -0.04954 -0.16594 318 GLY   B O   
4227 N N   . TYR   B 226 ? 1.02778 1.19546 0.92123 0.11280  -0.07731 -0.17401 319 TYR   B N   
4228 C CA  . TYR   B 226 ? 1.02752 1.20980 0.91792 0.13180  -0.07746 -0.19772 319 TYR   B CA  
4229 C C   . TYR   B 226 ? 1.24908 1.41920 1.11565 0.14008  -0.08710 -0.21194 319 TYR   B C   
4230 O O   . TYR   B 226 ? 1.15898 1.29476 1.01522 0.13692  -0.10287 -0.20839 319 TYR   B O   
4231 C CB  . TYR   B 226 ? 1.10212 1.26764 1.00550 0.14450  -0.08940 -0.20606 319 TYR   B CB  
4232 C CG  . TYR   B 226 ? 1.14458 1.32212 1.07062 0.13793  -0.08104 -0.19406 319 TYR   B CG  
4233 C CD1 . TYR   B 226 ? 1.20062 1.41298 1.13672 0.12674  -0.06115 -0.18457 319 TYR   B CD1 
4234 C CD2 . TYR   B 226 ? 1.09036 1.24185 1.02510 0.14217  -0.09365 -0.19205 319 TYR   B CD2 
4235 C CE1 . TYR   B 226 ? 1.19583 1.41835 1.15221 0.12060  -0.05419 -0.17443 319 TYR   B CE1 
4236 C CE2 . TYR   B 226 ? 1.11012 1.27222 1.06398 0.13646  -0.08660 -0.18169 319 TYR   B CE2 
4237 C CZ  . TYR   B 226 ? 0.98677 1.18522 0.95247 0.12598  -0.06693 -0.17341 319 TYR   B CZ  
4238 O OH  . TYR   B 226 ? 1.06989 1.27816 1.05424 0.12016  -0.06055 -0.16392 319 TYR   B OH  
4239 N N   . GLN   B 227 ? 1.22725 1.42716 1.08509 0.14975  -0.07705 -0.22880 320 GLN   B N   
4240 C CA  . GLN   B 227 ? 1.22229 1.41416 1.05612 0.15918  -0.08496 -0.24488 320 GLN   B CA  
4241 C C   . GLN   B 227 ? 1.24326 1.40605 1.07548 0.17808  -0.10538 -0.26338 320 GLN   B C   
4242 O O   . GLN   B 227 ? 1.28011 1.43647 1.12891 0.18684  -0.11098 -0.26717 320 GLN   B O   
4243 C CB  . GLN   B 227 ? 1.31485 1.54943 1.13953 0.16410  -0.06686 -0.25919 320 GLN   B CB  
4244 C CG  . GLN   B 227 ? 1.53933 1.76972 1.33388 0.16696  -0.07017 -0.26939 320 GLN   B CG  
4245 C CD  . GLN   B 227 ? 1.61573 1.89018 1.39946 0.17005  -0.05021 -0.28360 320 GLN   B CD  
4246 O OE1 . GLN   B 227 ? 1.56973 1.84595 1.32723 0.17331  -0.05044 -0.29420 320 GLN   B OE1 
4247 N NE2 . GLN   B 227 ? 1.62882 1.94002 1.43215 0.16797  -0.03246 -0.28440 320 GLN   B NE2 
4248 N N   . TRP   B 228 ? 1.12212 1.26426 0.93187 0.18446  -0.11796 -0.27496 321 TRP   B N   
4249 C CA  . TRP   B 228 ? 1.22146 1.33012 1.02493 0.20218  -0.13927 -0.29307 321 TRP   B CA  
4250 C C   . TRP   B 228 ? 1.34914 1.48131 1.16147 0.22583  -0.13677 -0.31797 321 TRP   B C   
4251 O O   . TRP   B 228 ? 1.38859 1.49443 1.20523 0.24074  -0.15337 -0.32842 321 TRP   B O   
4252 C CB  . TRP   B 228 ? 1.11433 1.20005 0.89090 0.20429  -0.15197 -0.30246 321 TRP   B CB  
4253 C CG  . TRP   B 228 ? 1.21598 1.27166 0.98205 0.22547  -0.17228 -0.32604 321 TRP   B CG  
4254 C CD1 . TRP   B 228 ? 1.32486 1.39263 1.07723 0.24600  -0.17408 -0.35343 321 TRP   B CD1 
4255 C CD2 . TRP   B 228 ? 1.19046 1.19691 0.95693 0.22836  -0.19420 -0.32486 321 TRP   B CD2 
4256 N NE1 . TRP   B 228 ? 1.38614 1.41351 1.13088 0.26306  -0.19720 -0.36986 321 TRP   B NE1 
4257 C CE2 . TRP   B 228 ? 1.27404 1.26143 1.02579 0.25182  -0.21008 -0.35194 321 TRP   B CE2 
4258 C CE3 . TRP   B 228 ? 1.05871 1.03444 0.83466 0.21277  -0.20181 -0.30379 321 TRP   B CE3 
4259 C CZ2 . TRP   B 228 ? 1.29077 1.22534 1.03506 0.25975  -0.23442 -0.35735 321 TRP   B CZ2 
4260 C CZ3 . TRP   B 228 ? 1.19110 1.11676 0.95920 0.21897  -0.22431 -0.30878 321 TRP   B CZ3 
4261 C CH2 . TRP   B 228 ? 1.27759 1.18100 1.02906 0.24211  -0.24099 -0.33477 321 TRP   B CH2 
4262 N N   . CYS   B 229 ? 1.47114 1.65256 1.28571 0.22939  -0.11669 -0.32825 322 CYS   B N   
4263 C CA  . CYS   B 229 ? 1.47097 1.68338 1.29792 0.25176  -0.11260 -0.35416 322 CYS   B CA  
4264 C C   . CYS   B 229 ? 1.39625 1.61734 1.25183 0.25405  -0.11092 -0.34869 322 CYS   B C   
4265 O O   . CYS   B 229 ? 1.36465 1.59579 1.23212 0.27633  -0.11722 -0.37051 322 CYS   B O   
4266 C CB  . CYS   B 229 ? 1.51166 1.77880 1.33435 0.25055  -0.08866 -0.36523 322 CYS   B CB  
4267 S SG  . CYS   B 229 ? 1.58884 1.88945 1.41947 0.22079  -0.06163 -0.33661 322 CYS   B SG  
4268 N N   . ASP   B 230 ? 1.36815 1.58558 1.23481 0.23270  -0.10363 -0.32122 323 ASP   B N   
4269 C CA  . ASP   B 230 ? 1.38271 1.60716 1.27497 0.23377  -0.10232 -0.31521 323 ASP   B CA  
4270 C C   . ASP   B 230 ? 1.27882 1.45301 1.17008 0.24493  -0.12774 -0.31653 323 ASP   B C   
4271 O O   . ASP   B 230 ? 1.15032 1.32823 1.05695 0.26022  -0.13400 -0.32694 323 ASP   B O   
4272 C CB  . ASP   B 230 ? 1.13915 1.37223 1.04132 0.20778  -0.08756 -0.28610 323 ASP   B CB  
4273 C CG  . ASP   B 230 ? 1.27827 1.55419 1.17695 0.19458  -0.06354 -0.28216 323 ASP   B CG  
4274 O OD1 . ASP   B 230 ? 1.47680 1.78759 1.37263 0.20553  -0.05392 -0.30332 323 ASP   B OD1 
4275 O OD2 . ASP   B 230 ? 1.14796 1.42202 1.04557 0.17313  -0.05445 -0.25825 323 ASP   B OD2 
4276 N N   . ILE   B 231 ? 1.18135 1.30746 1.05352 0.23681  -0.14320 -0.30618 324 ILE   B N   
4277 C CA  . ILE   B 231 ? 1.19975 1.27258 1.06664 0.24136  -0.16647 -0.30303 324 ILE   B CA  
4278 C C   . ILE   B 231 ? 1.19464 1.23450 1.04163 0.26262  -0.18809 -0.32623 324 ILE   B C   
4279 O O   . ILE   B 231 ? 1.10389 1.09482 0.94219 0.26835  -0.20952 -0.32616 324 ILE   B O   
4280 C CB  . ILE   B 231 ? 1.14464 1.18380 1.00537 0.21557  -0.16994 -0.27552 324 ILE   B CB  
4281 C CG1 . ILE   B 231 ? 1.19542 1.21300 1.03364 0.20915  -0.17755 -0.27669 324 ILE   B CG1 
4282 C CG2 . ILE   B 231 ? 1.04270 1.11543 0.92076 0.19531  -0.14833 -0.25403 324 ILE   B CG2 
4283 C CD1 . ILE   B 231 ? 1.15041 1.13238 0.98342 0.18618  -0.18502 -0.25428 324 ILE   B CD1 
4284 N N   . GLU   B 232 ? 1.14626 1.20929 0.98347 0.27414  -0.18349 -0.34624 325 GLU   B N   
4285 C CA  . GLU   B 232 ? 1.18900 1.21946 1.00579 0.29495  -0.20464 -0.36964 325 GLU   B CA  
4286 C C   . GLU   B 232 ? 1.17542 1.19151 0.99906 0.32144  -0.22107 -0.38844 325 GLU   B C   
4287 O O   . GLU   B 232 ? 1.22035 1.18214 1.02628 0.33242  -0.24637 -0.39584 325 GLU   B O   
4288 C CB  . GLU   B 232 ? 1.25358 1.31981 1.06044 0.30421  -0.19394 -0.39002 325 GLU   B CB  
4289 C CG  . GLU   B 232 ? 1.25285 1.28914 1.03898 0.32832  -0.21526 -0.41765 325 GLU   B CG  
4290 C CD  . GLU   B 232 ? 1.36960 1.44528 1.14564 0.33834  -0.20320 -0.43964 325 GLU   B CD  
4291 O OE1 . GLU   B 232 ? 1.35265 1.47882 1.13678 0.32580  -0.17775 -0.43283 325 GLU   B OE1 
4292 O OE2 . GLU   B 232 ? 1.52650 1.58091 1.28445 0.35826  -0.21935 -0.46382 325 GLU   B OE2 
4293 N N   . ASN   B 233 ? 1.09456 1.15748 0.94308 0.33188  -0.20813 -0.39670 326 ASN   B N   
4294 C CA  . ASN   B 233 ? 1.12353 1.17547 0.98087 0.35832  -0.22487 -0.41469 326 ASN   B CA  
4295 C C   . ASN   B 233 ? 1.20910 1.20454 1.06099 0.34987  -0.24288 -0.39430 326 ASN   B C   
4296 O O   . ASN   B 233 ? 1.11165 1.05967 0.95006 0.36837  -0.26873 -0.40546 326 ASN   B O   
4297 C CB  . ASN   B 233 ? 1.31611 1.43514 1.20463 0.36773  -0.20579 -0.42624 326 ASN   B CB  
4298 C CG  . ASN   B 233 ? 1.36488 1.48585 1.26322 0.40254  -0.22297 -0.45554 326 ASN   B CG  
4299 O OD1 . ASN   B 233 ? 1.21502 1.30036 1.09512 0.42466  -0.24523 -0.47561 326 ASN   B OD1 
4300 N ND2 . ASN   B 233 ? 1.37056 1.53267 1.29789 0.40825  -0.21393 -0.45903 326 ASN   B ND2 
4301 N N   . CYS   B 234 ? 1.05641 1.05415 0.91635 0.32174  -0.22994 -0.36448 327 CYS   B N   
4302 C CA  . CYS   B 234 ? 1.07966 1.02624 0.93293 0.31045  -0.24441 -0.34399 327 CYS   B CA  
4303 C C   . CYS   B 234 ? 1.17068 1.05290 0.99383 0.30119  -0.26399 -0.33717 327 CYS   B C   
4304 O O   . CYS   B 234 ? 1.16783 0.99436 0.97512 0.30547  -0.28633 -0.33492 327 CYS   B O   
4305 C CB  . CYS   B 234 ? 1.08059 1.05070 0.95122 0.28316  -0.22411 -0.31593 327 CYS   B CB  
4306 S SG  . CYS   B 234 ? 1.07793 0.99317 0.94159 0.26706  -0.23769 -0.29047 327 CYS   B SG  
4307 N N   . VAL   B 235 ? 1.15685 1.04452 0.97036 0.28752  -0.25652 -0.33370 328 VAL   B N   
4308 C CA  . VAL   B 235 ? 1.00684 0.83732 0.79345 0.27725  -0.27470 -0.32875 328 VAL   B CA  
4309 C C   . VAL   B 235 ? 1.27524 1.06348 1.04086 0.30414  -0.30093 -0.35386 328 VAL   B C   
4310 O O   . VAL   B 235 ? 1.32827 1.05321 1.07242 0.30069  -0.32322 -0.34892 328 VAL   B O   
4311 C CB  . VAL   B 235 ? 1.26791 1.11837 1.04960 0.26089  -0.26236 -0.32386 328 VAL   B CB  
4312 C CG1 . VAL   B 235 ? 1.25166 1.04790 1.00552 0.25667  -0.28338 -0.32768 328 VAL   B CG1 
4313 C CG2 . VAL   B 235 ? 1.07680 0.94980 0.87375 0.23184  -0.24329 -0.29552 328 VAL   B CG2 
4314 N N   . LYS   B 236 ? 1.30163 1.12354 1.07223 0.33113  -0.29883 -0.38174 329 LYS   B N   
4315 C CA  . LYS   B 236 ? 1.33713 1.12153 1.08920 0.36059  -0.32447 -0.40877 329 LYS   B CA  
4316 C C   . LYS   B 236 ? 1.36264 1.11094 1.11385 0.37539  -0.34374 -0.40989 329 LYS   B C   
4317 O O   . LYS   B 236 ? 1.44121 1.12836 1.16738 0.38949  -0.37174 -0.42029 329 LYS   B O   
4318 C CB  . LYS   B 236 ? 1.51137 1.34852 1.27293 0.38701  -0.31548 -0.43997 329 LYS   B CB  
4319 C CG  . LYS   B 236 ? 1.62997 1.42990 1.36999 0.41753  -0.34156 -0.47062 329 LYS   B CG  
4320 C CD  . LYS   B 236 ? 1.63889 1.49761 1.38987 0.44291  -0.33006 -0.50287 329 LYS   B CD  
4321 C CE  . LYS   B 236 ? 1.67279 1.58728 1.45604 0.46042  -0.31821 -0.51446 329 LYS   B CE  
4322 N NZ  . LYS   B 236 ? 1.62143 1.59834 1.42080 0.48049  -0.30580 -0.54056 329 LYS   B NZ  
4323 N N   . TRP   B 237 ? 1.33371 1.11598 1.10976 0.37245  -0.33048 -0.39934 330 TRP   B N   
4324 C CA  . TRP   B 237 ? 1.37163 1.11755 1.14485 0.38426  -0.34926 -0.39756 330 TRP   B CA  
4325 C C   . TRP   B 237 ? 1.35637 1.03686 1.10699 0.35764  -0.36113 -0.36928 330 TRP   B C   
4326 O O   . TRP   B 237 ? 1.31459 0.93287 1.04220 0.36713  -0.38735 -0.37071 330 TRP   B O   
4327 C CB  . TRP   B 237 ? 1.30129 1.10519 1.10818 0.38844  -0.33156 -0.39564 330 TRP   B CB  
4328 C CG  . TRP   B 237 ? 1.38678 1.15376 1.19023 0.39451  -0.34877 -0.38777 330 TRP   B CG  
4329 C CD1 . TRP   B 237 ? 1.41116 1.15688 1.21029 0.42722  -0.37252 -0.40914 330 TRP   B CD1 
4330 C CD2 . TRP   B 237 ? 1.38189 1.12775 1.18399 0.36782  -0.34454 -0.35690 330 TRP   B CD2 
4331 N NE1 . TRP   B 237 ? 1.41380 1.12429 1.20684 0.42200  -0.38389 -0.39234 330 TRP   B NE1 
4332 C CE2 . TRP   B 237 ? 1.49731 1.20797 1.29185 0.38514  -0.36619 -0.36029 330 TRP   B CE2 
4333 C CE3 . TRP   B 237 ? 1.34108 1.09476 1.14725 0.33195  -0.32515 -0.32777 330 TRP   B CE3 
4334 C CZ2 . TRP   B 237 ? 1.47803 1.16117 1.26705 0.36633  -0.36779 -0.33494 330 TRP   B CZ2 
4335 C CZ3 . TRP   B 237 ? 1.21718 0.94605 1.02054 0.31411  -0.32628 -0.30398 330 TRP   B CZ3 
4336 C CH2 . TRP   B 237 ? 1.32249 1.01630 1.11636 0.33056  -0.34688 -0.30735 330 TRP   B CH2 
4337 N N   . MET   B 238 ? 1.28129 0.97463 1.03718 0.32406  -0.34239 -0.34389 331 MET   B N   
4338 C CA  . MET   B 238 ? 1.27452 0.91407 1.01176 0.29542  -0.35003 -0.31764 331 MET   B CA  
4339 C C   . MET   B 238 ? 1.43241 1.01188 1.13699 0.28991  -0.37037 -0.32143 331 MET   B C   
4340 O O   . MET   B 238 ? 1.45897 0.98951 1.14516 0.26535  -0.37862 -0.30184 331 MET   B O   
4341 C CB  . MET   B 238 ? 1.14306 0.82258 0.90022 0.26374  -0.32309 -0.29256 331 MET   B CB  
4342 C CG  . MET   B 238 ? 1.24834 0.88967 0.99634 0.23465  -0.32515 -0.26485 331 MET   B CG  
4343 S SD  . MET   B 238 ? 1.21254 0.90879 0.98893 0.20375  -0.29350 -0.23958 331 MET   B SD  
4344 C CE  . MET   B 238 ? 1.08277 0.83438 0.88894 0.22091  -0.27836 -0.24401 331 MET   B CE  
4345 N N   . VAL   B 239 ? 1.45986 1.04282 1.15670 0.31153  -0.37831 -0.34695 332 VAL   B N   
4346 C CA  . VAL   B 239 ? 1.58241 1.10951 1.24819 0.30686  -0.39798 -0.35262 332 VAL   B CA  
4347 C C   . VAL   B 239 ? 1.61445 1.05776 1.24826 0.30470  -0.42663 -0.34660 332 VAL   B C   
4348 O O   . VAL   B 239 ? 1.57418 0.97384 1.18889 0.27632  -0.43266 -0.32957 332 VAL   B O   
4349 C CB  . VAL   B 239 ? 1.45861 1.00380 1.12086 0.33566  -0.40315 -0.38458 332 VAL   B CB  
4350 C CG1 . VAL   B 239 ? 1.50606 0.97762 1.13155 0.34328  -0.43355 -0.39749 332 VAL   B CG1 
4351 C CG2 . VAL   B 239 ? 1.51702 1.12134 1.19506 0.32340  -0.37824 -0.38352 332 VAL   B CG2 
4352 N N   . PRO   B 240 ? 1.59846 1.01523 1.22395 0.33232  -0.44543 -0.35959 333 PRO   B N   
4353 C CA  . PRO   B 240 ? 1.68808 1.01685 1.27638 0.32857  -0.47453 -0.35240 333 PRO   B CA  
4354 C C   . PRO   B 240 ? 1.69600 1.00273 1.27970 0.29248  -0.46737 -0.31898 333 PRO   B C   
4355 O O   . PRO   B 240 ? 1.62740 0.86797 1.17958 0.27053  -0.48245 -0.30609 333 PRO   B O   
4356 C CB  . PRO   B 240 ? 1.78216 1.10288 1.36982 0.36804  -0.49248 -0.37248 333 PRO   B CB  
4357 C CG  . PRO   B 240 ? 1.73329 1.12940 1.35219 0.39513  -0.47757 -0.39826 333 PRO   B CG  
4358 C CD  . PRO   B 240 ? 1.61843 1.08029 1.26550 0.36851  -0.44339 -0.38275 333 PRO   B CD  
4359 N N   . PHE   B 241 ? 1.65130 1.01239 1.26523 0.28473  -0.44423 -0.30517 334 PHE   B N   
4360 C CA  . PHE   B 241 ? 1.64897 0.99369 1.25985 0.25163  -0.43604 -0.27485 334 PHE   B CA  
4361 C C   . PHE   B 241 ? 1.46812 0.81283 1.07782 0.21418  -0.42359 -0.25738 334 PHE   B C   
4362 O O   . PHE   B 241 ? 1.43638 0.73897 1.02800 0.18518  -0.42719 -0.23658 334 PHE   B O   
4363 C CB  . PHE   B 241 ? 1.43960 0.84727 1.08519 0.25305  -0.41325 -0.26631 334 PHE   B CB  
4364 C CG  . PHE   B 241 ? 1.45771 0.88508 1.11449 0.29113  -0.42133 -0.28721 334 PHE   B CG  
4365 C CD1 . PHE   B 241 ? 1.55011 0.93249 1.18876 0.30331  -0.44153 -0.28552 334 PHE   B CD1 
4366 C CD2 . PHE   B 241 ? 1.46629 0.95858 1.15146 0.31423  -0.40874 -0.30906 334 PHE   B CD2 
4367 C CE1 . PHE   B 241 ? 1.51930 0.92290 1.17089 0.33961  -0.45032 -0.30646 334 PHE   B CE1 
4368 C CE2 . PHE   B 241 ? 1.52005 1.03614 1.21901 0.34868  -0.41548 -0.33026 334 PHE   B CE2 
4369 C CZ  . PHE   B 241 ? 1.52339 0.99618 1.20713 0.36222  -0.43687 -0.32954 334 PHE   B CZ  
4370 N N   . ALA   B 242 ? 1.43761 0.82963 1.06572 0.21403  -0.40925 -0.26613 335 ALA   B N   
4371 C CA  . ALA   B 242 ? 1.49939 0.89773 1.13000 0.18058  -0.39789 -0.25124 335 ALA   B CA  
4372 C C   . ALA   B 242 ? 1.52935 0.85485 1.12372 0.16657  -0.42111 -0.25149 335 ALA   B C   
4373 O O   . ALA   B 242 ? 1.49927 0.80542 1.08739 0.13236  -0.41783 -0.23246 335 ALA   B O   
4374 C CB  . ALA   B 242 ? 1.45729 0.91954 1.11191 0.18666  -0.37992 -0.26193 335 ALA   B CB  
4375 N N   . MET   B 243 ? 1.37201 0.65671 0.94239 0.19213  -0.44486 -0.27378 336 MET   B N   
4376 C CA  . MET   B 243 ? 1.62998 0.84347 1.16439 0.17890  -0.46789 -0.27561 336 MET   B CA  
4377 C C   . MET   B 243 ? 1.66625 0.80712 1.16919 0.16208  -0.48473 -0.25912 336 MET   B C   
4378 O O   . MET   B 243 ? 1.66856 0.76173 1.14850 0.13223  -0.49331 -0.24808 336 MET   B O   
4379 C CB  . MET   B 243 ? 1.67109 0.86093 1.18789 0.21259  -0.48912 -0.30575 336 MET   B CB  
4380 C CG  . MET   B 243 ? 1.83480 1.06750 1.36493 0.21471  -0.47915 -0.31954 336 MET   B CG  
4381 S SD  . MET   B 243 ? 2.02981 1.24285 1.55092 0.17085  -0.47761 -0.30407 336 MET   B SD  
4382 C CE  . MET   B 243 ? 1.63287 0.93576 1.19878 0.15043  -0.44051 -0.28538 336 MET   B CE  
4383 N N   . VAL   B 244 ? 1.66880 0.79965 1.16881 0.17973  -0.49002 -0.25747 337 VAL   B N   
4384 C CA  . VAL   B 244 ? 1.59320 0.65391 1.05972 0.16319  -0.50563 -0.24025 337 VAL   B CA  
4385 C C   . VAL   B 244 ? 1.74846 0.82122 1.22298 0.11807  -0.48553 -0.21171 337 VAL   B C   
4386 O O   . VAL   B 244 ? 1.81321 0.82435 1.25573 0.08981  -0.49646 -0.19686 337 VAL   B O   
4387 C CB  . VAL   B 244 ? 1.89173 0.94874 1.35750 0.19207  -0.51352 -0.24406 337 VAL   B CB  
4388 C CG1 . VAL   B 244 ? 1.89548 0.88270 1.32423 0.17472  -0.52879 -0.22313 337 VAL   B CG1 
4389 C CG2 . VAL   B 244 ? 1.79681 0.85805 1.26303 0.23692  -0.52997 -0.27104 337 VAL   B CG2 
4390 N N   . ILE   B 245 ? 1.65467 0.80672 1.17124 0.11019  -0.45593 -0.20432 338 ILE   B N   
4391 C CA  . ILE   B 245 ? 1.68633 0.85796 1.21530 0.06945  -0.43596 -0.18046 338 ILE   B CA  
4392 C C   . ILE   B 245 ? 1.66696 0.82412 1.18864 0.04366  -0.43841 -0.18035 338 ILE   B C   
4393 O O   . ILE   B 245 ? 1.73355 0.86394 1.24308 0.00734  -0.43682 -0.16344 338 ILE   B O   
4394 C CB  . ILE   B 245 ? 1.54482 0.80303 1.11991 0.07112  -0.40586 -0.17461 338 ILE   B CB  
4395 C CG1 . ILE   B 245 ? 1.50113 0.77218 1.08329 0.09384  -0.40407 -0.17438 338 ILE   B CG1 
4396 C CG2 . ILE   B 245 ? 1.65408 0.93534 1.24411 0.03143  -0.38598 -0.15254 338 ILE   B CG2 
4397 C CD1 . ILE   B 245 ? 1.69507 0.91584 1.25155 0.07686  -0.41165 -0.15613 338 ILE   B CD1 
4398 N N   . ARG   B 246 ? 1.53454 0.71059 1.06346 0.06131  -0.44219 -0.20000 339 ARG   B N   
4399 C CA  . ARG   B 246 ? 1.59439 0.75963 1.11769 0.03859  -0.44564 -0.20183 339 ARG   B CA  
4400 C C   . ARG   B 246 ? 1.66585 0.74154 1.14324 0.02625  -0.47341 -0.20307 339 ARG   B C   
4401 O O   . ARG   B 246 ? 1.70739 0.76321 1.17650 -0.00729 -0.47473 -0.19504 339 ARG   B O   
4402 C CB  . ARG   B 246 ? 1.61746 0.82441 1.15693 0.06219  -0.44331 -0.22325 339 ARG   B CB  
4403 C CG  . ARG   B 246 ? 1.55872 0.85245 1.14080 0.06606  -0.41499 -0.22005 339 ARG   B CG  
4404 C CD  . ARG   B 246 ? 1.48627 0.80975 1.08805 0.02914  -0.39786 -0.20147 339 ARG   B CD  
4405 N NE  . ARG   B 246 ? 1.34876 0.74762 0.98553 0.03456  -0.37576 -0.20225 339 ARG   B NE  
4406 C CZ  . ARG   B 246 ? 1.37976 0.81911 1.04111 0.00982  -0.35801 -0.18753 339 ARG   B CZ  
4407 N NH1 . ARG   B 246 ? 1.43925 0.85808 1.09798 -0.02290 -0.35732 -0.17160 339 ARG   B NH1 
4408 N NH2 . ARG   B 246 ? 1.31512 0.81688 1.00348 0.01804  -0.34072 -0.18935 339 ARG   B NH2 
4409 N N   . GLU   B 247 ? 1.82820 0.84864 1.27523 0.05255  -0.49653 -0.21362 340 GLU   B N   
4410 C CA  . GLU   B 247 ? 1.74494 0.69649 1.15471 0.04340  -0.51666 -0.20731 340 GLU   B CA  
4411 C C   . GLU   B 247 ? 1.79570 0.71165 1.18706 0.00405  -0.51320 -0.18020 340 GLU   B C   
4412 O O   . GLU   B 247 ? 1.86511 0.74464 1.23591 -0.02322 -0.51904 -0.17011 340 GLU   B O   
4413 C CB  . GLU   B 247 ? 1.83390 0.75525 1.22469 0.08396  -0.53676 -0.21907 340 GLU   B CB  
4414 C CG  . GLU   B 247 ? 1.93241 0.88377 1.33689 0.12134  -0.54171 -0.24658 340 GLU   B CG  
4415 C CD  . GLU   B 247 ? 2.16560 1.08512 1.55080 0.15896  -0.56390 -0.25824 340 GLU   B CD  
4416 O OE1 . GLU   B 247 ? 2.40052 1.26153 1.75346 0.15194  -0.58031 -0.24448 340 GLU   B OE1 
4417 O OE2 . GLU   B 247 ? 2.11091 1.06601 1.51284 0.19519  -0.56501 -0.28141 340 GLU   B OE2 
4418 N N   . THR   B 248 ? 1.76901 0.69656 1.16707 -0.00004 -0.50293 -0.16853 341 THR   B N   
4419 C CA  . THR   B 248 ? 1.83621 0.73458 1.21642 -0.03690 -0.49735 -0.14276 341 THR   B CA  
4420 C C   . THR   B 248 ? 1.97671 0.91443 1.38189 -0.07733 -0.47504 -0.13148 341 THR   B C   
4421 O O   . THR   B 248 ? 2.02102 0.93818 1.41239 -0.11412 -0.46887 -0.11155 341 THR   B O   
4422 C CB  . THR   B 248 ? 1.84464 0.73403 1.21732 -0.02250 -0.49785 -0.13471 341 THR   B CB  
4423 O OG1 . THR   B 248 ? 2.16489 1.02530 1.51635 -0.05910 -0.49194 -0.10939 341 THR   B OG1 
4424 C CG2 . THR   B 248 ? 1.88920 0.85334 1.30592 -0.00775 -0.47661 -0.13970 341 THR   B CG2 
4425 N N   . GLY   B 249 ? 2.06228 1.07496 1.51083 -0.06903 -0.45678 -0.13965 342 GLY   B N   
4426 C CA  . GLY   B 249 ? 1.93299 1.00307 1.41515 -0.10105 -0.43193 -0.12760 342 GLY   B CA  
4427 C C   . GLY   B 249 ? 1.99017 1.12458 1.50698 -0.09727 -0.40654 -0.11621 342 GLY   B C   
4428 O O   . GLY   B 249 ? 1.94874 1.08321 1.46340 -0.07244 -0.40755 -0.11646 342 GLY   B O   
4429 N N   . SER   B 250 ? 2.10091 1.29070 1.65054 -0.12237 -0.38454 -0.10714 343 SER   B N   
4430 C CA  . SER   B 250 ? 1.95502 1.20798 1.53949 -0.12316 -0.35939 -0.09607 343 SER   B CA  
4431 C C   . SER   B 250 ? 2.02306 1.25594 1.59543 -0.15591 -0.35151 -0.07597 343 SER   B C   
4432 O O   . SER   B 250 ? 2.14738 1.34105 1.69818 -0.18866 -0.35742 -0.06929 343 SER   B O   
4433 C CB  . SER   B 250 ? 2.00414 1.32969 1.63128 -0.12908 -0.34084 -0.09873 343 SER   B CB  
4434 O OG  . SER   B 250 ? 1.94094 1.28208 1.57464 -0.10217 -0.34817 -0.11698 343 SER   B OG  
4435 N N   . SER   B 251 ? 1.99543 1.25630 1.58123 -0.14793 -0.33760 -0.06683 344 SER   B N   
4436 C CA  . SER   B 251 ? 1.86132 1.10663 1.43494 -0.17573 -0.32875 -0.04833 344 SER   B CA  
4437 C C   . SER   B 251 ? 1.71247 1.01682 1.32168 -0.20521 -0.30414 -0.03943 344 SER   B C   
4438 O O   . SER   B 251 ? 1.62013 0.98504 1.26778 -0.19740 -0.29216 -0.04618 344 SER   B O   
4439 C CB  . SER   B 251 ? 1.83362 1.08170 1.40478 -0.15320 -0.32610 -0.04359 344 SER   B CB  
4440 O OG  . SER   B 251 ? 1.98608 1.17826 1.52398 -0.12577 -0.35056 -0.05257 344 SER   B OG  
4441 N N   . LYS   B 252 ? 1.62163 0.90693 1.21614 -0.23915 -0.29716 -0.02460 345 LYS   B N   
4442 C CA  . LYS   B 252 ? 1.56424 0.90294 1.19054 -0.26893 -0.27418 -0.01675 345 LYS   B CA  
4443 C C   . LYS   B 252 ? 1.51865 0.90025 1.16622 -0.26212 -0.25477 -0.00772 345 LYS   B C   
4444 O O   . LYS   B 252 ? 1.42453 0.77894 1.05109 -0.24664 -0.25980 -0.00290 345 LYS   B O   
4445 C CB  . LYS   B 252 ? 1.59087 0.88941 1.19044 -0.31326 -0.27542 -0.00711 345 LYS   B CB  
4446 C CG  . LYS   B 252 ? 1.70714 0.97569 1.29434 -0.32817 -0.29057 -0.01598 345 LYS   B CG  
4447 C CD  . LYS   B 252 ? 1.48363 0.82095 1.11835 -0.33385 -0.27860 -0.02488 345 LYS   B CD  
4448 C CE  . LYS   B 252 ? 1.72862 1.03682 1.35118 -0.35133 -0.29393 -0.03397 345 LYS   B CE  
4449 N NZ  . LYS   B 252 ? 1.57163 0.94674 1.23988 -0.35731 -0.28385 -0.04296 345 LYS   B NZ  
4450 N N   . LEU   B 253 ? 1.45901 0.90758 1.14854 -0.27303 -0.23372 -0.00637 346 LEU   B N   
4451 C CA  . LEU   B 253 ? 1.32019 0.81249 1.03237 -0.26891 -0.21436 0.00147  346 LEU   B CA  
4452 C C   . LEU   B 253 ? 1.46311 0.92912 1.15137 -0.29997 -0.20726 0.01565  346 LEU   B C   
4453 O O   . LEU   B 253 ? 1.53774 1.00872 1.22789 -0.33479 -0.19957 0.01937  346 LEU   B O   
4454 C CB  . LEU   B 253 ? 1.24720 0.81529 1.00961 -0.27025 -0.19626 -0.00257 346 LEU   B CB  
4455 C CG  . LEU   B 253 ? 1.29321 0.90881 1.08134 -0.27164 -0.17503 0.00515  346 LEU   B CG  
4456 C CD1 . LEU   B 253 ? 1.18755 0.80513 0.97455 -0.23883 -0.17575 0.00553  346 LEU   B CD1 
4457 C CD2 . LEU   B 253 ? 1.07710 0.76059 0.91158 -0.27572 -0.16040 0.00031  346 LEU   B CD2 
4458 N N   . LYS   B 254 ? 1.55905 0.99854 1.22456 -0.28804 -0.20971 0.02293  347 LYS   B N   
4459 C CA  . LYS   B 254 ? 1.48267 0.89357 1.12001 -0.31589 -0.20355 0.03695  347 LYS   B CA  
4460 C C   . LYS   B 254 ? 1.53480 1.00966 1.20745 -0.32886 -0.17722 0.04212  347 LYS   B C   
4461 O O   . LYS   B 254 ? 1.52256 1.05692 1.23722 -0.30921 -0.16605 0.03622  347 LYS   B O   
4462 C CB  . LYS   B 254 ? 1.43407 0.79120 1.03196 -0.29689 -0.21792 0.04236  347 LYS   B CB  
4463 C CG  . LYS   B 254 ? 1.46488 0.74629 1.01850 -0.28779 -0.24602 0.03860  347 LYS   B CG  
4464 C CD  . LYS   B 254 ? 1.60095 0.83059 1.11572 -0.26962 -0.26066 0.04417  347 LYS   B CD  
4465 C CE  . LYS   B 254 ? 1.84147 0.98949 1.30823 -0.26091 -0.29070 0.04041  347 LYS   B CE  
4466 N NZ  . LYS   B 254 ? 1.65077 0.74540 1.07746 -0.24336 -0.30714 0.04582  347 LYS   B NZ  
4467 N N   . HIS   B 255 ? 1.71691 1.17727 1.37005 -0.36301 -0.16750 0.05296  348 HIS   B N   
4468 C CA  . HIS   B 255 ? 1.66536 1.17708 1.34334 -0.37600 -0.14349 0.05824  348 HIS   B CA  
4469 C C   . HIS   B 255 ? 1.69362 1.16854 1.33526 -0.37543 -0.14408 0.06980  348 HIS   B C   
4470 O O   . HIS   B 255 ? 1.69018 1.09799 1.28119 -0.39128 -0.15652 0.07813  348 HIS   B O   
4471 C CB  . HIS   B 255 ? 1.75790 1.29272 1.44655 -0.41791 -0.12860 0.05962  348 HIS   B CB  
4472 C CG  . HIS   B 255 ? 1.87416 1.44877 1.57656 -0.43553 -0.10522 0.06560  348 HIS   B CG  
4473 N ND1 . HIS   B 255 ? 1.80918 1.44920 1.55614 -0.41679 -0.09000 0.06094  348 HIS   B ND1 
4474 C CD2 . HIS   B 255 ? 1.82943 1.38632 1.50485 -0.47027 -0.09452 0.07542  348 HIS   B CD2 
4475 C CE1 . HIS   B 255 ? 1.75808 1.42015 1.50666 -0.43774 -0.07133 0.06653  348 HIS   B CE1 
4476 N NE2 . HIS   B 255 ? 1.72537 1.33951 1.43104 -0.47071 -0.07289 0.07531  348 HIS   B NE2 
4477 N N   . PHE   B 256 ? 1.72807 1.24417 1.39339 -0.35731 -0.13184 0.07033  349 PHE   B N   
4478 C CA  . PHE   B 256 ? 1.71988 1.20810 1.35514 -0.35302 -0.13232 0.07992  349 PHE   B CA  
4479 C C   . PHE   B 256 ? 1.64568 1.17512 1.29525 -0.37701 -0.10760 0.08561  349 PHE   B C   
4480 O O   . PHE   B 256 ? 1.50960 1.10571 1.20687 -0.37002 -0.09114 0.07931  349 PHE   B O   
4481 C CB  . PHE   B 256 ? 1.55486 1.05364 1.20318 -0.31058 -0.14029 0.07464  349 PHE   B CB  
4482 C CG  . PHE   B 256 ? 1.49412 0.95503 1.12846 -0.28489 -0.16417 0.06709  349 PHE   B CG  
4483 C CD1 . PHE   B 256 ? 1.55876 0.94759 1.14282 -0.27895 -0.18589 0.07141  349 PHE   B CD1 
4484 C CD2 . PHE   B 256 ? 1.52147 1.01783 1.19125 -0.26612 -0.16562 0.05499  349 PHE   B CD2 
4485 C CE1 . PHE   B 256 ? 1.52864 0.88388 1.10084 -0.25350 -0.20843 0.06234  349 PHE   B CE1 
4486 C CE2 . PHE   B 256 ? 1.46938 0.93322 1.12617 -0.24224 -0.18670 0.04643  349 PHE   B CE2 
4487 C CZ  . PHE   B 256 ? 1.57429 0.96869 1.18363 -0.23534 -0.20805 0.04938  349 PHE   B CZ  
4488 N N   . ARG   B 257 ? 1.68936 1.17753 1.29571 -0.40516 -0.10552 0.09708  350 ARG   B N   
4489 C CA  . ARG   B 257 ? 1.61738 1.14138 1.23192 -0.43038 -0.08162 0.10195  350 ARG   B CA  
4490 C C   . ARG   B 257 ? 1.57940 1.14148 1.21686 -0.40423 -0.07274 0.10061  350 ARG   B C   
4491 O O   . ARG   B 257 ? 1.51622 1.04628 1.13202 -0.37954 -0.08636 0.10361  350 ARG   B O   
4492 C CB  . ARG   B 257 ? 1.82165 1.28515 1.37656 -0.46421 -0.08314 0.11551  350 ARG   B CB  
4493 C CG  . ARG   B 257 ? 1.90936 1.28723 1.40799 -0.45218 -0.11105 0.12253  350 ARG   B CG  
4494 C CD  . ARG   B 257 ? 2.15662 1.48863 1.60104 -0.47614 -0.11162 0.13308  350 ARG   B CD  
4495 N NE  . ARG   B 257 ? 2.36188 1.61333 1.75402 -0.46367 -0.14038 0.13783  350 ARG   B NE  
4496 C CZ  . ARG   B 257 ? 2.35204 1.55699 1.71047 -0.44144 -0.15765 0.14321  350 ARG   B CZ  
4497 N NH1 . ARG   B 257 ? 2.17950 1.40742 1.54883 -0.43041 -0.14912 0.14570  350 ARG   B NH1 
4498 N NH2 . ARG   B 257 ? 2.33446 1.46903 1.64771 -0.42876 -0.18500 0.14528  350 ARG   B NH2 
4499 N N   . GLY   B 258 ? 1.31392 0.94479 0.99597 -0.40941 -0.05068 0.09510  351 GLY   B N   
4500 C CA  . GLY   B 258 ? 1.35085 1.02306 1.06041 -0.38520 -0.04152 0.09219  351 GLY   B CA  
4501 C C   . GLY   B 258 ? 1.36331 1.07604 1.11837 -0.35171 -0.04510 0.08167  351 GLY   B C   
4502 O O   . GLY   B 258 ? 1.36578 1.12220 1.15133 -0.33517 -0.03466 0.07798  351 GLY   B O   
4503 N N   . VAL   B 259 ? 1.35887 1.05689 1.11729 -0.34204 -0.05955 0.07670  352 VAL   B N   
4504 C CA  . VAL   B 259 ? 1.32063 1.05390 1.11767 -0.31223 -0.06331 0.06691  352 VAL   B CA  
4505 C C   . VAL   B 259 ? 1.15156 0.92809 0.98451 -0.32510 -0.05473 0.05934  352 VAL   B C   
4506 O O   . VAL   B 259 ? 1.37494 1.13199 1.19482 -0.34854 -0.05843 0.05950  352 VAL   B O   
4507 C CB  . VAL   B 259 ? 1.31567 1.00440 1.09134 -0.28904 -0.08620 0.06472  352 VAL   B CB  
4508 C CG1 . VAL   B 259 ? 1.20141 0.92882 1.01495 -0.25910 -0.08799 0.05471  352 VAL   B CG1 
4509 C CG2 . VAL   B 259 ? 1.29743 0.94014 1.03523 -0.27746 -0.09718 0.07137  352 VAL   B CG2 
4510 N N   . ALA   B 260 ? 1.18502 1.01873 1.06221 -0.31008 -0.04435 0.05246  353 ALA   B N   
4511 C CA  . ALA   B 260 ? 1.32977 1.20684 1.24320 -0.31774 -0.03844 0.04406  353 ALA   B CA  
4512 C C   . ALA   B 260 ? 1.38698 1.24300 1.29625 -0.30948 -0.05525 0.03906  353 ALA   B C   
4513 O O   . ALA   B 260 ? 1.35408 1.18013 1.24713 -0.28681 -0.06927 0.03906  353 ALA   B O   
4514 C CB  . ALA   B 260 ? 1.17576 1.11054 1.13260 -0.29859 -0.02759 0.03811  353 ALA   B CB  
4515 N N   . ASP   B 261 ? 1.44058 1.31442 1.36548 -0.32809 -0.05392 0.03344  354 ASP   B N   
4516 C CA  . ASP   B 261 ? 1.46656 1.31967 1.38606 -0.32304 -0.07006 0.02793  354 ASP   B CA  
4517 C C   . ASP   B 261 ? 1.32372 1.20273 1.26837 -0.29022 -0.07542 0.02077  354 ASP   B C   
4518 O O   . ASP   B 261 ? 1.39874 1.25133 1.33035 -0.27615 -0.09061 0.01707  354 ASP   B O   
4519 C CB  . ASP   B 261 ? 1.59904 1.46869 1.53136 -0.35225 -0.06714 0.02279  354 ASP   B CB  
4520 C CG  . ASP   B 261 ? 1.66291 1.48927 1.55849 -0.38649 -0.06746 0.02991  354 ASP   B CG  
4521 O OD1 . ASP   B 261 ? 1.56553 1.33316 1.41852 -0.38342 -0.07873 0.03758  354 ASP   B OD1 
4522 O OD2 . ASP   B 261 ? 1.80048 1.65121 1.70904 -0.41674 -0.05687 0.02744  354 ASP   B OD2 
4523 N N   . GLU   B 262 ? 1.27178 1.20042 1.25019 -0.27801 -0.06337 0.01851  355 GLU   B N   
4524 C CA  . GLU   B 262 ? 1.28637 1.23709 1.28457 -0.24840 -0.06739 0.01333  355 GLU   B CA  
4525 C C   . GLU   B 262 ? 1.26254 1.18621 1.24096 -0.22421 -0.07396 0.01662  355 GLU   B C   
4526 O O   . GLU   B 262 ? 1.25421 1.18946 1.24275 -0.20080 -0.07848 0.01214  355 GLU   B O   
4527 C CB  . GLU   B 262 ? 1.33150 1.33778 1.36796 -0.24313 -0.05374 0.01062  355 GLU   B CB  
4528 C CG  . GLU   B 262 ? 1.37303 1.39135 1.41180 -0.25254 -0.03906 0.01603  355 GLU   B CG  
4529 C CD  . GLU   B 262 ? 1.40555 1.46819 1.47397 -0.27065 -0.02650 0.01117  355 GLU   B CD  
4530 O OE1 . GLU   B 262 ? 1.42175 1.51400 1.51609 -0.26869 -0.02920 0.00319  355 GLU   B OE1 
4531 O OE2 . GLU   B 262 ? 1.49957 1.56841 1.56520 -0.28642 -0.01430 0.01439  355 GLU   B OE2 
4532 N N   . ASP   B 263 ? 1.25127 1.14034 1.20146 -0.22964 -0.07477 0.02374  356 ASP   B N   
4533 C CA  . ASP   B 263 ? 1.05250 0.91438 0.98318 -0.20718 -0.08309 0.02544  356 ASP   B CA  
4534 C C   . ASP   B 263 ? 1.02363 0.82555 0.91338 -0.21162 -0.09928 0.02742  356 ASP   B C   
4535 O O   . ASP   B 263 ? 1.04211 0.81616 0.91156 -0.19514 -0.10775 0.02874  356 ASP   B O   
4536 C CB  . ASP   B 263 ? 1.08130 0.95545 1.01483 -0.20401 -0.07186 0.03139  356 ASP   B CB  
4537 C CG  . ASP   B 263 ? 1.24559 1.11099 1.17326 -0.17656 -0.07809 0.03032  356 ASP   B CG  
4538 O OD1 . ASP   B 263 ? 1.27212 1.16618 1.22226 -0.15735 -0.07666 0.02487  356 ASP   B OD1 
4539 O OD2 . ASP   B 263 ? 1.27425 1.10438 1.17420 -0.17476 -0.08465 0.03464  356 ASP   B OD2 
4540 N N   . ALA   B 264 ? 1.06728 0.84792 0.94434 -0.23317 -0.10492 0.02691  357 ALA   B N   
4541 C CA  . ALA   B 264 ? 1.05874 0.77623 0.89276 -0.24073 -0.12093 0.02986  357 ALA   B CA  
4542 C C   . ALA   B 264 ? 1.16474 0.85587 0.98632 -0.21300 -0.13906 0.02220  357 ALA   B C   
4543 O O   . ALA   B 264 ? 1.17454 0.81331 0.96048 -0.20742 -0.15393 0.02393  357 ALA   B O   
4544 C CB  . ALA   B 264 ? 1.14379 0.84692 0.96893 -0.27272 -0.12199 0.03052  357 ALA   B CB  
4545 N N   . HIS   B 265 ? 1.07167 0.79740 0.92051 -0.19505 -0.13866 0.01310  358 HIS   B N   
4546 C CA  . HIS   B 265 ? 1.09796 0.80373 0.93639 -0.16920 -0.15431 0.00387  358 HIS   B CA  
4547 C C   . HIS   B 265 ? 1.07090 0.77689 0.90699 -0.14226 -0.15604 0.00270  358 HIS   B C   
4548 O O   . HIS   B 265 ? 1.00378 0.68172 0.82256 -0.12202 -0.17123 -0.00471 358 HIS   B O   
4549 C CB  . HIS   B 265 ? 0.99118 0.73477 0.85698 -0.16012 -0.15236 -0.00533 358 HIS   B CB  
4550 C CG  . HIS   B 265 ? 0.97973 0.77999 0.88084 -0.15033 -0.13623 -0.00481 358 HIS   B CG  
4551 N ND1 . HIS   B 265 ? 0.98776 0.82134 0.91059 -0.16742 -0.12077 0.00144  358 HIS   B ND1 
4552 C CD2 . HIS   B 265 ? 0.85225 0.68016 0.76922 -0.12572 -0.13340 -0.01008 358 HIS   B CD2 
4553 C CE1 . HIS   B 265 ? 0.95963 0.83541 0.90904 -0.15272 -0.11061 0.00035  358 HIS   B CE1 
4554 N NE2 . HIS   B 265 ? 0.90095 0.77365 0.84653 -0.12868 -0.11754 -0.00588 358 HIS   B NE2 
4555 N N   . ASN   B 266 ? 1.01900 0.75695 0.87291 -0.14126 -0.14138 0.00850  359 ASN   B N   
4556 C CA  . ASN   B 266 ? 1.01121 0.75568 0.86721 -0.11729 -0.14177 0.00678  359 ASN   B CA  
4557 C C   . ASN   B 266 ? 1.05055 0.74759 0.87268 -0.11680 -0.15261 0.01177  359 ASN   B C   
4558 O O   . ASN   B 266 ? 0.99264 0.69250 0.81509 -0.09648 -0.15532 0.00929  359 ASN   B O   
4559 C CB  . ASN   B 266 ? 0.87027 0.66604 0.75805 -0.11688 -0.12268 0.01065  359 ASN   B CB  
4560 C CG  . ASN   B 266 ? 0.95753 0.79814 0.87659 -0.11104 -0.11440 0.00521  359 ASN   B CG  
4561 O OD1 . ASN   B 266 ? 1.00296 0.84459 0.92306 -0.09555 -0.12204 -0.00351 359 ASN   B OD1 
4562 N ND2 . ASN   B 266 ? 0.89008 0.76707 0.83323 -0.12284 -0.09936 0.00980  359 ASN   B ND2 
4563 N N   . ILE   B 267 ? 1.08198 0.73532 0.87406 -0.13902 -0.15934 0.01856  360 ILE   B N   
4564 C CA  . ILE   B 267 ? 1.06789 0.66946 0.82161 -0.14058 -0.17116 0.02481  360 ILE   B CA  
4565 C C   . ILE   B 267 ? 1.13929 0.69323 0.86597 -0.12100 -0.19518 0.01626  360 ILE   B C   
4566 O O   . ILE   B 267 ? 1.23292 0.77001 0.95324 -0.12471 -0.20382 0.01076  360 ILE   B O   
4567 C CB  . ILE   B 267 ? 1.16504 0.73903 0.89484 -0.17605 -0.16665 0.03684  360 ILE   B CB  
4568 C CG1 . ILE   B 267 ? 1.10096 0.72774 0.86135 -0.19388 -0.14240 0.04239  360 ILE   B CG1 
4569 C CG2 . ILE   B 267 ? 1.22945 0.74609 0.91451 -0.17815 -0.17940 0.04471  360 ILE   B CG2 
4570 C CD1 . ILE   B 267 ? 1.02303 0.67977 0.79939 -0.17861 -0.13284 0.04397  360 ILE   B CD1 
4571 N N   . GLN   B 268 ? 1.07188 0.60466 0.78321 -0.09918 -0.20693 0.01387  361 GLN   B N   
4572 C CA  . GLN   B 268 ? 1.09985 0.58884 0.78679 -0.07639 -0.23119 0.00359  361 GLN   B CA  
4573 C C   . GLN   B 268 ? 1.34668 0.76349 0.98588 -0.09523 -0.24804 0.01043  361 GLN   B C   
4574 O O   . GLN   B 268 ? 1.43676 0.82482 1.05015 -0.11677 -0.24626 0.02386  361 GLN   B O   
4575 C CB  . GLN   B 268 ? 1.12484 0.61283 0.80968 -0.04811 -0.23999 -0.00164 361 GLN   B CB  
4576 C CG  . GLN   B 268 ? 1.19047 0.63812 0.85372 -0.02011 -0.26599 -0.01514 361 GLN   B CG  
4577 C CD  . GLN   B 268 ? 1.24907 0.72997 0.93899 -0.00107 -0.26554 -0.03140 361 GLN   B CD  
4578 O OE1 . GLN   B 268 ? 1.13906 0.68147 0.86790 0.00471  -0.24764 -0.03542 361 GLN   B OE1 
4579 N NE2 . GLN   B 268 ? 1.19518 0.63337 0.86183 0.00823  -0.28556 -0.04082 361 GLN   B NE2 
4580 N N   . THR   B 269 ? 1.37250 0.75860 0.99792 -0.08806 -0.26435 0.00113  362 THR   B N   
4581 C CA  . THR   B 269 ? 1.48791 0.79916 1.06520 -0.10358 -0.28364 0.00594  362 THR   B CA  
4582 C C   . THR   B 269 ? 1.46489 0.72595 1.01361 -0.07191 -0.31186 -0.00500 362 THR   B C   
4583 O O   . THR   B 269 ? 1.40441 0.69476 0.97454 -0.03865 -0.31508 -0.01783 362 THR   B O   
4584 C CB  . THR   B 269 ? 1.47255 0.78235 1.05363 -0.12393 -0.28180 0.00362  362 THR   B CB  
4585 O OG1 . THR   B 269 ? 1.50896 0.84904 1.11602 -0.09806 -0.28517 -0.01318 362 THR   B OG1 
4586 C CG2 . THR   B 269 ? 1.44794 0.80512 1.05598 -0.15584 -0.25585 0.01364  362 THR   B CG2 
4587 N N   . HIS   B 270 ? 1.60116 0.78539 1.10050 -0.08285 -0.33287 -0.00046 363 HIS   B N   
4588 C CA  . HIS   B 270 ? 1.72138 0.84899 1.18842 -0.05280 -0.36311 -0.01103 363 HIS   B CA  
4589 C C   . HIS   B 270 ? 1.84206 0.89834 1.26755 -0.06639 -0.38346 -0.01131 363 HIS   B C   
4590 O O   . HIS   B 270 ? 1.91877 0.93031 1.31028 -0.10134 -0.38354 0.00446  363 HIS   B O   
4591 C CB  . HIS   B 270 ? 1.66755 0.75991 1.10494 -0.04548 -0.37382 -0.00259 363 HIS   B CB  
4592 C CG  . HIS   B 270 ? 1.76426 0.78928 1.16255 -0.01638 -0.40817 -0.01248 363 HIS   B CG  
4593 N ND1 . HIS   B 270 ? 1.95211 0.88730 1.29111 -0.03064 -0.43123 -0.00416 363 HIS   B ND1 
4594 C CD2 . HIS   B 270 ? 1.76365 0.79799 1.17358 0.02656  -0.42407 -0.03099 363 HIS   B CD2 
4595 C CE1 . HIS   B 270 ? 2.02158 0.91094 1.33646 0.00416  -0.46140 -0.01706 363 HIS   B CE1 
4596 N NE2 . HIS   B 270 ? 1.94086 0.89161 1.29973 0.03975  -0.45739 -0.03430 363 HIS   B NE2 
4597 N N   . ARG   B 271 ? 1.76669 0.81312 1.19449 -0.03979 -0.40012 -0.02975 364 ARG   B N   
4598 C CA  . ARG   B 271 ? 2.00213 0.97067 1.38542 -0.04266 -0.42654 -0.03378 364 ARG   B CA  
4599 C C   . ARG   B 271 ? 2.16954 1.08735 1.52376 -0.00415 -0.45718 -0.04563 364 ARG   B C   
4600 O O   . ARG   B 271 ? 2.18132 1.13815 1.56013 0.02748  -0.45613 -0.05516 364 ARG   B O   
4601 C CB  . ARG   B 271 ? 2.10428 1.09652 1.50983 -0.04147 -0.42421 -0.04763 364 ARG   B CB  
4602 C CG  . ARG   B 271 ? 2.13353 1.12843 1.54735 0.00272  -0.44212 -0.07224 364 ARG   B CG  
4603 C CD  . ARG   B 271 ? 2.06754 1.13108 1.52668 0.00834  -0.42538 -0.08515 364 ARG   B CD  
4604 N NE  . ARG   B 271 ? 2.06543 1.13078 1.52624 -0.02915 -0.41428 -0.07623 364 ARG   B NE  
4605 C CZ  . ARG   B 271 ? 2.05132 1.08265 1.49561 -0.03485 -0.42789 -0.08479 364 ARG   B CZ  
4606 N NH1 . ARG   B 271 ? 2.03499 1.02475 1.45784 -0.00521 -0.45342 -0.10268 364 ARG   B NH1 
4607 N NH2 . ARG   B 271 ? 2.02080 1.06148 1.47129 -0.07057 -0.41611 -0.07651 364 ARG   B NH2 
4608 N N   . ASP   B 272 ? 2.50554 1.33484 1.80658 -0.00744 -0.48541 -0.04535 365 ASP   B N   
4609 C CA  . ASP   B 272 ? 2.83165 1.62664 2.10749 0.02948  -0.51297 -0.05448 365 ASP   B CA  
4610 C C   . ASP   B 272 ? 2.76847 1.60152 2.07961 0.07596  -0.52028 -0.08246 365 ASP   B C   
4611 O O   . ASP   B 272 ? 2.73691 1.58512 2.05807 0.10782  -0.52770 -0.09156 365 ASP   B O   
4612 C CB  . ASP   B 272 ? 2.83575 1.56997 2.06507 0.01991  -0.53348 -0.04939 365 ASP   B CB  
4613 C CG  . ASP   B 272 ? 2.80204 1.52074 2.01532 -0.03061 -0.51842 -0.02986 365 ASP   B CG  
4614 O OD1 . ASP   B 272 ? 2.62083 1.36617 1.85959 -0.04453 -0.50593 -0.03525 365 ASP   B OD1 
4615 O OD2 . ASP   B 272 ? 2.87626 1.55945 2.05213 -0.05655 -0.51870 -0.01025 365 ASP   B OD2 
4616 N N   . SER   B 273 ? 2.36377 1.21711 1.69522 0.07966  -0.51716 -0.09717 366 SER   B N   
4617 C CA  . SER   B 273 ? 2.29798 1.20438 1.66793 0.11973  -0.51750 -0.12377 366 SER   B CA  
4618 C C   . SER   B 273 ? 2.41798 1.29357 1.76776 0.16021  -0.54672 -0.13793 366 SER   B C   
4619 O O   . SER   B 273 ? 2.50033 1.32044 1.80941 0.15667  -0.56749 -0.13202 366 SER   B O   
4620 C CB  . SER   B 273 ? 2.12566 1.12991 1.55194 0.12139  -0.48511 -0.12209 366 SER   B CB  
4621 O OG  . SER   B 273 ? 2.15191 1.21307 1.61547 0.15642  -0.48213 -0.14638 366 SER   B OG  
4622 N N   . LEU   B 274 ? 2.34563 1.26390 1.72481 0.19735  -0.54773 -0.15579 367 LEU   B N   
4623 C CA  . LEU   B 274 ? 2.34273 1.25017 1.71140 0.23625  -0.57316 -0.17022 367 LEU   B CA  
4624 C C   . LEU   B 274 ? 2.21889 1.10417 1.57310 0.25279  -0.59267 -0.18536 367 LEU   B C   
4625 O O   . LEU   B 274 ? 2.14405 1.06917 1.52535 0.28796  -0.59698 -0.21090 367 LEU   B O   
4626 C CB  . LEU   B 274 ? 2.31049 1.16645 1.63751 0.22685  -0.58853 -0.15121 367 LEU   B CB  
4627 C CG  . LEU   B 274 ? 2.27972 1.15581 1.61840 0.21363  -0.57163 -0.13643 367 LEU   B CG  
4628 C CD1 . LEU   B 274 ? 2.22332 1.04681 1.51598 0.20578  -0.58887 -0.11972 367 LEU   B CD1 
4629 C CD2 . LEU   B 274 ? 1.87493 0.82057 1.26425 0.24757  -0.56234 -0.15668 367 LEU   B CD2 
4630 N N   . ASP   B 275 ? 2.29677 1.12046 1.60847 0.22711  -0.60396 -0.17009 368 ASP   B N   
4631 C CA  . ASP   B 275 ? 2.36780 1.16798 1.66535 0.23881  -0.62106 -0.18290 368 ASP   B CA  
4632 C C   . ASP   B 275 ? 2.20444 1.05389 1.53980 0.24108  -0.60320 -0.19851 368 ASP   B C   
4633 O O   . ASP   B 275 ? 2.18596 1.04369 1.52731 0.26669  -0.61451 -0.21908 368 ASP   B O   
4634 C CB  . ASP   B 275 ? 2.40185 1.12952 1.64834 0.20489  -0.63253 -0.16162 368 ASP   B CB  
4635 C CG  . ASP   B 275 ? 2.60638 1.28331 1.81001 0.19812  -0.64875 -0.14487 368 ASP   B CG  
4636 O OD1 . ASP   B 275 ? 2.55472 1.25400 1.77018 0.21658  -0.64923 -0.14789 368 ASP   B OD1 
4637 O OD2 . ASP   B 275 ? 2.59990 1.21514 1.75708 0.17378  -0.66102 -0.12925 368 ASP   B OD2 
4638 N N   . LEU   B 276 ? 2.15003 1.03307 1.50984 0.21443  -0.57590 -0.18979 369 LEU   B N   
4639 C CA  . LEU   B 276 ? 2.16893 1.10225 1.56353 0.21604  -0.55870 -0.20547 369 LEU   B CA  
4640 C C   . LEU   B 276 ? 2.08095 1.07849 1.51509 0.25731  -0.55382 -0.23201 369 LEU   B C   
4641 O O   . LEU   B 276 ? 2.01385 1.04431 1.46689 0.27425  -0.55098 -0.25250 369 LEU   B O   
4642 C CB  . LEU   B 276 ? 2.11840 1.07232 1.52772 0.17655  -0.53265 -0.18990 369 LEU   B CB  
4643 C CG  . LEU   B 276 ? 2.14091 1.04333 1.51700 0.13108  -0.53200 -0.16221 369 LEU   B CG  
4644 C CD1 . LEU   B 276 ? 2.00179 0.95472 1.40712 0.09517  -0.50062 -0.14688 369 LEU   B CD1 
4645 C CD2 . LEU   B 276 ? 2.17873 1.03815 1.52739 0.12236  -0.54714 -0.16263 369 LEU   B CD2 
4646 N N   . LEU   B 277 ? 1.99245 1.01136 1.43979 0.27294  -0.55186 -0.23217 370 LEU   B N   
4647 C CA  . LEU   B 277 ? 1.93040 1.01414 1.41651 0.31167  -0.54701 -0.25760 370 LEU   B CA  
4648 C C   . LEU   B 277 ? 2.04394 1.12100 1.52276 0.34755  -0.57104 -0.27797 370 LEU   B C   
4649 O O   . LEU   B 277 ? 2.04389 1.17853 1.55525 0.37687  -0.56574 -0.30292 370 LEU   B O   
4650 C CB  . LEU   B 277 ? 1.76392 0.87041 1.26494 0.31829  -0.54089 -0.25150 370 LEU   B CB  
4651 C CG  . LEU   B 277 ? 1.76342 0.95087 1.31114 0.35232  -0.53040 -0.27390 370 LEU   B CG  
4652 C CD1 . LEU   B 277 ? 1.63777 0.91134 1.23034 0.33982  -0.49529 -0.27536 370 LEU   B CD1 
4653 C CD2 . LEU   B 277 ? 1.61711 0.81773 1.17324 0.35757  -0.52975 -0.26507 370 LEU   B CD2 
4654 N N   . ASP   B 278 ? 2.05159 1.06055 1.48724 0.34470  -0.59723 -0.26823 371 ASP   B N   
4655 C CA  . ASP   B 278 ? 2.23338 1.22991 1.65810 0.37746  -0.62289 -0.28764 371 ASP   B CA  
4656 C C   . ASP   B 278 ? 2.25078 1.24392 1.67367 0.37682  -0.62353 -0.29851 371 ASP   B C   
4657 O O   . ASP   B 278 ? 2.22705 1.24511 1.66251 0.40885  -0.63332 -0.32287 371 ASP   B O   
4658 C CB  . ASP   B 278 ? 2.28982 1.21223 1.66522 0.37489  -0.65234 -0.27389 371 ASP   B CB  
4659 C CG  . ASP   B 278 ? 2.34709 1.26695 1.71856 0.37183  -0.65232 -0.26110 371 ASP   B CG  
4660 O OD1 . ASP   B 278 ? 2.23492 1.21713 1.64677 0.38620  -0.63629 -0.27091 371 ASP   B OD1 
4661 O OD2 . ASP   B 278 ? 2.44286 1.29881 1.76982 0.35428  -0.66800 -0.24137 371 ASP   B OD2 
4662 N N   . LYS   B 279 ? 2.20626 1.17110 1.61427 0.34030  -0.61332 -0.28157 372 LYS   B N   
4663 C CA  . LYS   B 279 ? 2.15590 1.12092 1.56392 0.33754  -0.61240 -0.29188 372 LYS   B CA  
4664 C C   . LYS   B 279 ? 2.14703 1.19113 1.60034 0.35477  -0.59066 -0.31447 372 LYS   B C   
4665 O O   . LYS   B 279 ? 2.23593 1.29381 1.69435 0.36995  -0.59418 -0.33262 372 LYS   B O   
4666 C CB  . LYS   B 279 ? 1.98414 0.90888 1.37020 0.29175  -0.60453 -0.26883 372 LYS   B CB  
4667 C CG  . LYS   B 279 ? 2.10499 0.95273 1.44353 0.26945  -0.62306 -0.24519 372 LYS   B CG  
4668 C CD  . LYS   B 279 ? 2.03813 0.86069 1.36294 0.22033  -0.60931 -0.22193 372 LYS   B CD  
4669 C CE  . LYS   B 279 ? 2.20278 0.95519 1.48067 0.19530  -0.62372 -0.19726 372 LYS   B CE  
4670 N NZ  . LYS   B 279 ? 2.25032 0.98684 1.51879 0.14526  -0.60736 -0.17465 372 LYS   B NZ  
4671 N N   . ALA   B 280 ? 2.19135 1.28779 1.67600 0.35214  -0.56797 -0.31375 373 ALA   B N   
4672 C CA  . ALA   B 280 ? 2.25199 1.42597 1.77738 0.36676  -0.54580 -0.33458 373 ALA   B CA  
4673 C C   . ALA   B 280 ? 2.45263 1.67014 1.99950 0.41012  -0.55330 -0.36105 373 ALA   B C   
4674 O O   . ALA   B 280 ? 2.34989 1.62269 1.92197 0.42560  -0.54080 -0.38197 373 ALA   B O   
4675 C CB  . ALA   B 280 ? 1.99698 1.21212 1.54717 0.34962  -0.51996 -0.32558 373 ALA   B CB  
4676 N N   . ARG   B 281 ? 2.38702 1.58292 1.92378 0.42890  -0.57358 -0.36090 374 ARG   B N   
4677 C CA  . ARG   B 281 ? 2.25292 1.49275 1.81135 0.46900  -0.58259 -0.38705 374 ARG   B CA  
4678 C C   . ARG   B 281 ? 2.31835 1.54488 1.86492 0.48722  -0.59928 -0.40479 374 ARG   B C   
4679 O O   . ARG   B 281 ? 2.39556 1.67626 1.96811 0.51674  -0.59800 -0.43065 374 ARG   B O   
4680 C CB  . ARG   B 281 ? 2.44374 1.65913 1.99016 0.48265  -0.60352 -0.38242 374 ARG   B CB  
4681 C CG  . ARG   B 281 ? 2.54321 1.81160 2.11643 0.52207  -0.61216 -0.40997 374 ARG   B CG  
4682 C CD  . ARG   B 281 ? 2.61397 1.85906 2.17450 0.53247  -0.63248 -0.40484 374 ARG   B CD  
4683 N NE  . ARG   B 281 ? 2.62446 1.91936 2.20973 0.56907  -0.64327 -0.43291 374 ARG   B NE  
4684 C CZ  . ARG   B 281 ? 2.78172 2.07159 2.36291 0.58415  -0.66129 -0.43624 374 ARG   B CZ  
4685 N NH1 . ARG   B 281 ? 2.80895 2.04555 2.36080 0.56678  -0.67041 -0.41269 374 ARG   B NH1 
4686 N NH2 . ARG   B 281 ? 2.80269 2.14308 2.40909 0.61641  -0.67023 -0.46458 374 ARG   B NH2 
4687 N N   . ALA   B 282 ? 2.29855 1.45590 1.80691 0.46905  -0.61419 -0.39169 375 ALA   B N   
4688 C CA  . ALA   B 282 ? 2.32614 1.46446 1.82024 0.48446  -0.63100 -0.40722 375 ALA   B CA  
4689 C C   . ALA   B 282 ? 2.24271 1.43692 1.76337 0.48525  -0.60819 -0.42318 375 ALA   B C   
4690 O O   . ALA   B 282 ? 2.09977 1.32061 1.63475 0.46146  -0.58268 -0.41430 375 ALA   B O   
4691 C CB  . ALA   B 282 ? 2.33546 1.38553 1.78156 0.46063  -0.65093 -0.38723 375 ALA   B CB  
4692 C C11 . A1CAE C .   ? 0.42466 0.72559 0.67676 -0.09603 0.03505  -0.03504 301 A1CAE A C11 
4693 C C14 . A1CAE C .   ? 0.47009 0.78110 0.71863 -0.07484 0.02666  -0.03889 301 A1CAE A C14 
4694 C C15 . A1CAE C .   ? 0.48616 0.79429 0.72726 -0.06000 0.01888  -0.04048 301 A1CAE A C15 
4695 C C16 . A1CAE C .   ? 0.45458 0.74260 0.68110 -0.05810 0.02268  -0.02932 301 A1CAE A C16 
4696 C C17 . A1CAE C .   ? 0.49092 0.75361 0.69948 -0.05024 0.01465  -0.02520 301 A1CAE A C17 
4697 C C19 . A1CAE C .   ? 0.55350 0.77679 0.73762 -0.05462 0.01615  -0.01270 301 A1CAE A C19 
4698 C C21 . A1CAE C .   ? 0.64387 0.85887 0.83128 -0.06766 0.02456  -0.01097 301 A1CAE A C21 
4699 C C22 . A1CAE C .   ? 0.55877 0.78042 0.75047 -0.06858 0.01922  -0.01919 301 A1CAE A C22 
4700 C C23 . A1CAE C .   ? 0.77673 0.98069 0.96268 -0.07302 0.03218  -0.00497 301 A1CAE A C23 
4701 C C24 . A1CAE C .   ? 0.48622 0.70682 0.68385 -0.07462 0.03290  -0.00701 301 A1CAE A C24 
4702 C C26 . A1CAE C .   ? 0.45285 0.72325 0.66394 -0.04177 0.00274  -0.03590 301 A1CAE A C26 
4703 C C27 . A1CAE C .   ? 0.48447 0.77943 0.71520 -0.04916 0.00581  -0.04406 301 A1CAE A C27 
4704 C C28 . A1CAE C .   ? 0.37162 0.66330 0.61317 -0.08151 0.02800  -0.03382 301 A1CAE A C28 
4705 C C30 . A1CAE C .   ? 0.64589 0.91352 0.89794 -0.12302 0.03058  -0.04317 301 A1CAE A C30 
4706 C C03 . A1CAE C .   ? 0.85778 1.10092 1.10964 -0.14153 0.01258  -0.06834 301 A1CAE A C03 
4707 C C04 . A1CAE C .   ? 0.55511 0.80956 0.80142 -0.12140 0.01803  -0.05508 301 A1CAE A C04 
4708 C C05 . A1CAE C .   ? 0.61923 0.85116 0.84919 -0.11360 0.02048  -0.04648 301 A1CAE A C05 
4709 C C06 . A1CAE C .   ? 0.63611 0.86400 0.86248 -0.11062 0.02675  -0.03700 301 A1CAE A C06 
4710 C C07 . A1CAE C .   ? 0.62991 0.87395 0.86617 -0.11493 0.03159  -0.03459 301 A1CAE A C07 
4711 C C08 . A1CAE C .   ? 0.56261 0.80128 0.79311 -0.11118 0.03739  -0.02468 301 A1CAE A C08 
4712 C C09 . A1CAE C .   ? 0.47981 0.73691 0.71423 -0.10276 0.03583  -0.02600 301 A1CAE A C09 
4713 C C31 . A1CAE C .   ? 0.66694 0.94023 0.92489 -0.12621 0.02402  -0.05305 301 A1CAE A C31 
4714 N N10 . A1CAE C .   ? 0.45883 0.74291 0.70714 -0.10570 0.03734  -0.03180 301 A1CAE A N10 
4715 N N12 . A1CAE C .   ? 0.41249 0.74042 0.67782 -0.09950 0.03930  -0.04048 301 A1CAE A N12 
4716 N N13 . A1CAE C .   ? 0.42841 0.76301 0.69226 -0.08577 0.03419  -0.04337 301 A1CAE A N13 
4717 N N20 . A1CAE C .   ? 0.68078 0.89127 0.85879 -0.06017 0.01983  -0.00911 301 A1CAE A N20 
4718 O O01 . A1CAE C .   ? 0.91582 1.16264 1.15168 -0.11369 0.00077  -0.07029 301 A1CAE A O01 
4719 O O18 . A1CAE C .   ? 0.47495 0.71973 0.67574 -0.05765 0.01967  -0.01737 301 A1CAE A O18 
4720 O O25 . A1CAE C .   ? 0.69415 0.91011 0.86845 -0.04737 0.00990  -0.01246 301 A1CAE A O25 
4721 O O29 . A1CAE C .   ? 0.53476 0.78194 0.75892 -0.09267 0.03290  -0.02266 301 A1CAE A O29 
4722 O O32 . A1CAE C .   ? 0.82256 1.11528 1.09366 -0.12739 0.00416  -0.07833 301 A1CAE A O32 
4723 S S02 . A1CAE C .   ? 0.77529 1.03608 1.02717 -0.12518 0.00829  -0.06851 301 A1CAE A S02 
4724 O O   . HOH   D .   ? 0.50766 0.68683 0.63425 -0.03701 -0.00258 0.04568  401 HOH   A O   
4725 O O   . HOH   D .   ? 0.74309 0.96048 0.83257 0.02488  -0.01124 -0.04627 402 HOH   A O   
4726 O O   . HOH   D .   ? 0.67963 0.81665 0.82411 -0.21062 0.08496  0.04764  403 HOH   A O   
4727 O O   . HOH   D .   ? 0.88552 0.81187 0.80020 -0.07123 -0.05576 0.03962  404 HOH   A O   
4728 O O   . HOH   D .   ? 0.56001 0.80012 0.63933 0.00560  0.00981  -0.03118 405 HOH   A O   
4729 O O   . HOH   D .   ? 0.71733 0.74616 0.89637 -0.04156 0.01841  -0.01472 406 HOH   A O   
4730 O O   . HOH   D .   ? 0.75435 0.87646 0.86526 -0.10093 -0.00959 0.02477  407 HOH   A O   
4731 O O   . HOH   D .   ? 0.53502 0.73900 0.71186 -0.05930 -0.00245 0.02640  408 HOH   A O   
4732 O O   . HOH   D .   ? 0.48089 0.70780 0.68567 -0.06649 0.00412  0.02061  409 HOH   A O   
4733 O O   . HOH   D .   ? 0.47557 0.65098 0.62154 -0.05185 0.02249  0.01945  410 HOH   A O   
4734 O O   . HOH   D .   ? 0.71248 0.79209 0.77489 -0.04674 -0.01805 0.02063  411 HOH   A O   
4735 O O   . HOH   D .   ? 0.40026 0.61814 0.61065 -0.06095 0.03630  0.02276  412 HOH   A O   
4736 O O   . HOH   D .   ? 0.52377 1.05066 0.89096 -0.12746 0.06234  -0.10188 413 HOH   A O   
4737 O O   . HOH   D .   ? 0.54987 0.82886 0.75381 -0.14369 0.08242  -0.00345 414 HOH   A O   
4738 O O   . HOH   D .   ? 0.52170 0.72634 0.77518 -0.01665 0.03582  -0.01517 415 HOH   A O   
4739 O O   . HOH   D .   ? 0.54037 0.71662 0.64746 -0.04399 0.01448  0.05172  416 HOH   A O   
4740 O O   . HOH   D .   ? 0.46969 0.88248 0.71727 -0.12031 0.09552  -0.03165 417 HOH   A O   
4741 O O   . HOH   D .   ? 0.78308 0.89393 0.91137 -0.26718 0.09412  0.05039  418 HOH   A O   
4742 O O   . HOH   D .   ? 0.52797 0.93017 0.76578 -0.05982 0.06680  -0.04632 419 HOH   A O   
4743 O O   . HOH   D .   ? 0.96838 0.88655 0.79420 -0.12368 0.00673  0.15713  420 HOH   A O   
4744 O O   . HOH   D .   ? 0.54129 0.69323 0.76874 -0.01655 0.02520  0.00008  421 HOH   A O   
4745 O O   . HOH   D .   ? 0.50240 0.76794 0.70483 -0.04180 0.01984  -0.01913 422 HOH   A O   
4746 O O   . HOH   D .   ? 0.53161 0.71708 0.72258 -0.08505 0.04020  -0.00553 423 HOH   A O   
4747 O O   . HOH   D .   ? 0.56807 1.06095 0.91190 -0.16767 0.08486  -0.07793 424 HOH   A O   
4748 O O   . HOH   D .   ? 0.44993 0.86142 0.70378 -0.02405 0.03951  -0.07081 425 HOH   A O   
4749 O O   . HOH   D .   ? 0.49157 0.78334 0.70340 -0.05094 0.03653  -0.01683 426 HOH   A O   
4750 O O   . HOH   D .   ? 0.49492 0.68495 0.67442 -0.06032 0.03761  0.03278  427 HOH   A O   
4751 O O   . HOH   D .   ? 0.91624 0.86861 0.86799 -0.08787 -0.03985 0.04131  428 HOH   A O   
4752 O O   . HOH   D .   ? 0.39048 0.65169 0.66030 -0.03583 0.04163  -0.01172 429 HOH   A O   
4753 O O   . HOH   D .   ? 0.50673 0.68724 0.65713 -0.03250 -0.00768 0.04608  430 HOH   A O   
4754 O O   . HOH   D .   ? 0.63316 0.76059 0.69312 -0.01848 -0.03835 0.06680  431 HOH   A O   
4755 O O   . HOH   D .   ? 0.77541 0.84976 0.97066 -0.03343 0.02602  -0.01187 432 HOH   A O   
4756 O O   . HOH   D .   ? 0.59992 0.80627 0.80149 -0.08967 0.03198  -0.01839 433 HOH   A O   
4757 O O   . HOH   D .   ? 1.06694 0.84954 0.92560 0.01978  -0.14195 0.13922  434 HOH   A O   
4758 O O   . HOH   D .   ? 0.96623 0.89540 0.89670 0.01217  -0.10821 0.11564  435 HOH   A O   
4759 O O   . HOH   D .   ? 0.66226 0.80220 0.76788 -0.05562 0.00888  0.01128  436 HOH   A O   
4760 O O   . HOH   D .   ? 0.48411 0.72271 0.69700 -0.08507 0.00051  0.01253  437 HOH   A O   
4761 O O   . HOH   D .   ? 0.57147 1.18984 0.99792 -0.18360 0.08108  -0.13125 438 HOH   A O   
4762 O O   . HOH   D .   ? 0.49570 0.78347 0.81141 0.05123  -0.08098 -0.02759 439 HOH   A O   
4763 O O   . HOH   D .   ? 0.99032 0.82180 0.83340 -0.06310 -0.09478 0.04358  440 HOH   A O   
4764 O O   . HOH   D .   ? 1.04214 0.87949 0.92565 0.02998  -0.14352 0.12845  441 HOH   A O   
4765 O O   . HOH   D .   ? 0.68440 0.86141 0.85264 -0.07572 0.03584  -0.00757 442 HOH   A O   
4766 O O   . HOH   D .   ? 0.75237 0.85300 0.79780 -0.00386 -0.06267 0.07238  443 HOH   A O   
4767 O O   . HOH   E .   ? 0.57777 0.75446 0.65316 -0.04947 0.02254  0.05520  401 HOH   B O   
4768 O O   . HOH   E .   ? 1.11650 0.67849 0.85809 -0.16845 -0.19151 0.01108  402 HOH   B O   
4769 O O   . HOH   E .   ? 0.85960 0.66731 0.75483 -0.05383 -0.14246 -0.01684 403 HOH   B O   
4770 O O   . HOH   E .   ? 0.89222 0.76951 0.79024 -0.05945 -0.08260 0.03550  404 HOH   B O   
4771 O O   . HOH   E .   ? 1.33896 0.86499 0.96330 -0.18763 -0.14227 0.08754  405 HOH   B O   
4772 O O   . HOH   E .   ? 0.93140 0.76053 0.80967 -0.13255 -0.07559 0.04707  406 HOH   B O   
4773 O O   . HOH   E .   ? 0.84603 0.87705 0.85829 0.05865  -0.09920 -0.06302 407 HOH   B O   
4774 O O   . HOH   E .   ? 0.84345 1.07035 1.01817 0.35266  -0.31407 -0.28385 408 HOH   B O   
# 
