data_9GLA
# 
_entry.id   9GLA 
# 
_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   9GLA         pdb_00009gla 10.2210/pdb9gla/pdb 
WWPDB D_1292141201 ?            ?                   
# 
_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       2025-04-02 
_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                        9GLA 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rezacova@uochb.cas.cz 
_pdbx_contact_author.name_first         Pavlina 
_pdbx_contact_author.name_last          Rezacova 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9626-346X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Skerlova, J.'     1 0000-0002-9579-4047 
'Krejcirikova, V.' 2 ?                   
'Rezacova, P.'     3 0000-0001-9626-346X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            294 
_citation.language                  ? 
_citation.page_first                139117 
_citation.page_last                 139117 
_citation.title                     
'CDK2-based CDK7 mimic as a tool for structural analysis: Biochemical validation and crystal structure with SY5609.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.139117 
_citation.pdbx_database_id_PubMed   39733900 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Skerlova, J.'     1 ? 
primary 'Krejcirikova, V.' 2 ? 
primary 'Perina, M.'       3 ? 
primary 'Vojackova, V.'    4 ? 
primary 'Fabry, M.'        5 ? 
primary 'Krystof, V.'      6 ? 
primary 'Jorda, R.'        7 ? 
primary 'Rezacova, P.'     8 ? 
# 
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' 34023.328 1   2.7.11.22 ? ? 
'CDK2 containing 12 active-site mutations mimicking CDK7: E8D, K9F, I10L, T14Q, Y15F, V64I, L83M, H84E, Q85T, K88E, K89V, Q131N' 
2 polymer     man Cyclin-A2 29624.297 1   ?         ? ? ? 
3 non-polymer syn 
;7-dimethylphosphoryl-3-[2-[[(3~{S})-6,6-dimethylpiperidin-3-yl]amino]-5-(trifluoromethyl)pyrimidin-4-yl]-1~{H}-indole-6-carbonitrile
;
490.461   1   ?         ? ? ? 
4 non-polymer syn MONOTHIOGLYCEROL 108.159   1   ?         ? ? ? 
5 non-polymer syn 'SODIUM ION' 22.990    2   ?         ? ? ? 
6 water       nat water 18.015    105 ?         ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Cell division protein kinase 2,p33 protein kinase' 
2 'Cyclin-A,Cyclin A'                                 
# 
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 
;MENFQKVDFLGEGQFGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIIKLLDVIHTENKLYLVF
EFMETDLEVFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPNNLLINTEGAIKLADFGLARAFGVPVRTY
(TPO)HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPD
YKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
;MENFQKVDFLGEGQFGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIIKLLDVIHTENKLYLVF
EFMETDLEVFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPNNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
A ? 
2 'polypeptide(L)' no no  
;VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
;
;VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 
;7-dimethylphosphoryl-3-[2-[[(3~{S})-6,6-dimethylpiperidin-3-yl]amino]-5-(trifluoromethyl)pyrimidin-4-yl]-1~{H}-indole-6-carbonitrile
;
YNK 
4 MONOTHIOGLYCEROL SGM 
5 'SODIUM ION' NA  
6 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   ASN n 
1 4   PHE n 
1 5   GLN n 
1 6   LYS n 
1 7   VAL n 
1 8   ASP n 
1 9   PHE n 
1 10  LEU n 
1 11  GLY n 
1 12  GLU n 
1 13  GLY n 
1 14  GLN n 
1 15  PHE n 
1 16  GLY n 
1 17  VAL n 
1 18  VAL n 
1 19  TYR n 
1 20  LYS n 
1 21  ALA n 
1 22  ARG n 
1 23  ASN n 
1 24  LYS n 
1 25  LEU n 
1 26  THR n 
1 27  GLY n 
1 28  GLU n 
1 29  VAL n 
1 30  VAL n 
1 31  ALA n 
1 32  LEU n 
1 33  LYS n 
1 34  LYS n 
1 35  ILE n 
1 36  ARG n 
1 37  LEU n 
1 38  ASP n 
1 39  THR n 
1 40  GLU n 
1 41  THR n 
1 42  GLU n 
1 43  GLY n 
1 44  VAL n 
1 45  PRO n 
1 46  SER n 
1 47  THR n 
1 48  ALA n 
1 49  ILE n 
1 50  ARG n 
1 51  GLU n 
1 52  ILE n 
1 53  SER n 
1 54  LEU n 
1 55  LEU n 
1 56  LYS n 
1 57  GLU n 
1 58  LEU n 
1 59  ASN n 
1 60  HIS n 
1 61  PRO n 
1 62  ASN n 
1 63  ILE n 
1 64  ILE n 
1 65  LYS n 
1 66  LEU n 
1 67  LEU n 
1 68  ASP n 
1 69  VAL n 
1 70  ILE n 
1 71  HIS n 
1 72  THR n 
1 73  GLU n 
1 74  ASN n 
1 75  LYS n 
1 76  LEU n 
1 77  TYR n 
1 78  LEU n 
1 79  VAL n 
1 80  PHE n 
1 81  GLU n 
1 82  PHE n 
1 83  MET n 
1 84  GLU n 
1 85  THR n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  VAL n 
1 90  PHE n 
1 91  MET n 
1 92  ASP n 
1 93  ALA n 
1 94  SER n 
1 95  ALA n 
1 96  LEU n 
1 97  THR n 
1 98  GLY n 
1 99  ILE n 
1 100 PRO n 
1 101 LEU n 
1 102 PRO n 
1 103 LEU n 
1 104 ILE n 
1 105 LYS n 
1 106 SER n 
1 107 TYR n 
1 108 LEU n 
1 109 PHE n 
1 110 GLN n 
1 111 LEU n 
1 112 LEU n 
1 113 GLN n 
1 114 GLY n 
1 115 LEU n 
1 116 ALA n 
1 117 PHE n 
1 118 CYS n 
1 119 HIS n 
1 120 SER n 
1 121 HIS n 
1 122 ARG n 
1 123 VAL n 
1 124 LEU n 
1 125 HIS n 
1 126 ARG n 
1 127 ASP n 
1 128 LEU n 
1 129 LYS n 
1 130 PRO n 
1 131 ASN n 
1 132 ASN n 
1 133 LEU n 
1 134 LEU n 
1 135 ILE n 
1 136 ASN n 
1 137 THR n 
1 138 GLU n 
1 139 GLY n 
1 140 ALA n 
1 141 ILE n 
1 142 LYS n 
1 143 LEU n 
1 144 ALA n 
1 145 ASP n 
1 146 PHE n 
1 147 GLY n 
1 148 LEU n 
1 149 ALA n 
1 150 ARG n 
1 151 ALA n 
1 152 PHE n 
1 153 GLY n 
1 154 VAL n 
1 155 PRO n 
1 156 VAL n 
1 157 ARG n 
1 158 THR n 
1 159 TYR n 
1 160 TPO n 
1 161 HIS n 
1 162 GLU n 
1 163 VAL n 
1 164 VAL n 
1 165 THR n 
1 166 LEU n 
1 167 TRP n 
1 168 TYR n 
1 169 ARG n 
1 170 ALA n 
1 171 PRO n 
1 172 GLU n 
1 173 ILE n 
1 174 LEU n 
1 175 LEU n 
1 176 GLY n 
1 177 CYS n 
1 178 LYS n 
1 179 TYR n 
1 180 TYR n 
1 181 SER n 
1 182 THR n 
1 183 ALA n 
1 184 VAL n 
1 185 ASP n 
1 186 ILE n 
1 187 TRP n 
1 188 SER n 
1 189 LEU n 
1 190 GLY n 
1 191 CYS n 
1 192 ILE n 
1 193 PHE n 
1 194 ALA n 
1 195 GLU n 
1 196 MET n 
1 197 VAL n 
1 198 THR n 
1 199 ARG n 
1 200 ARG n 
1 201 ALA n 
1 202 LEU n 
1 203 PHE n 
1 204 PRO n 
1 205 GLY n 
1 206 ASP n 
1 207 SER n 
1 208 GLU n 
1 209 ILE n 
1 210 ASP n 
1 211 GLN n 
1 212 LEU n 
1 213 PHE n 
1 214 ARG n 
1 215 ILE n 
1 216 PHE n 
1 217 ARG n 
1 218 THR n 
1 219 LEU n 
1 220 GLY n 
1 221 THR n 
1 222 PRO n 
1 223 ASP n 
1 224 GLU n 
1 225 VAL n 
1 226 VAL n 
1 227 TRP n 
1 228 PRO n 
1 229 GLY n 
1 230 VAL n 
1 231 THR n 
1 232 SER n 
1 233 MET n 
1 234 PRO n 
1 235 ASP n 
1 236 TYR n 
1 237 LYS n 
1 238 PRO n 
1 239 SER n 
1 240 PHE n 
1 241 PRO n 
1 242 LYS n 
1 243 TRP n 
1 244 ALA n 
1 245 ARG n 
1 246 GLN n 
1 247 ASP n 
1 248 PHE n 
1 249 SER n 
1 250 LYS n 
1 251 VAL n 
1 252 VAL n 
1 253 PRO n 
1 254 PRO n 
1 255 LEU n 
1 256 ASP n 
1 257 GLU n 
1 258 ASP n 
1 259 GLY n 
1 260 ARG n 
1 261 SER n 
1 262 LEU n 
1 263 LEU n 
1 264 SER n 
1 265 GLN n 
1 266 MET n 
1 267 LEU n 
1 268 HIS n 
1 269 TYR n 
1 270 ASP n 
1 271 PRO n 
1 272 ASN n 
1 273 LYS n 
1 274 ARG n 
1 275 ILE n 
1 276 SER n 
1 277 ALA n 
1 278 LYS n 
1 279 ALA n 
1 280 ALA n 
1 281 LEU n 
1 282 ALA n 
1 283 HIS n 
1 284 PRO n 
1 285 PHE n 
1 286 PHE n 
1 287 GLN n 
1 288 ASP n 
1 289 VAL n 
1 290 THR n 
1 291 LYS n 
1 292 PRO n 
1 293 VAL n 
1 294 PRO n 
1 295 HIS n 
1 296 LEU n 
1 297 ARG n 
1 298 LEU n 
2 1   VAL n 
2 2   PRO n 
2 3   ASP n 
2 4   TYR n 
2 5   HIS n 
2 6   GLU n 
2 7   ASP n 
2 8   ILE n 
2 9   HIS n 
2 10  THR n 
2 11  TYR n 
2 12  LEU n 
2 13  ARG n 
2 14  GLU n 
2 15  MET n 
2 16  GLU n 
2 17  VAL n 
2 18  LYS n 
2 19  CYS n 
2 20  LYS n 
2 21  PRO n 
2 22  LYS n 
2 23  VAL n 
2 24  GLY n 
2 25  TYR n 
2 26  MET n 
2 27  LYS n 
2 28  LYS n 
2 29  GLN n 
2 30  PRO n 
2 31  ASP n 
2 32  ILE n 
2 33  THR n 
2 34  ASN n 
2 35  SER n 
2 36  MET n 
2 37  ARG n 
2 38  ALA n 
2 39  ILE n 
2 40  LEU n 
2 41  VAL n 
2 42  ASP n 
2 43  TRP n 
2 44  LEU n 
2 45  VAL n 
2 46  GLU n 
2 47  VAL n 
2 48  GLY n 
2 49  GLU n 
2 50  GLU n 
2 51  TYR n 
2 52  LYS n 
2 53  LEU n 
2 54  GLN n 
2 55  ASN n 
2 56  GLU n 
2 57  THR n 
2 58  LEU n 
2 59  HIS n 
2 60  LEU n 
2 61  ALA n 
2 62  VAL n 
2 63  ASN n 
2 64  TYR n 
2 65  ILE n 
2 66  ASP n 
2 67  ARG n 
2 68  PHE n 
2 69  LEU n 
2 70  SER n 
2 71  SER n 
2 72  MET n 
2 73  SER n 
2 74  VAL n 
2 75  LEU n 
2 76  ARG n 
2 77  GLY n 
2 78  LYS n 
2 79  LEU n 
2 80  GLN n 
2 81  LEU n 
2 82  VAL n 
2 83  GLY n 
2 84  THR n 
2 85  ALA n 
2 86  ALA n 
2 87  MET n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  SER n 
2 92  LYS n 
2 93  PHE n 
2 94  GLU n 
2 95  GLU n 
2 96  ILE n 
2 97  TYR n 
2 98  PRO n 
2 99  PRO n 
2 100 GLU n 
2 101 VAL n 
2 102 ALA n 
2 103 GLU n 
2 104 PHE n 
2 105 VAL n 
2 106 TYR n 
2 107 ILE n 
2 108 THR n 
2 109 ASP n 
2 110 ASP n 
2 111 THR n 
2 112 TYR n 
2 113 THR n 
2 114 LYS n 
2 115 LYS n 
2 116 GLN n 
2 117 VAL n 
2 118 LEU n 
2 119 ARG n 
2 120 MET n 
2 121 GLU n 
2 122 HIS n 
2 123 LEU n 
2 124 VAL n 
2 125 LEU n 
2 126 LYS n 
2 127 VAL n 
2 128 LEU n 
2 129 THR n 
2 130 PHE n 
2 131 ASP n 
2 132 LEU n 
2 133 ALA n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 VAL n 
2 138 ASN n 
2 139 GLN n 
2 140 PHE n 
2 141 LEU n 
2 142 THR n 
2 143 GLN n 
2 144 TYR n 
2 145 PHE n 
2 146 LEU n 
2 147 HIS n 
2 148 GLN n 
2 149 GLN n 
2 150 PRO n 
2 151 ALA n 
2 152 ASN n 
2 153 CYS n 
2 154 LYS n 
2 155 VAL n 
2 156 GLU n 
2 157 SER n 
2 158 LEU n 
2 159 ALA n 
2 160 MET n 
2 161 PHE n 
2 162 LEU n 
2 163 GLY n 
2 164 GLU n 
2 165 LEU n 
2 166 SER n 
2 167 LEU n 
2 168 ILE n 
2 169 ASP n 
2 170 ALA n 
2 171 ASP n 
2 172 PRO n 
2 173 TYR n 
2 174 LEU n 
2 175 LYS n 
2 176 TYR n 
2 177 LEU n 
2 178 PRO n 
2 179 SER n 
2 180 VAL n 
2 181 ILE n 
2 182 ALA n 
2 183 GLY n 
2 184 ALA n 
2 185 ALA n 
2 186 PHE n 
2 187 HIS n 
2 188 LEU n 
2 189 ALA n 
2 190 LEU n 
2 191 TYR n 
2 192 THR n 
2 193 VAL n 
2 194 THR n 
2 195 GLY n 
2 196 GLN n 
2 197 SER n 
2 198 TRP n 
2 199 PRO n 
2 200 GLU n 
2 201 SER n 
2 202 LEU n 
2 203 ILE n 
2 204 ARG n 
2 205 LYS n 
2 206 THR n 
2 207 GLY n 
2 208 TYR n 
2 209 THR n 
2 210 LEU n 
2 211 GLU n 
2 212 SER n 
2 213 LEU n 
2 214 LYS n 
2 215 PRO n 
2 216 CYS n 
2 217 LEU n 
2 218 MET n 
2 219 ASP n 
2 220 LEU n 
2 221 HIS n 
2 222 GLN n 
2 223 THR n 
2 224 TYR n 
2 225 LEU n 
2 226 LYS n 
2 227 ALA n 
2 228 PRO n 
2 229 GLN n 
2 230 HIS n 
2 231 ALA n 
2 232 GLN n 
2 233 GLN n 
2 234 SER n 
2 235 ILE n 
2 236 ARG n 
2 237 GLU n 
2 238 LYS n 
2 239 TYR n 
2 240 LYS n 
2 241 ASN n 
2 242 SER n 
2 243 LYS n 
2 244 TYR n 
2 245 HIS n 
2 246 GLY n 
2 247 VAL n 
2 248 SER n 
2 249 LEU n 
2 250 LEU n 
2 251 ASN n 
2 252 PRO n 
2 253 PRO n 
2 254 GLU n 
2 255 THR n 
2 256 LEU n 
2 257 ASN n 
2 258 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 298 human ? 'CDK2, CDKN2'       ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 258 human ? 'CCNA2, CCN1, CCNA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                  'C3 H7 N O2'        89.093  
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 
NA  non-polymer         . 'SODIUM ION' ?                  'Na 1'              22.990  
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 
SGM non-polymer         . MONOTHIOGLYCEROL ?                  'C3 H8 O2 S'        108.159 
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 
YNK non-polymer         . 
;7-dimethylphosphoryl-3-[2-[[(3~{S})-6,6-dimethylpiperidin-3-yl]amino]-5-(trifluoromethyl)pyrimidin-4-yl]-1~{H}-indole-6-carbonitrile
;
?                  'C23 H26 F3 N6 O P' 490.461 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   PHE 9   9   9   PHE PHE A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  THR 39  39  ?   ?   ?   A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  HIS 60  60  60  HIS HIS A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  MET 83  83  83  MET MET A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 GLN 113 113 113 GLN GLN A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 HIS 125 125 125 HIS HIS A . n 
A 1 126 ARG 126 126 126 ARG ARG A . n 
A 1 127 ASP 127 127 127 ASP ASP A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ARG 150 150 150 ARG ARG A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 TYR 159 159 159 TYR TYR A . n 
A 1 160 TPO 160 160 160 TPO TPO A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 ARG 169 169 169 ARG ARG A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 CYS 177 177 177 CYS CYS A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 TYR 179 179 179 TYR TYR A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 TRP 187 187 187 TRP TRP A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 CYS 191 191 191 CYS CYS A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 MET 196 196 196 MET MET A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 ARG 199 199 199 ARG ARG A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 ASP 223 223 223 ASP ASP A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 TRP 227 227 227 TRP TRP A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 VAL 230 230 230 VAL VAL A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 TRP 243 243 243 TRP TRP A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 ASP 247 247 247 ASP ASP A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 SER 249 249 249 SER SER A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 ASP 258 258 258 ASP ASP A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 GLN 265 265 265 GLN GLN A . n 
A 1 266 MET 266 266 266 MET MET A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 ASP 270 270 270 ASP ASP A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 SER 276 276 276 SER SER A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 PHE 285 285 285 PHE PHE A . n 
A 1 286 PHE 286 286 286 PHE PHE A . n 
A 1 287 GLN 287 287 287 GLN GLN A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 THR 290 290 290 THR THR A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 VAL 293 293 293 VAL VAL A . n 
A 1 294 PRO 294 294 294 PRO PRO A . n 
A 1 295 HIS 295 295 ?   ?   ?   A . n 
A 1 296 LEU 296 296 ?   ?   ?   A . n 
A 1 297 ARG 297 297 ?   ?   ?   A . n 
A 1 298 LEU 298 298 ?   ?   ?   A . n 
B 2 1   VAL 1   175 175 VAL VAL B . n 
B 2 2   PRO 2   176 176 PRO PRO B . n 
B 2 3   ASP 3   177 177 ASP ASP B . n 
B 2 4   TYR 4   178 178 TYR TYR B . n 
B 2 5   HIS 5   179 179 HIS HIS B . n 
B 2 6   GLU 6   180 180 GLU GLU B . n 
B 2 7   ASP 7   181 181 ASP ASP B . n 
B 2 8   ILE 8   182 182 ILE ILE B . n 
B 2 9   HIS 9   183 183 HIS HIS B . n 
B 2 10  THR 10  184 184 THR THR B . n 
B 2 11  TYR 11  185 185 TYR TYR B . n 
B 2 12  LEU 12  186 186 LEU LEU B . n 
B 2 13  ARG 13  187 187 ARG ARG B . n 
B 2 14  GLU 14  188 188 GLU GLU B . n 
B 2 15  MET 15  189 189 MET MET B . n 
B 2 16  GLU 16  190 190 GLU GLU B . n 
B 2 17  VAL 17  191 191 VAL VAL B . n 
B 2 18  LYS 18  192 192 LYS LYS B . n 
B 2 19  CYS 19  193 193 CYS CYS B . n 
B 2 20  LYS 20  194 194 LYS LYS B . n 
B 2 21  PRO 21  195 195 PRO PRO B . n 
B 2 22  LYS 22  196 196 LYS LYS B . n 
B 2 23  VAL 23  197 197 VAL VAL B . n 
B 2 24  GLY 24  198 198 GLY GLY B . n 
B 2 25  TYR 25  199 199 TYR TYR B . n 
B 2 26  MET 26  200 200 MET MET B . n 
B 2 27  LYS 27  201 201 LYS LYS B . n 
B 2 28  LYS 28  202 202 LYS LYS B . n 
B 2 29  GLN 29  203 203 GLN GLN B . n 
B 2 30  PRO 30  204 204 PRO PRO B . n 
B 2 31  ASP 31  205 205 ASP ASP B . n 
B 2 32  ILE 32  206 206 ILE ILE B . n 
B 2 33  THR 33  207 207 THR THR B . n 
B 2 34  ASN 34  208 208 ASN ASN B . n 
B 2 35  SER 35  209 209 SER SER B . n 
B 2 36  MET 36  210 210 MET MET B . n 
B 2 37  ARG 37  211 211 ARG ARG B . n 
B 2 38  ALA 38  212 212 ALA ALA B . n 
B 2 39  ILE 39  213 213 ILE ILE B . n 
B 2 40  LEU 40  214 214 LEU LEU B . n 
B 2 41  VAL 41  215 215 VAL VAL B . n 
B 2 42  ASP 42  216 216 ASP ASP B . n 
B 2 43  TRP 43  217 217 TRP TRP B . n 
B 2 44  LEU 44  218 218 LEU LEU B . n 
B 2 45  VAL 45  219 219 VAL VAL B . n 
B 2 46  GLU 46  220 220 GLU GLU B . n 
B 2 47  VAL 47  221 221 VAL VAL B . n 
B 2 48  GLY 48  222 222 GLY GLY B . n 
B 2 49  GLU 49  223 223 GLU GLU B . n 
B 2 50  GLU 50  224 224 GLU GLU B . n 
B 2 51  TYR 51  225 225 TYR TYR B . n 
B 2 52  LYS 52  226 226 LYS LYS B . n 
B 2 53  LEU 53  227 227 LEU LEU B . n 
B 2 54  GLN 54  228 228 GLN GLN B . n 
B 2 55  ASN 55  229 229 ASN ASN B . n 
B 2 56  GLU 56  230 230 GLU GLU B . n 
B 2 57  THR 57  231 231 THR THR B . n 
B 2 58  LEU 58  232 232 LEU LEU B . n 
B 2 59  HIS 59  233 233 HIS HIS B . n 
B 2 60  LEU 60  234 234 LEU LEU B . n 
B 2 61  ALA 61  235 235 ALA ALA B . n 
B 2 62  VAL 62  236 236 VAL VAL B . n 
B 2 63  ASN 63  237 237 ASN ASN B . n 
B 2 64  TYR 64  238 238 TYR TYR B . n 
B 2 65  ILE 65  239 239 ILE ILE B . n 
B 2 66  ASP 66  240 240 ASP ASP B . n 
B 2 67  ARG 67  241 241 ARG ARG B . n 
B 2 68  PHE 68  242 242 PHE PHE B . n 
B 2 69  LEU 69  243 243 LEU LEU B . n 
B 2 70  SER 70  244 244 SER SER B . n 
B 2 71  SER 71  245 245 SER SER B . n 
B 2 72  MET 72  246 246 MET MET B . n 
B 2 73  SER 73  247 247 SER SER B . n 
B 2 74  VAL 74  248 248 VAL VAL B . n 
B 2 75  LEU 75  249 249 LEU LEU B . n 
B 2 76  ARG 76  250 250 ARG ARG B . n 
B 2 77  GLY 77  251 251 GLY GLY B . n 
B 2 78  LYS 78  252 252 LYS LYS B . n 
B 2 79  LEU 79  253 253 LEU LEU B . n 
B 2 80  GLN 80  254 254 GLN GLN B . n 
B 2 81  LEU 81  255 255 LEU LEU B . n 
B 2 82  VAL 82  256 256 VAL VAL B . n 
B 2 83  GLY 83  257 257 GLY GLY B . n 
B 2 84  THR 84  258 258 THR THR B . n 
B 2 85  ALA 85  259 259 ALA ALA B . n 
B 2 86  ALA 86  260 260 ALA ALA B . n 
B 2 87  MET 87  261 261 MET MET B . n 
B 2 88  LEU 88  262 262 LEU LEU B . n 
B 2 89  LEU 89  263 263 LEU LEU B . n 
B 2 90  ALA 90  264 264 ALA ALA B . n 
B 2 91  SER 91  265 265 SER SER B . n 
B 2 92  LYS 92  266 266 LYS LYS B . n 
B 2 93  PHE 93  267 267 PHE PHE B . n 
B 2 94  GLU 94  268 268 GLU GLU B . n 
B 2 95  GLU 95  269 269 GLU GLU B . n 
B 2 96  ILE 96  270 270 ILE ILE B . n 
B 2 97  TYR 97  271 271 TYR TYR B . n 
B 2 98  PRO 98  272 272 PRO PRO B . n 
B 2 99  PRO 99  273 273 PRO PRO B . n 
B 2 100 GLU 100 274 274 GLU GLU B . n 
B 2 101 VAL 101 275 275 VAL VAL B . n 
B 2 102 ALA 102 276 276 ALA ALA B . n 
B 2 103 GLU 103 277 277 GLU GLU B . n 
B 2 104 PHE 104 278 278 PHE PHE B . n 
B 2 105 VAL 105 279 279 VAL VAL B . n 
B 2 106 TYR 106 280 280 TYR TYR B . n 
B 2 107 ILE 107 281 281 ILE ILE B . n 
B 2 108 THR 108 282 282 THR THR B . n 
B 2 109 ASP 109 283 283 ASP ASP B . n 
B 2 110 ASP 110 284 284 ASP ASP B . n 
B 2 111 THR 111 285 285 THR THR B . n 
B 2 112 TYR 112 286 286 TYR TYR B . n 
B 2 113 THR 113 287 287 THR THR B . n 
B 2 114 LYS 114 288 288 LYS LYS B . n 
B 2 115 LYS 115 289 289 LYS LYS B . n 
B 2 116 GLN 116 290 290 GLN GLN B . n 
B 2 117 VAL 117 291 291 VAL VAL B . n 
B 2 118 LEU 118 292 292 LEU LEU B . n 
B 2 119 ARG 119 293 293 ARG ARG B . n 
B 2 120 MET 120 294 294 MET MET B . n 
B 2 121 GLU 121 295 295 GLU GLU B . n 
B 2 122 HIS 122 296 296 HIS HIS B . n 
B 2 123 LEU 123 297 297 LEU LEU B . n 
B 2 124 VAL 124 298 298 VAL VAL B . n 
B 2 125 LEU 125 299 299 LEU LEU B . n 
B 2 126 LYS 126 300 300 LYS LYS B . n 
B 2 127 VAL 127 301 301 VAL VAL B . n 
B 2 128 LEU 128 302 302 LEU LEU B . n 
B 2 129 THR 129 303 303 THR THR B . n 
B 2 130 PHE 130 304 304 PHE PHE B . n 
B 2 131 ASP 131 305 305 ASP ASP B . n 
B 2 132 LEU 132 306 306 LEU LEU B . n 
B 2 133 ALA 133 307 307 ALA ALA B . n 
B 2 134 ALA 134 308 308 ALA ALA B . n 
B 2 135 PRO 135 309 309 PRO PRO B . n 
B 2 136 THR 136 310 310 THR THR B . n 
B 2 137 VAL 137 311 311 VAL VAL B . n 
B 2 138 ASN 138 312 312 ASN ASN B . n 
B 2 139 GLN 139 313 313 GLN GLN B . n 
B 2 140 PHE 140 314 314 PHE PHE B . n 
B 2 141 LEU 141 315 315 LEU LEU B . n 
B 2 142 THR 142 316 316 THR THR B . n 
B 2 143 GLN 143 317 317 GLN GLN B . n 
B 2 144 TYR 144 318 318 TYR TYR B . n 
B 2 145 PHE 145 319 319 PHE PHE B . n 
B 2 146 LEU 146 320 320 LEU LEU B . n 
B 2 147 HIS 147 321 321 HIS HIS B . n 
B 2 148 GLN 148 322 322 GLN GLN B . n 
B 2 149 GLN 149 323 323 GLN GLN B . n 
B 2 150 PRO 150 324 324 PRO PRO B . n 
B 2 151 ALA 151 325 325 ALA ALA B . n 
B 2 152 ASN 152 326 326 ASN ASN B . n 
B 2 153 CYS 153 327 327 CYS CYS B . n 
B 2 154 LYS 154 328 328 LYS LYS B . n 
B 2 155 VAL 155 329 329 VAL VAL B . n 
B 2 156 GLU 156 330 330 GLU GLU B . n 
B 2 157 SER 157 331 331 SER SER B . n 
B 2 158 LEU 158 332 332 LEU LEU B . n 
B 2 159 ALA 159 333 333 ALA ALA B . n 
B 2 160 MET 160 334 334 MET MET B . n 
B 2 161 PHE 161 335 335 PHE PHE B . n 
B 2 162 LEU 162 336 336 LEU LEU B . n 
B 2 163 GLY 163 337 337 GLY GLY B . n 
B 2 164 GLU 164 338 338 GLU GLU B . n 
B 2 165 LEU 165 339 339 LEU LEU B . n 
B 2 166 SER 166 340 340 SER SER B . n 
B 2 167 LEU 167 341 341 LEU LEU B . n 
B 2 168 ILE 168 342 342 ILE ILE B . n 
B 2 169 ASP 169 343 343 ASP ASP B . n 
B 2 170 ALA 170 344 344 ALA ALA B . n 
B 2 171 ASP 171 345 345 ASP ASP B . n 
B 2 172 PRO 172 346 346 PRO PRO B . n 
B 2 173 TYR 173 347 347 TYR TYR B . n 
B 2 174 LEU 174 348 348 LEU LEU B . n 
B 2 175 LYS 175 349 349 LYS LYS B . n 
B 2 176 TYR 176 350 350 TYR TYR B . n 
B 2 177 LEU 177 351 351 LEU LEU B . n 
B 2 178 PRO 178 352 352 PRO PRO B . n 
B 2 179 SER 179 353 353 SER SER B . n 
B 2 180 VAL 180 354 354 VAL VAL B . n 
B 2 181 ILE 181 355 355 ILE ILE B . n 
B 2 182 ALA 182 356 356 ALA ALA B . n 
B 2 183 GLY 183 357 357 GLY GLY B . n 
B 2 184 ALA 184 358 358 ALA ALA B . n 
B 2 185 ALA 185 359 359 ALA ALA B . n 
B 2 186 PHE 186 360 360 PHE PHE B . n 
B 2 187 HIS 187 361 361 HIS HIS B . n 
B 2 188 LEU 188 362 362 LEU LEU B . n 
B 2 189 ALA 189 363 363 ALA ALA B . n 
B 2 190 LEU 190 364 364 LEU LEU B . n 
B 2 191 TYR 191 365 365 TYR TYR B . n 
B 2 192 THR 192 366 366 THR THR B . n 
B 2 193 VAL 193 367 367 VAL VAL B . n 
B 2 194 THR 194 368 368 THR THR B . n 
B 2 195 GLY 195 369 369 GLY GLY B . n 
B 2 196 GLN 196 370 370 GLN GLN B . n 
B 2 197 SER 197 371 371 SER SER B . n 
B 2 198 TRP 198 372 372 TRP TRP B . n 
B 2 199 PRO 199 373 373 PRO PRO B . n 
B 2 200 GLU 200 374 374 GLU GLU B . n 
B 2 201 SER 201 375 375 SER SER B . n 
B 2 202 LEU 202 376 376 LEU LEU B . n 
B 2 203 ILE 203 377 377 ILE ILE B . n 
B 2 204 ARG 204 378 378 ARG ARG B . n 
B 2 205 LYS 205 379 379 LYS LYS B . n 
B 2 206 THR 206 380 380 THR THR B . n 
B 2 207 GLY 207 381 381 GLY GLY B . n 
B 2 208 TYR 208 382 382 TYR TYR B . n 
B 2 209 THR 209 383 383 THR THR B . n 
B 2 210 LEU 210 384 384 LEU LEU B . n 
B 2 211 GLU 211 385 385 GLU GLU B . n 
B 2 212 SER 212 386 386 SER SER B . n 
B 2 213 LEU 213 387 387 LEU LEU B . n 
B 2 214 LYS 214 388 388 LYS LYS B . n 
B 2 215 PRO 215 389 389 PRO PRO B . n 
B 2 216 CYS 216 390 390 CYS CYS B . n 
B 2 217 LEU 217 391 391 LEU LEU B . n 
B 2 218 MET 218 392 392 MET MET B . n 
B 2 219 ASP 219 393 393 ASP ASP B . n 
B 2 220 LEU 220 394 394 LEU LEU B . n 
B 2 221 HIS 221 395 395 HIS HIS B . n 
B 2 222 GLN 222 396 396 GLN GLN B . n 
B 2 223 THR 223 397 397 THR THR B . n 
B 2 224 TYR 224 398 398 TYR TYR B . n 
B 2 225 LEU 225 399 399 LEU LEU B . n 
B 2 226 LYS 226 400 400 LYS LYS B . n 
B 2 227 ALA 227 401 401 ALA ALA B . n 
B 2 228 PRO 228 402 402 PRO PRO B . n 
B 2 229 GLN 229 403 403 GLN GLN B . n 
B 2 230 HIS 230 404 404 HIS HIS B . n 
B 2 231 ALA 231 405 405 ALA ALA B . n 
B 2 232 GLN 232 406 406 GLN GLN B . n 
B 2 233 GLN 233 407 407 GLN GLN B . n 
B 2 234 SER 234 408 408 SER SER B . n 
B 2 235 ILE 235 409 409 ILE ILE B . n 
B 2 236 ARG 236 410 410 ARG ARG B . n 
B 2 237 GLU 237 411 411 GLU GLU B . n 
B 2 238 LYS 238 412 412 LYS LYS B . n 
B 2 239 TYR 239 413 413 TYR TYR B . n 
B 2 240 LYS 240 414 414 LYS LYS B . n 
B 2 241 ASN 241 415 415 ASN ASN B . n 
B 2 242 SER 242 416 416 SER SER B . n 
B 2 243 LYS 243 417 417 LYS LYS B . n 
B 2 244 TYR 244 418 418 TYR TYR B . n 
B 2 245 HIS 245 419 419 HIS HIS B . n 
B 2 246 GLY 246 420 420 GLY GLY B . n 
B 2 247 VAL 247 421 421 VAL VAL B . n 
B 2 248 SER 248 422 422 SER SER B . n 
B 2 249 LEU 249 423 423 LEU LEU B . n 
B 2 250 LEU 250 424 424 LEU LEU B . n 
B 2 251 ASN 251 425 425 ASN ASN B . n 
B 2 252 PRO 252 426 426 PRO PRO B . n 
B 2 253 PRO 253 427 427 PRO PRO B . n 
B 2 254 GLU 254 428 428 GLU GLU B . n 
B 2 255 THR 255 429 429 THR THR B . n 
B 2 256 LEU 256 430 430 LEU LEU B . n 
B 2 257 ASN 257 431 431 ASN ASN B . n 
B 2 258 LEU 258 432 432 LEU LEU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        YNK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   YNK 
_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 YNK 1  301 301 YNK LIG A . 
D 4 SGM 1  501 501 SGM SGM B . 
E 5 NA  1  502 1   NA  NA  B . 
F 5 NA  1  503 2   NA  NA  B . 
G 6 HOH 1  401 53  HOH HOH A . 
G 6 HOH 2  402 44  HOH HOH A . 
G 6 HOH 3  403 19  HOH HOH A . 
G 6 HOH 4  404 2   HOH HOH A . 
G 6 HOH 5  405 36  HOH HOH A . 
G 6 HOH 6  406 12  HOH HOH A . 
G 6 HOH 7  407 69  HOH HOH A . 
G 6 HOH 8  408 11  HOH HOH A . 
G 6 HOH 9  409 48  HOH HOH A . 
G 6 HOH 10 410 13  HOH HOH A . 
G 6 HOH 11 411 7   HOH HOH A . 
G 6 HOH 12 412 70  HOH HOH A . 
G 6 HOH 13 413 6   HOH HOH A . 
G 6 HOH 14 414 27  HOH HOH A . 
G 6 HOH 15 415 114 HOH HOH A . 
G 6 HOH 16 416 51  HOH HOH A . 
G 6 HOH 17 417 79  HOH HOH A . 
G 6 HOH 18 418 16  HOH HOH A . 
G 6 HOH 19 419 21  HOH HOH A . 
G 6 HOH 20 420 18  HOH HOH A . 
G 6 HOH 21 421 29  HOH HOH A . 
G 6 HOH 22 422 49  HOH HOH A . 
G 6 HOH 23 423 57  HOH HOH A . 
G 6 HOH 24 424 10  HOH HOH A . 
G 6 HOH 25 425 30  HOH HOH A . 
G 6 HOH 26 426 4   HOH HOH A . 
G 6 HOH 27 427 15  HOH HOH A . 
G 6 HOH 28 428 3   HOH HOH A . 
G 6 HOH 29 429 28  HOH HOH A . 
G 6 HOH 30 430 5   HOH HOH A . 
G 6 HOH 31 431 60  HOH HOH A . 
G 6 HOH 32 432 112 HOH HOH A . 
G 6 HOH 33 433 58  HOH HOH A . 
G 6 HOH 34 434 42  HOH HOH A . 
G 6 HOH 35 435 62  HOH HOH A . 
G 6 HOH 36 436 56  HOH HOH A . 
G 6 HOH 37 437 67  HOH HOH A . 
G 6 HOH 38 438 45  HOH HOH A . 
G 6 HOH 39 439 63  HOH HOH A . 
G 6 HOH 40 440 31  HOH HOH A . 
G 6 HOH 41 441 59  HOH HOH A . 
G 6 HOH 42 442 122 HOH HOH A . 
G 6 HOH 43 443 14  HOH HOH A . 
G 6 HOH 44 444 71  HOH HOH A . 
G 6 HOH 45 445 43  HOH HOH A . 
G 6 HOH 46 446 23  HOH HOH A . 
G 6 HOH 47 447 54  HOH HOH A . 
G 6 HOH 48 448 38  HOH HOH A . 
G 6 HOH 49 449 52  HOH HOH A . 
G 6 HOH 50 450 50  HOH HOH A . 
G 6 HOH 51 451 47  HOH HOH A . 
G 6 HOH 52 452 115 HOH HOH A . 
H 6 HOH 1  601 24  HOH HOH B . 
H 6 HOH 2  602 103 HOH HOH B . 
H 6 HOH 3  603 91  HOH HOH B . 
H 6 HOH 4  604 39  HOH HOH B . 
H 6 HOH 5  605 17  HOH HOH B . 
H 6 HOH 6  606 80  HOH HOH B . 
H 6 HOH 7  607 123 HOH HOH B . 
H 6 HOH 8  608 78  HOH HOH B . 
H 6 HOH 9  609 89  HOH HOH B . 
H 6 HOH 10 610 94  HOH HOH B . 
H 6 HOH 11 611 72  HOH HOH B . 
H 6 HOH 12 612 83  HOH HOH B . 
H 6 HOH 13 613 75  HOH HOH B . 
H 6 HOH 14 614 116 HOH HOH B . 
H 6 HOH 15 615 8   HOH HOH B . 
H 6 HOH 16 616 41  HOH HOH B . 
H 6 HOH 17 617 25  HOH HOH B . 
H 6 HOH 18 618 77  HOH HOH B . 
H 6 HOH 19 619 110 HOH HOH B . 
H 6 HOH 20 620 95  HOH HOH B . 
H 6 HOH 21 621 33  HOH HOH B . 
H 6 HOH 22 622 64  HOH HOH B . 
H 6 HOH 23 623 34  HOH HOH B . 
H 6 HOH 24 624 73  HOH HOH B . 
H 6 HOH 25 625 1   HOH HOH B . 
H 6 HOH 26 626 120 HOH HOH B . 
H 6 HOH 27 627 98  HOH HOH B . 
H 6 HOH 28 628 65  HOH HOH B . 
H 6 HOH 29 629 101 HOH HOH B . 
H 6 HOH 30 630 32  HOH HOH B . 
H 6 HOH 31 631 82  HOH HOH B . 
H 6 HOH 32 632 93  HOH HOH B . 
H 6 HOH 33 633 113 HOH HOH B . 
H 6 HOH 34 634 92  HOH HOH B . 
H 6 HOH 35 635 99  HOH HOH B . 
H 6 HOH 36 636 97  HOH HOH B . 
H 6 HOH 37 637 96  HOH HOH B . 
H 6 HOH 38 638 90  HOH HOH B . 
H 6 HOH 39 639 84  HOH HOH B . 
H 6 HOH 40 640 85  HOH HOH B . 
H 6 HOH 41 641 55  HOH HOH B . 
H 6 HOH 42 642 37  HOH HOH B . 
H 6 HOH 43 643 119 HOH HOH B . 
H 6 HOH 44 644 117 HOH HOH B . 
H 6 HOH 45 645 100 HOH HOH B . 
H 6 HOH 46 646 61  HOH HOH B . 
H 6 HOH 47 647 109 HOH HOH B . 
H 6 HOH 48 648 87  HOH HOH B . 
H 6 HOH 49 649 102 HOH HOH B . 
H 6 HOH 50 650 86  HOH HOH B . 
H 6 HOH 51 651 74  HOH HOH B . 
H 6 HOH 52 652 118 HOH HOH B . 
H 6 HOH 53 653 81  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GLA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.937 
_cell.length_a_esd                 ? 
_cell.length_b                     109.786 
_cell.length_b_esd                 ? 
_cell.length_c                     163.554 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GLA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GLA 
_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             2.54 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.51 
_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              7.0 
_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    '0.8 M succinic acid pH 7.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-08 
_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   0.98011 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98011 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GLA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.18 
_reflns.d_resolution_low                               48.47 
_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                                     33815 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.47 
_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                                0.335 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.322 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_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 
2.18 2.31  ? ? ? ? ? ? 5245 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1 1 0.358 ? ? 97.1 ? ? ? ? ? ? ? ? ? ? ? 
2.31 2.47  ? ? ? ? ? ? 5087 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 0.624 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
2.47 2.67  ? ? ? ? ? ? 4573 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 3 1 0.801 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
2.67 2.93  ? ? ? ? ? ? 4383 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 4 1 0.909 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
2.93 3.27  ? ? ? ? ? ? 4018 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 5 1 0.974 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
3.27 3.77  ? ? ? ? ? ? 3525 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 6 1 0.992 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
3.77 4.61  ? ? ? ? ? ? 3022 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 7 1 0.996 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
4.61 6.50  ? ? ? ? ? ? 2384 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 8 1 0.997 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
6.50 48.47 ? ? ? ? ? ? 1398 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 9 1 0.998 ? ? ?    ? ? ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -3.40 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            5.49 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -2.09 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               53.112 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9GLA 
_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                            2.18 
_refine.ls_d_res_low                             48.46 
_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                     32030 
_refine.ls_number_reflns_R_free                  1685 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.05 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20348 
_refine.ls_R_factor_R_free                       0.24906 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20109 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.265 
_refine.pdbx_overall_ESU_R_Free                  0.212 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.18 
_refine_hist.d_res_low                        48.46 
_refine_hist.number_atoms_solvent             105 
_refine_hist.number_atoms_total               4577 
_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        4430 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.012  4687  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4486  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.349  1.664  6388  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.822  1.578  10363 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.350  5.000  571   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 3.034  5.000  23    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.143 10.000 814   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.061  0.200  714   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  5351  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1040  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.747  5.112  2254  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.744  5.112  2254  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.726  9.213  2832  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.726  9.215  2833  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.576  5.691  2433  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.575  5.694  2434  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.385  10.226 3556  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.618  48.34  5251  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.623  48.35  5243  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.183 
_refine_ls_shell.d_res_low                        2.239 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             110 
_refine_ls_shell.number_reflns_R_work             2112 
_refine_ls_shell.percent_reflns_obs               90.07 
_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                  0.579 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.572 
# 
_struct.entry_id                     9GLA 
_struct.title                        'Crystal structure of a CDK2-based CDK7 mimic with inhibitor SY5609' 
_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        9GLA 
_struct_keywords.text            
'cyclin-dependent kinase, inhibitor, SY5609, selectivity, structure-assisted inhibitor design, 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 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CDK2_HUMAN  P24941 ? 1 
;MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
;
1   
2 UNP CCNA2_HUMAN P20248 ? 2 
;VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
;
175 
# 
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 9GLA A 1 ? 298 ? P24941 1   ? 298 ? 1   298 
2 2 9GLA B 1 ? 258 ? P20248 175 ? 432 ? 175 432 
# 
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 9GLA ASP A 8   ? UNP P24941 GLU 8   'engineered mutation' 8   1  
1 9GLA PHE A 9   ? UNP P24941 LYS 9   'engineered mutation' 9   2  
1 9GLA LEU A 10  ? UNP P24941 ILE 10  'engineered mutation' 10  3  
1 9GLA GLN A 14  ? UNP P24941 THR 14  'engineered mutation' 14  4  
1 9GLA PHE A 15  ? UNP P24941 TYR 15  'engineered mutation' 15  5  
1 9GLA ILE A 64  ? UNP P24941 VAL 64  'engineered mutation' 64  6  
1 9GLA MET A 83  ? UNP P24941 LEU 83  'engineered mutation' 83  7  
1 9GLA GLU A 84  ? UNP P24941 HIS 84  'engineered mutation' 84  8  
1 9GLA THR A 85  ? UNP P24941 GLN 85  'engineered mutation' 85  9  
1 9GLA GLU A 88  ? UNP P24941 LYS 88  'engineered mutation' 88  10 
1 9GLA VAL A 89  ? UNP P24941 LYS 89  'engineered mutation' 89  11 
1 9GLA ASN A 131 ? UNP P24941 GLN 131 'engineered mutation' 131 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 3670  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  23580 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 45  ? LYS A 56  ? PRO A 45  LYS A 56  1 ? 12 
HELX_P HELX_P2  AA2 LEU A 87  ? ALA A 93  ? LEU A 87  ALA A 93  1 ? 7  
HELX_P HELX_P3  AA3 PRO A 100 ? HIS A 121 ? PRO A 100 HIS A 121 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 129 ? ASN A 131 ? LYS A 129 ASN A 131 5 ? 3  
HELX_P HELX_P5  AA5 THR A 165 ? ARG A 169 ? THR A 165 ARG A 169 5 ? 5  
HELX_P HELX_P6  AA6 ALA A 170 ? LEU A 175 ? ALA A 170 LEU A 175 1 ? 6  
HELX_P HELX_P7  AA7 THR A 182 ? ARG A 199 ? THR A 182 ARG A 199 1 ? 18 
HELX_P HELX_P8  AA8 SER A 207 ? GLY A 220 ? SER A 207 GLY A 220 1 ? 14 
HELX_P HELX_P9  AA9 GLY A 229 ? MET A 233 ? GLY A 229 MET A 233 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 247 ? VAL A 252 ? ASP A 247 VAL A 252 1 ? 6  
HELX_P HELX_P11 AB2 ASP A 256 ? LEU A 267 ? ASP A 256 LEU A 267 1 ? 12 
HELX_P HELX_P12 AB3 SER A 276 ? ALA A 282 ? SER A 276 ALA A 282 1 ? 7  
HELX_P HELX_P13 AB4 HIS A 283 ? GLN A 287 ? HIS A 283 GLN A 287 5 ? 5  
HELX_P HELX_P14 AB5 TYR B 4   ? CYS B 19  ? TYR B 178 CYS B 193 1 ? 16 
HELX_P HELX_P15 AB6 GLY B 24  ? GLN B 29  ? GLY B 198 GLN B 203 5 ? 6  
HELX_P HELX_P16 AB7 THR B 33  ? TYR B 51  ? THR B 207 TYR B 225 1 ? 19 
HELX_P HELX_P17 AB8 GLN B 54  ? SER B 70  ? GLN B 228 SER B 244 1 ? 17 
HELX_P HELX_P18 AB9 LEU B 75  ? GLY B 77  ? LEU B 249 GLY B 251 5 ? 3  
HELX_P HELX_P19 AC1 LYS B 78  ? GLU B 95  ? LYS B 252 GLU B 269 1 ? 18 
HELX_P HELX_P20 AC2 GLU B 100 ? THR B 108 ? GLU B 274 THR B 282 1 ? 9  
HELX_P HELX_P21 AC3 THR B 113 ? LEU B 128 ? THR B 287 LEU B 302 1 ? 16 
HELX_P HELX_P22 AC4 THR B 136 ? LEU B 146 ? THR B 310 LEU B 320 1 ? 11 
HELX_P HELX_P23 AC5 ASN B 152 ? LEU B 167 ? ASN B 326 LEU B 341 1 ? 16 
HELX_P HELX_P24 AC6 ASP B 169 ? LEU B 174 ? ASP B 343 LEU B 348 1 ? 6  
HELX_P HELX_P25 AC7 LEU B 177 ? GLY B 195 ? LEU B 351 GLY B 369 1 ? 19 
HELX_P HELX_P26 AC8 PRO B 199 ? GLY B 207 ? PRO B 373 GLY B 381 1 ? 9  
HELX_P HELX_P27 AC9 LEU B 210 ? SER B 212 ? LEU B 384 SER B 386 5 ? 3  
HELX_P HELX_P28 AD1 LEU B 213 ? LYS B 226 ? LEU B 387 LYS B 400 1 ? 14 
HELX_P HELX_P29 AD2 ALA B 227 ? HIS B 230 ? ALA B 401 HIS B 404 5 ? 4  
HELX_P HELX_P30 AD3 GLN B 233 ? TYR B 239 ? GLN B 407 TYR B 413 1 ? 7  
HELX_P HELX_P31 AD4 LYS B 240 ? HIS B 245 ? LYS B 414 HIS B 419 5 ? 6  
HELX_P HELX_P32 AD5 GLY B 246 ? LEU B 250 ? GLY B 420 LEU B 424 5 ? 5  
# 
_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 
disulf1 disulf ?    ? B CYS 153 SG  B ? ? 1_555 B CYS 153 SG B ? B CYS 327 B CYS 327 4_555 ? ? ? ? ? ? ? 2.106 ? ? 
covale1 covale both ? A TYR 159 C   ? ? ? 1_555 A TPO 160 N  ? ? A TYR 159 A TPO 160 1_555 ? ? ? ? ? ? ? 1.344 ? ? 
covale2 covale both ? A TPO 160 C   ? ? ? 1_555 A HIS 161 N  ? ? A TPO 160 A HIS 161 1_555 ? ? ? ? ? ? ? 1.343 ? ? 
covale3 covale none ? B CYS 19  SG  ? ? ? 1_555 D SGM .   S1 ? ? B CYS 193 B SGM 501 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc1 metalc ?    ? B MET 26  O   ? ? ? 1_555 F NA  .   NA ? ? B MET 200 B NA  503 1_555 ? ? ? ? ? ? ? 2.624 ? ? 
metalc2 metalc ?    ? B GLN 29  O   ? ? ? 1_555 F NA  .   NA ? ? B GLN 203 B NA  503 1_555 ? ? ? ? ? ? ? 2.783 ? ? 
metalc3 metalc ?    ? B ILE 32  O   ? ? ? 1_555 F NA  .   NA ? ? B ILE 206 B NA  503 1_555 ? ? ? ? ? ? ? 2.514 ? ? 
metalc4 metalc ?    ? B GLN 143 OE1 ? ? ? 1_555 E NA  .   NA ? ? B GLN 317 B NA  502 1_555 ? ? ? ? ? ? ? 3.051 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 O ? B MET 26 ? B MET 200 ? 1_555 NA ? F NA . ? B NA 503 ? 1_555 O ? B GLN 29 ? B GLN 203 ? 1_555 83.5  ? 
2 O ? B MET 26 ? B MET 200 ? 1_555 NA ? F NA . ? B NA 503 ? 1_555 O ? B ILE 32 ? B ILE 206 ? 1_555 104.9 ? 
3 O ? B GLN 29 ? B GLN 203 ? 1_555 NA ? F NA . ? B NA 503 ? 1_555 O ? B ILE 32 ? B ILE 206 ? 1_555 87.9  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_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 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_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 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 TPO A 160 ? .   . .   . TPO A 160 ? 1_555 .   . .   . .     .  .  THR 1 TPO Phosphorylation 'Named protein modification'     
2 SGM D .   ? CYS B 19  ? SGM B 501 ? 1_555 CYS B 193 ? 1_555 S1 SG CYS 1 SGM None            'Covalent chemical modification' 
3 CYS B 153 B CYS B 153 B CYS B 327 ? 1_555 CYS B 327 ? 4_555 SG SG .   . .   None            'Disulfide bridge'               
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 VAL 154 A . ? VAL 154 A PRO 155 A ? PRO 155 A 1 -4.15 
2 ASP 171 B . ? ASP 345 B PRO 172 B ? PRO 346 B 1 4.78  
# 
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 4   ? GLU A 12  ? PHE A 4   GLU A 12  
AA1 2 GLY A 16  ? ASN A 23  ? GLY A 16  ASN A 23  
AA1 3 VAL A 29  ? ILE A 35  ? VAL A 29  ILE A 35  
AA1 4 LYS A 75  ? GLU A 81  ? LYS A 75  GLU A 81  
AA1 5 LEU A 66  ? THR A 72  ? LEU A 66  THR A 72  
AA2 1 THR A 85  ? ASP A 86  ? THR A 85  ASP A 86  
AA2 2 LEU A 133 ? ILE A 135 ? LEU A 133 ILE A 135 
AA2 3 ILE A 141 ? LEU A 143 ? ILE A 141 LEU A 143 
AA3 1 VAL A 123 ? LEU A 124 ? VAL A 123 LEU A 124 
AA3 2 ARG A 150 ? ALA A 151 ? 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 ASP A 8   ? N ASP A 8   O LYS A 20  ? O LYS A 20  
AA1 2 3 N VAL A 17  ? N VAL A 17  O LYS A 34  ? O LYS A 34  
AA1 3 4 N ILE A 35  ? N ILE A 35  O LEU A 76  ? O LEU A 76  
AA1 4 5 O VAL A 79  ? O VAL A 79  N LEU A 67  ? N LEU A 67  
AA2 1 2 N THR A 85  ? N THR A 85  O ILE A 135 ? O ILE A 135 
AA2 2 3 N LEU A 134 ? N LEU A 134 O LYS A 142 ? O LYS A 142 
AA3 1 2 N LEU A 124 ? N LEU A 124 O ARG A 150 ? O ARG A 150 
# 
_pdbx_entry_details.entry_id                   9GLA 
_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 THR A 72  ? ? -117.52 -165.97 
2  1 THR A 72  ? ? -115.78 -165.97 
3  1 ASN A 74  ? ? 39.82   48.73   
4  1 LYS A 75  ? ? -174.09 122.04  
5  1 ASP A 127 ? ? -146.19 37.29   
6  1 ASP A 145 ? ? 58.88   75.50   
7  1 GLU A 162 ? ? -69.34  77.54   
8  1 VAL A 164 ? ? 71.55   133.57  
9  1 SER A 181 ? ? -146.57 -146.08 
10 1 TRP B 372 ? ? -5.96   101.58  
11 1 ASN B 415 ? A -47.42  156.95  
# 
_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     160 
_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_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A THR 39  ? A THR 39  
3 1 Y 1 A HIS 295 ? A HIS 295 
4 1 Y 1 A LEU 296 ? A LEU 296 
5 1 Y 1 A ARG 297 ? A ARG 297 
6 1 Y 1 A LEU 298 ? A LEU 298 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
NA  NA   NA N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
SGM C1   C  N N 305 
SGM C2   C  N R 306 
SGM O2   O  N N 307 
SGM C3   C  N N 308 
SGM O3   O  N N 309 
SGM S1   S  N N 310 
SGM H11  H  N N 311 
SGM H12  H  N N 312 
SGM H2   H  N N 313 
SGM HO2  H  N N 314 
SGM H31  H  N N 315 
SGM H32  H  N N 316 
SGM HO3  H  N N 317 
SGM HS1  H  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TPO N    N  N N 336 
TPO CA   C  N S 337 
TPO CB   C  N R 338 
TPO CG2  C  N N 339 
TPO OG1  O  N N 340 
TPO P    P  N N 341 
TPO O1P  O  N N 342 
TPO O2P  O  N N 343 
TPO O3P  O  N N 344 
TPO C    C  N N 345 
TPO O    O  N N 346 
TPO OXT  O  N N 347 
TPO H    H  N N 348 
TPO H2   H  N N 349 
TPO HA   H  N N 350 
TPO HB   H  N N 351 
TPO HG21 H  N N 352 
TPO HG22 H  N N 353 
TPO HG23 H  N N 354 
TPO HOP2 H  N N 355 
TPO HOP3 H  N N 356 
TPO HXT  H  N N 357 
TRP N    N  N N 358 
TRP CA   C  N S 359 
TRP C    C  N N 360 
TRP O    O  N N 361 
TRP CB   C  N N 362 
TRP CG   C  Y N 363 
TRP CD1  C  Y N 364 
TRP CD2  C  Y N 365 
TRP NE1  N  Y N 366 
TRP CE2  C  Y N 367 
TRP CE3  C  Y N 368 
TRP CZ2  C  Y N 369 
TRP CZ3  C  Y N 370 
TRP CH2  C  Y N 371 
TRP OXT  O  N N 372 
TRP H    H  N N 373 
TRP H2   H  N N 374 
TRP HA   H  N N 375 
TRP HB2  H  N N 376 
TRP HB3  H  N N 377 
TRP HD1  H  N N 378 
TRP HE1  H  N N 379 
TRP HE3  H  N N 380 
TRP HZ2  H  N N 381 
TRP HZ3  H  N N 382 
TRP HH2  H  N N 383 
TRP HXT  H  N N 384 
TYR N    N  N N 385 
TYR CA   C  N S 386 
TYR C    C  N N 387 
TYR O    O  N N 388 
TYR CB   C  N N 389 
TYR CG   C  Y N 390 
TYR CD1  C  Y N 391 
TYR CD2  C  Y N 392 
TYR CE1  C  Y N 393 
TYR CE2  C  Y N 394 
TYR CZ   C  Y N 395 
TYR OH   O  N N 396 
TYR OXT  O  N N 397 
TYR H    H  N N 398 
TYR H2   H  N N 399 
TYR HA   H  N N 400 
TYR HB2  H  N N 401 
TYR HB3  H  N N 402 
TYR HD1  H  N N 403 
TYR HD2  H  N N 404 
TYR HE1  H  N N 405 
TYR HE2  H  N N 406 
TYR HH   H  N N 407 
TYR HXT  H  N N 408 
VAL N    N  N N 409 
VAL CA   C  N S 410 
VAL C    C  N N 411 
VAL O    O  N N 412 
VAL CB   C  N N 413 
VAL CG1  C  N N 414 
VAL CG2  C  N N 415 
VAL OXT  O  N N 416 
VAL H    H  N N 417 
VAL H2   H  N N 418 
VAL HA   H  N N 419 
VAL HB   H  N N 420 
VAL HG11 H  N N 421 
VAL HG12 H  N N 422 
VAL HG13 H  N N 423 
VAL HG21 H  N N 424 
VAL HG22 H  N N 425 
VAL HG23 H  N N 426 
VAL HXT  H  N N 427 
YNK C1   C  N N 428 
YNK C2   C  N N 429 
YNK C3   C  N N 430 
YNK C5   C  N N 431 
YNK C6   C  N S 432 
YNK C7   C  N N 433 
YNK C10  C  Y N 434 
YNK C12  C  Y N 435 
YNK C13  C  Y N 436 
YNK C14  C  Y N 437 
YNK C16  C  Y N 438 
YNK N18  N  Y N 439 
YNK C19  C  Y N 440 
YNK C21  C  Y N 441 
YNK C22  C  N N 442 
YNK C24  C  Y N 443 
YNK C25  C  Y N 444 
YNK C26  C  Y N 445 
YNK C31  C  N N 446 
YNK C4   C  N N 447 
YNK N8   N  N N 448 
YNK N9   N  N N 449 
YNK N11  N  Y N 450 
YNK N15  N  Y N 451 
YNK C17  C  Y N 452 
YNK C20  C  Y N 453 
YNK N23  N  N N 454 
YNK P27  P  N N 455 
YNK O28  O  N N 456 
YNK C29  C  N N 457 
YNK C30  C  N N 458 
YNK F32  F  N N 459 
YNK F33  F  N N 460 
YNK F34  F  N N 461 
YNK H41  H  N N 462 
YNK H40  H  N N 463 
YNK H39  H  N N 464 
YNK H43  H  N N 465 
YNK H42  H  N N 466 
YNK H44  H  N N 467 
YNK H47  H  N N 468 
YNK H48  H  N N 469 
YNK H35  H  N N 470 
YNK H49  H  N N 471 
YNK H50  H  N N 472 
YNK H52  H  N N 473 
YNK H38  H  N N 474 
YNK H54  H  N N 475 
YNK H55  H  N N 476 
YNK H45  H  N N 477 
YNK H46  H  N N 478 
YNK H37  H  N N 479 
YNK H51  H  N N 480 
YNK H53  H  N N 481 
YNK H57  H  N N 482 
YNK H56  H  N N 483 
YNK H58  H  N N 484 
YNK H60  H  N N 485 
YNK H59  H  N N 486 
YNK H61  H  N N 487 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SGM C1  C2   sing N N 290 
SGM C1  S1   sing N N 291 
SGM C1  H11  sing N N 292 
SGM C1  H12  sing N N 293 
SGM C2  O2   sing N N 294 
SGM C2  C3   sing N N 295 
SGM C2  H2   sing N N 296 
SGM O2  HO2  sing N N 297 
SGM C3  O3   sing N N 298 
SGM C3  H31  sing N N 299 
SGM C3  H32  sing N N 300 
SGM O3  HO3  sing N N 301 
SGM S1  HS1  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TPO N   CA   sing N N 319 
TPO N   H    sing N N 320 
TPO N   H2   sing N N 321 
TPO CA  CB   sing N N 322 
TPO CA  C    sing N N 323 
TPO CA  HA   sing N N 324 
TPO CB  CG2  sing N N 325 
TPO CB  OG1  sing N N 326 
TPO CB  HB   sing N N 327 
TPO CG2 HG21 sing N N 328 
TPO CG2 HG22 sing N N 329 
TPO CG2 HG23 sing N N 330 
TPO OG1 P    sing N N 331 
TPO P   O1P  doub N N 332 
TPO P   O2P  sing N N 333 
TPO P   O3P  sing N N 334 
TPO O2P HOP2 sing N N 335 
TPO O3P HOP3 sing N N 336 
TPO C   O    doub N N 337 
TPO C   OXT  sing N N 338 
TPO OXT HXT  sing N N 339 
TRP N   CA   sing N N 340 
TRP N   H    sing N N 341 
TRP N   H2   sing N N 342 
TRP CA  C    sing N N 343 
TRP CA  CB   sing N N 344 
TRP CA  HA   sing N N 345 
TRP C   O    doub N N 346 
TRP C   OXT  sing N N 347 
TRP CB  CG   sing N N 348 
TRP CB  HB2  sing N N 349 
TRP CB  HB3  sing N N 350 
TRP CG  CD1  doub Y N 351 
TRP CG  CD2  sing Y N 352 
TRP CD1 NE1  sing Y N 353 
TRP CD1 HD1  sing N N 354 
TRP CD2 CE2  doub Y N 355 
TRP CD2 CE3  sing Y N 356 
TRP NE1 CE2  sing Y N 357 
TRP NE1 HE1  sing N N 358 
TRP CE2 CZ2  sing Y N 359 
TRP CE3 CZ3  doub Y N 360 
TRP CE3 HE3  sing N N 361 
TRP CZ2 CH2  doub Y N 362 
TRP CZ2 HZ2  sing N N 363 
TRP CZ3 CH2  sing Y N 364 
TRP CZ3 HZ3  sing N N 365 
TRP CH2 HH2  sing N N 366 
TRP OXT HXT  sing N N 367 
TYR N   CA   sing N N 368 
TYR N   H    sing N N 369 
TYR N   H2   sing N N 370 
TYR CA  C    sing N N 371 
TYR CA  CB   sing N N 372 
TYR CA  HA   sing N N 373 
TYR C   O    doub N N 374 
TYR C   OXT  sing N N 375 
TYR CB  CG   sing N N 376 
TYR CB  HB2  sing N N 377 
TYR CB  HB3  sing N N 378 
TYR CG  CD1  doub Y N 379 
TYR CG  CD2  sing Y N 380 
TYR CD1 CE1  sing Y N 381 
TYR CD1 HD1  sing N N 382 
TYR CD2 CE2  doub Y N 383 
TYR CD2 HD2  sing N N 384 
TYR CE1 CZ   doub Y N 385 
TYR CE1 HE1  sing N N 386 
TYR CE2 CZ   sing Y N 387 
TYR CE2 HE2  sing N N 388 
TYR CZ  OH   sing N N 389 
TYR OH  HH   sing N N 390 
TYR OXT HXT  sing N N 391 
VAL N   CA   sing N N 392 
VAL N   H    sing N N 393 
VAL N   H2   sing N N 394 
VAL CA  C    sing N N 395 
VAL CA  CB   sing N N 396 
VAL CA  HA   sing N N 397 
VAL C   O    doub N N 398 
VAL C   OXT  sing N N 399 
VAL CB  CG1  sing N N 400 
VAL CB  CG2  sing N N 401 
VAL CB  HB   sing N N 402 
VAL CG1 HG11 sing N N 403 
VAL CG1 HG12 sing N N 404 
VAL CG1 HG13 sing N N 405 
VAL CG2 HG21 sing N N 406 
VAL CG2 HG22 sing N N 407 
VAL CG2 HG23 sing N N 408 
VAL OXT HXT  sing N N 409 
YNK N23 C22  trip N N 410 
YNK C29 P27  sing N N 411 
YNK C30 P27  sing N N 412 
YNK C22 C21  sing N N 413 
YNK P27 O28  doub N N 414 
YNK P27 C20  sing N N 415 
YNK C21 C20  doub Y N 416 
YNK C21 C24  sing Y N 417 
YNK C20 C19  sing Y N 418 
YNK C24 C25  doub Y N 419 
YNK C19 N18  sing Y N 420 
YNK C19 C26  doub Y N 421 
YNK N18 C17  sing Y N 422 
YNK C25 C26  sing Y N 423 
YNK C26 C16  sing Y N 424 
YNK C17 C16  doub Y N 425 
YNK C16 C14  sing N N 426 
YNK C1  C2   sing N N 427 
YNK F32 C31  sing N N 428 
YNK C14 N15  doub Y N 429 
YNK C14 C13  sing Y N 430 
YNK N8  C2   sing N N 431 
YNK N8  C7   sing N N 432 
YNK N15 C10  sing Y N 433 
YNK C4  C2   sing N N 434 
YNK C4  C5   sing N N 435 
YNK C2  C3   sing N N 436 
YNK F34 C31  sing N N 437 
YNK C31 C13  sing N N 438 
YNK C31 F33  sing N N 439 
YNK C13 C12  doub Y N 440 
YNK C6  C7   sing N N 441 
YNK C6  C5   sing N N 442 
YNK C6  N9   sing N N 443 
YNK C10 N9   sing N N 444 
YNK C10 N11  doub Y N 445 
YNK C12 N11  sing Y N 446 
YNK C1  H41  sing N N 447 
YNK C1  H40  sing N N 448 
YNK C1  H39  sing N N 449 
YNK C3  H43  sing N N 450 
YNK C3  H42  sing N N 451 
YNK C3  H44  sing N N 452 
YNK C5  H47  sing N N 453 
YNK C5  H48  sing N N 454 
YNK C6  H35  sing N N 455 
YNK C7  H49  sing N N 456 
YNK C7  H50  sing N N 457 
YNK C12 H52  sing N N 458 
YNK N18 H38  sing N N 459 
YNK C24 H54  sing N N 460 
YNK C25 H55  sing N N 461 
YNK C4  H45  sing N N 462 
YNK C4  H46  sing N N 463 
YNK N8  H37  sing N N 464 
YNK N9  H51  sing N N 465 
YNK C17 H53  sing N N 466 
YNK C29 H57  sing N N 467 
YNK C29 H56  sing N N 468 
YNK C29 H58  sing N N 469 
YNK C30 H60  sing N N 470 
YNK C30 H59  sing N N 471 
YNK C30 H61  sing N N 472 
# 
_pdbx_audit_support.funding_organization   'European Union (EU)' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           'Programme EXCELES, ID Project No. LX22NPO5102' 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   7qhl 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GLA 
_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]   0.013901 
_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]   0.009109 
_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]   0.006114 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLU A 1 2   ? 9.398   -34.378 -40.412 1.00 82.22  ? 2   GLU A N   1 
ATOM   2    C  CA  . GLU A 1 2   ? 9.368   -32.936 -40.772 1.00 78.52  ? 2   GLU A CA  1 
ATOM   3    C  C   . GLU A 1 2   ? 10.518  -32.602 -41.737 1.00 76.12  ? 2   GLU A C   1 
ATOM   4    O  O   . GLU A 1 2   ? 11.199  -33.487 -42.265 1.00 61.96  ? 2   GLU A O   1 
ATOM   5    C  CB  . GLU A 1 2   ? 9.376   -32.123 -39.472 1.00 78.44  ? 2   GLU A CB  1 
ATOM   6    C  CG  . GLU A 1 2   ? 8.026   -31.499 -39.156 1.00 83.31  ? 2   GLU A CG  1 
ATOM   7    C  CD  . GLU A 1 2   ? 7.633   -30.385 -40.118 1.00 88.98  ? 2   GLU A CD  1 
ATOM   8    O  OE1 . GLU A 1 2   ? 6.414   -30.111 -40.258 1.00 86.32  ? 2   GLU A OE1 1 
ATOM   9    O  OE2 . GLU A 1 2   ? 8.550   -29.775 -40.722 1.00 84.95  ? 2   GLU A OE2 1 
ATOM   10   N  N   . ASN A 1 3   ? 10.713  -31.298 -41.986 1.00 71.68  ? 3   ASN A N   1 
ATOM   11   C  CA  . ASN A 1 3   ? 11.939  -30.776 -42.584 1.00 65.69  ? 3   ASN A CA  1 
ATOM   12   C  C   . ASN A 1 3   ? 13.102  -30.774 -41.577 1.00 57.98  ? 3   ASN A C   1 
ATOM   13   O  O   . ASN A 1 3   ? 14.135  -30.186 -41.886 1.00 56.31  ? 3   ASN A O   1 
ATOM   14   C  CB  . ASN A 1 3   ? 11.784  -29.339 -43.117 1.00 70.61  ? 3   ASN A CB  1 
ATOM   15   C  CG  . ASN A 1 3   ? 10.533  -29.087 -43.943 1.00 77.17  ? 3   ASN A CG  1 
ATOM   16   O  OD1 . ASN A 1 3   ? 10.175  -29.880 -44.816 1.00 77.29  ? 3   ASN A OD1 1 
ATOM   17   N  ND2 . ASN A 1 3   ? 9.869   -27.969 -43.684 1.00 71.40  ? 3   ASN A ND2 1 
ATOM   18   N  N   . PHE A 1 4   ? 12.947  -31.408 -40.388 1.00 53.50  ? 4   PHE A N   1 
ATOM   19   C  CA  . PHE A 1 4   ? 13.961  -31.430 -39.326 1.00 50.10  ? 4   PHE A CA  1 
ATOM   20   C  C   . PHE A 1 4   ? 14.632  -32.800 -39.184 1.00 52.45  ? 4   PHE A C   1 
ATOM   21   O  O   . PHE A 1 4   ? 13.955  -33.831 -39.200 1.00 48.20  ? 4   PHE A O   1 
ATOM   22   C  CB  . PHE A 1 4   ? 13.350  -31.049 -37.979 1.00 48.72  ? 4   PHE A CB  1 
ATOM   23   C  CG  . PHE A 1 4   ? 12.893  -29.616 -37.945 1.00 51.78  ? 4   PHE A CG  1 
ATOM   24   C  CD1 . PHE A 1 4   ? 13.819  -28.588 -38.008 1.00 48.48  ? 4   PHE A CD1 1 
ATOM   25   C  CD2 . PHE A 1 4   ? 11.547  -29.294 -37.904 1.00 52.13  ? 4   PHE A CD2 1 
ATOM   26   C  CE1 . PHE A 1 4   ? 13.408  -27.267 -38.021 1.00 50.49  ? 4   PHE A CE1 1 
ATOM   27   C  CE2 . PHE A 1 4   ? 11.140  -27.971 -37.920 1.00 52.86  ? 4   PHE A CE2 1 
ATOM   28   C  CZ  . PHE A 1 4   ? 12.069  -26.961 -37.985 1.00 51.93  ? 4   PHE A CZ  1 
ATOM   29   N  N   . GLN A 1 5   ? 15.969  -32.773 -39.037 1.00 47.37  ? 5   GLN A N   1 
ATOM   30   C  CA  . GLN A 1 5   ? 16.806  -33.933 -38.751 1.00 52.88  ? 5   GLN A CA  1 
ATOM   31   C  C   . GLN A 1 5   ? 17.229  -33.904 -37.278 1.00 52.66  ? 5   GLN A C   1 
ATOM   32   O  O   . GLN A 1 5   ? 17.904  -32.957 -36.880 1.00 49.79  ? 5   GLN A O   1 
ATOM   33   C  CB  . GLN A 1 5   ? 18.060  -33.871 -39.636 1.00 61.77  ? 5   GLN A CB  1 
ATOM   34   C  CG  . GLN A 1 5   ? 19.051  -35.011 -39.431 1.00 69.33  ? 5   GLN A CG  1 
ATOM   35   C  CD  . GLN A 1 5   ? 18.481  -36.329 -39.892 1.00 79.92  ? 5   GLN A CD  1 
ATOM   36   O  OE1 . GLN A 1 5   ? 18.068  -37.165 -39.088 1.00 89.98  ? 5   GLN A OE1 1 
ATOM   37   N  NE2 . GLN A 1 5   ? 18.438  -36.515 -41.202 1.00 85.01  ? 5   GLN A NE2 1 
ATOM   38   N  N   . LYS A 1 6   ? 16.866  -34.934 -36.486 1.00 54.10  ? 6   LYS A N   1 
ATOM   39   C  CA  . LYS A 1 6   ? 17.283  -35.048 -35.084 1.00 55.64  ? 6   LYS A CA  1 
ATOM   40   C  C   . LYS A 1 6   ? 18.793  -35.303 -35.057 1.00 53.97  ? 6   LYS A C   1 
ATOM   41   O  O   . LYS A 1 6   ? 19.261  -36.307 -35.581 1.00 55.10  ? 6   LYS A O   1 
ATOM   42   C  CB  . LYS A 1 6   ? 16.427  -36.080 -34.322 1.00 57.38  ? 6   LYS A CB  1 
ATOM   43   C  CG  . LYS A 1 6   ? 15.004  -35.591 -34.017 1.00 69.68  ? 6   LYS A CG  1 
ATOM   44   C  CD  . LYS A 1 6   ? 13.978  -36.588 -33.464 1.00 76.45  ? 6   LYS A CD  1 
ATOM   45   C  CE  . LYS A 1 6   ? 12.553  -36.070 -33.595 1.00 82.82  ? 6   LYS A CE  1 
ATOM   46   N  NZ  . LYS A 1 6   ? 11.704  -36.409 -32.423 1.00 87.87  ? 6   LYS A NZ  1 
ATOM   47   N  N   . VAL A 1 7   ? 19.550  -34.341 -34.505 1.00 48.00  ? 7   VAL A N   1 
ATOM   48   C  CA  . VAL A 1 7   ? 21.007  -34.398 -34.437 1.00 55.59  ? 7   VAL A CA  1 
ATOM   49   C  C   . VAL A 1 7   ? 21.428  -35.038 -33.111 1.00 57.78  ? 7   VAL A C   1 
ATOM   50   O  O   . VAL A 1 7   ? 22.222  -35.980 -33.137 1.00 67.59  ? 7   VAL A O   1 
ATOM   51   C  CB  . VAL A 1 7   ? 21.643  -33.001 -34.636 1.00 59.58  ? 7   VAL A CB  1 
ATOM   52   C  CG1 . VAL A 1 7   ? 23.152  -32.995 -34.427 1.00 62.23  ? 7   VAL A CG1 1 
ATOM   53   C  CG2 . VAL A 1 7   ? 21.317  -32.425 -36.007 1.00 58.71  ? 7   VAL A CG2 1 
ATOM   54   N  N   . ASP A 1 8   ? 20.910  -34.515 -31.978 1.00 56.80  ? 8   ASP A N   1 
ATOM   55   C  CA  . ASP A 1 8   ? 21.224  -34.997 -30.631 1.00 58.31  ? 8   ASP A CA  1 
ATOM   56   C  C   . ASP A 1 8   ? 20.075  -34.771 -29.633 1.00 54.79  ? 8   ASP A C   1 
ATOM   57   O  O   . ASP A 1 8   ? 19.414  -33.729 -29.631 1.00 51.19  ? 8   ASP A O   1 
ATOM   58   C  CB  . ASP A 1 8   ? 22.445  -34.287 -30.024 1.00 64.96  ? 8   ASP A CB  1 
ATOM   59   C  CG  . ASP A 1 8   ? 23.819  -34.606 -30.615 1.00 78.03  ? 8   ASP A CG  1 
ATOM   60   O  OD1 . ASP A 1 8   ? 24.082  -35.794 -30.961 1.00 80.79  ? 8   ASP A OD1 1 
ATOM   61   O  OD2 . ASP A 1 8   ? 24.660  -33.672 -30.658 1.00 74.26  ? 8   ASP A OD2 1 
ATOM   62   N  N   . PHE A 1 9   ? 19.889  -35.746 -28.730 1.00 50.00  ? 9   PHE A N   1 
ATOM   63   C  CA  . PHE A 1 9   ? 18.988  -35.651 -27.589 1.00 49.24  ? 9   PHE A CA  1 
ATOM   64   C  C   . PHE A 1 9   ? 19.625  -34.803 -26.484 1.00 47.52  ? 9   PHE A C   1 
ATOM   65   O  O   . PHE A 1 9   ? 20.762  -35.057 -26.115 1.00 43.38  ? 9   PHE A O   1 
ATOM   66   C  CB  . PHE A 1 9   ? 18.666  -37.050 -27.059 1.00 50.91  ? 9   PHE A CB  1 
ATOM   67   C  CG  . PHE A 1 9   ? 17.813  -37.067 -25.816 1.00 53.31  ? 9   PHE A CG  1 
ATOM   68   C  CD1 . PHE A 1 9   ? 16.462  -36.762 -25.875 1.00 53.36  ? 9   PHE A CD1 1 
ATOM   69   C  CD2 . PHE A 1 9   ? 18.361  -37.373 -24.580 1.00 55.21  ? 9   PHE A CD2 1 
ATOM   70   C  CE1 . PHE A 1 9   ? 15.671  -36.791 -24.735 1.00 48.16  ? 9   PHE A CE1 1 
ATOM   71   C  CE2 . PHE A 1 9   ? 17.573  -37.375 -23.438 1.00 54.98  ? 9   PHE A CE2 1 
ATOM   72   C  CZ  . PHE A 1 9   ? 16.229  -37.092 -23.520 1.00 52.65  ? 9   PHE A CZ  1 
ATOM   73   N  N   . LEU A 1 10  ? 18.870  -33.829 -25.937 1.00 46.71  ? 10  LEU A N   1 
ATOM   74   C  CA  . LEU A 1 10  ? 19.372  -32.879 -24.948 1.00 44.35  ? 10  LEU A CA  1 
ATOM   75   C  C   . LEU A 1 10  ? 18.803  -33.167 -23.550 1.00 44.05  ? 10  LEU A C   1 
ATOM   76   O  O   . LEU A 1 10  ? 19.464  -32.882 -22.554 1.00 50.57  ? 10  LEU A O   1 
ATOM   77   C  CB  . LEU A 1 10  ? 19.058  -31.446 -25.408 1.00 42.32  ? 10  LEU A CB  1 
ATOM   78   C  CG  . LEU A 1 10  ? 19.763  -30.975 -26.681 1.00 40.90  ? 10  LEU A CG  1 
ATOM   79   C  CD1 . LEU A 1 10  ? 19.436  -29.521 -26.966 1.00 41.09  ? 10  LEU A CD1 1 
ATOM   80   C  CD2 . LEU A 1 10  ? 21.282  -31.149 -26.603 1.00 43.52  ? 10  LEU A CD2 1 
ATOM   81   N  N   . GLY A 1 11  ? 17.590  -33.721 -23.431 1.00 52.20  ? 11  GLY A N   1 
ATOM   82   C  CA  . GLY A 1 11  ? 17.050  -34.041 -22.114 1.00 49.15  ? 11  GLY A CA  1 
ATOM   83   C  C   . GLY A 1 11  ? 15.529  -34.145 -22.103 1.00 55.06  ? 11  GLY A C   1 
ATOM   84   O  O   . GLY A 1 11  ? 14.867  -33.498 -22.909 1.00 59.39  ? 11  GLY A O   1 
ATOM   85   N  N   . GLU A 1 12  ? 15.018  -35.001 -21.201 1.00 62.00  ? 12  GLU A N   1 
ATOM   86   C  CA  . GLU A 1 12  ? 13.597  -35.246 -20.955 1.00 65.38  ? 12  GLU A CA  1 
ATOM   87   C  C   . GLU A 1 12  ? 13.256  -34.551 -19.638 1.00 69.80  ? 12  GLU A C   1 
ATOM   88   O  O   . GLU A 1 12  ? 14.023  -34.630 -18.672 1.00 64.56  ? 12  GLU A O   1 
ATOM   89   C  CB  . GLU A 1 12  ? 13.295  -36.751 -20.836 1.00 68.77  ? 12  GLU A CB  1 
ATOM   90   C  CG  . GLU A 1 12  ? 12.238  -37.274 -21.804 1.00 79.62  ? 12  GLU A CG  1 
ATOM   91   C  CD  . GLU A 1 12  ? 11.995  -38.780 -21.804 1.00 88.74  ? 12  GLU A CD  1 
ATOM   92   O  OE1 . GLU A 1 12  ? 12.257  -39.430 -22.846 1.00 86.78  ? 12  GLU A OE1 1 
ATOM   93   O  OE2 . GLU A 1 12  ? 11.528  -39.305 -20.771 1.00 104.56 ? 12  GLU A OE2 1 
ATOM   94   N  N   . GLY A 1 13  ? 12.120  -33.851 -19.611 1.00 71.82  ? 13  GLY A N   1 
ATOM   95   C  CA  . GLY A 1 13  ? 11.614  -33.215 -18.405 1.00 72.44  ? 13  GLY A CA  1 
ATOM   96   C  C   . GLY A 1 13  ? 10.204  -33.714 -18.128 1.00 70.70  ? 13  GLY A C   1 
ATOM   97   O  O   . GLY A 1 13  ? 9.743   -34.611 -18.830 1.00 65.66  ? 13  GLY A O   1 
ATOM   98   N  N   . GLN A 1 14  ? 9.543   -33.145 -17.110 1.00 74.88  ? 14  GLN A N   1 
ATOM   99   C  CA  . GLN A 1 14  ? 8.109   -33.324 -16.946 1.00 83.35  ? 14  GLN A CA  1 
ATOM   100  C  C   . GLN A 1 14  ? 7.417   -32.572 -18.084 1.00 83.05  ? 14  GLN A C   1 
ATOM   101  O  O   . GLN A 1 14  ? 6.484   -33.098 -18.688 1.00 78.63  ? 14  GLN A O   1 
ATOM   102  C  CB  . GLN A 1 14  ? 7.635   -32.880 -15.555 1.00 91.51  ? 14  GLN A CB  1 
ATOM   103  C  CG  . GLN A 1 14  ? 6.273   -33.455 -15.154 1.00 103.51 ? 14  GLN A CG  1 
ATOM   104  C  CD  . GLN A 1 14  ? 6.183   -34.970 -15.204 1.00 112.42 ? 14  GLN A CD  1 
ATOM   105  O  OE1 . GLN A 1 14  ? 6.813   -35.688 -14.423 1.00 103.12 ? 14  GLN A OE1 1 
ATOM   106  N  NE2 . GLN A 1 14  ? 5.373   -35.479 -16.123 1.00 104.86 ? 14  GLN A NE2 1 
ATOM   107  N  N   . PHE A 1 15  ? 7.944   -31.377 -18.405 1.00 86.79  ? 15  PHE A N   1 
ATOM   108  C  CA  . PHE A 1 15  ? 7.391   -30.462 -19.400 1.00 87.50  ? 15  PHE A CA  1 
ATOM   109  C  C   . PHE A 1 15  ? 7.531   -31.047 -20.805 1.00 75.83  ? 15  PHE A C   1 
ATOM   110  O  O   . PHE A 1 15  ? 6.668   -30.839 -21.649 1.00 74.57  ? 15  PHE A O   1 
ATOM   111  C  CB  . PHE A 1 15  ? 8.075   -29.091 -19.324 1.00 94.30  ? 15  PHE A CB  1 
ATOM   112  C  CG  . PHE A 1 15  ? 7.704   -28.257 -18.119 1.00 107.62 ? 15  PHE A CG  1 
ATOM   113  C  CD1 . PHE A 1 15  ? 7.607   -28.826 -16.856 1.00 107.59 ? 15  PHE A CD1 1 
ATOM   114  C  CD2 . PHE A 1 15  ? 7.469   -26.892 -18.240 1.00 115.84 ? 15  PHE A CD2 1 
ATOM   115  C  CE1 . PHE A 1 15  ? 7.272   -28.061 -15.750 1.00 110.91 ? 15  PHE A CE1 1 
ATOM   116  C  CE2 . PHE A 1 15  ? 7.137   -26.126 -17.131 1.00 116.50 ? 15  PHE A CE2 1 
ATOM   117  C  CZ  . PHE A 1 15  ? 7.037   -26.712 -15.889 1.00 115.86 ? 15  PHE A CZ  1 
ATOM   118  N  N   . GLY A 1 16  ? 8.630   -31.765 -21.051 1.00 69.35  ? 16  GLY A N   1 
ATOM   119  C  CA  . GLY A 1 16  ? 8.773   -32.538 -22.273 1.00 71.55  ? 16  GLY A CA  1 
ATOM   120  C  C   . GLY A 1 16  ? 10.226  -32.749 -22.707 1.00 67.08  ? 16  GLY A C   1 
ATOM   121  O  O   . GLY A 1 16  ? 11.159  -32.494 -21.944 1.00 60.90  ? 16  GLY A O   1 
ATOM   122  N  N   . VAL A 1 17  ? 10.365  -33.165 -23.979 1.00 60.63  ? 17  VAL A N   1 
ATOM   123  C  CA  . VAL A 1 17  ? 11.589  -33.671 -24.593 1.00 57.72  ? 17  VAL A CA  1 
ATOM   124  C  C   . VAL A 1 17  ? 12.197  -32.578 -25.479 1.00 50.47  ? 17  VAL A C   1 
ATOM   125  O  O   . VAL A 1 17  ? 11.476  -31.928 -26.231 1.00 52.80  ? 17  VAL A O   1 
ATOM   126  C  CB  . VAL A 1 17  ? 11.277  -34.947 -25.405 1.00 60.56  ? 17  VAL A CB  1 
ATOM   127  C  CG1 . VAL A 1 17  ? 12.533  -35.694 -25.811 1.00 62.05  ? 17  VAL A CG1 1 
ATOM   128  C  CG2 . VAL A 1 17  ? 10.342  -35.885 -24.653 1.00 62.45  ? 17  VAL A CG2 1 
ATOM   129  N  N   . VAL A 1 18  ? 13.522  -32.381 -25.376 1.00 43.19  ? 18  VAL A N   1 
ATOM   130  C  CA  . VAL A 1 18  ? 14.262  -31.422 -26.197 1.00 43.12  ? 18  VAL A CA  1 
ATOM   131  C  C   . VAL A 1 18  ? 15.348  -32.125 -27.018 1.00 41.91  ? 18  VAL A C   1 
ATOM   132  O  O   . VAL A 1 18  ? 16.173  -32.860 -26.462 1.00 39.30  ? 18  VAL A O   1 
ATOM   133  C  CB  . VAL A 1 18  ? 14.878  -30.293 -25.352 1.00 40.02  ? 18  VAL A CB  1 
ATOM   134  C  CG1 . VAL A 1 18  ? 15.652  -29.310 -26.218 1.00 40.24  ? 18  VAL A CG1 1 
ATOM   135  C  CG2 . VAL A 1 18  ? 13.818  -29.582 -24.534 1.00 40.59  ? 18  VAL A CG2 1 
ATOM   136  N  N   . TYR A 1 19  ? 15.333  -31.856 -28.341 1.00 44.88  ? 19  TYR A N   1 
ATOM   137  C  CA  . TYR A 1 19  ? 16.339  -32.320 -29.294 1.00 43.34  ? 19  TYR A CA  1 
ATOM   138  C  C   . TYR A 1 19  ? 17.060  -31.135 -29.939 1.00 40.46  ? 19  TYR A C   1 
ATOM   139  O  O   . TYR A 1 19  ? 16.435  -30.121 -30.232 1.00 41.89  ? 19  TYR A O   1 
ATOM   140  C  CB  . TYR A 1 19  ? 15.674  -33.157 -30.387 1.00 44.52  ? 19  TYR A CB  1 
ATOM   141  C  CG  . TYR A 1 19  ? 15.327  -34.564 -29.983 1.00 45.94  ? 19  TYR A CG  1 
ATOM   142  C  CD1 . TYR A 1 19  ? 16.265  -35.580 -30.072 1.00 49.06  ? 19  TYR A CD1 1 
ATOM   143  C  CD2 . TYR A 1 19  ? 14.044  -34.893 -29.584 1.00 49.63  ? 19  TYR A CD2 1 
ATOM   144  C  CE1 . TYR A 1 19  ? 15.954  -36.881 -29.716 1.00 54.53  ? 19  TYR A CE1 1 
ATOM   145  C  CE2 . TYR A 1 19  ? 13.713  -36.188 -29.224 1.00 54.67  ? 19  TYR A CE2 1 
ATOM   146  C  CZ  . TYR A 1 19  ? 14.675  -37.183 -29.276 1.00 58.85  ? 19  TYR A CZ  1 
ATOM   147  O  OH  . TYR A 1 19  ? 14.366  -38.481 -28.937 1.00 69.52  ? 19  TYR A OH  1 
ATOM   148  N  N   . LYS A 1 20  ? 18.371  -31.287 -30.168 1.00 43.55  ? 20  LYS A N   1 
ATOM   149  C  CA  . LYS A 1 20  ? 19.102  -30.494 -31.152 1.00 44.56  ? 20  LYS A CA  1 
ATOM   150  C  C   . LYS A 1 20  ? 18.763  -31.030 -32.545 1.00 46.56  ? 20  LYS A C   1 
ATOM   151  O  O   . LYS A 1 20  ? 18.821  -32.233 -32.771 1.00 55.19  ? 20  LYS A O   1 
ATOM   152  C  CB  . LYS A 1 20  ? 20.616  -30.545 -30.896 1.00 45.41  ? 20  LYS A CB  1 
ATOM   153  C  CG  . LYS A 1 20  ? 21.470  -29.789 -31.904 1.00 44.73  ? 20  LYS A CG  1 
ATOM   154  C  CD  . LYS A 1 20  ? 22.946  -29.721 -31.600 1.00 49.32  ? 20  LYS A CD  1 
ATOM   155  C  CE  . LYS A 1 20  ? 23.668  -28.748 -32.518 1.00 55.15  ? 20  LYS A CE  1 
ATOM   156  N  NZ  . LYS A 1 20  ? 25.143  -28.906 -32.477 1.00 59.03  ? 20  LYS A NZ  1 
ATOM   157  N  N   . ALA A 1 21  ? 18.407  -30.138 -33.479 1.00 46.64  ? 21  ALA A N   1 
ATOM   158  C  CA  . ALA A 1 21  ? 17.955  -30.514 -34.816 1.00 43.89  ? 21  ALA A CA  1 
ATOM   159  C  C   . ALA A 1 21  ? 18.461  -29.527 -35.880 1.00 42.70  ? 21  ALA A C   1 
ATOM   160  O  O   . ALA A 1 21  ? 18.815  -28.374 -35.580 1.00 37.82  ? 21  ALA A O   1 
ATOM   161  C  CB  . ALA A 1 21  ? 16.449  -30.606 -34.819 1.00 44.81  ? 21  ALA A CB  1 
ATOM   162  N  N   . ARG A 1 22  ? 18.509  -30.031 -37.128 1.00 45.33  ? 22  ARG A N   1 
ATOM   163  C  CA  . ARG A 1 22  ? 18.900  -29.290 -38.327 1.00 49.10  ? 22  ARG A CA  1 
ATOM   164  C  C   . ARG A 1 22  ? 17.669  -29.173 -39.235 1.00 48.06  ? 22  ARG A C   1 
ATOM   165  O  O   . ARG A 1 22  ? 16.926  -30.148 -39.430 1.00 41.09  ? 22  ARG A O   1 
ATOM   166  C  CB  . ARG A 1 22  ? 20.062  -30.027 -39.013 1.00 54.79  ? 22  ARG A CB  1 
ATOM   167  C  CG  . ARG A 1 22  ? 20.975  -29.185 -39.898 1.00 68.31  ? 22  ARG A CG  1 
ATOM   168  C  CD  . ARG A 1 22  ? 22.270  -29.908 -40.285 1.00 77.68  ? 22  ARG A CD  1 
ATOM   169  N  NE  . ARG A 1 22  ? 22.192  -31.376 -40.320 1.00 86.89  ? 22  ARG A NE  1 
ATOM   170  C  CZ  . ARG A 1 22  ? 21.564  -32.113 -41.245 1.00 95.12  ? 22  ARG A CZ  1 
ATOM   171  N  NH1 . ARG A 1 22  ? 21.553  -33.433 -41.136 1.00 94.21  ? 22  ARG A NH1 1 
ATOM   172  N  NH2 . ARG A 1 22  ? 20.941  -31.547 -42.269 1.00 93.12  ? 22  ARG A NH2 1 
ATOM   173  N  N   . ASN A 1 23  ? 17.420  -27.960 -39.742 1.00 47.57  ? 23  ASN A N   1 
ATOM   174  C  CA  . ASN A 1 23  ? 16.570  -27.776 -40.912 1.00 49.49  ? 23  ASN A CA  1 
ATOM   175  C  C   . ASN A 1 23  ? 17.291  -28.337 -42.150 1.00 46.40  ? 23  ASN A C   1 
ATOM   176  O  O   . ASN A 1 23  ? 18.300  -27.791 -42.588 1.00 41.81  ? 23  ASN A O   1 
ATOM   177  C  CB  . ASN A 1 23  ? 16.199  -26.297 -41.061 1.00 53.41  ? 23  ASN A CB  1 
ATOM   178  C  CG  . ASN A 1 23  ? 15.022  -26.084 -41.982 1.00 52.87  ? 23  ASN A CG  1 
ATOM   179  O  OD1 . ASN A 1 23  ? 14.895  -26.798 -42.971 1.00 49.32  ? 23  ASN A OD1 1 
ATOM   180  N  ND2 . ASN A 1 23  ? 14.169  -25.121 -41.660 1.00 51.52  ? 23  ASN A ND2 1 
ATOM   181  N  N   . LYS A 1 24  ? 16.764  -29.436 -42.706 1.00 49.77  ? 24  LYS A N   1 
ATOM   182  C  CA  . LYS A 1 24  ? 17.331  -30.151 -43.848 1.00 53.85  ? 24  LYS A CA  1 
ATOM   183  C  C   . LYS A 1 24  ? 17.317  -29.340 -45.155 1.00 53.73  ? 24  LYS A C   1 
ATOM   184  O  O   . LYS A 1 24  ? 17.980  -29.734 -46.114 1.00 57.30  ? 24  LYS A O   1 
ATOM   185  C  CB  . LYS A 1 24  ? 16.544  -31.452 -44.055 1.00 56.12  ? 24  LYS A CB  1 
ATOM   186  C  CG  . LYS A 1 24  ? 16.667  -32.460 -42.924 1.00 60.93  ? 24  LYS A CG  1 
ATOM   187  C  CD  . LYS A 1 24  ? 16.161  -33.846 -43.259 1.00 66.62  ? 24  LYS A CD  1 
ATOM   188  C  CE  . LYS A 1 24  ? 14.683  -34.020 -42.990 1.00 74.53  ? 24  LYS A CE  1 
ATOM   189  N  NZ  . LYS A 1 24  ? 14.336  -35.444 -42.767 1.00 82.69  ? 24  LYS A NZ  1 
ATOM   190  N  N   . LEU A 1 25  ? 16.550  -28.237 -45.213 1.00 49.45  ? 25  LEU A N   1 
ATOM   191  C  CA  . LEU A 1 25  ? 16.440  -27.402 -46.405 1.00 45.31  ? 25  LEU A CA  1 
ATOM   192  C  C   . LEU A 1 25  ? 17.257  -26.107 -46.269 1.00 46.09  ? 25  LEU A C   1 
ATOM   193  O  O   . LEU A 1 25  ? 17.844  -25.657 -47.247 1.00 46.27  ? 25  LEU A O   1 
ATOM   194  C  CB  . LEU A 1 25  ? 14.957  -27.095 -46.675 1.00 44.68  ? 25  LEU A CB  1 
ATOM   195  C  CG  . LEU A 1 25  ? 14.040  -28.288 -46.972 1.00 44.24  ? 25  LEU A CG  1 
ATOM   196  C  CD1 . LEU A 1 25  ? 12.619  -27.830 -47.262 1.00 43.88  ? 25  LEU A CD1 1 
ATOM   197  C  CD2 . LEU A 1 25  ? 14.538  -29.128 -48.133 1.00 43.37  ? 25  LEU A CD2 1 
ATOM   198  N  N   . THR A 1 26  ? 17.285  -25.488 -45.081 1.00 42.41  ? 26  THR A N   1 
ATOM   199  C  CA  . THR A 1 26  ? 17.987  -24.226 -44.869 1.00 44.27  ? 26  THR A CA  1 
ATOM   200  C  C   . THR A 1 26  ? 19.298  -24.382 -44.092 1.00 42.49  ? 26  THR A C   1 
ATOM   201  O  O   . THR A 1 26  ? 20.088  -23.440 -44.067 1.00 44.60  ? 26  THR A O   1 
ATOM   202  C  CB  . THR A 1 26  ? 17.130  -23.219 -44.093 1.00 47.54  ? 26  THR A CB  1 
ATOM   203  O  OG1 . THR A 1 26  ? 17.037  -23.635 -42.729 1.00 46.53  ? 26  THR A OG1 1 
ATOM   204  C  CG2 . THR A 1 26  ? 15.753  -23.062 -44.699 1.00 52.38  ? 26  THR A CG2 1 
ATOM   205  N  N   . GLY A 1 27  ? 19.491  -25.516 -43.404 1.00 43.58  ? 27  GLY A N   1 
ATOM   206  C  CA  . GLY A 1 27  ? 20.687  -25.766 -42.611 1.00 43.05  ? 27  GLY A CA  1 
ATOM   207  C  C   . GLY A 1 27  ? 20.616  -25.210 -41.181 1.00 47.00  ? 27  GLY A C   1 
ATOM   208  O  O   . GLY A 1 27  ? 21.419  -25.598 -40.335 1.00 47.66  ? 27  GLY A O   1 
ATOM   209  N  N   . GLU A 1 28  ? 19.674  -24.294 -40.909 1.00 54.19  ? 28  GLU A N   1 
ATOM   210  C  CA  . GLU A 1 28  ? 19.524  -23.661 -39.598 1.00 53.35  ? 28  GLU A CA  1 
ATOM   211  C  C   . GLU A 1 28  ? 19.465  -24.735 -38.501 1.00 51.18  ? 28  GLU A C   1 
ATOM   212  O  O   . GLU A 1 28  ? 18.697  -25.688 -38.616 1.00 52.90  ? 28  GLU A O   1 
ATOM   213  C  CB  . GLU A 1 28  ? 18.278  -22.765 -39.618 1.00 56.81  ? 28  GLU A CB  1 
ATOM   214  C  CG  . GLU A 1 28  ? 18.072  -21.910 -38.369 1.00 66.44  ? 28  GLU A CG  1 
ATOM   215  C  CD  . GLU A 1 28  ? 16.760  -21.126 -38.312 1.00 72.19  ? 28  GLU A CD  1 
ATOM   216  O  OE1 . GLU A 1 28  ? 15.721  -21.649 -38.790 1.00 69.49  ? 28  GLU A OE1 1 
ATOM   217  O  OE2 . GLU A 1 28  ? 16.765  -20.001 -37.756 1.00 68.40  ? 28  GLU A OE2 1 
ATOM   218  N  N   . VAL A 1 29  ? 20.308  -24.594 -37.458 1.00 53.28  ? 29  VAL A N   1 
ATOM   219  C  CA  . VAL A 1 29  ? 20.324  -25.462 -36.275 1.00 51.51  ? 29  VAL A CA  1 
ATOM   220  C  C   . VAL A 1 29  ? 19.323  -24.916 -35.247 1.00 45.46  ? 29  VAL A C   1 
ATOM   221  O  O   . VAL A 1 29  ? 19.357  -23.724 -34.948 1.00 41.63  ? 29  VAL A O   1 
ATOM   222  C  CB  . VAL A 1 29  ? 21.745  -25.564 -35.666 1.00 54.42  ? 29  VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 29  ? 21.771  -26.460 -34.435 1.00 56.65  ? 29  VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 29  ? 22.788  -26.048 -36.672 1.00 54.40  ? 29  VAL A CG2 1 
ATOM   225  N  N   . VAL A 1 30  ? 18.442  -25.784 -34.710 1.00 43.74  ? 30  VAL A N   1 
ATOM   226  C  CA  . VAL A 1 30  ? 17.404  -25.388 -33.757 1.00 41.77  ? 30  VAL A CA  1 
ATOM   227  C  C   . VAL A 1 30  ? 17.391  -26.330 -32.558 1.00 41.31  ? 30  VAL A C   1 
ATOM   228  O  O   . VAL A 1 30  ? 17.939  -27.420 -32.628 1.00 41.38  ? 30  VAL A O   1 
ATOM   229  C  CB  . VAL A 1 30  ? 15.995  -25.401 -34.383 1.00 41.43  ? 30  VAL A CB  1 
ATOM   230  C  CG1 . VAL A 1 30  ? 15.871  -24.397 -35.513 1.00 42.57  ? 30  VAL A CG1 1 
ATOM   231  C  CG2 . VAL A 1 30  ? 15.595  -26.807 -34.815 1.00 39.15  ? 30  VAL A CG2 1 
ATOM   232  N  N   . ALA A 1 31  ? 16.695  -25.908 -31.494 1.00 42.12  ? 31  ALA A N   1 
ATOM   233  C  CA  . ALA A 1 31  ? 16.277  -26.784 -30.411 1.00 41.30  ? 31  ALA A CA  1 
ATOM   234  C  C   . ALA A 1 31  ? 14.781  -27.016 -30.553 1.00 42.60  ? 31  ALA A C   1 
ATOM   235  O  O   . ALA A 1 31  ? 14.051  -26.036 -30.608 1.00 45.51  ? 31  ALA A O   1 
ATOM   236  C  CB  . ALA A 1 31  ? 16.592  -26.130 -29.095 1.00 41.24  ? 31  ALA A CB  1 
ATOM   237  N  N   . LEU A 1 32  ? 14.359  -28.285 -30.683 1.00 46.35  ? 32  LEU A N   1 
ATOM   238  C  CA  . LEU A 1 32  ? 12.957  -28.690 -30.754 1.00 45.40  ? 32  LEU A CA  1 
ATOM   239  C  C   . LEU A 1 32  ? 12.497  -29.154 -29.379 1.00 48.05  ? 32  LEU A C   1 
ATOM   240  O  O   . LEU A 1 32  ? 13.037  -30.139 -28.882 1.00 46.52  ? 32  LEU A O   1 
ATOM   241  C  CB  . LEU A 1 32  ? 12.776  -29.901 -31.678 1.00 51.54  ? 32  LEU A CB  1 
ATOM   242  C  CG  . LEU A 1 32  ? 12.849  -29.693 -33.183 1.00 59.54  ? 32  LEU A CG  1 
ATOM   243  C  CD1 . LEU A 1 32  ? 12.519  -31.000 -33.889 1.00 65.16  ? 32  LEU A CD1 1 
ATOM   244  C  CD2 . LEU A 1 32  ? 11.902  -28.598 -33.629 1.00 60.81  ? 32  LEU A CD2 1 
ATOM   245  N  N   . LYS A 1 33  ? 11.467  -28.499 -28.829 1.00 51.86  ? 33  LYS A N   1 
ATOM   246  C  CA  . LYS A 1 33  ? 10.790  -28.913 -27.603 1.00 53.03  ? 33  LYS A CA  1 
ATOM   247  C  C   . LYS A 1 33  ? 9.521   -29.662 -28.008 1.00 50.37  ? 33  LYS A C   1 
ATOM   248  O  O   . LYS A 1 33  ? 8.590   -29.039 -28.508 1.00 52.51  ? 33  LYS A O   1 
ATOM   249  C  CB  . LYS A 1 33  ? 10.492  -27.684 -26.725 1.00 54.90  ? 33  LYS A CB  1 
ATOM   250  C  CG  . LYS A 1 33  ? 9.980   -27.970 -25.315 1.00 60.48  ? 33  LYS A CG  1 
ATOM   251  C  CD  . LYS A 1 33  ? 9.866   -26.744 -24.417 1.00 62.88  ? 33  LYS A CD  1 
ATOM   252  C  CE  . LYS A 1 33  ? 11.216  -26.179 -24.022 1.00 66.53  ? 33  LYS A CE  1 
ATOM   253  N  NZ  . LYS A 1 33  ? 11.119  -25.300 -22.833 1.00 65.17  ? 33  LYS A NZ  1 
ATOM   254  N  N   . LYS A 1 34  ? 9.524   -30.999 -27.884 1.00 52.84  ? 34  LYS A N   1 
ATOM   255  C  CA  . LYS A 1 34  ? 8.310   -31.798 -28.021 1.00 61.18  ? 34  LYS A CA  1 
ATOM   256  C  C   . LYS A 1 34  ? 7.545   -31.700 -26.701 1.00 58.59  ? 34  LYS A C   1 
ATOM   257  O  O   . LYS A 1 34  ? 8.045   -32.169 -25.682 1.00 53.91  ? 34  LYS A O   1 
ATOM   258  C  CB  . LYS A 1 34  ? 8.600   -33.269 -28.367 1.00 68.63  ? 34  LYS A CB  1 
ATOM   259  C  CG  . LYS A 1 34  ? 7.355   -34.132 -28.600 1.00 79.40  ? 34  LYS A CG  1 
ATOM   260  C  CD  . LYS A 1 34  ? 7.597   -35.635 -28.719 1.00 90.03  ? 34  LYS A CD  1 
ATOM   261  C  CE  . LYS A 1 34  ? 8.287   -36.041 -30.007 1.00 99.43  ? 34  LYS A CE  1 
ATOM   262  N  NZ  . LYS A 1 34  ? 8.929   -37.373 -29.894 1.00 104.97 ? 34  LYS A NZ  1 
ATOM   263  N  N   . ILE A 1 35  ? 6.366   -31.060 -26.711 1.00 59.07  ? 35  ILE A N   1 
ATOM   264  C  CA  . ILE A 1 35  ? 5.577   -30.923 -25.492 1.00 63.21  ? 35  ILE A CA  1 
ATOM   265  C  C   . ILE A 1 35  ? 4.934   -32.281 -25.193 1.00 73.96  ? 35  ILE A C   1 
ATOM   266  O  O   . ILE A 1 35  ? 4.363   -32.931 -26.098 1.00 68.26  ? 35  ILE A O   1 
ATOM   267  C  CB  . ILE A 1 35  ? 4.557   -29.767 -25.580 1.00 61.62  ? 35  ILE A CB  1 
ATOM   268  C  CG1 . ILE A 1 35  ? 5.244   -28.398 -25.562 1.00 57.88  ? 35  ILE A CG1 1 
ATOM   269  C  CG2 . ILE A 1 35  ? 3.511   -29.869 -24.479 1.00 61.35  ? 35  ILE A CG2 1 
ATOM   270  C  CD1 . ILE A 1 35  ? 6.138   -28.182 -24.367 1.00 59.26  ? 35  ILE A CD1 1 
ATOM   271  N  N   . ARG A 1 36  ? 5.063   -32.690 -23.911 1.00 82.48  ? 36  ARG A N   1 
ATOM   272  C  CA  . ARG A 1 36  ? 4.484   -33.933 -23.415 1.00 89.14  ? 36  ARG A CA  1 
ATOM   273  C  C   . ARG A 1 36  ? 2.970   -33.703 -23.448 1.00 88.93  ? 36  ARG A C   1 
ATOM   274  O  O   . ARG A 1 36  ? 2.439   -32.943 -22.632 1.00 83.02  ? 36  ARG A O   1 
ATOM   275  C  CB  . ARG A 1 36  ? 5.069   -34.274 -22.032 1.00 89.64  ? 36  ARG A CB  1 
ATOM   276  C  CG  . ARG A 1 36  ? 4.661   -35.625 -21.450 1.00 94.12  ? 36  ARG A CG  1 
ATOM   277  C  CD  . ARG A 1 36  ? 5.347   -35.977 -20.135 1.00 91.31  ? 36  ARG A CD  1 
ATOM   278  N  NE  . ARG A 1 36  ? 6.809   -35.938 -20.181 1.00 95.41  ? 36  ARG A NE  1 
ATOM   279  C  CZ  . ARG A 1 36  ? 7.597   -36.855 -20.744 1.00 95.24  ? 36  ARG A CZ  1 
ATOM   280  N  NH1 . ARG A 1 36  ? 7.082   -37.919 -21.338 1.00 92.00  ? 36  ARG A NH1 1 
ATOM   281  N  NH2 . ARG A 1 36  ? 8.912   -36.705 -20.706 1.00 94.63  ? 36  ARG A NH2 1 
ATOM   282  N  N   . LEU A 1 37  ? 2.308   -34.259 -24.472 1.00 92.49  ? 37  LEU A N   1 
ATOM   283  C  CA  . LEU A 1 37  ? 0.856   -34.201 -24.587 1.00 97.21  ? 37  LEU A CA  1 
ATOM   284  C  C   . LEU A 1 37  ? 0.286   -35.511 -24.049 1.00 111.90 ? 37  LEU A C   1 
ATOM   285  O  O   . LEU A 1 37  ? -0.609  -35.494 -23.203 1.00 108.13 ? 37  LEU A O   1 
ATOM   286  C  CB  . LEU A 1 37  ? 0.450   -33.984 -26.052 1.00 87.14  ? 37  LEU A CB  1 
ATOM   287  C  CG  . LEU A 1 37  ? 0.452   -32.539 -26.550 1.00 79.43  ? 37  LEU A CG  1 
ATOM   288  C  CD1 . LEU A 1 37  ? -0.387  -32.395 -27.807 1.00 76.50  ? 37  LEU A CD1 1 
ATOM   289  C  CD2 . LEU A 1 37  ? -0.053  -31.585 -25.483 1.00 82.72  ? 37  LEU A CD2 1 
ATOM   290  N  N   . ASP A 1 38  ? 0.832   -36.628 -24.562 1.00 124.08 ? 38  ASP A N   1 
ATOM   291  C  CA  . ASP A 1 38  ? 0.542   -37.987 -24.113 1.00 121.95 ? 38  ASP A CA  1 
ATOM   292  C  C   . ASP A 1 38  ? -0.972  -38.230 -24.071 1.00 115.26 ? 38  ASP A C   1 
ATOM   293  O  O   . ASP A 1 38  ? -1.596  -38.127 -25.192 1.00 112.61 ? 38  ASP A O   1 
ATOM   294  C  CB  . ASP A 1 38  ? 1.200   -38.299 -22.764 1.00 122.43 ? 38  ASP A CB  1 
ATOM   295  C  CG  . ASP A 1 38  ? 0.850   -37.334 -21.642 1.00 123.33 ? 38  ASP A CG  1 
ATOM   296  O  OD1 . ASP A 1 38  ? -0.206  -37.536 -21.007 1.00 113.98 ? 38  ASP A OD1 1 
ATOM   297  O  OD2 . ASP A 1 38  ? 1.634   -36.388 -21.412 1.00 118.44 ? 38  ASP A OD2 1 
ATOM   298  N  N   . GLU A 1 40  ? -3.516  -36.500 -22.919 1.00 126.61 ? 40  GLU A N   1 
ATOM   299  C  CA  . GLU A 1 40  ? -3.856  -35.174 -22.338 1.00 122.33 ? 40  GLU A CA  1 
ATOM   300  C  C   . GLU A 1 40  ? -5.345  -35.179 -21.999 1.00 125.54 ? 40  GLU A C   1 
ATOM   301  O  O   . GLU A 1 40  ? -6.199  -35.167 -22.896 1.00 137.06 ? 40  GLU A O   1 
ATOM   302  C  CB  . GLU A 1 40  ? -3.506  -34.042 -23.309 1.00 127.71 ? 40  GLU A CB  1 
ATOM   303  C  CG  . GLU A 1 40  ? -4.419  -33.953 -24.527 1.00 128.50 ? 40  GLU A CG  1 
ATOM   304  C  CD  . GLU A 1 40  ? -4.186  -34.986 -25.622 1.00 133.02 ? 40  GLU A CD  1 
ATOM   305  O  OE1 . GLU A 1 40  ? -3.268  -35.819 -25.486 1.00 131.30 ? 40  GLU A OE1 1 
ATOM   306  O  OE2 . GLU A 1 40  ? -4.923  -34.952 -26.622 1.00 131.57 ? 40  GLU A OE2 1 
ATOM   307  N  N   . THR A 1 41  ? -5.651  -35.250 -20.702 1.00 111.98 ? 41  THR A N   1 
ATOM   308  C  CA  . THR A 1 41  ? -7.028  -35.178 -20.242 1.00 105.64 ? 41  THR A CA  1 
ATOM   309  C  C   . THR A 1 41  ? -7.591  -33.790 -20.547 1.00 89.53  ? 41  THR A C   1 
ATOM   310  O  O   . THR A 1 41  ? -8.750  -33.685 -20.936 1.00 79.82  ? 41  THR A O   1 
ATOM   311  C  CB  . THR A 1 41  ? -7.143  -35.532 -18.752 1.00 113.08 ? 41  THR A CB  1 
ATOM   312  O  OG1 . THR A 1 41  ? -6.346  -34.619 -17.997 1.00 113.47 ? 41  THR A OG1 1 
ATOM   313  C  CG2 . THR A 1 41  ? -6.702  -36.947 -18.446 1.00 111.78 ? 41  THR A CG2 1 
ATOM   314  N  N   . GLU A 1 42  ? -6.756  -32.746 -20.392 1.00 71.96  ? 42  GLU A N   1 
ATOM   315  C  CA  . GLU A 1 42  ? -7.199  -31.362 -20.499 1.00 68.80  ? 42  GLU A CA  1 
ATOM   316  C  C   . GLU A 1 42  ? -6.734  -30.679 -21.784 1.00 57.59  ? 42  GLU A C   1 
ATOM   317  O  O   . GLU A 1 42  ? -6.868  -29.464 -21.886 1.00 58.62  ? 42  GLU A O   1 
ATOM   318  C  CB  . GLU A 1 42  ? -6.725  -30.539 -19.298 1.00 80.07  ? 42  GLU A CB  1 
ATOM   319  C  CG  . GLU A 1 42  ? -7.034  -31.187 -17.957 1.00 88.26  ? 42  GLU A CG  1 
ATOM   320  C  CD  . GLU A 1 42  ? -8.424  -31.791 -17.812 1.00 88.35  ? 42  GLU A CD  1 
ATOM   321  O  OE1 . GLU A 1 42  ? -9.302  -31.474 -18.635 1.00 87.40  ? 42  GLU A OE1 1 
ATOM   322  O  OE2 . GLU A 1 42  ? -8.626  -32.591 -16.874 1.00 80.39  ? 42  GLU A OE2 1 
ATOM   323  N  N   . GLY A 1 43  ? -6.244  -31.410 -22.788 1.00 51.78  ? 43  GLY A N   1 
ATOM   324  C  CA  . GLY A 1 43  ? -5.854  -30.717 -24.009 1.00 53.12  ? 43  GLY A CA  1 
ATOM   325  C  C   . GLY A 1 43  ? -4.477  -30.078 -23.850 1.00 54.38  ? 43  GLY A C   1 
ATOM   326  O  O   . GLY A 1 43  ? -3.572  -30.726 -23.330 1.00 59.49  ? 43  GLY A O   1 
ATOM   327  N  N   . VAL A 1 44  ? -4.309  -28.818 -24.274 1.00 51.87  ? 44  VAL A N   1 
ATOM   328  C  CA  . VAL A 1 44  ? -2.990  -28.192 -24.261 1.00 51.28  ? 44  VAL A CA  1 
ATOM   329  C  C   . VAL A 1 44  ? -2.673  -27.754 -22.835 1.00 48.66  ? 44  VAL A C   1 
ATOM   330  O  O   . VAL A 1 44  ? -3.491  -27.097 -22.203 1.00 50.40  ? 44  VAL A O   1 
ATOM   331  C  CB  . VAL A 1 44  ? -2.887  -27.006 -25.240 1.00 55.84  ? 44  VAL A CB  1 
ATOM   332  C  CG1 . VAL A 1 44  ? -1.528  -26.331 -25.149 1.00 57.40  ? 44  VAL A CG1 1 
ATOM   333  C  CG2 . VAL A 1 44  ? -3.169  -27.423 -26.677 1.00 56.17  ? 44  VAL A CG2 1 
ATOM   334  N  N   . PRO A 1 45  ? -1.489  -28.107 -22.283 1.00 45.31  ? 45  PRO A N   1 
ATOM   335  C  CA  . PRO A 1 45  ? -1.091  -27.666 -20.947 1.00 42.78  ? 45  PRO A CA  1 
ATOM   336  C  C   . PRO A 1 45  ? -1.014  -26.149 -20.808 1.00 41.02  ? 45  PRO A C   1 
ATOM   337  O  O   . PRO A 1 45  ? -0.536  -25.494 -21.719 1.00 48.32  ? 45  PRO A O   1 
ATOM   338  C  CB  . PRO A 1 45  ? 0.333   -28.221 -20.792 1.00 45.75  ? 45  PRO A CB  1 
ATOM   339  C  CG  . PRO A 1 45  ? 0.394   -29.394 -21.743 1.00 48.29  ? 45  PRO A CG  1 
ATOM   340  C  CD  . PRO A 1 45  ? -0.487  -28.986 -22.906 1.00 48.34  ? 45  PRO A CD  1 
ATOM   341  N  N   . SER A 1 46  ? -1.468  -25.608 -19.669 1.00 42.41  ? 46  SER A N   1 
ATOM   342  C  CA  . SER A 1 46  ? -1.340  -24.186 -19.350 1.00 46.26  ? 46  SER A CA  1 
ATOM   343  C  C   . SER A 1 46  ? 0.094   -23.683 -19.540 1.00 45.08  ? 46  SER A C   1 
ATOM   344  O  O   . SER A 1 46  ? 0.283   -22.551 -19.986 1.00 50.25  ? 46  SER A O   1 
ATOM   345  C  CB  . SER A 1 46  ? -1.845  -23.845 -17.950 1.00 48.67  ? 46  SER A CB  1 
ATOM   346  O  OG  . SER A 1 46  ? -1.411  -24.786 -16.974 1.00 48.87  ? 46  SER A OG  1 
ATOM   347  N  N   . THR A 1 47  ? 1.095   -24.496 -19.176 1.00 40.44  ? 47  THR A N   1 
ATOM   348  C  CA  . THR A 1 47  ? 2.485   -24.064 -19.255 1.00 42.31  ? 47  THR A CA  1 
ATOM   349  C  C   . THR A 1 47  ? 2.860   -23.843 -20.715 1.00 41.77  ? 47  THR A C   1 
ATOM   350  O  O   . THR A 1 47  ? 3.519   -22.853 -21.020 1.00 42.96  ? 47  THR A O   1 
ATOM   351  C  CB  . THR A 1 47  ? 3.473   -25.019 -18.571 1.00 44.53  ? 47  THR A CB  1 
ATOM   352  O  OG1 . THR A 1 47  ? 3.249   -26.321 -19.106 1.00 43.85  ? 47  THR A OG1 1 
ATOM   353  C  CG2 . THR A 1 47  ? 3.344   -25.024 -17.063 1.00 46.48  ? 47  THR A CG2 1 
ATOM   354  N  N   . ALA A 1 48  ? 2.373   -24.708 -21.614 1.00 41.66  ? 48  ALA A N   1 
ATOM   355  C  CA  . ALA A 1 48  ? 2.623   -24.554 -23.041 1.00 41.44  ? 48  ALA A CA  1 
ATOM   356  C  C   . ALA A 1 48  ? 1.953   -23.280 -23.551 1.00 43.38  ? 48  ALA A C   1 
ATOM   357  O  O   . ALA A 1 48  ? 2.580   -22.507 -24.276 1.00 44.63  ? 48  ALA A O   1 
ATOM   358  C  CB  . ALA A 1 48  ? 2.136   -25.756 -23.793 1.00 45.15  ? 48  ALA A CB  1 
ATOM   359  N  N   . ILE A 1 49  ? 0.694   -23.054 -23.148 1.00 44.68  ? 49  ILE A N   1 
ATOM   360  C  CA  . ILE A 1 49  ? -0.070  -21.890 -23.590 1.00 44.63  ? 49  ILE A CA  1 
ATOM   361  C  C   . ILE A 1 49  ? 0.598   -20.598 -23.120 1.00 38.90  ? 49  ILE A C   1 
ATOM   362  O  O   . ILE A 1 49  ? 0.727   -19.669 -23.899 1.00 43.41  ? 49  ILE A O   1 
ATOM   363  C  CB  . ILE A 1 49  ? -1.543  -21.974 -23.138 1.00 48.74  ? 49  ILE A CB  1 
ATOM   364  C  CG1 . ILE A 1 49  ? -2.328  -22.988 -23.971 1.00 53.96  ? 49  ILE A CG1 1 
ATOM   365  C  CG2 . ILE A 1 49  ? -2.203  -20.611 -23.194 1.00 48.98  ? 49  ILE A CG2 1 
ATOM   366  C  CD1 . ILE A 1 49  ? -3.449  -23.645 -23.212 1.00 58.07  ? 49  ILE A CD1 1 
ATOM   367  N  N   . ARG A 1 50  ? 1.005   -20.529 -21.851 1.00 45.63  ? 50  ARG A N   1 
ATOM   368  C  CA  . ARG A 1 50  ? 1.701   -19.362 -21.319 1.00 45.44  ? 50  ARG A CA  1 
ATOM   369  C  C   . ARG A 1 50  ? 3.034   -19.138 -22.034 1.00 41.95  ? 50  ARG A C   1 
ATOM   370  O  O   . ARG A 1 50  ? 3.327   -18.009 -22.425 1.00 40.76  ? 50  ARG A O   1 
ATOM   371  C  CB  . ARG A 1 50  ? 1.907   -19.487 -19.807 1.00 45.62  ? 50  ARG A CB  1 
ATOM   372  C  CG  . ARG A 1 50  ? 0.759   -18.917 -18.989 1.00 42.96  ? 50  ARG A CG  1 
ATOM   373  C  CD  . ARG A 1 50  ? 0.720   -19.639 -17.677 1.00 44.15  ? 50  ARG A CD  1 
ATOM   374  N  NE  . ARG A 1 50  ? -0.468  -19.391 -16.878 1.00 48.02  ? 50  ARG A NE  1 
ATOM   375  C  CZ  . ARG A 1 50  ? -0.541  -19.661 -15.580 1.00 47.63  ? 50  ARG A CZ  1 
ATOM   376  N  NH1 . ARG A 1 50  ? 0.504   -20.162 -14.948 1.00 48.20  ? 50  ARG A NH1 1 
ATOM   377  N  NH2 . ARG A 1 50  ? -1.649  -19.420 -14.910 1.00 50.42  ? 50  ARG A NH2 1 
ATOM   378  N  N   . GLU A 1 51  ? 3.826   -20.200 -22.223 1.00 43.75  ? 51  GLU A N   1 
ATOM   379  C  CA  . GLU A 1 51  ? 5.173   -20.070 -22.780 1.00 46.01  ? 51  GLU A CA  1 
ATOM   380  C  C   . GLU A 1 51  ? 5.133   -19.452 -24.177 1.00 47.67  ? 51  GLU A C   1 
ATOM   381  O  O   . GLU A 1 51  ? 5.938   -18.565 -24.475 1.00 51.38  ? 51  GLU A O   1 
ATOM   382  C  CB  . GLU A 1 51  ? 5.893   -21.422 -22.786 1.00 48.70  ? 51  GLU A CB  1 
ATOM   383  C  CG  . GLU A 1 51  ? 7.218   -21.421 -23.535 1.00 52.14  ? 51  GLU A CG  1 
ATOM   384  C  CD  . GLU A 1 51  ? 8.225   -22.459 -23.058 1.00 61.25  ? 51  GLU A CD  1 
ATOM   385  O  OE1 . GLU A 1 51  ? 7.790   -23.615 -22.788 1.00 64.19  ? 51  GLU A OE1 1 
ATOM   386  O  OE2 . GLU A 1 51  ? 9.453   -22.114 -22.971 1.00 57.85  ? 51  GLU A OE2 1 
ATOM   387  N  N   . ILE A 1 52  ? 4.180   -19.890 -25.012 1.00 45.08  ? 52  ILE A N   1 
ATOM   388  C  CA  . ILE A 1 52  ? 4.107   -19.449 -26.399 1.00 41.87  ? 52  ILE A CA  1 
ATOM   389  C  C   . ILE A 1 52  ? 3.578   -18.017 -26.428 1.00 42.25  ? 52  ILE A C   1 
ATOM   390  O  O   . ILE A 1 52  ? 4.185   -17.150 -27.053 1.00 43.36  ? 52  ILE A O   1 
ATOM   391  C  CB  . ILE A 1 52  ? 3.253   -20.422 -27.244 1.00 42.00  ? 52  ILE A CB  1 
ATOM   392  C  CG1 . ILE A 1 52  ? 3.896   -21.810 -27.319 1.00 46.13  ? 52  ILE A CG1 1 
ATOM   393  C  CG2 . ILE A 1 52  ? 2.988   -19.879 -28.635 1.00 39.90  ? 52  ILE A CG2 1 
ATOM   394  C  CD1 . ILE A 1 52  ? 2.923   -22.917 -27.660 1.00 48.41  ? 52  ILE A CD1 1 
ATOM   395  N  N   A SER A 1 53  ? 2.455   -17.784 -25.737 0.50 40.99  ? 53  SER A N   1 
ATOM   396  N  N   B SER A 1 53  ? 2.432   -17.783 -25.776 0.50 41.21  ? 53  SER A N   1 
ATOM   397  C  CA  A SER A 1 53  ? 1.769   -16.500 -25.773 0.50 42.92  ? 53  SER A CA  1 
ATOM   398  C  CA  B SER A 1 53  ? 1.808   -16.469 -25.818 0.50 43.15  ? 53  SER A CA  1 
ATOM   399  C  C   A SER A 1 53  ? 2.660   -15.376 -25.229 0.50 41.84  ? 53  SER A C   1 
ATOM   400  C  C   B SER A 1 53  ? 2.799   -15.414 -25.328 0.50 41.42  ? 53  SER A C   1 
ATOM   401  O  O   A SER A 1 53  ? 2.645   -14.271 -25.754 0.50 42.70  ? 53  SER A O   1 
ATOM   402  O  O   B SER A 1 53  ? 3.031   -14.429 -26.013 0.50 40.91  ? 53  SER A O   1 
ATOM   403  C  CB  A SER A 1 53  ? 0.428   -16.585 -25.056 0.50 42.51  ? 53  SER A CB  1 
ATOM   404  C  CB  B SER A 1 53  ? 0.505   -16.417 -25.047 0.50 43.78  ? 53  SER A CB  1 
ATOM   405  O  OG  A SER A 1 53  ? 0.530   -17.336 -23.859 0.50 40.47  ? 53  SER A OG  1 
ATOM   406  O  OG  B SER A 1 53  ? -0.091  -15.129 -25.179 0.50 41.54  ? 53  SER A OG  1 
ATOM   407  N  N   . LEU A 1 54  ? 3.434   -15.648 -24.174 1.00 43.35  ? 54  LEU A N   1 
ATOM   408  C  CA  . LEU A 1 54  ? 4.326   -14.646 -23.592 1.00 42.73  ? 54  LEU A CA  1 
ATOM   409  C  C   . LEU A 1 54  ? 5.611   -14.492 -24.406 1.00 41.96  ? 54  LEU A C   1 
ATOM   410  O  O   . LEU A 1 54  ? 6.018   -13.366 -24.638 1.00 41.03  ? 54  LEU A O   1 
ATOM   411  C  CB  . LEU A 1 54  ? 4.588   -15.000 -22.127 1.00 46.55  ? 54  LEU A CB  1 
ATOM   412  C  CG  . LEU A 1 54  ? 3.326   -15.024 -21.262 1.00 47.00  ? 54  LEU A CG  1 
ATOM   413  C  CD1 . LEU A 1 54  ? 3.643   -15.419 -19.832 1.00 49.26  ? 54  LEU A CD1 1 
ATOM   414  C  CD2 . LEU A 1 54  ? 2.611   -13.681 -21.301 1.00 47.02  ? 54  LEU A CD2 1 
ATOM   415  N  N   . LEU A 1 55  ? 6.187   -15.585 -24.925 1.00 45.46  ? 55  LEU A N   1 
ATOM   416  C  CA  . LEU A 1 55  ? 7.368   -15.503 -25.783 1.00 45.84  ? 55  LEU A CA  1 
ATOM   417  C  C   . LEU A 1 55  ? 7.093   -14.807 -27.114 1.00 51.28  ? 55  LEU A C   1 
ATOM   418  O  O   . LEU A 1 55  ? 7.955   -14.086 -27.598 1.00 54.24  ? 55  LEU A O   1 
ATOM   419  C  CB  . LEU A 1 55  ? 7.922   -16.902 -26.050 1.00 46.67  ? 55  LEU A CB  1 
ATOM   420  C  CG  . LEU A 1 55  ? 8.957   -17.380 -25.036 1.00 45.97  ? 55  LEU A CG  1 
ATOM   421  C  CD1 . LEU A 1 55  ? 9.489   -18.742 -25.413 1.00 46.80  ? 55  LEU A CD1 1 
ATOM   422  C  CD2 . LEU A 1 55  ? 10.104  -16.395 -24.928 1.00 47.86  ? 55  LEU A CD2 1 
ATOM   423  N  N   . LYS A 1 56  ? 5.916   -15.023 -27.716 1.00 59.41  ? 56  LYS A N   1 
ATOM   424  C  CA  . LYS A 1 56  ? 5.566   -14.352 -28.963 1.00 56.39  ? 56  LYS A CA  1 
ATOM   425  C  C   . LYS A 1 56  ? 5.604   -12.831 -28.776 1.00 55.42  ? 56  LYS A C   1 
ATOM   426  O  O   . LYS A 1 56  ? 5.839   -12.109 -29.744 1.00 57.55  ? 56  LYS A O   1 
ATOM   427  C  CB  . LYS A 1 56  ? 4.214   -14.843 -29.497 1.00 60.71  ? 56  LYS A CB  1 
ATOM   428  C  CG  . LYS A 1 56  ? 4.273   -16.161 -30.267 1.00 63.65  ? 56  LYS A CG  1 
ATOM   429  C  CD  . LYS A 1 56  ? 3.149   -16.354 -31.279 1.00 70.07  ? 56  LYS A CD  1 
ATOM   430  C  CE  . LYS A 1 56  ? 3.115   -15.305 -32.374 1.00 73.06  ? 56  LYS A CE  1 
ATOM   431  N  NZ  . LYS A 1 56  ? 1.986   -15.518 -33.312 1.00 79.73  ? 56  LYS A NZ  1 
ATOM   432  N  N   . GLU A 1 57  ? 5.409   -12.353 -27.535 1.00 50.94  ? 57  GLU A N   1 
ATOM   433  C  CA  . GLU A 1 57  ? 5.392   -10.926 -27.228 1.00 58.66  ? 57  GLU A CA  1 
ATOM   434  C  C   . GLU A 1 57  ? 6.767   -10.374 -26.831 1.00 60.86  ? 57  GLU A C   1 
ATOM   435  O  O   . GLU A 1 57  ? 6.926   -9.154  -26.780 1.00 65.32  ? 57  GLU A O   1 
ATOM   436  C  CB  . GLU A 1 57  ? 4.390   -10.647 -26.103 1.00 69.47  ? 57  GLU A CB  1 
ATOM   437  C  CG  . GLU A 1 57  ? 2.965   -11.047 -26.463 1.00 83.75  ? 57  GLU A CG  1 
ATOM   438  C  CD  . GLU A 1 57  ? 1.852   -10.209 -25.858 1.00 94.43  ? 57  GLU A CD  1 
ATOM   439  O  OE1 . GLU A 1 57  ? 2.123   -9.491  -24.872 1.00 86.22  ? 57  GLU A OE1 1 
ATOM   440  O  OE2 . GLU A 1 57  ? 0.715   -10.259 -26.398 1.00 109.29 ? 57  GLU A OE2 1 
ATOM   441  N  N   . LEU A 1 58  ? 7.747   -11.245 -26.532 1.00 51.50  ? 58  LEU A N   1 
ATOM   442  C  CA  . LEU A 1 58  ? 9.031   -10.825 -25.974 1.00 52.42  ? 58  LEU A CA  1 
ATOM   443  C  C   . LEU A 1 58  ? 10.157  -10.964 -27.005 1.00 50.80  ? 58  LEU A C   1 
ATOM   444  O  O   . LEU A 1 58  ? 10.812  -12.009 -27.084 1.00 48.63  ? 58  LEU A O   1 
ATOM   445  C  CB  . LEU A 1 58  ? 9.341   -11.674 -24.738 1.00 50.99  ? 58  LEU A CB  1 
ATOM   446  C  CG  . LEU A 1 58  ? 8.405   -11.497 -23.548 1.00 44.51  ? 58  LEU A CG  1 
ATOM   447  C  CD1 . LEU A 1 58  ? 8.713   -12.529 -22.481 1.00 43.71  ? 58  LEU A CD1 1 
ATOM   448  C  CD2 . LEU A 1 58  ? 8.501   -10.094 -22.976 1.00 44.49  ? 58  LEU A CD2 1 
ATOM   449  N  N   . ASN A 1 59  ? 10.369  -9.888  -27.776 1.00 46.08  ? 59  ASN A N   1 
ATOM   450  C  CA  . ASN A 1 59  ? 11.436  -9.795  -28.761 1.00 49.96  ? 59  ASN A CA  1 
ATOM   451  C  C   . ASN A 1 59  ? 12.541  -8.916  -28.159 1.00 47.42  ? 59  ASN A C   1 
ATOM   452  O  O   . ASN A 1 59  ? 12.383  -7.691  -28.057 1.00 45.68  ? 59  ASN A O   1 
ATOM   453  C  CB  . ASN A 1 59  ? 10.898  -9.319  -30.118 1.00 62.35  ? 59  ASN A CB  1 
ATOM   454  C  CG  . ASN A 1 59  ? 12.000  -8.975  -31.100 1.00 79.32  ? 59  ASN A CG  1 
ATOM   455  O  OD1 . ASN A 1 59  ? 12.833  -9.820  -31.434 1.00 89.64  ? 59  ASN A OD1 1 
ATOM   456  N  ND2 . ASN A 1 59  ? 12.034  -7.726  -31.542 1.00 85.16  ? 59  ASN A ND2 1 
ATOM   457  N  N   . HIS A 1 60  ? 13.622  -9.575  -27.697 1.00 42.27  ? 60  HIS A N   1 
ATOM   458  C  CA  . HIS A 1 60  ? 14.740  -8.934  -27.007 1.00 41.51  ? 60  HIS A CA  1 
ATOM   459  C  C   . HIS A 1 60  ? 16.004  -9.756  -27.261 1.00 41.75  ? 60  HIS A C   1 
ATOM   460  O  O   . HIS A 1 60  ? 15.929  -10.978 -27.362 1.00 43.45  ? 60  HIS A O   1 
ATOM   461  C  CB  . HIS A 1 60  ? 14.447  -8.776  -25.509 1.00 40.96  ? 60  HIS A CB  1 
ATOM   462  C  CG  . HIS A 1 60  ? 15.326  -7.793  -24.810 1.00 42.63  ? 60  HIS A CG  1 
ATOM   463  N  ND1 . HIS A 1 60  ? 16.514  -8.153  -24.207 1.00 42.33  ? 60  HIS A ND1 1 
ATOM   464  C  CD2 . HIS A 1 60  ? 15.227  -6.463  -24.680 1.00 41.79  ? 60  HIS A CD2 1 
ATOM   465  C  CE1 . HIS A 1 60  ? 17.109  -7.068  -23.740 1.00 43.43  ? 60  HIS A CE1 1 
ATOM   466  N  NE2 . HIS A 1 60  ? 16.337  -6.028  -24.002 1.00 42.72  ? 60  HIS A NE2 1 
ATOM   467  N  N   . PRO A 1 61  ? 17.186  -9.114  -27.407 1.00 44.87  ? 61  PRO A N   1 
ATOM   468  C  CA  . PRO A 1 61  ? 18.459  -9.830  -27.566 1.00 47.54  ? 61  PRO A CA  1 
ATOM   469  C  C   . PRO A 1 61  ? 18.817  -10.822 -26.461 1.00 49.73  ? 61  PRO A C   1 
ATOM   470  O  O   . PRO A 1 61  ? 19.562  -11.763 -26.700 1.00 49.28  ? 61  PRO A O   1 
ATOM   471  C  CB  . PRO A 1 61  ? 19.523  -8.722  -27.510 1.00 46.06  ? 61  PRO A CB  1 
ATOM   472  C  CG  . PRO A 1 61  ? 18.783  -7.470  -27.939 1.00 47.07  ? 61  PRO A CG  1 
ATOM   473  C  CD  . PRO A 1 61  ? 17.353  -7.653  -27.473 1.00 46.25  ? 61  PRO A CD  1 
ATOM   474  N  N   . ASN A 1 62  ? 18.297  -10.580 -25.253 1.00 48.91  ? 62  ASN A N   1 
ATOM   475  C  CA  . ASN A 1 62  ? 18.641  -11.360 -24.075 1.00 48.26  ? 62  ASN A CA  1 
ATOM   476  C  C   . ASN A 1 62  ? 17.469  -12.251 -23.664 1.00 46.18  ? 62  ASN A C   1 
ATOM   477  O  O   . ASN A 1 62  ? 17.452  -12.749 -22.542 1.00 41.99  ? 62  ASN A O   1 
ATOM   478  C  CB  . ASN A 1 62  ? 19.113  -10.421 -22.966 1.00 46.34  ? 62  ASN A CB  1 
ATOM   479  C  CG  . ASN A 1 62  ? 20.356  -9.670  -23.381 1.00 46.56  ? 62  ASN A CG  1 
ATOM   480  O  OD1 . ASN A 1 62  ? 20.325  -8.451  -23.535 1.00 43.91  ? 62  ASN A OD1 1 
ATOM   481  N  ND2 . ASN A 1 62  ? 21.432  -10.410 -23.609 1.00 43.73  ? 62  ASN A ND2 1 
ATOM   482  N  N   . ILE A 1 63  ? 16.523  -12.475 -24.590 1.00 43.77  ? 63  ILE A N   1 
ATOM   483  C  CA  . ILE A 1 63  ? 15.477  -13.475 -24.421 1.00 42.06  ? 63  ILE A CA  1 
ATOM   484  C  C   . ILE A 1 63  ? 15.491  -14.451 -25.601 1.00 39.18  ? 63  ILE A C   1 
ATOM   485  O  O   . ILE A 1 63  ? 15.471  -14.018 -26.750 1.00 40.38  ? 63  ILE A O   1 
ATOM   486  C  CB  . ILE A 1 63  ? 14.115  -12.775 -24.259 1.00 39.79  ? 63  ILE A CB  1 
ATOM   487  C  CG1 . ILE A 1 63  ? 14.190  -11.787 -23.096 1.00 40.47  ? 63  ILE A CG1 1 
ATOM   488  C  CG2 . ILE A 1 63  ? 13.000  -13.796 -24.082 1.00 38.50  ? 63  ILE A CG2 1 
ATOM   489  C  CD1 . ILE A 1 63  ? 12.946  -10.979 -22.865 1.00 46.93  ? 63  ILE A CD1 1 
ATOM   490  N  N   . ILE A 1 64  ? 15.464  -15.762 -25.297 1.00 35.17  ? 64  ILE A N   1 
ATOM   491  C  CA  . ILE A 1 64  ? 15.431  -16.837 -26.288 1.00 37.42  ? 64  ILE A CA  1 
ATOM   492  C  C   . ILE A 1 64  ? 14.410  -16.493 -27.388 1.00 44.87  ? 64  ILE A C   1 
ATOM   493  O  O   . ILE A 1 64  ? 13.321  -15.995 -27.094 1.00 35.84  ? 64  ILE A O   1 
ATOM   494  C  CB  . ILE A 1 64  ? 15.175  -18.198 -25.587 1.00 38.76  ? 64  ILE A CB  1 
ATOM   495  C  CG1 . ILE A 1 64  ? 15.549  -19.402 -26.454 1.00 41.65  ? 64  ILE A CG1 1 
ATOM   496  C  CG2 . ILE A 1 64  ? 13.752  -18.330 -25.064 1.00 39.35  ? 64  ILE A CG2 1 
ATOM   497  C  CD1 . ILE A 1 64  ? 17.036  -19.576 -26.637 1.00 43.91  ? 64  ILE A CD1 1 
ATOM   498  N  N   . LYS A 1 65  ? 14.799  -16.711 -28.663 1.00 51.39  ? 65  LYS A N   1 
ATOM   499  C  CA  . LYS A 1 65  ? 13.916  -16.572 -29.826 1.00 52.68  ? 65  LYS A CA  1 
ATOM   500  C  C   . LYS A 1 65  ? 13.107  -17.852 -30.058 1.00 48.60  ? 65  LYS A C   1 
ATOM   501  O  O   . LYS A 1 65  ? 13.684  -18.921 -30.283 1.00 41.61  ? 65  LYS A O   1 
ATOM   502  C  CB  . LYS A 1 65  ? 14.720  -16.223 -31.085 1.00 57.63  ? 65  LYS A CB  1 
ATOM   503  C  CG  . LYS A 1 65  ? 15.083  -14.750 -31.195 1.00 66.12  ? 65  LYS A CG  1 
ATOM   504  C  CD  . LYS A 1 65  ? 16.171  -14.429 -32.196 1.00 73.83  ? 65  LYS A CD  1 
ATOM   505  C  CE  . LYS A 1 65  ? 16.797  -13.078 -31.911 1.00 81.13  ? 65  LYS A CE  1 
ATOM   506  N  NZ  . LYS A 1 65  ? 16.854  -12.229 -33.123 1.00 84.80  ? 65  LYS A NZ  1 
ATOM   507  N  N   . LEU A 1 66  ? 11.768  -17.729 -29.979 1.00 49.79  ? 66  LEU A N   1 
ATOM   508  C  CA  . LEU A 1 66  ? 10.839  -18.747 -30.468 1.00 50.67  ? 66  LEU A CA  1 
ATOM   509  C  C   . LEU A 1 66  ? 10.726  -18.564 -31.980 1.00 52.67  ? 66  LEU A C   1 
ATOM   510  O  O   . LEU A 1 66  ? 10.377  -17.475 -32.433 1.00 52.25  ? 66  LEU A O   1 
ATOM   511  C  CB  . LEU A 1 66  ? 9.467   -18.598 -29.792 1.00 46.51  ? 66  LEU A CB  1 
ATOM   512  C  CG  . LEU A 1 66  ? 8.402   -19.619 -30.197 1.00 45.00  ? 66  LEU A CG  1 
ATOM   513  C  CD1 . LEU A 1 66  ? 8.748   -21.026 -29.733 1.00 45.67  ? 66  LEU A CD1 1 
ATOM   514  C  CD2 . LEU A 1 66  ? 7.043   -19.231 -29.640 1.00 50.14  ? 66  LEU A CD2 1 
ATOM   515  N  N   . LEU A 1 67  ? 11.099  -19.596 -32.750 1.00 50.08  ? 67  LEU A N   1 
ATOM   516  C  CA  . LEU A 1 67  ? 11.155  -19.479 -34.199 1.00 51.44  ? 67  LEU A CA  1 
ATOM   517  C  C   . LEU A 1 67  ? 9.810   -19.871 -34.805 1.00 49.24  ? 67  LEU A C   1 
ATOM   518  O  O   . LEU A 1 67  ? 9.339   -19.188 -35.711 1.00 47.13  ? 67  LEU A O   1 
ATOM   519  C  CB  . LEU A 1 67  ? 12.283  -20.348 -34.763 1.00 48.55  ? 67  LEU A CB  1 
ATOM   520  C  CG  . LEU A 1 67  ? 13.693  -19.981 -34.315 1.00 48.12  ? 67  LEU A CG  1 
ATOM   521  C  CD1 . LEU A 1 67  ? 14.707  -20.793 -35.100 1.00 48.33  ? 67  LEU A CD1 1 
ATOM   522  C  CD2 . LEU A 1 67  ? 13.960  -18.492 -34.467 1.00 47.86  ? 67  LEU A CD2 1 
ATOM   523  N  N   . ASP A 1 68  ? 9.229   -20.972 -34.314 1.00 49.37  ? 68  ASP A N   1 
ATOM   524  C  CA  . ASP A 1 68  ? 8.020   -21.546 -34.885 1.00 52.08  ? 68  ASP A CA  1 
ATOM   525  C  C   . ASP A 1 68  ? 7.331   -22.442 -33.858 1.00 49.08  ? 68  ASP A C   1 
ATOM   526  O  O   . ASP A 1 68  ? 7.975   -22.945 -32.933 1.00 47.94  ? 68  ASP A O   1 
ATOM   527  C  CB  . ASP A 1 68  ? 8.335   -22.366 -36.141 1.00 62.50  ? 68  ASP A CB  1 
ATOM   528  C  CG  . ASP A 1 68  ? 7.196   -22.478 -37.148 1.00 72.91  ? 68  ASP A CG  1 
ATOM   529  O  OD1 . ASP A 1 68  ? 6.195   -21.735 -37.002 1.00 81.03  ? 68  ASP A OD1 1 
ATOM   530  O  OD2 . ASP A 1 68  ? 7.320   -23.304 -38.082 1.00 78.12  ? 68  ASP A OD2 1 
ATOM   531  N  N   . VAL A 1 69  ? 6.022   -22.652 -34.070 1.00 46.64  ? 69  VAL A N   1 
ATOM   532  C  CA  . VAL A 1 69  ? 5.192   -23.597 -33.330 1.00 45.35  ? 69  VAL A CA  1 
ATOM   533  C  C   . VAL A 1 69  ? 4.578   -24.567 -34.341 1.00 45.69  ? 69  VAL A C   1 
ATOM   534  O  O   . VAL A 1 69  ? 3.870   -24.118 -35.222 1.00 46.18  ? 69  VAL A O   1 
ATOM   535  C  CB  . VAL A 1 69  ? 4.083   -22.840 -32.564 1.00 45.34  ? 69  VAL A CB  1 
ATOM   536  C  CG1 . VAL A 1 69  ? 3.167   -23.763 -31.772 1.00 48.61  ? 69  VAL A CG1 1 
ATOM   537  C  CG2 . VAL A 1 69  ? 4.658   -21.767 -31.661 1.00 45.65  ? 69  VAL A CG2 1 
ATOM   538  N  N   . ILE A 1 70  ? 4.831   -25.878 -34.230 1.00 50.90  ? 70  ILE A N   1 
ATOM   539  C  CA  . ILE A 1 70  ? 4.159   -26.878 -35.060 1.00 55.65  ? 70  ILE A CA  1 
ATOM   540  C  C   . ILE A 1 70  ? 3.135   -27.633 -34.201 1.00 57.31  ? 70  ILE A C   1 
ATOM   541  O  O   . ILE A 1 70  ? 3.522   -28.360 -33.285 1.00 56.18  ? 70  ILE A O   1 
ATOM   542  C  CB  . ILE A 1 70  ? 5.174   -27.835 -35.728 1.00 61.30  ? 70  ILE A CB  1 
ATOM   543  C  CG1 . ILE A 1 70  ? 5.950   -27.152 -36.860 1.00 64.52  ? 70  ILE A CG1 1 
ATOM   544  C  CG2 . ILE A 1 70  ? 4.489   -29.101 -36.228 1.00 61.40  ? 70  ILE A CG2 1 
ATOM   545  C  CD1 . ILE A 1 70  ? 7.104   -26.300 -36.391 1.00 65.18  ? 70  ILE A CD1 1 
ATOM   546  N  N   A HIS A 1 71  ? 1.839   -27.438 -34.507 0.50 58.16  ? 71  HIS A N   1 
ATOM   547  N  N   B HIS A 1 71  ? 1.851   -27.514 -34.574 0.50 63.58  ? 71  HIS A N   1 
ATOM   548  C  CA  A HIS A 1 71  ? 0.719   -27.954 -33.717 0.50 59.27  ? 71  HIS A CA  1 
ATOM   549  C  CA  B HIS A 1 71  ? 0.715   -27.929 -33.756 0.50 69.31  ? 71  HIS A CA  1 
ATOM   550  C  C   A HIS A 1 71  ? -0.226  -28.770 -34.606 0.50 64.49  ? 71  HIS A C   1 
ATOM   551  C  C   B HIS A 1 71  ? -0.262  -28.761 -34.595 0.50 70.31  ? 71  HIS A C   1 
ATOM   552  O  O   A HIS A 1 71  ? -0.790  -28.240 -35.567 0.50 60.21  ? 71  HIS A O   1 
ATOM   553  O  O   B HIS A 1 71  ? -0.888  -28.231 -35.516 0.50 66.25  ? 71  HIS A O   1 
ATOM   554  C  CB  A HIS A 1 71  ? -0.014  -26.808 -32.996 0.50 55.40  ? 71  HIS A CB  1 
ATOM   555  C  CB  B HIS A 1 71  ? 0.088   -26.682 -33.107 0.50 72.74  ? 71  HIS A CB  1 
ATOM   556  C  CG  A HIS A 1 71  ? -1.026  -27.237 -31.973 0.50 52.59  ? 71  HIS A CG  1 
ATOM   557  C  CG  B HIS A 1 71  ? -1.389  -26.723 -32.866 0.50 77.82  ? 71  HIS A CG  1 
ATOM   558  N  ND1 A HIS A 1 71  ? -0.909  -28.406 -31.252 0.50 50.23  ? 71  HIS A ND1 1 
ATOM   559  N  ND1 B HIS A 1 71  ? -2.211  -25.669 -33.210 0.50 77.86  ? 71  HIS A ND1 1 
ATOM   560  C  CD2 A HIS A 1 71  ? -2.174  -26.668 -31.569 0.50 50.60  ? 71  HIS A CD2 1 
ATOM   561  C  CD2 B HIS A 1 71  ? -2.184  -27.644 -32.301 0.50 78.56  ? 71  HIS A CD2 1 
ATOM   562  C  CE1 A HIS A 1 71  ? -1.951  -28.530 -30.445 0.50 49.57  ? 71  HIS A CE1 1 
ATOM   563  C  CE1 B HIS A 1 71  ? -3.460  -25.960 -32.880 0.50 74.05  ? 71  HIS A CE1 1 
ATOM   564  N  NE2 A HIS A 1 71  ? -2.725  -27.481 -30.613 0.50 49.28  ? 71  HIS A NE2 1 
ATOM   565  N  NE2 B HIS A 1 71  ? -3.468  -27.157 -32.330 0.50 78.25  ? 71  HIS A NE2 1 
ATOM   566  N  N   . THR A 1 72  ? -0.363  -30.065 -34.271 1.00 69.05  ? 72  THR A N   1 
ATOM   567  C  CA  . THR A 1 72  ? -1.338  -30.990 -34.851 1.00 74.47  ? 72  THR A CA  1 
ATOM   568  C  C   . THR A 1 72  ? -2.253  -31.433 -33.704 1.00 79.82  ? 72  THR A C   1 
ATOM   569  O  O   . THR A 1 72  ? -2.223  -30.792 -32.654 1.00 72.97  ? 72  THR A O   1 
ATOM   570  C  CB  . THR A 1 72  ? -0.625  -32.159 -35.555 1.00 77.59  ? 72  THR A CB  1 
ATOM   571  O  OG1 . THR A 1 72  ? -0.120  -33.069 -34.577 1.00 73.51  ? 72  THR A OG1 1 
ATOM   572  C  CG2 . THR A 1 72  ? 0.519   -31.718 -36.447 1.00 78.95  ? 72  THR A CG2 1 
ATOM   573  N  N   . GLU A 1 73  ? -3.062  -32.497 -33.883 1.00 91.08  ? 73  GLU A N   1 
ATOM   574  C  CA  . GLU A 1 73  ? -3.644  -33.218 -32.746 1.00 100.78 ? 73  GLU A CA  1 
ATOM   575  C  C   . GLU A 1 73  ? -2.606  -34.247 -32.274 1.00 99.35  ? 73  GLU A C   1 
ATOM   576  O  O   . GLU A 1 73  ? -1.862  -34.777 -33.098 1.00 90.65  ? 73  GLU A O   1 
ATOM   577  C  CB  . GLU A 1 73  ? -5.003  -33.855 -33.085 1.00 110.67 ? 73  GLU A CB  1 
ATOM   578  C  CG  . GLU A 1 73  ? -5.873  -34.183 -31.860 1.00 118.06 ? 73  GLU A CG  1 
ATOM   579  C  CD  . GLU A 1 73  ? -6.628  -33.029 -31.207 1.00 119.41 ? 73  GLU A CD  1 
ATOM   580  O  OE1 . GLU A 1 73  ? -6.943  -32.055 -31.918 1.00 123.76 ? 73  GLU A OE1 1 
ATOM   581  O  OE2 . GLU A 1 73  ? -6.907  -33.101 -29.985 1.00 105.11 ? 73  GLU A OE2 1 
ATOM   582  N  N   . ASN A 1 74  ? -2.555  -34.491 -30.949 1.00 103.22 ? 74  ASN A N   1 
ATOM   583  C  CA  . ASN A 1 74  ? -1.550  -35.287 -30.230 1.00 108.22 ? 74  ASN A CA  1 
ATOM   584  C  C   . ASN A 1 74  ? -0.120  -35.070 -30.755 1.00 92.03  ? 74  ASN A C   1 
ATOM   585  O  O   . ASN A 1 74  ? 0.628   -36.029 -30.933 1.00 96.69  ? 74  ASN A O   1 
ATOM   586  C  CB  . ASN A 1 74  ? -1.965  -36.765 -30.071 1.00 113.60 ? 74  ASN A CB  1 
ATOM   587  C  CG  . ASN A 1 74  ? -2.105  -37.564 -31.353 1.00 113.35 ? 74  ASN A CG  1 
ATOM   588  O  OD1 . ASN A 1 74  ? -1.653  -37.147 -32.417 1.00 119.47 ? 74  ASN A OD1 1 
ATOM   589  N  ND2 . ASN A 1 74  ? -2.705  -38.741 -31.254 1.00 105.15 ? 74  ASN A ND2 1 
ATOM   590  N  N   . LYS A 1 75  ? 0.285   -33.797 -30.911 1.00 77.89  ? 75  LYS A N   1 
ATOM   591  C  CA  . LYS A 1 75  ? 1.669   -33.422 -31.198 1.00 76.50  ? 75  LYS A CA  1 
ATOM   592  C  C   . LYS A 1 75  ? 1.821   -31.890 -31.170 1.00 64.42  ? 75  LYS A C   1 
ATOM   593  O  O   . LYS A 1 75  ? 1.129   -31.187 -31.905 1.00 67.61  ? 75  LYS A O   1 
ATOM   594  C  CB  . LYS A 1 75  ? 2.077   -34.081 -32.525 1.00 87.82  ? 75  LYS A CB  1 
ATOM   595  C  CG  . LYS A 1 75  ? 2.997   -33.291 -33.447 1.00 92.73  ? 75  LYS A CG  1 
ATOM   596  C  CD  . LYS A 1 75  ? 3.220   -33.948 -34.812 1.00 99.82  ? 75  LYS A CD  1 
ATOM   597  C  CE  . LYS A 1 75  ? 3.830   -35.335 -34.740 1.00 99.58  ? 75  LYS A CE  1 
ATOM   598  N  NZ  . LYS A 1 75  ? 4.517   -35.702 -36.002 1.00 93.16  ? 75  LYS A NZ  1 
ATOM   599  N  N   . LEU A 1 76  ? 2.714   -31.368 -30.307 1.00 53.44  ? 76  LEU A N   1 
ATOM   600  C  CA  . LEU A 1 76  ? 3.024   -29.936 -30.249 1.00 51.53  ? 76  LEU A CA  1 
ATOM   601  C  C   . LEU A 1 76  ? 4.537   -29.742 -30.110 1.00 51.16  ? 76  LEU A C   1 
ATOM   602  O  O   . LEU A 1 76  ? 5.106   -30.154 -29.106 1.00 54.07  ? 76  LEU A O   1 
ATOM   603  C  CB  . LEU A 1 76  ? 2.301   -29.281 -29.058 1.00 49.41  ? 76  LEU A CB  1 
ATOM   604  C  CG  . LEU A 1 76  ? 2.597   -27.794 -28.823 1.00 49.28  ? 76  LEU A CG  1 
ATOM   605  C  CD1 . LEU A 1 76  ? 2.271   -26.958 -30.048 1.00 47.65  ? 76  LEU A CD1 1 
ATOM   606  C  CD2 . LEU A 1 76  ? 1.815   -27.259 -27.637 1.00 53.07  ? 76  LEU A CD2 1 
ATOM   607  N  N   . TYR A 1 77  ? 5.177   -29.098 -31.098 1.00 48.71  ? 77  TYR A N   1 
ATOM   608  C  CA  . TYR A 1 77  ? 6.615   -28.840 -31.080 1.00 47.36  ? 77  TYR A CA  1 
ATOM   609  C  C   . TYR A 1 77  ? 6.848   -27.330 -31.002 1.00 41.89  ? 77  TYR A C   1 
ATOM   610  O  O   . TYR A 1 77  ? 6.149   -26.566 -31.657 1.00 38.16  ? 77  TYR A O   1 
ATOM   611  C  CB  . TYR A 1 77  ? 7.307   -29.436 -32.315 1.00 51.37  ? 77  TYR A CB  1 
ATOM   612  C  CG  . TYR A 1 77  ? 7.239   -30.938 -32.476 1.00 53.10  ? 77  TYR A CG  1 
ATOM   613  C  CD1 . TYR A 1 77  ? 8.155   -31.776 -31.861 1.00 59.01  ? 77  TYR A CD1 1 
ATOM   614  C  CD2 . TYR A 1 77  ? 6.281   -31.527 -33.282 1.00 58.25  ? 77  TYR A CD2 1 
ATOM   615  C  CE1 . TYR A 1 77  ? 8.115   -33.154 -32.029 1.00 65.51  ? 77  TYR A CE1 1 
ATOM   616  C  CE2 . TYR A 1 77  ? 6.221   -32.903 -33.452 1.00 64.99  ? 77  TYR A CE2 1 
ATOM   617  C  CZ  . TYR A 1 77  ? 7.135   -33.727 -32.820 1.00 69.19  ? 77  TYR A CZ  1 
ATOM   618  O  OH  . TYR A 1 77  ? 7.068   -35.099 -32.982 1.00 77.05  ? 77  TYR A OH  1 
ATOM   619  N  N   . LEU A 1 78  ? 7.805   -26.909 -30.163 1.00 43.88  ? 78  LEU A N   1 
ATOM   620  C  CA  . LEU A 1 78  ? 8.311   -25.542 -30.157 1.00 43.51  ? 78  LEU A CA  1 
ATOM   621  C  C   . LEU A 1 78  ? 9.713   -25.537 -30.756 1.00 45.82  ? 78  LEU A C   1 
ATOM   622  O  O   . LEU A 1 78  ? 10.531  -26.379 -30.400 1.00 40.22  ? 78  LEU A O   1 
ATOM   623  C  CB  . LEU A 1 78  ? 8.340   -25.010 -28.723 1.00 48.20  ? 78  LEU A CB  1 
ATOM   624  C  CG  . LEU A 1 78  ? 7.039   -24.407 -28.207 1.00 51.35  ? 78  LEU A CG  1 
ATOM   625  C  CD1 . LEU A 1 78  ? 5.829   -25.244 -28.598 1.00 54.60  ? 78  LEU A CD1 1 
ATOM   626  C  CD2 . LEU A 1 78  ? 7.104   -24.250 -26.702 1.00 52.44  ? 78  LEU A CD2 1 
ATOM   627  N  N   . VAL A 1 79  ? 9.974   -24.593 -31.671 1.00 45.62  ? 79  VAL A N   1 
ATOM   628  C  CA  . VAL A 1 79  ? 11.259  -24.503 -32.348 1.00 39.71  ? 79  VAL A CA  1 
ATOM   629  C  C   . VAL A 1 79  ? 11.949  -23.227 -31.888 1.00 36.43  ? 79  VAL A C   1 
ATOM   630  O  O   . VAL A 1 79  ? 11.503  -22.125 -32.212 1.00 34.67  ? 79  VAL A O   1 
ATOM   631  C  CB  . VAL A 1 79  ? 11.105  -24.511 -33.879 1.00 41.89  ? 79  VAL A CB  1 
ATOM   632  C  CG1 . VAL A 1 79  ? 12.458  -24.418 -34.580 1.00 45.01  ? 79  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A 1 79  ? 10.339  -25.730 -34.371 1.00 41.97  ? 79  VAL A CG2 1 
ATOM   634  N  N   . PHE A 1 80  ? 13.073  -23.392 -31.187 1.00 35.71  ? 80  PHE A N   1 
ATOM   635  C  CA  . PHE A 1 80  ? 13.798  -22.272 -30.614 1.00 35.37  ? 80  PHE A CA  1 
ATOM   636  C  C   . PHE A 1 80  ? 15.140  -22.159 -31.316 1.00 34.91  ? 80  PHE A C   1 
ATOM   637  O  O   . PHE A 1 80  ? 15.615  -23.162 -31.845 1.00 35.97  ? 80  PHE A O   1 
ATOM   638  C  CB  . PHE A 1 80  ? 14.026  -22.521 -29.123 1.00 37.91  ? 80  PHE A CB  1 
ATOM   639  C  CG  . PHE A 1 80  ? 12.807  -22.488 -28.241 1.00 33.18  ? 80  PHE A CG  1 
ATOM   640  C  CD1 . PHE A 1 80  ? 12.393  -21.302 -27.667 1.00 35.19  ? 80  PHE A CD1 1 
ATOM   641  C  CD2 . PHE A 1 80  ? 12.131  -23.651 -27.924 1.00 37.47  ? 80  PHE A CD2 1 
ATOM   642  C  CE1 . PHE A 1 80  ? 11.286  -21.267 -26.834 1.00 36.18  ? 80  PHE A CE1 1 
ATOM   643  C  CE2 . PHE A 1 80  ? 11.022  -23.619 -27.093 1.00 37.52  ? 80  PHE A CE2 1 
ATOM   644  C  CZ  . PHE A 1 80  ? 10.611  -22.428 -26.541 1.00 36.48  ? 80  PHE A CZ  1 
ATOM   645  N  N   . GLU A 1 81  ? 15.779  -20.986 -31.243 1.00 36.16  ? 81  GLU A N   1 
ATOM   646  C  CA  . GLU A 1 81  ? 17.185  -20.901 -31.613 1.00 39.17  ? 81  GLU A CA  1 
ATOM   647  C  C   . GLU A 1 81  ? 18.001  -21.830 -30.707 1.00 39.44  ? 81  GLU A C   1 
ATOM   648  O  O   . GLU A 1 81  ? 17.730  -21.912 -29.522 1.00 40.36  ? 81  GLU A O   1 
ATOM   649  C  CB  . GLU A 1 81  ? 17.691  -19.464 -31.537 1.00 40.74  ? 81  GLU A CB  1 
ATOM   650  C  CG  . GLU A 1 81  ? 17.787  -18.893 -30.149 1.00 45.05  ? 81  GLU A CG  1 
ATOM   651  C  CD  . GLU A 1 81  ? 18.194  -17.426 -30.138 1.00 53.48  ? 81  GLU A CD  1 
ATOM   652  O  OE1 . GLU A 1 81  ? 19.102  -17.057 -30.920 1.00 60.96  ? 81  GLU A OE1 1 
ATOM   653  O  OE2 . GLU A 1 81  ? 17.600  -16.645 -29.354 1.00 58.72  ? 81  GLU A OE2 1 
ATOM   654  N  N   . PHE A 1 82  ? 18.970  -22.559 -31.277 1.00 41.79  ? 82  PHE A N   1 
ATOM   655  C  CA  . PHE A 1 82  ? 19.869  -23.430 -30.526 1.00 43.88  ? 82  PHE A CA  1 
ATOM   656  C  C   . PHE A 1 82  ? 20.998  -22.603 -29.892 1.00 46.15  ? 82  PHE A C   1 
ATOM   657  O  O   . PHE A 1 82  ? 21.622  -21.777 -30.559 1.00 50.24  ? 82  PHE A O   1 
ATOM   658  C  CB  . PHE A 1 82  ? 20.441  -24.535 -31.424 1.00 42.25  ? 82  PHE A CB  1 
ATOM   659  C  CG  . PHE A 1 82  ? 21.461  -25.390 -30.724 1.00 41.68  ? 82  PHE A CG  1 
ATOM   660  C  CD1 . PHE A 1 82  ? 21.060  -26.371 -29.839 1.00 40.72  ? 82  PHE A CD1 1 
ATOM   661  C  CD2 . PHE A 1 82  ? 22.820  -25.164 -30.895 1.00 44.04  ? 82  PHE A CD2 1 
ATOM   662  C  CE1 . PHE A 1 82  ? 21.996  -27.130 -29.154 1.00 45.18  ? 82  PHE A CE1 1 
ATOM   663  C  CE2 . PHE A 1 82  ? 23.756  -25.934 -30.225 1.00 45.56  ? 82  PHE A CE2 1 
ATOM   664  C  CZ  . PHE A 1 82  ? 23.341  -26.907 -29.345 1.00 46.32  ? 82  PHE A CZ  1 
ATOM   665  N  N   A MET A 1 83  ? 21.245  -22.825 -28.594 0.50 46.31  ? 83  MET A N   1 
ATOM   666  N  N   B MET A 1 83  ? 21.252  -22.847 -28.599 0.50 43.56  ? 83  MET A N   1 
ATOM   667  C  CA  A MET A 1 83  ? 22.291  -22.123 -27.862 0.50 45.62  ? 83  MET A CA  1 
ATOM   668  C  CA  B MET A 1 83  ? 22.284  -22.149 -27.842 0.50 41.12  ? 83  MET A CA  1 
ATOM   669  C  C   A MET A 1 83  ? 23.385  -23.122 -27.489 0.50 45.48  ? 83  MET A C   1 
ATOM   670  C  C   B MET A 1 83  ? 23.391  -23.139 -27.492 0.50 42.97  ? 83  MET A C   1 
ATOM   671  O  O   A MET A 1 83  ? 23.083  -24.209 -27.002 0.50 44.30  ? 83  MET A O   1 
ATOM   672  O  O   B MET A 1 83  ? 23.102  -24.238 -27.024 0.50 42.13  ? 83  MET A O   1 
ATOM   673  C  CB  A MET A 1 83  ? 21.717  -21.477 -26.600 0.50 46.71  ? 83  MET A CB  1 
ATOM   674  C  CB  B MET A 1 83  ? 21.693  -21.562 -26.561 0.50 38.85  ? 83  MET A CB  1 
ATOM   675  C  CG  A MET A 1 83  ? 20.590  -20.498 -26.892 0.50 47.83  ? 83  MET A CG  1 
ATOM   676  C  CG  B MET A 1 83  ? 20.433  -20.767 -26.830 0.50 36.90  ? 83  MET A CG  1 
ATOM   677  S  SD  A MET A 1 83  ? 21.183  -18.827 -27.247 0.50 52.91  ? 83  MET A SD  1 
ATOM   678  S  SD  B MET A 1 83  ? 20.771  -19.289 -27.788 0.50 35.45  ? 83  MET A SD  1 
ATOM   679  C  CE  A MET A 1 83  ? 21.296  -18.917 -29.033 0.50 55.57  ? 83  MET A CE  1 
ATOM   680  C  CE  B MET A 1 83  ? 21.449  -18.191 -26.539 0.50 33.70  ? 83  MET A CE  1 
ATOM   681  N  N   . GLU A 1 84  ? 24.645  -22.734 -27.745 1.00 49.49  ? 84  GLU A N   1 
ATOM   682  C  CA  . GLU A 1 84  ? 25.819  -23.596 -27.643 1.00 52.58  ? 84  GLU A CA  1 
ATOM   683  C  C   . GLU A 1 84  ? 26.045  -24.075 -26.213 1.00 48.88  ? 84  GLU A C   1 
ATOM   684  O  O   . GLU A 1 84  ? 26.352  -25.248 -26.009 1.00 50.35  ? 84  GLU A O   1 
ATOM   685  C  CB  . GLU A 1 84  ? 27.062  -22.855 -28.153 1.00 66.16  ? 84  GLU A CB  1 
ATOM   686  C  CG  . GLU A 1 84  ? 27.311  -23.041 -29.643 1.00 80.95  ? 84  GLU A CG  1 
ATOM   687  C  CD  . GLU A 1 84  ? 28.160  -24.241 -30.035 1.00 93.28  ? 84  GLU A CD  1 
ATOM   688  O  OE1 . GLU A 1 84  ? 28.782  -24.857 -29.136 1.00 96.06  ? 84  GLU A OE1 1 
ATOM   689  O  OE2 . GLU A 1 84  ? 28.206  -24.554 -31.248 1.00 103.71 ? 84  GLU A OE2 1 
ATOM   690  N  N   . THR A 1 85  ? 25.917  -23.168 -25.236 1.00 46.65  ? 85  THR A N   1 
ATOM   691  C  CA  . THR A 1 85  ? 26.230  -23.490 -23.844 1.00 49.39  ? 85  THR A CA  1 
ATOM   692  C  C   . THR A 1 85  ? 25.183  -22.885 -22.895 1.00 46.27  ? 85  THR A C   1 
ATOM   693  O  O   . THR A 1 85  ? 24.192  -22.305 -23.336 1.00 48.67  ? 85  THR A O   1 
ATOM   694  C  CB  . THR A 1 85  ? 27.701  -23.140 -23.569 1.00 44.64  ? 85  THR A CB  1 
ATOM   695  O  OG1 . THR A 1 85  ? 28.036  -23.607 -22.264 1.00 48.64  ? 85  THR A OG1 1 
ATOM   696  C  CG2 . THR A 1 85  ? 28.008  -21.665 -23.653 1.00 45.75  ? 85  THR A CG2 1 
ATOM   697  N  N   . ASP A 1 86  ? 25.349  -23.098 -21.581 1.00 46.62  ? 86  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 86  ? 24.478  -22.507 -20.563 1.00 47.71  ? 86  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 86  ? 25.335  -22.089 -19.369 1.00 44.32  ? 86  ASP A C   1 
ATOM   700  O  O   . ASP A 1 86  ? 26.525  -22.387 -19.337 1.00 49.81  ? 86  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 86  ? 23.303  -23.428 -20.203 1.00 47.60  ? 86  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 86  ? 23.686  -24.734 -19.530 1.00 54.83  ? 86  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 86  ? 24.456  -24.676 -18.559 1.00 67.77  ? 86  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 86  ? 23.186  -25.800 -19.960 1.00 62.87  ? 86  ASP A OD2 1 
ATOM   705  N  N   . LEU A 1 87  ? 24.744  -21.378 -18.399 1.00 41.50  ? 87  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 87  ? 25.530  -20.801 -17.324 1.00 42.80  ? 87  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 87  ? 26.006  -21.913 -16.385 1.00 47.86  ? 87  LEU A C   1 
ATOM   708  O  O   . LEU A 1 87  ? 27.158  -21.891 -15.962 1.00 52.01  ? 87  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 87  ? 24.736  -19.716 -16.592 1.00 39.64  ? 87  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 87  ? 25.559  -18.863 -15.625 1.00 40.24  ? 87  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 87  ? 26.647  -18.083 -16.352 1.00 40.22  ? 87  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 87  ? 24.669  -17.912 -14.848 1.00 39.83  ? 87  LEU A CD2 1 
ATOM   713  N  N   . GLU A 1 88  ? 25.150  -22.908 -16.120 1.00 46.37  ? 88  GLU A N   1 
ATOM   714  C  CA  . GLU A 1 88  ? 25.516  -24.050 -15.294 1.00 53.74  ? 88  GLU A CA  1 
ATOM   715  C  C   . GLU A 1 88  ? 26.796  -24.716 -15.821 1.00 55.76  ? 88  GLU A C   1 
ATOM   716  O  O   . GLU A 1 88  ? 27.674  -25.064 -15.037 1.00 63.54  ? 88  GLU A O   1 
ATOM   717  C  CB  . GLU A 1 88  ? 24.357  -25.050 -15.216 1.00 54.86  ? 88  GLU A CB  1 
ATOM   718  C  CG  . GLU A 1 88  ? 24.631  -26.216 -14.272 1.00 63.66  ? 88  GLU A CG  1 
ATOM   719  C  CD  . GLU A 1 88  ? 23.651  -27.379 -14.315 1.00 76.12  ? 88  GLU A CD  1 
ATOM   720  O  OE1 . GLU A 1 88  ? 23.158  -27.708 -15.421 1.00 84.99  ? 88  GLU A OE1 1 
ATOM   721  O  OE2 . GLU A 1 88  ? 23.414  -27.983 -13.243 1.00 91.39  ? 88  GLU A OE2 1 
ATOM   722  N  N   . VAL A 1 89  ? 26.903  -24.883 -17.147 1.00 56.74  ? 89  VAL A N   1 
ATOM   723  C  CA  . VAL A 1 89  ? 27.980  -25.634 -17.788 1.00 57.12  ? 89  VAL A CA  1 
ATOM   724  C  C   . VAL A 1 89  ? 29.259  -24.793 -17.810 1.00 54.33  ? 89  VAL A C   1 
ATOM   725  O  O   . VAL A 1 89  ? 30.331  -25.316 -17.524 1.00 57.30  ? 89  VAL A O   1 
ATOM   726  C  CB  . VAL A 1 89  ? 27.547  -26.108 -19.195 1.00 58.53  ? 89  VAL A CB  1 
ATOM   727  C  CG1 . VAL A 1 89  ? 28.714  -26.406 -20.136 1.00 57.19  ? 89  VAL A CG1 1 
ATOM   728  C  CG2 . VAL A 1 89  ? 26.607  -27.305 -19.097 1.00 55.55  ? 89  VAL A CG2 1 
ATOM   729  N  N   . PHE A 1 90  ? 29.125  -23.500 -18.142 1.00 51.50  ? 90  PHE A N   1 
ATOM   730  C  CA  . PHE A 1 90  ? 30.225  -22.542 -18.179 1.00 55.11  ? 90  PHE A CA  1 
ATOM   731  C  C   . PHE A 1 90  ? 30.873  -22.359 -16.806 1.00 59.19  ? 90  PHE A C   1 
ATOM   732  O  O   . PHE A 1 90  ? 32.078  -22.127 -16.723 1.00 66.48  ? 90  PHE A O   1 
ATOM   733  C  CB  . PHE A 1 90  ? 29.737  -21.180 -18.684 1.00 55.14  ? 90  PHE A CB  1 
ATOM   734  C  CG  . PHE A 1 90  ? 30.834  -20.200 -19.010 1.00 60.16  ? 90  PHE A CG  1 
ATOM   735  C  CD1 . PHE A 1 90  ? 31.778  -20.495 -19.982 1.00 67.98  ? 90  PHE A CD1 1 
ATOM   736  C  CD2 . PHE A 1 90  ? 30.932  -18.988 -18.344 1.00 68.01  ? 90  PHE A CD2 1 
ATOM   737  C  CE1 . PHE A 1 90  ? 32.789  -19.595 -20.286 1.00 72.41  ? 90  PHE A CE1 1 
ATOM   738  C  CE2 . PHE A 1 90  ? 31.943  -18.087 -18.650 1.00 70.80  ? 90  PHE A CE2 1 
ATOM   739  C  CZ  . PHE A 1 90  ? 32.868  -18.391 -19.622 1.00 72.03  ? 90  PHE A CZ  1 
ATOM   740  N  N   . MET A 1 91  ? 30.066  -22.409 -15.737 1.00 61.10  ? 91  MET A N   1 
ATOM   741  C  CA  . MET A 1 91  ? 30.570  -22.261 -14.376 1.00 65.60  ? 91  MET A CA  1 
ATOM   742  C  C   . MET A 1 91  ? 31.418  -23.476 -14.007 1.00 65.19  ? 91  MET A C   1 
ATOM   743  O  O   . MET A 1 91  ? 32.437  -23.311 -13.344 1.00 65.84  ? 91  MET A O   1 
ATOM   744  C  CB  . MET A 1 91  ? 29.449  -22.146 -13.339 1.00 65.40  ? 91  MET A CB  1 
ATOM   745  C  CG  . MET A 1 91  ? 28.988  -20.743 -13.052 1.00 63.77  ? 91  MET A CG  1 
ATOM   746  S  SD  . MET A 1 91  ? 27.407  -20.859 -12.169 1.00 70.75  ? 91  MET A SD  1 
ATOM   747  C  CE  . MET A 1 91  ? 26.987  -19.124 -12.074 1.00 72.67  ? 91  MET A CE  1 
ATOM   748  N  N   . ASP A 1 92  ? 30.971  -24.678 -14.409 1.00 64.47  ? 92  ASP A N   1 
ATOM   749  C  CA  . ASP A 1 92  ? 31.677  -25.923 -14.120 1.00 73.49  ? 92  ASP A CA  1 
ATOM   750  C  C   . ASP A 1 92  ? 33.036  -25.955 -14.814 1.00 66.95  ? 92  ASP A C   1 
ATOM   751  O  O   . ASP A 1 92  ? 34.011  -26.381 -14.207 1.00 73.07  ? 92  ASP A O   1 
ATOM   752  C  CB  . ASP A 1 92  ? 30.867  -27.158 -14.523 1.00 83.36  ? 92  ASP A CB  1 
ATOM   753  C  CG  . ASP A 1 92  ? 29.724  -27.472 -13.573 1.00 94.86  ? 92  ASP A CG  1 
ATOM   754  O  OD1 . ASP A 1 92  ? 29.524  -26.696 -12.619 1.00 97.14  ? 92  ASP A OD1 1 
ATOM   755  O  OD2 . ASP A 1 92  ? 29.041  -28.491 -13.797 1.00 110.95 ? 92  ASP A OD2 1 
ATOM   756  N  N   . ALA A 1 93  ? 33.084  -25.501 -16.074 1.00 65.88  ? 93  ALA A N   1 
ATOM   757  C  CA  . ALA A 1 93  ? 34.306  -25.433 -16.868 1.00 67.99  ? 93  ALA A CA  1 
ATOM   758  C  C   . ALA A 1 93  ? 35.151  -24.228 -16.454 1.00 70.74  ? 93  ALA A C   1 
ATOM   759  O  O   . ALA A 1 93  ? 36.113  -23.890 -17.141 1.00 75.52  ? 93  ALA A O   1 
ATOM   760  C  CB  . ALA A 1 93  ? 33.954  -25.351 -18.339 1.00 66.04  ? 93  ALA A CB  1 
ATOM   761  N  N   . SER A 1 94  ? 34.739  -23.554 -15.372 1.00 67.52  ? 94  SER A N   1 
ATOM   762  C  CA  . SER A 1 94  ? 35.438  -22.410 -14.804 1.00 69.24  ? 94  SER A CA  1 
ATOM   763  C  C   . SER A 1 94  ? 35.662  -22.611 -13.300 1.00 74.92  ? 94  SER A C   1 
ATOM   764  O  O   . SER A 1 94  ? 36.157  -21.711 -12.627 1.00 79.09  ? 94  SER A O   1 
ATOM   765  C  CB  . SER A 1 94  ? 34.658  -21.138 -15.062 1.00 67.27  ? 94  SER A CB  1 
ATOM   766  O  OG  . SER A 1 94  ? 34.409  -20.955 -16.445 1.00 66.81  ? 94  SER A OG  1 
ATOM   767  N  N   . ALA A 1 95  ? 35.318  -23.805 -12.791 1.00 76.29  ? 95  ALA A N   1 
ATOM   768  C  CA  . ALA A 1 95  ? 35.276  -24.117 -11.365 1.00 79.98  ? 95  ALA A CA  1 
ATOM   769  C  C   . ALA A 1 95  ? 36.608  -23.804 -10.662 1.00 88.67  ? 95  ALA A C   1 
ATOM   770  O  O   . ALA A 1 95  ? 36.604  -23.505 -9.466  1.00 80.07  ? 95  ALA A O   1 
ATOM   771  C  CB  . ALA A 1 95  ? 34.860  -25.567 -11.182 1.00 78.01  ? 95  ALA A CB  1 
ATOM   772  N  N   . LEU A 1 96  ? 37.740  -23.862 -11.395 1.00 91.81  ? 96  LEU A N   1 
ATOM   773  C  CA  . LEU A 1 96  ? 39.078  -23.652 -10.836 1.00 92.21  ? 96  LEU A CA  1 
ATOM   774  C  C   . LEU A 1 96  ? 39.642  -22.296 -11.278 1.00 86.06  ? 96  LEU A C   1 
ATOM   775  O  O   . LEU A 1 96  ? 39.962  -21.458 -10.439 1.00 72.91  ? 96  LEU A O   1 
ATOM   776  C  CB  . LEU A 1 96  ? 39.989  -24.814 -11.262 1.00 92.88  ? 96  LEU A CB  1 
ATOM   777  C  CG  . LEU A 1 96  ? 39.517  -26.210 -10.838 1.00 97.97  ? 96  LEU A CG  1 
ATOM   778  C  CD1 . LEU A 1 96  ? 40.262  -27.305 -11.597 1.00 95.49  ? 96  LEU A CD1 1 
ATOM   779  C  CD2 . LEU A 1 96  ? 39.660  -26.418 -9.331  1.00 91.81  ? 96  LEU A CD2 1 
ATOM   780  N  N   . THR A 1 97  ? 39.765  -22.091 -12.596 1.00 90.41  ? 97  THR A N   1 
ATOM   781  C  CA  . THR A 1 97  ? 40.215  -20.829 -13.182 1.00 94.42  ? 97  THR A CA  1 
ATOM   782  C  C   . THR A 1 97  ? 39.478  -19.634 -12.565 1.00 89.85  ? 97  THR A C   1 
ATOM   783  O  O   . THR A 1 97  ? 40.108  -18.677 -12.108 1.00 87.00  ? 97  THR A O   1 
ATOM   784  C  CB  . THR A 1 97  ? 40.044  -20.847 -14.712 1.00 99.35  ? 97  THR A CB  1 
ATOM   785  O  OG1 . THR A 1 97  ? 38.761  -21.413 -14.990 1.00 88.20  ? 97  THR A OG1 1 
ATOM   786  C  CG2 . THR A 1 97  ? 41.122  -21.629 -15.438 1.00 102.76 ? 97  THR A CG2 1 
ATOM   787  N  N   . GLY A 1 98  ? 38.139  -19.710 -12.546 1.00 82.28  ? 98  GLY A N   1 
ATOM   788  C  CA  . GLY A 1 98  ? 37.270  -18.569 -12.275 1.00 76.40  ? 98  GLY A CA  1 
ATOM   789  C  C   . GLY A 1 98  ? 36.657  -18.004 -13.563 1.00 74.04  ? 98  GLY A C   1 
ATOM   790  O  O   . GLY A 1 98  ? 37.167  -18.264 -14.655 1.00 68.93  ? 98  GLY A O   1 
ATOM   791  N  N   . ILE A 1 99  ? 35.536  -17.274 -13.434 1.00 66.07  ? 99  ILE A N   1 
ATOM   792  C  CA  . ILE A 1 99  ? 35.007  -16.448 -14.516 1.00 59.69  ? 99  ILE A CA  1 
ATOM   793  C  C   . ILE A 1 99  ? 35.553  -15.045 -14.304 1.00 53.87  ? 99  ILE A C   1 
ATOM   794  O  O   . ILE A 1 99  ? 35.354  -14.464 -13.248 1.00 52.89  ? 99  ILE A O   1 
ATOM   795  C  CB  . ILE A 1 99  ? 33.463  -16.420 -14.566 1.00 61.40  ? 99  ILE A CB  1 
ATOM   796  C  CG1 . ILE A 1 99  ? 32.853  -17.824 -14.536 1.00 65.37  ? 99  ILE A CG1 1 
ATOM   797  C  CG2 . ILE A 1 99  ? 32.988  -15.626 -15.778 1.00 62.69  ? 99  ILE A CG2 1 
ATOM   798  C  CD1 . ILE A 1 99  ? 31.335  -17.863 -14.419 1.00 66.56  ? 99  ILE A CD1 1 
ATOM   799  N  N   . PRO A 1 100 ? 36.239  -14.424 -15.281 1.00 58.33  ? 100 PRO A N   1 
ATOM   800  C  CA  . PRO A 1 100 ? 36.717  -13.054 -15.084 1.00 57.42  ? 100 PRO A CA  1 
ATOM   801  C  C   . PRO A 1 100 ? 35.571  -12.104 -14.713 1.00 56.25  ? 100 PRO A C   1 
ATOM   802  O  O   . PRO A 1 100 ? 34.509  -12.168 -15.324 1.00 51.00  ? 100 PRO A O   1 
ATOM   803  C  CB  . PRO A 1 100 ? 37.322  -12.688 -16.448 1.00 56.71  ? 100 PRO A CB  1 
ATOM   804  C  CG  . PRO A 1 100 ? 37.620  -14.021 -17.113 1.00 58.49  ? 100 PRO A CG  1 
ATOM   805  C  CD  . PRO A 1 100 ? 36.545  -14.964 -16.614 1.00 57.62  ? 100 PRO A CD  1 
ATOM   806  N  N   . LEU A 1 101 ? 35.822  -11.199 -13.755 1.00 55.37  ? 101 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 101 ? 34.838  -10.254 -13.231 1.00 65.65  ? 101 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 101 ? 34.148  -9.461  -14.347 1.00 56.91  ? 101 LEU A C   1 
ATOM   809  O  O   . LEU A 1 101 ? 32.928  -9.312  -14.330 1.00 51.48  ? 101 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 101 ? 35.528  -9.353  -12.192 1.00 77.53  ? 101 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 101 ? 35.867  -10.062 -10.871 1.00 89.78  ? 101 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 101 ? 37.078  -9.462  -10.158 1.00 90.38  ? 101 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 101 ? 34.667  -10.070 -9.929  1.00 90.90  ? 101 LEU A CD2 1 
ATOM   814  N  N   . PRO A 1 102 ? 34.859  -8.932  -15.365 1.00 51.89  ? 102 PRO A N   1 
ATOM   815  C  CA  . PRO A 1 102 ? 34.208  -8.138  -16.415 1.00 50.71  ? 102 PRO A CA  1 
ATOM   816  C  C   . PRO A 1 102 ? 33.197  -8.926  -17.254 1.00 51.70  ? 102 PRO A C   1 
ATOM   817  O  O   . PRO A 1 102 ? 32.243  -8.372  -17.789 1.00 43.51  ? 102 PRO A O   1 
ATOM   818  C  CB  . PRO A 1 102 ? 35.375  -7.674  -17.297 1.00 49.53  ? 102 PRO A CB  1 
ATOM   819  C  CG  . PRO A 1 102 ? 36.590  -7.801  -16.402 1.00 52.59  ? 102 PRO A CG  1 
ATOM   820  C  CD  . PRO A 1 102 ? 36.314  -9.013  -15.540 1.00 53.79  ? 102 PRO A CD  1 
ATOM   821  N  N   . LEU A 1 103 ? 33.422  -10.232 -17.390 1.00 51.05  ? 103 LEU A N   1 
ATOM   822  C  CA  . LEU A 1 103 ? 32.472  -11.085 -18.074 1.00 49.18  ? 103 LEU A CA  1 
ATOM   823  C  C   . LEU A 1 103 ? 31.275  -11.351 -17.163 1.00 45.96  ? 103 LEU A C   1 
ATOM   824  O  O   . LEU A 1 103 ? 30.145  -11.231 -17.612 1.00 40.40  ? 103 LEU A O   1 
ATOM   825  C  CB  . LEU A 1 103 ? 33.170  -12.382 -18.486 1.00 53.52  ? 103 LEU A CB  1 
ATOM   826  C  CG  . LEU A 1 103 ? 32.299  -13.365 -19.260 1.00 56.73  ? 103 LEU A CG  1 
ATOM   827  C  CD1 . LEU A 1 103 ? 31.748  -12.718 -20.525 1.00 57.38  ? 103 LEU A CD1 1 
ATOM   828  C  CD2 . LEU A 1 103 ? 33.082  -14.632 -19.584 1.00 57.36  ? 103 LEU A CD2 1 
ATOM   829  N  N   . ILE A 1 104 ? 31.519  -11.715 -15.898 1.00 41.56  ? 104 ILE A N   1 
ATOM   830  C  CA  . ILE A 1 104 ? 30.457  -11.782 -14.901 1.00 45.67  ? 104 ILE A CA  1 
ATOM   831  C  C   . ILE A 1 104 ? 29.575  -10.535 -15.006 1.00 46.11  ? 104 ILE A C   1 
ATOM   832  O  O   . ILE A 1 104 ? 28.357  -10.653 -15.051 1.00 42.44  ? 104 ILE A O   1 
ATOM   833  C  CB  . ILE A 1 104 ? 31.021  -11.940 -13.472 1.00 47.65  ? 104 ILE A CB  1 
ATOM   834  C  CG1 . ILE A 1 104 ? 31.617  -13.333 -13.269 1.00 46.13  ? 104 ILE A CG1 1 
ATOM   835  C  CG2 . ILE A 1 104 ? 29.961  -11.623 -12.411 1.00 49.31  ? 104 ILE A CG2 1 
ATOM   836  C  CD1 . ILE A 1 104 ? 32.375  -13.489 -11.981 1.00 48.02  ? 104 ILE A CD1 1 
ATOM   837  N  N   . LYS A 1 105 ? 30.201  -9.352  -15.009 1.00 42.07  ? 105 LYS A N   1 
ATOM   838  C  CA  . LYS A 1 105 ? 29.491  -8.086  -14.978 1.00 42.82  ? 105 LYS A CA  1 
ATOM   839  C  C   . LYS A 1 105 ? 28.639  -7.948  -16.235 1.00 44.74  ? 105 LYS A C   1 
ATOM   840  O  O   . LYS A 1 105 ? 27.469  -7.587  -16.166 1.00 46.87  ? 105 LYS A O   1 
ATOM   841  C  CB  . LYS A 1 105 ? 30.492  -6.937  -14.861 1.00 46.09  ? 105 LYS A CB  1 
ATOM   842  C  CG  . LYS A 1 105 ? 29.890  -5.547  -14.721 1.00 49.56  ? 105 LYS A CG  1 
ATOM   843  C  CD  . LYS A 1 105 ? 30.916  -4.457  -14.572 1.00 52.02  ? 105 LYS A CD  1 
ATOM   844  C  CE  . LYS A 1 105 ? 31.838  -4.688  -13.393 1.00 56.89  ? 105 LYS A CE  1 
ATOM   845  N  NZ  . LYS A 1 105 ? 32.592  -3.454  -13.063 1.00 63.13  ? 105 LYS A NZ  1 
ATOM   846  N  N   . SER A 1 106 ? 29.246  -8.243  -17.382 1.00 45.23  ? 106 SER A N   1 
ATOM   847  C  CA  . SER A 1 106 ? 28.558  -8.240  -18.667 1.00 44.90  ? 106 SER A CA  1 
ATOM   848  C  C   . SER A 1 106 ? 27.337  -9.171  -18.688 1.00 41.39  ? 106 SER A C   1 
ATOM   849  O  O   . SER A 1 106 ? 26.294  -8.796  -19.218 1.00 43.38  ? 106 SER A O   1 
ATOM   850  C  CB  . SER A 1 106 ? 29.522  -8.583  -19.776 1.00 44.59  ? 106 SER A CB  1 
ATOM   851  O  OG  . SER A 1 106 ? 28.819  -8.965  -20.945 1.00 47.74  ? 106 SER A OG  1 
ATOM   852  N  N   . TYR A 1 107 ? 27.491  -10.395 -18.164 1.00 40.20  ? 107 TYR A N   1 
ATOM   853  C  CA  . TYR A 1 107 ? 26.437  -11.405 -18.124 1.00 43.36  ? 107 TYR A CA  1 
ATOM   854  C  C   . TYR A 1 107 ? 25.302  -10.928 -17.211 1.00 44.55  ? 107 TYR A C   1 
ATOM   855  O  O   . TYR A 1 107 ? 24.133  -11.001 -17.572 1.00 46.56  ? 107 TYR A O   1 
ATOM   856  C  CB  . TYR A 1 107 ? 26.986  -12.769 -17.665 1.00 42.81  ? 107 TYR A CB  1 
ATOM   857  C  CG  . TYR A 1 107 ? 27.636  -13.651 -18.709 1.00 44.95  ? 107 TYR A CG  1 
ATOM   858  C  CD1 . TYR A 1 107 ? 27.669  -13.322 -20.057 1.00 44.28  ? 107 TYR A CD1 1 
ATOM   859  C  CD2 . TYR A 1 107 ? 28.223  -14.850 -18.336 1.00 50.96  ? 107 TYR A CD2 1 
ATOM   860  C  CE1 . TYR A 1 107 ? 28.274  -14.149 -20.991 1.00 49.02  ? 107 TYR A CE1 1 
ATOM   861  C  CE2 . TYR A 1 107 ? 28.815  -15.698 -19.260 1.00 53.07  ? 107 TYR A CE2 1 
ATOM   862  C  CZ  . TYR A 1 107 ? 28.852  -15.344 -20.595 1.00 53.69  ? 107 TYR A CZ  1 
ATOM   863  O  OH  . TYR A 1 107 ? 29.461  -16.194 -21.495 1.00 59.23  ? 107 TYR A OH  1 
ATOM   864  N  N   . LEU A 1 108 ? 25.651  -10.432 -16.023 1.00 40.22  ? 108 LEU A N   1 
ATOM   865  C  CA  . LEU A 1 108 ? 24.661  -9.877  -15.123 1.00 41.01  ? 108 LEU A CA  1 
ATOM   866  C  C   . LEU A 1 108 ? 23.951  -8.670  -15.752 1.00 41.47  ? 108 LEU A C   1 
ATOM   867  O  O   . LEU A 1 108 ? 22.754  -8.527  -15.550 1.00 38.77  ? 108 LEU A O   1 
ATOM   868  C  CB  . LEU A 1 108 ? 25.327  -9.510  -13.797 1.00 41.94  ? 108 LEU A CB  1 
ATOM   869  C  CG  . LEU A 1 108 ? 24.368  -8.965  -12.741 1.00 46.09  ? 108 LEU A CG  1 
ATOM   870  C  CD1 . LEU A 1 108 ? 23.294  -9.995  -12.407 1.00 44.03  ? 108 LEU A CD1 1 
ATOM   871  C  CD2 . LEU A 1 108 ? 25.124  -8.537  -11.489 1.00 49.37  ? 108 LEU A CD2 1 
ATOM   872  N  N   . PHE A 1 109 ? 24.671  -7.796  -16.477 1.00 38.72  ? 109 PHE A N   1 
ATOM   873  C  CA  . PHE A 1 109 ? 24.078  -6.626  -17.119 1.00 39.87  ? 109 PHE A CA  1 
ATOM   874  C  C   . PHE A 1 109 ? 23.016  -7.068  -18.132 1.00 43.84  ? 109 PHE A C   1 
ATOM   875  O  O   . PHE A 1 109 ? 21.875  -6.614  -18.109 1.00 45.24  ? 109 PHE A O   1 
ATOM   876  C  CB  . PHE A 1 109 ? 25.144  -5.785  -17.831 1.00 37.54  ? 109 PHE A CB  1 
ATOM   877  C  CG  . PHE A 1 109 ? 24.680  -4.425  -18.298 1.00 38.51  ? 109 PHE A CG  1 
ATOM   878  C  CD1 . PHE A 1 109 ? 24.266  -3.464  -17.384 1.00 39.33  ? 109 PHE A CD1 1 
ATOM   879  C  CD2 . PHE A 1 109 ? 24.658  -4.100  -19.648 1.00 41.94  ? 109 PHE A CD2 1 
ATOM   880  C  CE1 . PHE A 1 109 ? 23.856  -2.207  -17.808 1.00 42.36  ? 109 PHE A CE1 1 
ATOM   881  C  CE2 . PHE A 1 109 ? 24.234  -2.848  -20.077 1.00 43.76  ? 109 PHE A CE2 1 
ATOM   882  C  CZ  . PHE A 1 109 ? 23.834  -1.900  -19.157 1.00 44.46  ? 109 PHE A CZ  1 
ATOM   883  N  N   . GLN A 1 110 ? 23.419  -7.967  -19.027 1.00 41.52  ? 110 GLN A N   1 
ATOM   884  C  CA  . GLN A 1 110 ? 22.553  -8.559  -20.032 1.00 43.05  ? 110 GLN A CA  1 
ATOM   885  C  C   . GLN A 1 110 ? 21.288  -9.166  -19.404 1.00 42.21  ? 110 GLN A C   1 
ATOM   886  O  O   . GLN A 1 110 ? 20.170  -8.895  -19.851 1.00 38.34  ? 110 GLN A O   1 
ATOM   887  C  CB  . GLN A 1 110 ? 23.378  -9.610  -20.783 1.00 44.53  ? 110 GLN A CB  1 
ATOM   888  C  CG  . GLN A 1 110 ? 24.344  -9.022  -21.804 1.00 41.77  ? 110 GLN A CG  1 
ATOM   889  C  CD  . GLN A 1 110 ? 25.039  -10.112 -22.587 1.00 42.98  ? 110 GLN A CD  1 
ATOM   890  O  OE1 . GLN A 1 110 ? 24.479  -10.723 -23.497 1.00 40.68  ? 110 GLN A OE1 1 
ATOM   891  N  NE2 . GLN A 1 110 ? 26.285  -10.371 -22.234 1.00 44.88  ? 110 GLN A NE2 1 
ATOM   892  N  N   . LEU A 1 111 ? 21.486  -10.041 -18.410 1.00 40.21  ? 111 LEU A N   1 
ATOM   893  C  CA  . LEU A 1 111 ? 20.413  -10.715 -17.702 1.00 39.54  ? 111 LEU A CA  1 
ATOM   894  C  C   . LEU A 1 111 ? 19.440  -9.706  -17.105 1.00 40.44  ? 111 LEU A C   1 
ATOM   895  O  O   . LEU A 1 111 ? 18.235  -9.914  -17.173 1.00 39.95  ? 111 LEU A O   1 
ATOM   896  C  CB  . LEU A 1 111 ? 21.010  -11.569 -16.589 1.00 40.46  ? 111 LEU A CB  1 
ATOM   897  C  CG  . LEU A 1 111 ? 21.708  -12.838 -17.058 1.00 42.78  ? 111 LEU A CG  1 
ATOM   898  C  CD1 . LEU A 1 111 ? 22.524  -13.452 -15.925 1.00 43.37  ? 111 LEU A CD1 1 
ATOM   899  C  CD2 . LEU A 1 111 ? 20.697  -13.833 -17.585 1.00 44.14  ? 111 LEU A CD2 1 
ATOM   900  N  N   . LEU A 1 112 ? 19.954  -8.623  -16.519 1.00 39.71  ? 112 LEU A N   1 
ATOM   901  C  CA  . LEU A 1 112 ? 19.080  -7.589  -15.974 1.00 41.22  ? 112 LEU A CA  1 
ATOM   902  C  C   . LEU A 1 112 ? 18.327  -6.881  -17.095 1.00 41.03  ? 112 LEU A C   1 
ATOM   903  O  O   . LEU A 1 112 ? 17.185  -6.475  -16.899 1.00 42.36  ? 112 LEU A O   1 
ATOM   904  C  CB  . LEU A 1 112 ? 19.889  -6.583  -15.155 1.00 37.37  ? 112 LEU A CB  1 
ATOM   905  C  CG  . LEU A 1 112 ? 20.432  -7.112  -13.831 1.00 38.29  ? 112 LEU A CG  1 
ATOM   906  C  CD1 . LEU A 1 112 ? 21.476  -6.155  -13.264 1.00 39.40  ? 112 LEU A CD1 1 
ATOM   907  C  CD2 . LEU A 1 112 ? 19.317  -7.327  -12.822 1.00 39.99  ? 112 LEU A CD2 1 
ATOM   908  N  N   . GLN A 1 113 ? 18.976  -6.723  -18.253 1.00 41.87  ? 113 GLN A N   1 
ATOM   909  C  CA  . GLN A 1 113 ? 18.352  -6.085  -19.404 1.00 45.41  ? 113 GLN A CA  1 
ATOM   910  C  C   . GLN A 1 113 ? 17.155  -6.909  -19.892 1.00 41.32  ? 113 GLN A C   1 
ATOM   911  O  O   . GLN A 1 113 ? 16.092  -6.344  -20.132 1.00 36.95  ? 113 GLN A O   1 
ATOM   912  C  CB  . GLN A 1 113 ? 19.387  -5.836  -20.497 1.00 45.70  ? 113 GLN A CB  1 
ATOM   913  C  CG  . GLN A 1 113 ? 20.161  -4.539  -20.320 1.00 49.88  ? 113 GLN A CG  1 
ATOM   914  C  CD  . GLN A 1 113 ? 21.088  -4.369  -21.496 1.00 55.34  ? 113 GLN A CD  1 
ATOM   915  O  OE1 . GLN A 1 113 ? 21.789  -5.297  -21.882 1.00 56.82  ? 113 GLN A OE1 1 
ATOM   916  N  NE2 . GLN A 1 113 ? 21.048  -3.208  -22.129 1.00 66.92  ? 113 GLN A NE2 1 
ATOM   917  N  N   . GLY A 1 114 ? 17.320  -8.235  -19.984 1.00 38.77  ? 114 GLY A N   1 
ATOM   918  C  CA  . GLY A 1 114 ? 16.236  -9.154  -20.311 1.00 40.11  ? 114 GLY A CA  1 
ATOM   919  C  C   . GLY A 1 114 ? 15.105  -9.132  -19.278 1.00 44.17  ? 114 GLY A C   1 
ATOM   920  O  O   . GLY A 1 114 ? 13.927  -9.102  -19.637 1.00 40.63  ? 114 GLY A O   1 
ATOM   921  N  N   . LEU A 1 115 ? 15.465  -9.141  -17.990 1.00 42.72  ? 115 LEU A N   1 
ATOM   922  C  CA  . LEU A 1 115 ? 14.471  -9.165  -16.930 1.00 42.97  ? 115 LEU A CA  1 
ATOM   923  C  C   . LEU A 1 115 ? 13.702  -7.846  -16.904 1.00 41.54  ? 115 LEU A C   1 
ATOM   924  O  O   . LEU A 1 115 ? 12.470  -7.858  -16.810 1.00 41.96  ? 115 LEU A O   1 
ATOM   925  C  CB  . LEU A 1 115 ? 15.151  -9.448  -15.586 1.00 48.51  ? 115 LEU A CB  1 
ATOM   926  C  CG  . LEU A 1 115 ? 14.287  -10.130 -14.530 1.00 53.30  ? 115 LEU A CG  1 
ATOM   927  C  CD1 . LEU A 1 115 ? 13.797  -11.493 -15.015 1.00 54.99  ? 115 LEU A CD1 1 
ATOM   928  C  CD2 . LEU A 1 115 ? 15.063  -10.274 -13.229 1.00 54.36  ? 115 LEU A CD2 1 
ATOM   929  N  N   . ALA A 1 116 ? 14.409  -6.714  -17.022 1.00 36.27  ? 116 ALA A N   1 
ATOM   930  C  CA  . ALA A 1 116 ? 13.729  -5.427  -17.025 1.00 39.58  ? 116 ALA A CA  1 
ATOM   931  C  C   . ALA A 1 116 ? 12.687  -5.394  -18.148 1.00 45.29  ? 116 ALA A C   1 
ATOM   932  O  O   . ALA A 1 116 ? 11.611  -4.812  -17.998 1.00 48.52  ? 116 ALA A O   1 
ATOM   933  C  CB  . ALA A 1 116 ? 14.713  -4.301  -17.160 1.00 40.19  ? 116 ALA A CB  1 
ATOM   934  N  N   . PHE A 1 117 ? 13.019  -6.031  -19.277 1.00 43.69  ? 117 PHE A N   1 
ATOM   935  C  CA  . PHE A 1 117 ? 12.178  -6.009  -20.457 1.00 38.47  ? 117 PHE A CA  1 
ATOM   936  C  C   . PHE A 1 117 ? 10.938  -6.846  -20.165 1.00 40.81  ? 117 PHE A C   1 
ATOM   937  O  O   . PHE A 1 117 ? 9.827   -6.399  -20.447 1.00 38.99  ? 117 PHE A O   1 
ATOM   938  C  CB  . PHE A 1 117 ? 12.938  -6.492  -21.694 1.00 39.93  ? 117 PHE A CB  1 
ATOM   939  C  CG  . PHE A 1 117 ? 12.176  -6.342  -22.992 1.00 41.73  ? 117 PHE A CG  1 
ATOM   940  C  CD1 . PHE A 1 117 ? 12.188  -5.140  -23.692 1.00 45.97  ? 117 PHE A CD1 1 
ATOM   941  C  CD2 . PHE A 1 117 ? 11.409  -7.386  -23.498 1.00 44.80  ? 117 PHE A CD2 1 
ATOM   942  C  CE1 . PHE A 1 117 ? 11.456  -4.981  -24.865 1.00 47.36  ? 117 PHE A CE1 1 
ATOM   943  C  CE2 . PHE A 1 117 ? 10.675  -7.226  -24.668 1.00 47.79  ? 117 PHE A CE2 1 
ATOM   944  C  CZ  . PHE A 1 117 ? 10.707  -6.030  -25.356 1.00 45.32  ? 117 PHE A CZ  1 
ATOM   945  N  N   . CYS A 1 118 ? 11.142  -8.041  -19.589 1.00 41.01  ? 118 CYS A N   1 
ATOM   946  C  CA  . CYS A 1 118 ? 10.043  -8.897  -19.161 1.00 38.15  ? 118 CYS A CA  1 
ATOM   947  C  C   . CYS A 1 118 ? 9.110   -8.132  -18.236 1.00 36.14  ? 118 CYS A C   1 
ATOM   948  O  O   . CYS A 1 118 ? 7.908   -8.051  -18.492 1.00 40.22  ? 118 CYS A O   1 
ATOM   949  C  CB  . CYS A 1 118 ? 10.516  -10.114 -18.380 1.00 40.60  ? 118 CYS A CB  1 
ATOM   950  S  SG  . CYS A 1 118 ? 11.250  -11.379 -19.431 1.00 48.24  ? 118 CYS A SG  1 
ATOM   951  N  N   . HIS A 1 119 ? 9.677   -7.601  -17.149 1.00 35.88  ? 119 HIS A N   1 
ATOM   952  C  CA  . HIS A 1 119 ? 8.888   -6.981  -16.096 1.00 37.42  ? 119 HIS A CA  1 
ATOM   953  C  C   . HIS A 1 119 ? 8.104   -5.786  -16.644 1.00 39.95  ? 119 HIS A C   1 
ATOM   954  O  O   . HIS A 1 119 ? 6.951   -5.603  -16.272 1.00 43.18  ? 119 HIS A O   1 
ATOM   955  C  CB  . HIS A 1 119 ? 9.784   -6.620  -14.913 1.00 35.96  ? 119 HIS A CB  1 
ATOM   956  C  CG  . HIS A 1 119 ? 10.259  -7.801  -14.166 1.00 33.68  ? 119 HIS A CG  1 
ATOM   957  N  ND1 . HIS A 1 119 ? 11.217  -7.688  -13.182 1.00 33.74  ? 119 HIS A ND1 1 
ATOM   958  C  CD2 . HIS A 1 119 ? 9.932   -9.102  -14.245 1.00 34.04  ? 119 HIS A CD2 1 
ATOM   959  C  CE1 . HIS A 1 119 ? 11.447  -8.894  -12.674 1.00 34.13  ? 119 HIS A CE1 1 
ATOM   960  N  NE2 . HIS A 1 119 ? 10.701  -9.777  -13.319 1.00 32.57  ? 119 HIS A NE2 1 
ATOM   961  N  N   . SER A 1 120 ? 8.728   -5.005  -17.540 1.00 40.66  ? 120 SER A N   1 
ATOM   962  C  CA  . SER A 1 120 ? 8.115   -3.827  -18.143 1.00 40.55  ? 120 SER A CA  1 
ATOM   963  C  C   . SER A 1 120 ? 7.053   -4.233  -19.175 1.00 40.36  ? 120 SER A C   1 
ATOM   964  O  O   . SER A 1 120 ? 6.278   -3.399  -19.629 1.00 40.77  ? 120 SER A O   1 
ATOM   965  C  CB  . SER A 1 120 ? 9.175   -2.940  -18.749 1.00 37.37  ? 120 SER A CB  1 
ATOM   966  O  OG  . SER A 1 120 ? 9.553   -3.445  -20.012 1.00 43.84  ? 120 SER A OG  1 
ATOM   967  N  N   . HIS A 1 121 ? 7.048   -5.516  -19.564 1.00 41.87  ? 121 HIS A N   1 
ATOM   968  C  CA  . HIS A 1 121 ? 6.015   -6.116  -20.403 1.00 45.39  ? 121 HIS A CA  1 
ATOM   969  C  C   . HIS A 1 121 ? 5.154   -7.087  -19.581 1.00 41.96  ? 121 HIS A C   1 
ATOM   970  O  O   . HIS A 1 121 ? 4.675   -8.076  -20.129 1.00 38.00  ? 121 HIS A O   1 
ATOM   971  C  CB  . HIS A 1 121 ? 6.668   -6.789  -21.618 1.00 48.33  ? 121 HIS A CB  1 
ATOM   972  C  CG  . HIS A 1 121 ? 7.304   -5.799  -22.537 1.00 59.12  ? 121 HIS A CG  1 
ATOM   973  N  ND1 . HIS A 1 121 ? 8.036   -4.731  -22.062 1.00 65.14  ? 121 HIS A ND1 1 
ATOM   974  C  CD2 . HIS A 1 121 ? 7.286   -5.680  -23.873 1.00 62.60  ? 121 HIS A CD2 1 
ATOM   975  C  CE1 . HIS A 1 121 ? 8.459   -4.005  -23.082 1.00 65.88  ? 121 HIS A CE1 1 
ATOM   976  N  NE2 . HIS A 1 121 ? 8.016   -4.566  -24.191 1.00 67.70  ? 121 HIS A NE2 1 
ATOM   977  N  N   . ARG A 1 122 ? 5.013   -6.783  -18.273 1.00 37.30  ? 122 ARG A N   1 
ATOM   978  C  CA  . ARG A 1 122 ? 4.181   -7.451  -17.276 1.00 39.49  ? 122 ARG A CA  1 
ATOM   979  C  C   . ARG A 1 122 ? 4.305   -8.978  -17.298 1.00 38.87  ? 122 ARG A C   1 
ATOM   980  O  O   . ARG A 1 122 ? 3.310   -9.662  -17.042 1.00 38.49  ? 122 ARG A O   1 
ATOM   981  C  CB  . ARG A 1 122 ? 2.719   -6.962  -17.314 1.00 43.09  ? 122 ARG A CB  1 
ATOM   982  C  CG  . ARG A 1 122 ? 1.997   -7.047  -18.653 1.00 45.54  ? 122 ARG A CG  1 
ATOM   983  C  CD  . ARG A 1 122 ? 1.182   -8.310  -18.823 1.00 50.08  ? 122 ARG A CD  1 
ATOM   984  N  NE  . ARG A 1 122 ? 0.482   -8.351  -20.105 1.00 51.96  ? 122 ARG A NE  1 
ATOM   985  C  CZ  . ARG A 1 122 ? 0.984   -8.789  -21.257 1.00 52.65  ? 122 ARG A CZ  1 
ATOM   986  N  NH1 . ARG A 1 122 ? 0.204   -8.830  -22.322 1.00 55.68  ? 122 ARG A NH1 1 
ATOM   987  N  NH2 . ARG A 1 122 ? 2.243   -9.192  -21.357 1.00 57.97  ? 122 ARG A NH2 1 
ATOM   988  N  N   . VAL A 1 123 ? 5.537   -9.494  -17.433 1.00 37.04  ? 123 VAL A N   1 
ATOM   989  C  CA  . VAL A 1 123 ? 5.809   -10.930 -17.336 1.00 37.47  ? 123 VAL A CA  1 
ATOM   990  C  C   . VAL A 1 123 ? 6.760   -11.202 -16.164 1.00 39.90  ? 123 VAL A C   1 
ATOM   991  O  O   . VAL A 1 123 ? 7.819   -10.579 -16.079 1.00 39.41  ? 123 VAL A O   1 
ATOM   992  C  CB  . VAL A 1 123 ? 6.397   -11.477 -18.653 1.00 38.53  ? 123 VAL A CB  1 
ATOM   993  C  CG1 . VAL A 1 123 ? 6.886   -12.910 -18.522 1.00 41.76  ? 123 VAL A CG1 1 
ATOM   994  C  CG2 . VAL A 1 123 ? 5.424   -11.379 -19.809 1.00 40.61  ? 123 VAL A CG2 1 
ATOM   995  N  N   . LEU A 1 124 ? 6.355   -12.123 -15.266 1.00 39.68  ? 124 LEU A N   1 
ATOM   996  C  CA  . LEU A 1 124 ? 7.207   -12.740 -14.248 1.00 40.07  ? 124 LEU A CA  1 
ATOM   997  C  C   . LEU A 1 124 ? 7.793   -14.033 -14.812 1.00 39.05  ? 124 LEU A C   1 
ATOM   998  O  O   . LEU A 1 124 ? 7.036   -14.841 -15.352 1.00 36.18  ? 124 LEU A O   1 
ATOM   999  C  CB  . LEU A 1 124 ? 6.373   -13.118 -13.015 1.00 41.27  ? 124 LEU A CB  1 
ATOM   1000 C  CG  . LEU A 1 124 ? 5.725   -11.982 -12.236 1.00 45.98  ? 124 LEU A CG  1 
ATOM   1001 C  CD1 . LEU A 1 124 ? 5.088   -12.514 -10.962 1.00 48.36  ? 124 LEU A CD1 1 
ATOM   1002 C  CD2 . LEU A 1 124 ? 6.739   -10.899 -11.916 1.00 50.33  ? 124 LEU A CD2 1 
ATOM   1003 N  N   . HIS A 1 125 ? 9.110   -14.258 -14.655 1.00 34.19  ? 125 HIS A N   1 
ATOM   1004 C  CA  . HIS A 1 125 ? 9.727   -15.480 -15.157 1.00 35.18  ? 125 HIS A CA  1 
ATOM   1005 C  C   . HIS A 1 125 ? 9.455   -16.667 -14.228 1.00 38.10  ? 125 HIS A C   1 
ATOM   1006 O  O   . HIS A 1 125 ? 8.944   -17.688 -14.693 1.00 38.95  ? 125 HIS A O   1 
ATOM   1007 C  CB  . HIS A 1 125 ? 11.222  -15.292 -15.425 1.00 34.35  ? 125 HIS A CB  1 
ATOM   1008 C  CG  . HIS A 1 125 ? 11.802  -16.485 -16.100 1.00 36.81  ? 125 HIS A CG  1 
ATOM   1009 N  ND1 . HIS A 1 125 ? 12.018  -17.668 -15.432 1.00 40.30  ? 125 HIS A ND1 1 
ATOM   1010 C  CD2 . HIS A 1 125 ? 12.174  -16.693 -17.372 1.00 41.34  ? 125 HIS A CD2 1 
ATOM   1011 C  CE1 . HIS A 1 125 ? 12.515  -18.560 -16.280 1.00 44.07  ? 125 HIS A CE1 1 
ATOM   1012 N  NE2 . HIS A 1 125 ? 12.617  -17.990 -17.464 1.00 42.75  ? 125 HIS A NE2 1 
ATOM   1013 N  N   . ARG A 1 126 ? 9.885   -16.541 -12.960 1.00 37.27  ? 126 ARG A N   1 
ATOM   1014 C  CA  . ARG A 1 126 ? 9.530   -17.428 -11.853 1.00 40.03  ? 126 ARG A CA  1 
ATOM   1015 C  C   . ARG A 1 126 ? 10.277  -18.759 -11.907 1.00 39.95  ? 126 ARG A C   1 
ATOM   1016 O  O   . ARG A 1 126 ? 9.946   -19.661 -11.143 1.00 43.56  ? 126 ARG A O   1 
ATOM   1017 C  CB  . ARG A 1 126 ? 8.021   -17.713 -11.788 1.00 38.58  ? 126 ARG A CB  1 
ATOM   1018 C  CG  . ARG A 1 126 ? 7.178   -16.469 -11.594 1.00 40.36  ? 126 ARG A CG  1 
ATOM   1019 C  CD  . ARG A 1 126 ? 5.768   -16.780 -11.136 1.00 41.74  ? 126 ARG A CD  1 
ATOM   1020 N  NE  . ARG A 1 126 ? 5.069   -17.662 -12.053 1.00 41.94  ? 126 ARG A NE  1 
ATOM   1021 C  CZ  . ARG A 1 126 ? 3.838   -18.119 -11.866 1.00 44.35  ? 126 ARG A CZ  1 
ATOM   1022 N  NH1 . ARG A 1 126 ? 3.147   -17.778 -10.788 1.00 44.78  ? 126 ARG A NH1 1 
ATOM   1023 N  NH2 . ARG A 1 126 ? 3.303   -18.925 -12.767 1.00 44.13  ? 126 ARG A NH2 1 
ATOM   1024 N  N   . ASP A 1 127 ? 11.269  -18.903 -12.786 1.00 40.13  ? 127 ASP A N   1 
ATOM   1025 C  CA  . ASP A 1 127 ? 12.111  -20.089 -12.741 1.00 43.53  ? 127 ASP A CA  1 
ATOM   1026 C  C   . ASP A 1 127 ? 13.548  -19.748 -13.151 1.00 40.65  ? 127 ASP A C   1 
ATOM   1027 O  O   . ASP A 1 127 ? 14.212  -20.560 -13.773 1.00 36.45  ? 127 ASP A O   1 
ATOM   1028 C  CB  . ASP A 1 127 ? 11.526  -21.211 -13.604 1.00 48.42  ? 127 ASP A CB  1 
ATOM   1029 C  CG  . ASP A 1 127 ? 12.055  -22.603 -13.273 1.00 56.34  ? 127 ASP A CG  1 
ATOM   1030 O  OD1 . ASP A 1 127 ? 12.210  -22.915 -12.063 1.00 55.00  ? 127 ASP A OD1 1 
ATOM   1031 O  OD2 . ASP A 1 127 ? 12.268  -23.392 -14.230 1.00 63.34  ? 127 ASP A OD2 1 
ATOM   1032 N  N   . LEU A 1 128 ? 14.062  -18.576 -12.770 1.00 37.30  ? 128 LEU A N   1 
ATOM   1033 C  CA  . LEU A 1 128 ? 15.447  -18.257 -13.090 1.00 39.81  ? 128 LEU A CA  1 
ATOM   1034 C  C   . LEU A 1 128 ? 16.364  -19.241 -12.363 1.00 41.42  ? 128 LEU A C   1 
ATOM   1035 O  O   . LEU A 1 128 ? 16.155  -19.533 -11.186 1.00 44.15  ? 128 LEU A O   1 
ATOM   1036 C  CB  . LEU A 1 128 ? 15.749  -16.808 -12.691 1.00 40.10  ? 128 LEU A CB  1 
ATOM   1037 C  CG  . LEU A 1 128 ? 15.037  -15.729 -13.502 1.00 38.68  ? 128 LEU A CG  1 
ATOM   1038 C  CD1 . LEU A 1 128 ? 15.455  -14.364 -13.015 1.00 40.93  ? 128 LEU A CD1 1 
ATOM   1039 C  CD2 . LEU A 1 128 ? 15.349  -15.854 -14.983 1.00 40.38  ? 128 LEU A CD2 1 
ATOM   1040 N  N   . LYS A 1 129 ? 17.349  -19.769 -13.102 1.00 44.64  ? 129 LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 129 ? 18.426  -20.592 -12.572 1.00 47.22  ? 129 LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 129 ? 19.504  -20.801 -13.643 1.00 47.90  ? 129 LYS A C   1 
ATOM   1043 O  O   . LYS A 1 129 ? 19.275  -20.579 -14.827 1.00 42.12  ? 129 LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 129 ? 17.865  -21.926 -12.077 1.00 46.81  ? 129 LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 129 ? 17.055  -22.698 -13.093 1.00 47.40  ? 129 LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 129 ? 16.509  -23.965 -12.506 1.00 51.38  ? 129 LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 129 ? 15.494  -24.610 -13.419 1.00 57.63  ? 129 LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 129 ? 15.566  -26.083 -13.328 1.00 63.98  ? 129 LYS A NZ  1 
ATOM   1049 N  N   . PRO A 1 130 ? 20.735  -21.221 -13.278 1.00 50.63  ? 130 PRO A N   1 
ATOM   1050 C  CA  . PRO A 1 130 ? 21.829  -21.307 -14.256 1.00 51.55  ? 130 PRO A CA  1 
ATOM   1051 C  C   . PRO A 1 130 ? 21.552  -22.106 -15.536 1.00 45.10  ? 130 PRO A C   1 
ATOM   1052 O  O   . PRO A 1 130 ? 21.922  -21.648 -16.608 1.00 44.98  ? 130 PRO A O   1 
ATOM   1053 C  CB  . PRO A 1 130 ? 22.958  -21.911 -13.410 1.00 51.87  ? 130 PRO A CB  1 
ATOM   1054 C  CG  . PRO A 1 130 ? 22.678  -21.366 -12.030 1.00 50.64  ? 130 PRO A CG  1 
ATOM   1055 C  CD  . PRO A 1 130 ? 21.178  -21.511 -11.904 1.00 50.36  ? 130 PRO A CD  1 
ATOM   1056 N  N   . ASN A 1 131 ? 20.870  -23.255 -15.449 1.00 43.75  ? 131 ASN A N   1 
ATOM   1057 C  CA  . ASN A 1 131 ? 20.577  -24.064 -16.630 1.00 49.30  ? 131 ASN A CA  1 
ATOM   1058 C  C   . ASN A 1 131 ? 19.467  -23.463 -17.519 1.00 48.43  ? 131 ASN A C   1 
ATOM   1059 O  O   . ASN A 1 131 ? 19.282  -23.956 -18.624 1.00 51.78  ? 131 ASN A O   1 
ATOM   1060 C  CB  . ASN A 1 131 ? 20.297  -25.528 -16.263 1.00 55.94  ? 131 ASN A CB  1 
ATOM   1061 C  CG  . ASN A 1 131 ? 19.006  -25.765 -15.507 1.00 62.31  ? 131 ASN A CG  1 
ATOM   1062 O  OD1 . ASN A 1 131 ? 17.987  -25.119 -15.752 1.00 71.50  ? 131 ASN A OD1 1 
ATOM   1063 N  ND2 . ASN A 1 131 ? 19.042  -26.712 -14.587 1.00 66.99  ? 131 ASN A ND2 1 
ATOM   1064 N  N   . ASN A 1 132 ? 18.747  -22.416 -17.081 1.00 43.69  ? 132 ASN A N   1 
ATOM   1065 C  CA  . ASN A 1 132 ? 17.783  -21.700 -17.918 1.00 47.00  ? 132 ASN A CA  1 
ATOM   1066 C  C   . ASN A 1 132 ? 18.410  -20.461 -18.550 1.00 45.32  ? 132 ASN A C   1 
ATOM   1067 O  O   . ASN A 1 132 ? 17.724  -19.701 -19.228 1.00 51.40  ? 132 ASN A O   1 
ATOM   1068 C  CB  . ASN A 1 132 ? 16.568  -21.195 -17.126 1.00 46.57  ? 132 ASN A CB  1 
ATOM   1069 C  CG  . ASN A 1 132 ? 15.644  -22.321 -16.736 1.00 55.08  ? 132 ASN A CG  1 
ATOM   1070 O  OD1 . ASN A 1 132 ? 15.671  -23.393 -17.336 1.00 65.51  ? 132 ASN A OD1 1 
ATOM   1071 N  ND2 . ASN A 1 132 ? 14.820  -22.092 -15.730 1.00 63.44  ? 132 ASN A ND2 1 
ATOM   1072 N  N   . LEU A 1 133 ? 19.687  -20.210 -18.266 1.00 42.72  ? 133 LEU A N   1 
ATOM   1073 C  CA  . LEU A 1 133 ? 20.371  -19.046 -18.809 1.00 43.11  ? 133 LEU A CA  1 
ATOM   1074 C  C   . LEU A 1 133 ? 21.391  -19.536 -19.844 1.00 45.66  ? 133 LEU A C   1 
ATOM   1075 O  O   . LEU A 1 133 ? 22.440  -20.094 -19.500 1.00 44.93  ? 133 LEU A O   1 
ATOM   1076 C  CB  . LEU A 1 133 ? 21.004  -18.262 -17.653 1.00 41.93  ? 133 LEU A CB  1 
ATOM   1077 C  CG  . LEU A 1 133 ? 20.047  -17.893 -16.521 1.00 40.19  ? 133 LEU A CG  1 
ATOM   1078 C  CD1 . LEU A 1 133 ? 20.786  -17.230 -15.372 1.00 40.13  ? 133 LEU A CD1 1 
ATOM   1079 C  CD2 . LEU A 1 133 ? 18.925  -16.995 -17.019 1.00 38.22  ? 133 LEU A CD2 1 
ATOM   1080 N  N   . LEU A 1 134 ? 21.034  -19.356 -21.126 1.00 42.80  ? 134 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 134 ? 21.738  -19.968 -22.242 1.00 41.85  ? 134 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 134 ? 22.699  -18.951 -22.851 1.00 41.02  ? 134 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 134 ? 22.384  -17.757 -22.856 1.00 33.56  ? 134 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 134 ? 20.710  -20.428 -23.275 1.00 41.79  ? 134 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 134 ? 19.556  -21.276 -22.756 1.00 44.08  ? 134 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 134 ? 18.820  -21.902 -23.925 1.00 46.27  ? 134 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 134 ? 20.023  -22.357 -21.799 1.00 45.57  ? 134 LEU A CD2 1 
ATOM   1088 N  N   . ILE A 1 135 ? 23.856  -19.449 -23.332 1.00 42.65  ? 135 ILE A N   1 
ATOM   1089 C  CA  . ILE A 1 135 ? 24.925  -18.636 -23.906 1.00 44.71  ? 135 ILE A CA  1 
ATOM   1090 C  C   . ILE A 1 135 ? 25.214  -19.078 -25.350 1.00 46.66  ? 135 ILE A C   1 
ATOM   1091 O  O   . ILE A 1 135 ? 25.357  -20.270 -25.621 1.00 42.68  ? 135 ILE A O   1 
ATOM   1092 C  CB  . ILE A 1 135 ? 26.169  -18.736 -23.004 1.00 45.87  ? 135 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A 1 135 ? 25.824  -18.327 -21.571 1.00 44.18  ? 135 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A 1 135 ? 27.340  -17.933 -23.562 1.00 44.57  ? 135 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A 1 135 ? 26.731  -18.933 -20.525 1.00 48.59  ? 135 ILE A CD1 1 
ATOM   1096 N  N   . ASN A 1 136 ? 25.296  -18.110 -26.277 1.00 44.14  ? 136 ASN A N   1 
ATOM   1097 C  CA  . ASN A 1 136 ? 25.619  -18.378 -27.671 1.00 49.19  ? 136 ASN A CA  1 
ATOM   1098 C  C   . ASN A 1 136 ? 27.068  -17.947 -27.941 1.00 52.62  ? 136 ASN A C   1 
ATOM   1099 O  O   . ASN A 1 136 ? 27.700  -17.276 -27.113 1.00 44.87  ? 136 ASN A O   1 
ATOM   1100 C  CB  . ASN A 1 136 ? 24.594  -17.729 -28.610 1.00 46.61  ? 136 ASN A CB  1 
ATOM   1101 C  CG  . ASN A 1 136 ? 24.665  -16.217 -28.631 1.00 47.81  ? 136 ASN A CG  1 
ATOM   1102 O  OD1 . ASN A 1 136 ? 25.640  -15.645 -28.146 1.00 43.52  ? 136 ASN A OD1 1 
ATOM   1103 N  ND2 . ASN A 1 136 ? 23.650  -15.572 -29.200 1.00 46.00  ? 136 ASN A ND2 1 
ATOM   1104 N  N   . THR A 1 137 ? 27.576  -18.312 -29.129 1.00 57.62  ? 137 THR A N   1 
ATOM   1105 C  CA  . THR A 1 137 ? 28.989  -18.153 -29.473 1.00 60.27  ? 137 THR A CA  1 
ATOM   1106 C  C   . THR A 1 137 ? 29.389  -16.678 -29.543 1.00 57.32  ? 137 THR A C   1 
ATOM   1107 O  O   . THR A 1 137 ? 30.571  -16.380 -29.449 1.00 61.18  ? 137 THR A O   1 
ATOM   1108 C  CB  . THR A 1 137 ? 29.322  -18.805 -30.822 1.00 63.28  ? 137 THR A CB  1 
ATOM   1109 O  OG1 . THR A 1 137 ? 28.606  -18.056 -31.807 1.00 65.23  ? 137 THR A OG1 1 
ATOM   1110 C  CG2 . THR A 1 137 ? 28.951  -20.271 -30.896 1.00 62.54  ? 137 THR A CG2 1 
ATOM   1111 N  N   . GLU A 1 138 ? 28.408  -15.773 -29.716 1.00 60.31  ? 138 GLU A N   1 
ATOM   1112 C  CA  . GLU A 1 138 ? 28.646  -14.341 -29.888 1.00 59.27  ? 138 GLU A CA  1 
ATOM   1113 C  C   . GLU A 1 138 ? 28.704  -13.617 -28.547 1.00 57.54  ? 138 GLU A C   1 
ATOM   1114 O  O   . GLU A 1 138 ? 28.770  -12.386 -28.545 1.00 55.78  ? 138 GLU A O   1 
ATOM   1115 C  CB  . GLU A 1 138 ? 27.523  -13.688 -30.697 1.00 64.80  ? 138 GLU A CB  1 
ATOM   1116 C  CG  . GLU A 1 138 ? 27.224  -14.386 -32.013 1.00 73.61  ? 138 GLU A CG  1 
ATOM   1117 C  CD  . GLU A 1 138 ? 25.903  -13.972 -32.638 1.00 85.14  ? 138 GLU A CD  1 
ATOM   1118 O  OE1 . GLU A 1 138 ? 25.816  -12.816 -33.104 1.00 84.49  ? 138 GLU A OE1 1 
ATOM   1119 O  OE2 . GLU A 1 138 ? 24.953  -14.800 -32.636 1.00 93.57  ? 138 GLU A OE2 1 
ATOM   1120 N  N   . GLY A 1 139 ? 28.621  -14.380 -27.437 1.00 53.86  ? 139 GLY A N   1 
ATOM   1121 C  CA  . GLY A 1 139 ? 28.766  -13.868 -26.078 1.00 55.66  ? 139 GLY A CA  1 
ATOM   1122 C  C   . GLY A 1 139 ? 27.466  -13.325 -25.463 1.00 56.17  ? 139 GLY A C   1 
ATOM   1123 O  O   . GLY A 1 139 ? 27.505  -12.651 -24.429 1.00 46.69  ? 139 GLY A O   1 
ATOM   1124 N  N   . ALA A 1 140 ? 26.318  -13.589 -26.111 1.00 52.85  ? 140 ALA A N   1 
ATOM   1125 C  CA  . ALA A 1 140 ? 25.007  -13.244 -25.565 1.00 52.65  ? 140 ALA A CA  1 
ATOM   1126 C  C   . ALA A 1 140 ? 24.570  -14.314 -24.554 1.00 47.12  ? 140 ALA A C   1 
ATOM   1127 O  O   . ALA A 1 140 ? 24.803  -15.504 -24.759 1.00 48.14  ? 140 ALA A O   1 
ATOM   1128 C  CB  . ALA A 1 140 ? 23.994  -13.080 -26.683 1.00 52.46  ? 140 ALA A CB  1 
ATOM   1129 N  N   . ILE A 1 141 ? 23.968  -13.883 -23.439 1.00 42.88  ? 141 ILE A N   1 
ATOM   1130 C  CA  . ILE A 1 141 ? 23.270  -14.790 -22.536 1.00 42.56  ? 141 ILE A CA  1 
ATOM   1131 C  C   . ILE A 1 141 ? 21.796  -14.388 -22.515 1.00 41.11  ? 141 ILE A C   1 
ATOM   1132 O  O   . ILE A 1 141 ? 21.484  -13.201 -22.462 1.00 43.16  ? 141 ILE A O   1 
ATOM   1133 C  CB  . ILE A 1 141 ? 23.928  -14.782 -21.141 1.00 41.46  ? 141 ILE A CB  1 
ATOM   1134 C  CG1 . ILE A 1 141 ? 23.348  -15.869 -20.239 1.00 40.66  ? 141 ILE A CG1 1 
ATOM   1135 C  CG2 . ILE A 1 141 ? 23.856  -13.406 -20.497 1.00 42.63  ? 141 ILE A CG2 1 
ATOM   1136 C  CD1 . ILE A 1 141 ? 24.040  -16.008 -18.912 1.00 39.51  ? 141 ILE A CD1 1 
ATOM   1137 N  N   . LYS A 1 142 ? 20.899  -15.377 -22.589 1.00 43.00  ? 142 LYS A N   1 
ATOM   1138 C  CA  . LYS A 1 142 ? 19.471  -15.135 -22.761 1.00 43.44  ? 142 LYS A CA  1 
ATOM   1139 C  C   . LYS A 1 142 ? 18.645  -15.933 -21.750 1.00 40.29  ? 142 LYS A C   1 
ATOM   1140 O  O   . LYS A 1 142 ? 18.919  -17.114 -21.568 1.00 40.82  ? 142 LYS A O   1 
ATOM   1141 C  CB  . LYS A 1 142 ? 19.026  -15.579 -24.154 1.00 46.13  ? 142 LYS A CB  1 
ATOM   1142 C  CG  . LYS A 1 142 ? 19.902  -15.109 -25.297 1.00 48.94  ? 142 LYS A CG  1 
ATOM   1143 C  CD  . LYS A 1 142 ? 19.319  -15.423 -26.659 1.00 50.78  ? 142 LYS A CD  1 
ATOM   1144 C  CE  . LYS A 1 142 ? 20.199  -14.912 -27.783 1.00 52.20  ? 142 LYS A CE  1 
ATOM   1145 N  NZ  . LYS A 1 142 ? 19.403  -14.530 -28.974 1.00 54.16  ? 142 LYS A NZ  1 
ATOM   1146 N  N   . LEU A 1 143 ? 17.612  -15.306 -21.147 1.00 38.93  ? 143 LEU A N   1 
ATOM   1147 C  CA  . LEU A 1 143 ? 16.589  -16.025 -20.383 1.00 36.83  ? 143 LEU A CA  1 
ATOM   1148 C  C   . LEU A 1 143 ? 15.818  -16.965 -21.315 1.00 35.35  ? 143 LEU A C   1 
ATOM   1149 O  O   . LEU A 1 143 ? 15.420  -16.555 -22.392 1.00 37.99  ? 143 LEU A O   1 
ATOM   1150 C  CB  . LEU A 1 143 ? 15.607  -15.054 -19.716 1.00 40.09  ? 143 LEU A CB  1 
ATOM   1151 C  CG  . LEU A 1 143 ? 16.155  -13.750 -19.141 1.00 42.31  ? 143 LEU A CG  1 
ATOM   1152 C  CD1 . LEU A 1 143 ? 15.068  -13.018 -18.380 1.00 45.31  ? 143 LEU A CD1 1 
ATOM   1153 C  CD2 . LEU A 1 143 ? 17.347  -13.982 -18.242 1.00 48.40  ? 143 LEU A CD2 1 
ATOM   1154 N  N   . ALA A 1 144 ? 15.630  -18.225 -20.898 1.00 37.31  ? 144 ALA A N   1 
ATOM   1155 C  CA  . ALA A 1 144 ? 14.877  -19.248 -21.620 1.00 36.89  ? 144 ALA A CA  1 
ATOM   1156 C  C   . ALA A 1 144 ? 13.836  -19.876 -20.688 1.00 39.41  ? 144 ALA A C   1 
ATOM   1157 O  O   . ALA A 1 144 ? 13.783  -19.522 -19.520 1.00 43.30  ? 144 ALA A O   1 
ATOM   1158 C  CB  . ALA A 1 144 ? 15.838  -20.298 -22.112 1.00 34.78  ? 144 ALA A CB  1 
ATOM   1159 N  N   . ASP A 1 145 ? 13.028  -20.822 -21.189 1.00 41.19  ? 145 ASP A N   1 
ATOM   1160 C  CA  . ASP A 1 145 ? 12.138  -21.642 -20.365 1.00 43.75  ? 145 ASP A CA  1 
ATOM   1161 C  C   . ASP A 1 145 ? 11.152  -20.762 -19.585 1.00 43.47  ? 145 ASP A C   1 
ATOM   1162 O  O   . ASP A 1 145 ? 11.285  -20.573 -18.387 1.00 46.84  ? 145 ASP A O   1 
ATOM   1163 C  CB  . ASP A 1 145 ? 12.965  -22.638 -19.546 1.00 49.32  ? 145 ASP A CB  1 
ATOM   1164 C  CG  . ASP A 1 145 ? 13.595  -23.736 -20.403 1.00 56.37  ? 145 ASP A CG  1 
ATOM   1165 O  OD1 . ASP A 1 145 ? 13.275  -23.814 -21.618 1.00 53.56  ? 145 ASP A OD1 1 
ATOM   1166 O  OD2 . ASP A 1 145 ? 14.399  -24.516 -19.862 1.00 59.21  ? 145 ASP A OD2 1 
ATOM   1167 N  N   . PHE A 1 146 ? 10.145  -20.254 -20.316 1.00 45.14  ? 146 PHE A N   1 
ATOM   1168 C  CA  . PHE A 1 146 ? 9.081   -19.384 -19.835 1.00 41.70  ? 146 PHE A CA  1 
ATOM   1169 C  C   . PHE A 1 146 ? 7.795   -20.159 -19.536 1.00 42.39  ? 146 PHE A C   1 
ATOM   1170 O  O   . PHE A 1 146 ? 6.745   -19.542 -19.390 1.00 43.23  ? 146 PHE A O   1 
ATOM   1171 C  CB  . PHE A 1 146 ? 8.780   -18.308 -20.882 1.00 38.54  ? 146 PHE A CB  1 
ATOM   1172 C  CG  . PHE A 1 146 ? 9.741   -17.158 -20.846 1.00 37.18  ? 146 PHE A CG  1 
ATOM   1173 C  CD1 . PHE A 1 146 ? 11.017  -17.293 -21.348 1.00 40.17  ? 146 PHE A CD1 1 
ATOM   1174 C  CD2 . PHE A 1 146 ? 9.378   -15.955 -20.270 1.00 38.86  ? 146 PHE A CD2 1 
ATOM   1175 C  CE1 . PHE A 1 146 ? 11.917  -16.237 -21.269 1.00 46.10  ? 146 PHE A CE1 1 
ATOM   1176 C  CE2 . PHE A 1 146 ? 10.260  -14.887 -20.217 1.00 39.65  ? 146 PHE A CE2 1 
ATOM   1177 C  CZ  . PHE A 1 146 ? 11.532  -15.032 -20.714 1.00 46.37  ? 146 PHE A CZ  1 
ATOM   1178 N  N   . GLY A 1 147 ? 7.887   -21.488 -19.408 1.00 42.38  ? 147 GLY A N   1 
ATOM   1179 C  CA  . GLY A 1 147 ? 6.755   -22.355 -19.113 1.00 40.34  ? 147 GLY A CA  1 
ATOM   1180 C  C   . GLY A 1 147 ? 6.133   -22.098 -17.740 1.00 40.14  ? 147 GLY A C   1 
ATOM   1181 O  O   . GLY A 1 147 ? 4.936   -22.332 -17.559 1.00 39.63  ? 147 GLY A O   1 
ATOM   1182 N  N   . LEU A 1 148 ? 6.942   -21.619 -16.785 1.00 35.60  ? 148 LEU A N   1 
ATOM   1183 C  CA  . LEU A 1 148 ? 6.460   -21.296 -15.452 1.00 39.95  ? 148 LEU A CA  1 
ATOM   1184 C  C   . LEU A 1 148 ? 6.219   -19.794 -15.281 1.00 36.24  ? 148 LEU A C   1 
ATOM   1185 O  O   . LEU A 1 148 ? 5.888   -19.361 -14.192 1.00 43.25  ? 148 LEU A O   1 
ATOM   1186 C  CB  . LEU A 1 148 ? 7.482   -21.836 -14.450 1.00 50.69  ? 148 LEU A CB  1 
ATOM   1187 C  CG  . LEU A 1 148 ? 7.407   -23.348 -14.225 1.00 58.24  ? 148 LEU A CG  1 
ATOM   1188 C  CD1 . LEU A 1 148 ? 8.664   -23.866 -13.548 1.00 60.65  ? 148 LEU A CD1 1 
ATOM   1189 C  CD2 . LEU A 1 148 ? 6.181   -23.705 -13.390 1.00 64.14  ? 148 LEU A CD2 1 
ATOM   1190 N  N   . ALA A 1 149 ? 6.306   -19.017 -16.363 1.00 34.84  ? 149 ALA A N   1 
ATOM   1191 C  CA  . ALA A 1 149 ? 6.064   -17.577 -16.349 1.00 36.74  ? 149 ALA A CA  1 
ATOM   1192 C  C   . ALA A 1 149 ? 4.569   -17.280 -16.279 1.00 39.31  ? 149 ALA A C   1 
ATOM   1193 O  O   . ALA A 1 149 ? 3.756   -18.190 -16.428 1.00 33.53  ? 149 ALA A O   1 
ATOM   1194 C  CB  . ALA A 1 149 ? 6.647   -16.934 -17.588 1.00 39.61  ? 149 ALA A CB  1 
ATOM   1195 N  N   . ARG A 1 150 ? 4.233   -15.990 -16.097 1.00 40.01  ? 150 ARG A N   1 
ATOM   1196 C  CA  . ARG A 1 150 ? 2.853   -15.534 -15.993 1.00 42.70  ? 150 ARG A CA  1 
ATOM   1197 C  C   . ARG A 1 150 ? 2.785   -14.024 -16.244 1.00 38.47  ? 150 ARG A C   1 
ATOM   1198 O  O   . ARG A 1 150 ? 3.670   -13.288 -15.803 1.00 33.51  ? 150 ARG A O   1 
ATOM   1199 C  CB  . ARG A 1 150 ? 2.306   -15.901 -14.606 1.00 47.42  ? 150 ARG A CB  1 
ATOM   1200 C  CG  . ARG A 1 150 ? 1.067   -15.122 -14.194 1.00 50.94  ? 150 ARG A CG  1 
ATOM   1201 C  CD  . ARG A 1 150 ? 0.656   -15.370 -12.765 1.00 50.47  ? 150 ARG A CD  1 
ATOM   1202 N  NE  . ARG A 1 150 ? -0.282  -16.473 -12.673 1.00 52.57  ? 150 ARG A NE  1 
ATOM   1203 C  CZ  . ARG A 1 150 ? -1.575  -16.378 -12.951 1.00 49.45  ? 150 ARG A CZ  1 
ATOM   1204 N  NH1 . ARG A 1 150 ? -2.365  -17.418 -12.757 1.00 50.85  ? 150 ARG A NH1 1 
ATOM   1205 N  NH2 . ARG A 1 150 ? -2.078  -15.233 -13.375 1.00 47.82  ? 150 ARG A NH2 1 
ATOM   1206 N  N   . ALA A 1 151 ? 1.756   -13.595 -16.997 1.00 38.52  ? 151 ALA A N   1 
ATOM   1207 C  CA  . ALA A 1 151 ? 1.359   -12.194 -17.092 1.00 39.64  ? 151 ALA A CA  1 
ATOM   1208 C  C   . ALA A 1 151 ? 0.806   -11.741 -15.736 1.00 45.15  ? 151 ALA A C   1 
ATOM   1209 O  O   . ALA A 1 151 ? 0.129   -12.491 -15.037 1.00 52.24  ? 151 ALA A O   1 
ATOM   1210 C  CB  . ALA A 1 151 ? 0.356   -12.026 -18.201 1.00 40.92  ? 151 ALA A CB  1 
ATOM   1211 N  N   . PHE A 1 152 ? 1.153   -10.531 -15.306 1.00 44.83  ? 152 PHE A N   1 
ATOM   1212 C  CA  . PHE A 1 152 ? 0.834   -10.114 -13.952 1.00 42.49  ? 152 PHE A CA  1 
ATOM   1213 C  C   . PHE A 1 152 ? 0.159   -8.747  -14.030 1.00 46.23  ? 152 PHE A C   1 
ATOM   1214 O  O   . PHE A 1 152 ? 0.281   -8.053  -15.035 1.00 52.48  ? 152 PHE A O   1 
ATOM   1215 C  CB  . PHE A 1 152 ? 2.082   -10.212 -13.071 1.00 40.10  ? 152 PHE A CB  1 
ATOM   1216 C  CG  . PHE A 1 152 ? 3.079   -9.104  -13.260 1.00 36.12  ? 152 PHE A CG  1 
ATOM   1217 C  CD1 . PHE A 1 152 ? 2.832   -7.843  -12.761 1.00 35.79  ? 152 PHE A CD1 1 
ATOM   1218 C  CD2 . PHE A 1 152 ? 4.271   -9.334  -13.913 1.00 34.07  ? 152 PHE A CD2 1 
ATOM   1219 C  CE1 . PHE A 1 152 ? 3.762   -6.831  -12.916 1.00 35.00  ? 152 PHE A CE1 1 
ATOM   1220 C  CE2 . PHE A 1 152 ? 5.194   -8.319  -14.081 1.00 31.98  ? 152 PHE A CE2 1 
ATOM   1221 C  CZ  . PHE A 1 152 ? 4.938   -7.071  -13.578 1.00 32.82  ? 152 PHE A CZ  1 
ATOM   1222 N  N   . GLY A 1 153 ? -0.610  -8.418  -12.988 1.00 49.13  ? 153 GLY A N   1 
ATOM   1223 C  CA  . GLY A 1 153 ? -1.502  -7.271  -12.990 1.00 48.42  ? 153 GLY A CA  1 
ATOM   1224 C  C   . GLY A 1 153 ? -0.902  -6.112  -12.207 1.00 48.38  ? 153 GLY A C   1 
ATOM   1225 O  O   . GLY A 1 153 ? 0.018   -6.312  -11.422 1.00 51.39  ? 153 GLY A O   1 
ATOM   1226 N  N   . VAL A 1 154 ? -1.423  -4.912  -12.466 1.00 50.97  ? 154 VAL A N   1 
ATOM   1227 C  CA  . VAL A 1 154 ? -1.100  -3.687  -11.747 1.00 56.68  ? 154 VAL A CA  1 
ATOM   1228 C  C   . VAL A 1 154 ? -2.371  -3.251  -11.019 1.00 57.65  ? 154 VAL A C   1 
ATOM   1229 O  O   . VAL A 1 154 ? -3.299  -2.756  -11.659 1.00 57.02  ? 154 VAL A O   1 
ATOM   1230 C  CB  . VAL A 1 154 ? -0.573  -2.625  -12.741 1.00 62.19  ? 154 VAL A CB  1 
ATOM   1231 C  CG1 . VAL A 1 154 ? -0.493  -1.209  -12.184 1.00 66.49  ? 154 VAL A CG1 1 
ATOM   1232 C  CG2 . VAL A 1 154 ? 0.782   -3.033  -13.293 1.00 67.69  ? 154 VAL A CG2 1 
ATOM   1233 N  N   . PRO A 1 155 ? -2.507  -3.478  -9.685  1.00 73.95  ? 155 PRO A N   1 
ATOM   1234 C  CA  . PRO A 1 155 ? -1.523  -4.212  -8.886  1.00 69.68  ? 155 PRO A CA  1 
ATOM   1235 C  C   . PRO A 1 155 ? -1.744  -5.720  -8.968  1.00 66.72  ? 155 PRO A C   1 
ATOM   1236 O  O   . PRO A 1 155 ? -2.685  -6.177  -9.622  1.00 71.15  ? 155 PRO A O   1 
ATOM   1237 C  CB  . PRO A 1 155 ? -1.804  -3.710  -7.462  1.00 72.19  ? 155 PRO A CB  1 
ATOM   1238 C  CG  . PRO A 1 155 ? -3.309  -3.485  -7.450  1.00 68.94  ? 155 PRO A CG  1 
ATOM   1239 C  CD  . PRO A 1 155 ? -3.649  -3.032  -8.860  1.00 72.23  ? 155 PRO A CD  1 
ATOM   1240 N  N   . VAL A 1 156 ? -0.880  -6.476  -8.277  1.00 61.66  ? 156 VAL A N   1 
ATOM   1241 C  CA  . VAL A 1 156 ? -0.885  -7.934  -8.334  1.00 60.13  ? 156 VAL A CA  1 
ATOM   1242 C  C   . VAL A 1 156 ? -2.039  -8.465  -7.485  1.00 58.71  ? 156 VAL A C   1 
ATOM   1243 O  O   . VAL A 1 156 ? -2.559  -7.728  -6.647  1.00 55.94  ? 156 VAL A O   1 
ATOM   1244 C  CB  . VAL A 1 156 ? 0.459   -8.535  -7.871  1.00 62.94  ? 156 VAL A CB  1 
ATOM   1245 C  CG1 . VAL A 1 156 ? 1.611   -8.131  -8.787  1.00 62.35  ? 156 VAL A CG1 1 
ATOM   1246 C  CG2 . VAL A 1 156 ? 0.775   -8.193  -6.419  1.00 62.07  ? 156 VAL A CG2 1 
ATOM   1247 N  N   . ARG A 1 157 ? -2.424  -9.726  -7.754  1.00 55.30  ? 157 ARG A N   1 
ATOM   1248 C  CA  . ARG A 1 157 ? -3.247  -10.562 -6.883  1.00 61.24  ? 157 ARG A CA  1 
ATOM   1249 C  C   . ARG A 1 157 ? -2.478  -11.860 -6.575  1.00 58.40  ? 157 ARG A C   1 
ATOM   1250 O  O   . ARG A 1 157 ? -1.330  -12.009 -6.989  1.00 58.62  ? 157 ARG A O   1 
ATOM   1251 C  CB  . ARG A 1 157 ? -4.627  -10.798 -7.523  1.00 68.37  ? 157 ARG A CB  1 
ATOM   1252 C  CG  . ARG A 1 157 ? -4.619  -11.481 -8.886  1.00 71.60  ? 157 ARG A CG  1 
ATOM   1253 C  CD  . ARG A 1 157 ? -5.986  -11.964 -9.359  1.00 70.76  ? 157 ARG A CD  1 
ATOM   1254 N  NE  . ARG A 1 157 ? -5.907  -13.359 -9.798  1.00 71.14  ? 157 ARG A NE  1 
ATOM   1255 C  CZ  . ARG A 1 157 ? -5.645  -13.776 -11.036 1.00 67.52  ? 157 ARG A CZ  1 
ATOM   1256 N  NH1 . ARG A 1 157 ? -5.538  -12.923 -12.043 1.00 61.07  ? 157 ARG A NH1 1 
ATOM   1257 N  NH2 . ARG A 1 157 ? -5.491  -15.070 -11.264 1.00 69.51  ? 157 ARG A NH2 1 
ATOM   1258 N  N   . THR A 1 158 ? -3.088  -12.787 -5.815  1.00 53.10  ? 158 THR A N   1 
ATOM   1259 C  CA  . THR A 1 158 ? -2.482  -14.074 -5.479  1.00 55.35  ? 158 THR A CA  1 
ATOM   1260 C  C   . THR A 1 158 ? -2.256  -14.902 -6.751  1.00 51.35  ? 158 THR A C   1 
ATOM   1261 O  O   . THR A 1 158 ? -3.175  -15.054 -7.555  1.00 53.83  ? 158 THR A O   1 
ATOM   1262 C  CB  . THR A 1 158 ? -3.325  -14.804 -4.415  1.00 60.10  ? 158 THR A CB  1 
ATOM   1263 O  OG1 . THR A 1 158 ? -3.252  -13.993 -3.242  1.00 69.01  ? 158 THR A OG1 1 
ATOM   1264 C  CG2 . THR A 1 158 ? -2.850  -16.203 -4.072  1.00 59.95  ? 158 THR A CG2 1 
ATOM   1265 N  N   . TYR A 1 159 ? -1.022  -15.421 -6.914  1.00 43.59  ? 159 TYR A N   1 
ATOM   1266 C  CA  . TYR A 1 159 ? -0.630  -16.321 -7.995  1.00 43.80  ? 159 TYR A CA  1 
ATOM   1267 C  C   . TYR A 1 159 ? -0.186  -17.658 -7.399  1.00 40.23  ? 159 TYR A C   1 
ATOM   1268 O  O   . TYR A 1 159 ? -0.326  -17.860 -6.200  1.00 40.38  ? 159 TYR A O   1 
ATOM   1269 C  CB  . TYR A 1 159 ? 0.456   -15.669 -8.858  1.00 46.93  ? 159 TYR A CB  1 
ATOM   1270 C  CG  . TYR A 1 159 ? 0.066   -14.336 -9.448  1.00 43.10  ? 159 TYR A CG  1 
ATOM   1271 C  CD1 . TYR A 1 159 ? -1.143  -14.161 -10.087 1.00 47.23  ? 159 TYR A CD1 1 
ATOM   1272 C  CD2 . TYR A 1 159 ? 0.923   -13.257 -9.396  1.00 44.74  ? 159 TYR A CD2 1 
ATOM   1273 C  CE1 . TYR A 1 159 ? -1.501  -12.942 -10.641 1.00 48.33  ? 159 TYR A CE1 1 
ATOM   1274 C  CE2 . TYR A 1 159 ? 0.587   -12.030 -9.936  1.00 42.46  ? 159 TYR A CE2 1 
ATOM   1275 C  CZ  . TYR A 1 159 ? -0.635  -11.869 -10.560 1.00 43.83  ? 159 TYR A CZ  1 
ATOM   1276 O  OH  . TYR A 1 159 ? -0.978  -10.651 -11.108 1.00 46.27  ? 159 TYR A OH  1 
HETATM 1277 N  N   . TPO A 1 160 ? 0.317   -18.578 -8.239  1.00 41.05  ? 160 TPO A N   1 
HETATM 1278 C  CA  . TPO A 1 160 ? 0.694   -19.924 -7.806  1.00 45.70  ? 160 TPO A CA  1 
HETATM 1279 C  CB  . TPO A 1 160 ? 1.187   -20.759 -9.001  1.00 44.33  ? 160 TPO A CB  1 
HETATM 1280 C  CG2 . TPO A 1 160 ? 1.533   -22.187 -8.644  1.00 44.37  ? 160 TPO A CG2 1 
HETATM 1281 O  OG1 . TPO A 1 160 ? 0.089   -20.785 -9.982  1.00 45.13  ? 160 TPO A OG1 1 
HETATM 1282 P  P   . TPO A 1 160 ? 0.172   -19.940 -11.407 1.00 40.34  ? 160 TPO A P   1 
HETATM 1283 O  O1P . TPO A 1 160 ? -1.182  -20.098 -12.040 1.00 39.64  ? 160 TPO A O1P 1 
HETATM 1284 O  O2P . TPO A 1 160 ? 0.456   -18.487 -11.041 1.00 34.71  ? 160 TPO A O2P 1 
HETATM 1285 O  O3P . TPO A 1 160 ? 1.285   -20.585 -12.211 1.00 35.62  ? 160 TPO A O3P 1 
HETATM 1286 C  C   . TPO A 1 160 ? 1.765   -19.873 -6.707  1.00 51.51  ? 160 TPO A C   1 
HETATM 1287 O  O   . TPO A 1 160 ? 2.706   -19.085 -6.800  1.00 46.86  ? 160 TPO A O   1 
ATOM   1288 N  N   . HIS A 1 161 ? 1.632   -20.740 -5.690  1.00 53.42  ? 161 HIS A N   1 
ATOM   1289 C  CA  . HIS A 1 161 ? 2.556   -20.777 -4.565  1.00 59.57  ? 161 HIS A CA  1 
ATOM   1290 C  C   . HIS A 1 161 ? 3.792   -21.640 -4.862  1.00 61.73  ? 161 HIS A C   1 
ATOM   1291 O  O   . HIS A 1 161 ? 4.917   -21.234 -4.561  1.00 56.85  ? 161 HIS A O   1 
ATOM   1292 C  CB  . HIS A 1 161 ? 1.823   -21.227 -3.297  1.00 67.51  ? 161 HIS A CB  1 
ATOM   1293 C  CG  . HIS A 1 161 ? 2.733   -21.394 -2.121  1.00 84.71  ? 161 HIS A CG  1 
ATOM   1294 N  ND1 . HIS A 1 161 ? 3.193   -20.335 -1.364  1.00 86.85  ? 161 HIS A ND1 1 
ATOM   1295 C  CD2 . HIS A 1 161 ? 3.261   -22.503 -1.569  1.00 90.29  ? 161 HIS A CD2 1 
ATOM   1296 C  CE1 . HIS A 1 161 ? 3.972   -20.798 -0.394  1.00 85.88  ? 161 HIS A CE1 1 
ATOM   1297 N  NE2 . HIS A 1 161 ? 4.030   -22.109 -0.500  1.00 85.91  ? 161 HIS A NE2 1 
ATOM   1298 N  N   . GLU A 1 162 ? 3.596   -22.846 -5.418  1.00 67.66  ? 162 GLU A N   1 
ATOM   1299 C  CA  . GLU A 1 162 ? 4.704   -23.736 -5.763  1.00 72.43  ? 162 GLU A CA  1 
ATOM   1300 C  C   . GLU A 1 162 ? 5.485   -23.142 -6.940  1.00 68.75  ? 162 GLU A C   1 
ATOM   1301 O  O   . GLU A 1 162 ? 5.309   -23.593 -8.068  1.00 68.51  ? 162 GLU A O   1 
ATOM   1302 C  CB  . GLU A 1 162 ? 4.215   -25.146 -6.141  1.00 76.44  ? 162 GLU A CB  1 
ATOM   1303 C  CG  . GLU A 1 162 ? 3.700   -25.977 -4.972  1.00 86.02  ? 162 GLU A CG  1 
ATOM   1304 C  CD  . GLU A 1 162 ? 2.317   -25.617 -4.442  1.00 94.88  ? 162 GLU A CD  1 
ATOM   1305 O  OE1 . GLU A 1 162 ? 1.694   -24.657 -4.958  1.00 91.19  ? 162 GLU A OE1 1 
ATOM   1306 O  OE2 . GLU A 1 162 ? 1.862   -26.300 -3.504  1.00 100.27 ? 162 GLU A OE2 1 
ATOM   1307 N  N   . VAL A 1 163 ? 6.337   -22.128 -6.696  1.00 61.19  ? 163 VAL A N   1 
ATOM   1308 C  CA  . VAL A 1 163 ? 7.113   -21.512 -7.775  1.00 55.47  ? 163 VAL A CA  1 
ATOM   1309 C  C   . VAL A 1 163 ? 8.571   -21.280 -7.350  1.00 48.29  ? 163 VAL A C   1 
ATOM   1310 O  O   . VAL A 1 163 ? 8.840   -21.053 -6.180  1.00 49.15  ? 163 VAL A O   1 
ATOM   1311 C  CB  . VAL A 1 163 ? 6.464   -20.207 -8.278  1.00 51.58  ? 163 VAL A CB  1 
ATOM   1312 C  CG1 . VAL A 1 163 ? 5.103   -20.470 -8.895  1.00 54.33  ? 163 VAL A CG1 1 
ATOM   1313 C  CG2 . VAL A 1 163 ? 6.370   -19.148 -7.193  1.00 52.65  ? 163 VAL A CG2 1 
ATOM   1314 N  N   . VAL A 1 164 ? 9.482   -21.297 -8.343  1.00 44.26  ? 164 VAL A N   1 
ATOM   1315 C  CA  . VAL A 1 164 ? 10.933  -21.140 -8.225  1.00 39.73  ? 164 VAL A CA  1 
ATOM   1316 C  C   . VAL A 1 164 ? 11.548  -22.387 -7.586  1.00 39.15  ? 164 VAL A C   1 
ATOM   1317 O  O   . VAL A 1 164 ? 11.113  -22.829 -6.529  1.00 47.82  ? 164 VAL A O   1 
ATOM   1318 C  CB  . VAL A 1 164 ? 11.368  -19.860 -7.475  1.00 38.10  ? 164 VAL A CB  1 
ATOM   1319 C  CG1 . VAL A 1 164 ? 12.855  -19.581 -7.646  1.00 38.57  ? 164 VAL A CG1 1 
ATOM   1320 C  CG2 . VAL A 1 164 ? 10.593  -18.626 -7.902  1.00 38.76  ? 164 VAL A CG2 1 
ATOM   1321 N  N   . THR A 1 165 ? 12.637  -22.869 -8.192  1.00 43.27  ? 165 THR A N   1 
ATOM   1322 C  CA  . THR A 1 165 ? 13.465  -23.947 -7.669  1.00 46.80  ? 165 THR A CA  1 
ATOM   1323 C  C   . THR A 1 165 ? 13.988  -23.506 -6.310  1.00 47.02  ? 165 THR A C   1 
ATOM   1324 O  O   . THR A 1 165 ? 14.258  -22.319 -6.117  1.00 51.20  ? 165 THR A O   1 
ATOM   1325 C  CB  . THR A 1 165 ? 14.622  -24.284 -8.625  1.00 44.89  ? 165 THR A CB  1 
ATOM   1326 O  OG1 . THR A 1 165 ? 14.010  -24.868 -9.776  1.00 48.11  ? 165 THR A OG1 1 
ATOM   1327 C  CG2 . THR A 1 165 ? 15.650  -25.235 -8.049  1.00 47.05  ? 165 THR A CG2 1 
ATOM   1328 N  N   . LEU A 1 166 ? 14.145  -24.474 -5.401  1.00 48.58  ? 166 LEU A N   1 
ATOM   1329 C  CA  . LEU A 1 166 ? 14.380  -24.212 -3.987  1.00 47.12  ? 166 LEU A CA  1 
ATOM   1330 C  C   . LEU A 1 166 ? 15.541  -23.243 -3.762  1.00 41.40  ? 166 LEU A C   1 
ATOM   1331 O  O   . LEU A 1 166 ? 15.381  -22.240 -3.060  1.00 44.83  ? 166 LEU A O   1 
ATOM   1332 C  CB  . LEU A 1 166 ? 14.656  -25.549 -3.310  1.00 49.81  ? 166 LEU A CB  1 
ATOM   1333 C  CG  . LEU A 1 166 ? 14.588  -25.526 -1.790  1.00 48.16  ? 166 LEU A CG  1 
ATOM   1334 C  CD1 . LEU A 1 166 ? 13.228  -25.048 -1.312  1.00 49.17  ? 166 LEU A CD1 1 
ATOM   1335 C  CD2 . LEU A 1 166 ? 14.881  -26.913 -1.258  1.00 48.05  ? 166 LEU A CD2 1 
ATOM   1336 N  N   . TRP A 1 167 ? 16.682  -23.523 -4.402  1.00 39.90  ? 167 TRP A N   1 
ATOM   1337 C  CA  . TRP A 1 167 ? 17.931  -22.815 -4.144  1.00 39.78  ? 167 TRP A CA  1 
ATOM   1338 C  C   . TRP A 1 167 ? 17.831  -21.348 -4.533  1.00 39.85  ? 167 TRP A C   1 
ATOM   1339 O  O   . TRP A 1 167 ? 18.623  -20.553 -4.044  1.00 44.17  ? 167 TRP A O   1 
ATOM   1340 C  CB  . TRP A 1 167 ? 19.095  -23.460 -4.885  1.00 42.17  ? 167 TRP A CB  1 
ATOM   1341 C  CG  . TRP A 1 167 ? 19.473  -24.814 -4.384  1.00 43.47  ? 167 TRP A CG  1 
ATOM   1342 C  CD1 . TRP A 1 167 ? 18.883  -25.529 -3.385  1.00 43.58  ? 167 TRP A CD1 1 
ATOM   1343 C  CD2 . TRP A 1 167 ? 20.530  -25.634 -4.897  1.00 45.96  ? 167 TRP A CD2 1 
ATOM   1344 N  NE1 . TRP A 1 167 ? 19.502  -26.739 -3.237  1.00 45.34  ? 167 TRP A NE1 1 
ATOM   1345 C  CE2 . TRP A 1 167 ? 20.519  -26.831 -4.150  1.00 49.65  ? 167 TRP A CE2 1 
ATOM   1346 C  CE3 . TRP A 1 167 ? 21.471  -25.475 -5.918  1.00 54.25  ? 167 TRP A CE3 1 
ATOM   1347 C  CZ2 . TRP A 1 167 ? 21.431  -27.859 -4.381  1.00 51.41  ? 167 TRP A CZ2 1 
ATOM   1348 C  CZ3 . TRP A 1 167 ? 22.371  -26.493 -6.152  1.00 57.34  ? 167 TRP A CZ3 1 
ATOM   1349 C  CH2 . TRP A 1 167 ? 22.343  -27.670 -5.397  1.00 55.17  ? 167 TRP A CH2 1 
ATOM   1350 N  N   . TYR A 1 168 ? 16.882  -21.021 -5.423  1.00 39.84  ? 168 TYR A N   1 
ATOM   1351 C  CA  . TYR A 1 168 ? 16.739  -19.679 -5.964  1.00 36.24  ? 168 TYR A CA  1 
ATOM   1352 C  C   . TYR A 1 168 ? 15.440  -19.028 -5.500  1.00 36.22  ? 168 TYR A C   1 
ATOM   1353 O  O   . TYR A 1 168 ? 15.132  -17.951 -6.000  1.00 40.27  ? 168 TYR A O   1 
ATOM   1354 C  CB  . TYR A 1 168 ? 16.867  -19.748 -7.487  1.00 36.69  ? 168 TYR A CB  1 
ATOM   1355 C  CG  . TYR A 1 168 ? 18.156  -20.414 -7.887  1.00 35.28  ? 168 TYR A CG  1 
ATOM   1356 C  CD1 . TYR A 1 168 ? 19.369  -19.762 -7.743  1.00 35.04  ? 168 TYR A CD1 1 
ATOM   1357 C  CD2 . TYR A 1 168 ? 18.183  -21.750 -8.251  1.00 37.12  ? 168 TYR A CD2 1 
ATOM   1358 C  CE1 . TYR A 1 168 ? 20.567  -20.394 -8.042  1.00 37.99  ? 168 TYR A CE1 1 
ATOM   1359 C  CE2 . TYR A 1 168 ? 19.373  -22.407 -8.521  1.00 38.61  ? 168 TYR A CE2 1 
ATOM   1360 C  CZ  . TYR A 1 168 ? 20.574  -21.730 -8.410  1.00 39.75  ? 168 TYR A CZ  1 
ATOM   1361 O  OH  . TYR A 1 168 ? 21.753  -22.377 -8.717  1.00 41.69  ? 168 TYR A OH  1 
ATOM   1362 N  N   . ARG A 1 169 ? 14.731  -19.636 -4.528  1.00 34.27  ? 169 ARG A N   1 
ATOM   1363 C  CA  . ARG A 1 169 ? 13.404  -19.174 -4.096  1.00 35.93  ? 169 ARG A CA  1 
ATOM   1364 C  C   . ARG A 1 169 ? 13.494  -18.058 -3.053  1.00 34.96  ? 169 ARG A C   1 
ATOM   1365 O  O   . ARG A 1 169 ? 14.092  -18.237 -1.993  1.00 33.41  ? 169 ARG A O   1 
ATOM   1366 C  CB  . ARG A 1 169 ? 12.565  -20.312 -3.496  1.00 35.72  ? 169 ARG A CB  1 
ATOM   1367 C  CG  . ARG A 1 169 ? 11.129  -19.915 -3.173  1.00 37.88  ? 169 ARG A CG  1 
ATOM   1368 C  CD  . ARG A 1 169 ? 10.256  -21.098 -2.788  1.00 41.55  ? 169 ARG A CD  1 
ATOM   1369 N  NE  . ARG A 1 169 ? 10.330  -22.183 -3.757  1.00 45.94  ? 169 ARG A NE  1 
ATOM   1370 C  CZ  . ARG A 1 169 ? 10.086  -23.464 -3.495  1.00 47.52  ? 169 ARG A CZ  1 
ATOM   1371 N  NH1 . ARG A 1 169 ? 9.708   -23.853 -2.287  1.00 47.34  ? 169 ARG A NH1 1 
ATOM   1372 N  NH2 . ARG A 1 169 ? 10.232  -24.360 -4.455  1.00 45.18  ? 169 ARG A NH2 1 
ATOM   1373 N  N   . ALA A 1 170 ? 12.840  -16.928 -3.348  1.00 39.27  ? 170 ALA A N   1 
ATOM   1374 C  CA  . ALA A 1 170 ? 12.804  -15.768 -2.461  1.00 41.25  ? 170 ALA A CA  1 
ATOM   1375 C  C   . ALA A 1 170 ? 12.095  -16.105 -1.147  1.00 43.54  ? 170 ALA A C   1 
ATOM   1376 O  O   . ALA A 1 170 ? 11.167  -16.917 -1.108  1.00 37.52  ? 170 ALA A O   1 
ATOM   1377 C  CB  . ALA A 1 170 ? 12.150  -14.582 -3.146  1.00 40.65  ? 170 ALA A CB  1 
ATOM   1378 N  N   . PRO A 1 171 ? 12.528  -15.472 -0.030  1.00 44.30  ? 171 PRO A N   1 
ATOM   1379 C  CA  . PRO A 1 171 ? 12.002  -15.780 1.294   1.00 44.43  ? 171 PRO A CA  1 
ATOM   1380 C  C   . PRO A 1 171 ? 10.501  -15.529 1.446   1.00 46.14  ? 171 PRO A C   1 
ATOM   1381 O  O   . PRO A 1 171 ? 9.834   -16.329 2.090   1.00 48.77  ? 171 PRO A O   1 
ATOM   1382 C  CB  . PRO A 1 171 ? 12.856  -14.894 2.210   1.00 42.38  ? 171 PRO A CB  1 
ATOM   1383 C  CG  . PRO A 1 171 ? 13.262  -13.761 1.332   1.00 42.93  ? 171 PRO A CG  1 
ATOM   1384 C  CD  . PRO A 1 171 ? 13.576  -14.440 0.025   1.00 43.43  ? 171 PRO A CD  1 
ATOM   1385 N  N   . GLU A 1 172 ? 9.961   -14.477 0.814   1.00 46.58  ? 172 GLU A N   1 
ATOM   1386 C  CA  . GLU A 1 172 ? 8.533   -14.174 0.892   1.00 44.55  ? 172 GLU A CA  1 
ATOM   1387 C  C   . GLU A 1 172 ? 7.703   -15.348 0.368   1.00 48.26  ? 172 GLU A C   1 
ATOM   1388 O  O   . GLU A 1 172 ? 6.550   -15.498 0.776   1.00 51.62  ? 172 GLU A O   1 
ATOM   1389 C  CB  . GLU A 1 172 ? 8.144   -12.878 0.161   1.00 46.39  ? 172 GLU A CB  1 
ATOM   1390 C  CG  . GLU A 1 172 ? 8.416   -12.876 -1.337  1.00 48.19  ? 172 GLU A CG  1 
ATOM   1391 C  CD  . GLU A 1 172 ? 9.804   -12.379 -1.707  1.00 48.17  ? 172 GLU A CD  1 
ATOM   1392 O  OE1 . GLU A 1 172 ? 9.944   -11.738 -2.766  1.00 41.86  ? 172 GLU A OE1 1 
ATOM   1393 O  OE2 . GLU A 1 172 ? 10.746  -12.607 -0.907  1.00 51.99  ? 172 GLU A OE2 1 
ATOM   1394 N  N   . ILE A 1 173 ? 8.264   -16.171 -0.536  1.00 48.43  ? 173 ILE A N   1 
ATOM   1395 C  CA  . ILE A 1 173 ? 7.551   -17.345 -1.036  1.00 47.93  ? 173 ILE A CA  1 
ATOM   1396 C  C   . ILE A 1 173 ? 7.701   -18.503 -0.046  1.00 48.32  ? 173 ILE A C   1 
ATOM   1397 O  O   . ILE A 1 173 ? 6.729   -19.216 0.210   1.00 50.20  ? 173 ILE A O   1 
ATOM   1398 C  CB  . ILE A 1 173 ? 7.994   -17.750 -2.455  1.00 50.19  ? 173 ILE A CB  1 
ATOM   1399 C  CG1 . ILE A 1 173 ? 7.825   -16.614 -3.467  1.00 52.35  ? 173 ILE A CG1 1 
ATOM   1400 C  CG2 . ILE A 1 173 ? 7.246   -19.000 -2.901  1.00 51.94  ? 173 ILE A CG2 1 
ATOM   1401 C  CD1 . ILE A 1 173 ? 8.515   -16.887 -4.785  1.00 56.04  ? 173 ILE A CD1 1 
ATOM   1402 N  N   . LEU A 1 174 ? 8.912   -18.688 0.504   1.00 45.38  ? 174 LEU A N   1 
ATOM   1403 C  CA  . LEU A 1 174 ? 9.167   -19.690 1.540   1.00 42.58  ? 174 LEU A CA  1 
ATOM   1404 C  C   . LEU A 1 174 ? 8.311   -19.462 2.800   1.00 41.28  ? 174 LEU A C   1 
ATOM   1405 O  O   . LEU A 1 174 ? 7.895   -20.431 3.425   1.00 44.58  ? 174 LEU A O   1 
ATOM   1406 C  CB  . LEU A 1 174 ? 10.658  -19.673 1.881   1.00 39.89  ? 174 LEU A CB  1 
ATOM   1407 C  CG  . LEU A 1 174 ? 11.602  -20.282 0.842   1.00 40.41  ? 174 LEU A CG  1 
ATOM   1408 C  CD1 . LEU A 1 174 ? 13.040  -19.844 1.094   1.00 41.85  ? 174 LEU A CD1 1 
ATOM   1409 C  CD2 . LEU A 1 174 ? 11.524  -21.802 0.832   1.00 40.47  ? 174 LEU A CD2 1 
ATOM   1410 N  N   . LEU A 1 175 ? 8.030   -18.199 3.157   1.00 41.21  ? 175 LEU A N   1 
ATOM   1411 C  CA  . LEU A 1 175 ? 7.256   -17.811 4.335   1.00 49.81  ? 175 LEU A CA  1 
ATOM   1412 C  C   . LEU A 1 175 ? 5.775   -17.572 4.000   1.00 59.02  ? 175 LEU A C   1 
ATOM   1413 O  O   . LEU A 1 175 ? 5.034   -17.041 4.836   1.00 63.11  ? 175 LEU A O   1 
ATOM   1414 C  CB  . LEU A 1 175 ? 7.879   -16.531 4.914   1.00 51.51  ? 175 LEU A CB  1 
ATOM   1415 C  CG  . LEU A 1 175 ? 9.281   -16.680 5.504   1.00 51.49  ? 175 LEU A CG  1 
ATOM   1416 C  CD1 . LEU A 1 175 ? 9.900   -15.321 5.825   1.00 49.10  ? 175 LEU A CD1 1 
ATOM   1417 C  CD2 . LEU A 1 175 ? 9.252   -17.561 6.745   1.00 51.67  ? 175 LEU A CD2 1 
ATOM   1418 N  N   . GLY A 1 176 ? 5.374   -17.920 2.764   1.00 60.13  ? 176 GLY A N   1 
ATOM   1419 C  CA  . GLY A 1 176 ? 3.986   -17.999 2.320   1.00 57.10  ? 176 GLY A CA  1 
ATOM   1420 C  C   . GLY A 1 176 ? 3.201   -16.683 2.360   1.00 56.43  ? 176 GLY A C   1 
ATOM   1421 O  O   . GLY A 1 176 ? 2.077   -16.665 2.845   1.00 58.42  ? 176 GLY A O   1 
ATOM   1422 N  N   A CYS A 1 177 ? 3.788   -15.586 1.849   0.50 56.70  ? 177 CYS A N   1 
ATOM   1423 N  N   B CYS A 1 177 ? 3.789   -15.605 1.831   0.50 57.73  ? 177 CYS A N   1 
ATOM   1424 C  CA  A CYS A 1 177 ? 3.063   -14.333 1.652   0.50 57.63  ? 177 CYS A CA  1 
ATOM   1425 C  CA  B CYS A 1 177 ? 3.078   -14.351 1.621   0.50 59.24  ? 177 CYS A CA  1 
ATOM   1426 C  C   A CYS A 1 177 ? 1.955   -14.541 0.618   0.50 60.33  ? 177 CYS A C   1 
ATOM   1427 C  C   B CYS A 1 177 ? 1.952   -14.546 0.605   0.50 61.14  ? 177 CYS A C   1 
ATOM   1428 O  O   A CYS A 1 177 ? 2.109   -15.335 -0.307  0.50 55.65  ? 177 CYS A O   1 
ATOM   1429 O  O   B CYS A 1 177 ? 2.089   -15.337 -0.325  0.50 56.17  ? 177 CYS A O   1 
ATOM   1430 C  CB  A CYS A 1 177 ? 3.968   -13.198 1.178   0.50 57.94  ? 177 CYS A CB  1 
ATOM   1431 C  CB  B CYS A 1 177 ? 4.031   -13.272 1.127   0.50 60.75  ? 177 CYS A CB  1 
ATOM   1432 S  SG  A CYS A 1 177 ? 3.120   -11.602 0.989   0.50 60.00  ? 177 CYS A SG  1 
ATOM   1433 S  SG  B CYS A 1 177 ? 5.260   -12.797 2.369   0.50 66.44  ? 177 CYS A SG  1 
ATOM   1434 N  N   . LYS A 1 178 ? 0.837   -13.825 0.794   1.00 63.98  ? 178 LYS A N   1 
ATOM   1435 C  CA  . LYS A 1 178 ? -0.281  -13.847 -0.145  1.00 70.48  ? 178 LYS A CA  1 
ATOM   1436 C  C   . LYS A 1 178 ? 0.223   -13.389 -1.517  1.00 61.00  ? 178 LYS A C   1 
ATOM   1437 O  O   . LYS A 1 178 ? 0.215   -14.160 -2.472  1.00 68.42  ? 178 LYS A O   1 
ATOM   1438 C  CB  . LYS A 1 178 ? -1.418  -12.966 0.401   1.00 79.23  ? 178 LYS A CB  1 
ATOM   1439 C  CG  . LYS A 1 178 ? -2.706  -12.932 -0.412  1.00 87.68  ? 178 LYS A CG  1 
ATOM   1440 C  CD  . LYS A 1 178 ? -3.808  -12.080 0.204   1.00 94.56  ? 178 LYS A CD  1 
ATOM   1441 C  CE  . LYS A 1 178 ? -5.113  -12.167 -0.566  1.00 97.71  ? 178 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A 1 178 ? -6.267  -11.641 0.198   1.00 98.48  ? 178 LYS A NZ  1 
ATOM   1443 N  N   . TYR A 1 179 ? 0.724   -12.149 -1.564  1.00 53.23  ? 179 TYR A N   1 
ATOM   1444 C  CA  . TYR A 1 179 ? 1.172   -11.481 -2.776  1.00 53.16  ? 179 TYR A CA  1 
ATOM   1445 C  C   . TYR A 1 179 ? 2.694   -11.600 -2.945  1.00 49.89  ? 179 TYR A C   1 
ATOM   1446 O  O   . TYR A 1 179 ? 3.448   -11.421 -1.996  1.00 48.35  ? 179 TYR A O   1 
ATOM   1447 C  CB  . TYR A 1 179 ? 0.740   -10.010 -2.728  1.00 59.58  ? 179 TYR A CB  1 
ATOM   1448 C  CG  . TYR A 1 179 ? -0.744  -9.780  -2.538  1.00 73.14  ? 179 TYR A CG  1 
ATOM   1449 C  CD1 . TYR A 1 179 ? -1.681  -10.564 -3.195  1.00 73.69  ? 179 TYR A CD1 1 
ATOM   1450 C  CD2 . TYR A 1 179 ? -1.221  -8.749  -1.735  1.00 80.30  ? 179 TYR A CD2 1 
ATOM   1451 C  CE1 . TYR A 1 179 ? -3.043  -10.346 -3.052  1.00 80.53  ? 179 TYR A CE1 1 
ATOM   1452 C  CE2 . TYR A 1 179 ? -2.580  -8.515  -1.585  1.00 83.76  ? 179 TYR A CE2 1 
ATOM   1453 C  CZ  . TYR A 1 179 ? -3.496  -9.319  -2.244  1.00 83.32  ? 179 TYR A CZ  1 
ATOM   1454 O  OH  . TYR A 1 179 ? -4.849  -9.129  -2.100  1.00 82.72  ? 179 TYR A OH  1 
ATOM   1455 N  N   . TYR A 1 180 ? 3.133   -11.945 -4.165  1.00 45.77  ? 180 TYR A N   1 
ATOM   1456 C  CA  . TYR A 1 180 ? 4.500   -11.743 -4.642  1.00 44.32  ? 180 TYR A CA  1 
ATOM   1457 C  C   . TYR A 1 180 ? 4.451   -11.186 -6.065  1.00 41.19  ? 180 TYR A C   1 
ATOM   1458 O  O   . TYR A 1 180 ? 3.451   -11.384 -6.757  1.00 43.15  ? 180 TYR A O   1 
ATOM   1459 C  CB  . TYR A 1 180 ? 5.296   -13.049 -4.596  1.00 40.48  ? 180 TYR A CB  1 
ATOM   1460 C  CG  . TYR A 1 180 ? 4.829   -14.131 -5.538  1.00 43.92  ? 180 TYR A CG  1 
ATOM   1461 C  CD1 . TYR A 1 180 ? 5.179   -14.103 -6.877  1.00 44.08  ? 180 TYR A CD1 1 
ATOM   1462 C  CD2 . TYR A 1 180 ? 4.065   -15.206 -5.095  1.00 46.35  ? 180 TYR A CD2 1 
ATOM   1463 C  CE1 . TYR A 1 180 ? 4.791   -15.110 -7.750  1.00 44.89  ? 180 TYR A CE1 1 
ATOM   1464 C  CE2 . TYR A 1 180 ? 3.664   -16.217 -5.958  1.00 43.72  ? 180 TYR A CE2 1 
ATOM   1465 C  CZ  . TYR A 1 180 ? 4.022   -16.164 -7.295  1.00 45.54  ? 180 TYR A CZ  1 
ATOM   1466 O  OH  . TYR A 1 180 ? 3.656   -17.136 -8.195  1.00 47.71  ? 180 TYR A OH  1 
ATOM   1467 N  N   . SER A 1 181 ? 5.544   -10.528 -6.485  1.00 40.12  ? 181 SER A N   1 
ATOM   1468 C  CA  . SER A 1 181 ? 5.669   -9.823  -7.764  1.00 38.15  ? 181 SER A CA  1 
ATOM   1469 C  C   . SER A 1 181 ? 7.106   -9.909  -8.302  1.00 38.05  ? 181 SER A C   1 
ATOM   1470 O  O   . SER A 1 181 ? 7.795   -10.886 -8.053  1.00 41.71  ? 181 SER A O   1 
ATOM   1471 C  CB  . SER A 1 181 ? 5.218   -8.381  -7.602  1.00 41.96  ? 181 SER A CB  1 
ATOM   1472 O  OG  . SER A 1 181 ? 5.156   -7.692  -8.848  1.00 47.59  ? 181 SER A OG  1 
ATOM   1473 N  N   . THR A 1 182 ? 7.574   -8.851  -8.987  1.00 36.63  ? 182 THR A N   1 
ATOM   1474 C  CA  . THR A 1 182 ? 8.816   -8.834  -9.754  1.00 35.66  ? 182 THR A CA  1 
ATOM   1475 C  C   . THR A 1 182 ? 10.035  -9.104  -8.869  1.00 37.83  ? 182 THR A C   1 
ATOM   1476 O  O   . THR A 1 182 ? 11.056  -9.577  -9.363  1.00 40.05  ? 182 THR A O   1 
ATOM   1477 C  CB  . THR A 1 182 ? 8.934   -7.502  -10.511 1.00 34.43  ? 182 THR A CB  1 
ATOM   1478 O  OG1 . THR A 1 182 ? 9.003   -6.453  -9.555  1.00 33.37  ? 182 THR A OG1 1 
ATOM   1479 C  CG2 . THR A 1 182 ? 7.757   -7.233  -11.422 1.00 37.65  ? 182 THR A CG2 1 
ATOM   1480 N  N   . ALA A 1 183 ? 9.907   -8.846  -7.561  1.00 41.65  ? 183 ALA A N   1 
ATOM   1481 C  CA  . ALA A 1 183 ? 11.006  -8.971  -6.616  1.00 40.40  ? 183 ALA A CA  1 
ATOM   1482 C  C   . ALA A 1 183 ? 11.532  -10.404 -6.533  1.00 39.68  ? 183 ALA A C   1 
ATOM   1483 O  O   . ALA A 1 183 ? 12.712  -10.563 -6.244  1.00 39.71  ? 183 ALA A O   1 
ATOM   1484 C  CB  . ALA A 1 183 ? 10.580  -8.470  -5.266  1.00 41.55  ? 183 ALA A CB  1 
ATOM   1485 N  N   . VAL A 1 184 ? 10.706  -11.429 -6.813  1.00 36.91  ? 184 VAL A N   1 
ATOM   1486 C  CA  . VAL A 1 184 ? 11.138  -12.825 -6.662  1.00 41.25  ? 184 VAL A CA  1 
ATOM   1487 C  C   . VAL A 1 184 ? 12.157  -13.214 -7.736  1.00 39.37  ? 184 VAL A C   1 
ATOM   1488 O  O   . VAL A 1 184 ? 12.883  -14.189 -7.547  1.00 39.52  ? 184 VAL A O   1 
ATOM   1489 C  CB  . VAL A 1 184 ? 9.981   -13.848 -6.688  1.00 42.23  ? 184 VAL A CB  1 
ATOM   1490 C  CG1 . VAL A 1 184 ? 8.827   -13.411 -5.806  1.00 42.91  ? 184 VAL A CG1 1 
ATOM   1491 C  CG2 . VAL A 1 184 ? 9.499   -14.143 -8.100  1.00 42.63  ? 184 VAL A CG2 1 
ATOM   1492 N  N   . ASP A 1 185 ? 12.106  -12.532 -8.891  1.00 37.83  ? 185 ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 185 ? 13.021  -12.739 -10.007 1.00 36.49  ? 185 ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 185 ? 14.367  -12.100 -9.653  1.00 36.13  ? 185 ASP A C   1 
ATOM   1495 O  O   . ASP A 1 185 ? 15.417  -12.660 -9.926  1.00 33.84  ? 185 ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 185 ? 12.434  -12.202 -11.321 1.00 36.43  ? 185 ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 185 ? 11.442  -13.105 -12.050 1.00 38.40  ? 185 ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 185 ? 11.413  -14.329 -11.778 1.00 38.97  ? 185 ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 185 ? 10.673  -12.562 -12.884 1.00 38.75  ? 185 ASP A OD2 1 
ATOM   1500 N  N   . ILE A 1 186 ? 14.331  -10.938 -9.003  1.00 35.28  ? 186 ILE A N   1 
ATOM   1501 C  CA  . ILE A 1 186 ? 15.535  -10.273 -8.538  1.00 34.97  ? 186 ILE A CA  1 
ATOM   1502 C  C   . ILE A 1 186 ? 16.248  -11.106 -7.471  1.00 34.84  ? 186 ILE A C   1 
ATOM   1503 O  O   . ILE A 1 186 ? 17.448  -11.271 -7.560  1.00 34.10  ? 186 ILE A O   1 
ATOM   1504 C  CB  . ILE A 1 186 ? 15.201  -8.860  -8.034  1.00 37.71  ? 186 ILE A CB  1 
ATOM   1505 C  CG1 . ILE A 1 186 ? 14.616  -7.994  -9.159  1.00 38.31  ? 186 ILE A CG1 1 
ATOM   1506 C  CG2 . ILE A 1 186 ? 16.422  -8.227  -7.380  1.00 38.79  ? 186 ILE A CG2 1 
ATOM   1507 C  CD1 . ILE A 1 186 ? 15.608  -7.584  -10.231 1.00 38.50  ? 186 ILE A CD1 1 
ATOM   1508 N  N   . TRP A 1 187 ? 15.546  -11.635 -6.460  1.00 37.94  ? 187 TRP A N   1 
ATOM   1509 C  CA  . TRP A 1 187 ? 16.196  -12.575 -5.559  1.00 36.84  ? 187 TRP A CA  1 
ATOM   1510 C  C   . TRP A 1 187 ? 16.947  -13.641 -6.364  1.00 37.99  ? 187 TRP A C   1 
ATOM   1511 O  O   . TRP A 1 187 ? 18.086  -13.972 -6.043  1.00 39.72  ? 187 TRP A O   1 
ATOM   1512 C  CB  . TRP A 1 187 ? 15.199  -13.241 -4.612  1.00 36.11  ? 187 TRP A CB  1 
ATOM   1513 C  CG  . TRP A 1 187 ? 15.814  -14.152 -3.590  1.00 33.95  ? 187 TRP A CG  1 
ATOM   1514 C  CD1 . TRP A 1 187 ? 16.036  -15.500 -3.683  1.00 36.02  ? 187 TRP A CD1 1 
ATOM   1515 C  CD2 . TRP A 1 187 ? 16.244  -13.773 -2.281  1.00 36.03  ? 187 TRP A CD2 1 
ATOM   1516 N  NE1 . TRP A 1 187 ? 16.594  -15.985 -2.532  1.00 35.26  ? 187 TRP A NE1 1 
ATOM   1517 C  CE2 . TRP A 1 187 ? 16.725  -14.944 -1.652  1.00 37.42  ? 187 TRP A CE2 1 
ATOM   1518 C  CE3 . TRP A 1 187 ? 16.269  -12.558 -1.586  1.00 39.03  ? 187 TRP A CE3 1 
ATOM   1519 C  CZ2 . TRP A 1 187 ? 17.235  -14.917 -0.361  1.00 34.42  ? 187 TRP A CZ2 1 
ATOM   1520 C  CZ3 . TRP A 1 187 ? 16.768  -12.541 -0.303  1.00 36.62  ? 187 TRP A CZ3 1 
ATOM   1521 C  CH2 . TRP A 1 187 ? 17.226  -13.710 0.300   1.00 35.21  ? 187 TRP A CH2 1 
ATOM   1522 N  N   . SER A 1 188 ? 16.271  -14.237 -7.350  1.00 37.95  ? 188 SER A N   1 
ATOM   1523 C  CA  . SER A 1 188 ? 16.828  -15.363 -8.085  1.00 40.49  ? 188 SER A CA  1 
ATOM   1524 C  C   . SER A 1 188 ? 18.160  -14.949 -8.718  1.00 42.77  ? 188 SER A C   1 
ATOM   1525 O  O   . SER A 1 188 ? 19.139  -15.688 -8.641  1.00 41.04  ? 188 SER A O   1 
ATOM   1526 C  CB  . SER A 1 188 ? 15.852  -15.877 -9.106  1.00 38.12  ? 188 SER A CB  1 
ATOM   1527 O  OG  . SER A 1 188 ? 14.738  -16.491 -8.478  1.00 46.28  ? 188 SER A OG  1 
ATOM   1528 N  N   . LEU A 1 189 ? 18.193  -13.740 -9.294  1.00 42.83  ? 189 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 189 ? 19.376  -13.206 -9.955  1.00 46.31  ? 189 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 189 ? 20.487  -12.884 -8.955  1.00 42.15  ? 189 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 189 ? 21.647  -13.024 -9.303  1.00 44.89  ? 189 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 189 ? 18.996  -11.951 -10.754 1.00 51.12  ? 189 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 189 ? 18.672  -12.163 -12.231 1.00 52.89  ? 189 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 189 ? 18.635  -10.830 -12.965 1.00 51.54  ? 189 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 189 ? 19.688  -13.083 -12.885 1.00 59.63  ? 189 LEU A CD2 1 
ATOM   1536 N  N   . GLY A 1 190 ? 20.141  -12.422 -7.748  1.00 39.84  ? 190 GLY A N   1 
ATOM   1537 C  CA  . GLY A 1 190 ? 21.110  -12.159 -6.699  1.00 40.52  ? 190 GLY A CA  1 
ATOM   1538 C  C   . GLY A 1 190 ? 21.892  -13.419 -6.348  1.00 38.52  ? 190 GLY A C   1 
ATOM   1539 O  O   . GLY A 1 190 ? 23.119  -13.381 -6.260  1.00 37.26  ? 190 GLY A O   1 
ATOM   1540 N  N   . CYS A 1 191 ? 21.157  -14.530 -6.213  1.00 37.15  ? 191 CYS A N   1 
ATOM   1541 C  CA  . CYS A 1 191 ? 21.725  -15.830 -5.885  1.00 39.30  ? 191 CYS A CA  1 
ATOM   1542 C  C   . CYS A 1 191 ? 22.700  -16.284 -6.970  1.00 40.62  ? 191 CYS A C   1 
ATOM   1543 O  O   . CYS A 1 191 ? 23.711  -16.914 -6.667  1.00 40.40  ? 191 CYS A O   1 
ATOM   1544 C  CB  . CYS A 1 191 ? 20.630  -16.873 -5.707  1.00 40.79  ? 191 CYS A CB  1 
ATOM   1545 S  SG  . CYS A 1 191 ? 19.583  -16.546 -4.263  1.00 46.72  ? 191 CYS A SG  1 
ATOM   1546 N  N   . ILE A 1 192 ? 22.378  -15.940 -8.224  1.00 40.00  ? 192 ILE A N   1 
ATOM   1547 C  CA  . ILE A 1 192 ? 23.092  -16.404 -9.404  1.00 40.41  ? 192 ILE A CA  1 
ATOM   1548 C  C   . ILE A 1 192 ? 24.356  -15.552 -9.561  1.00 40.60  ? 192 ILE A C   1 
ATOM   1549 O  O   . ILE A 1 192 ? 25.441  -16.101 -9.702  1.00 43.64  ? 192 ILE A O   1 
ATOM   1550 C  CB  . ILE A 1 192 ? 22.147  -16.408 -10.630 1.00 41.51  ? 192 ILE A CB  1 
ATOM   1551 C  CG1 . ILE A 1 192 ? 21.144  -17.565 -10.535 1.00 44.89  ? 192 ILE A CG1 1 
ATOM   1552 C  CG2 . ILE A 1 192 ? 22.918  -16.451 -11.943 1.00 41.63  ? 192 ILE A CG2 1 
ATOM   1553 C  CD1 . ILE A 1 192 ? 19.914  -17.420 -11.419 1.00 45.71  ? 192 ILE A CD1 1 
ATOM   1554 N  N   . PHE A 1 193 ? 24.221  -14.224 -9.471  1.00 40.42  ? 193 PHE A N   1 
ATOM   1555 C  CA  . PHE A 1 193 ? 25.345  -13.300 -9.350  1.00 43.16  ? 193 PHE A CA  1 
ATOM   1556 C  C   . PHE A 1 193 ? 26.374  -13.816 -8.337  1.00 44.17  ? 193 PHE A C   1 
ATOM   1557 O  O   . PHE A 1 193 ? 27.557  -13.883 -8.631  1.00 44.91  ? 193 PHE A O   1 
ATOM   1558 C  CB  . PHE A 1 193 ? 24.812  -11.914 -8.971  1.00 42.47  ? 193 PHE A CB  1 
ATOM   1559 C  CG  . PHE A 1 193 ? 25.827  -10.820 -8.766  1.00 42.10  ? 193 PHE A CG  1 
ATOM   1560 C  CD1 . PHE A 1 193 ? 27.073  -10.860 -9.371  1.00 44.76  ? 193 PHE A CD1 1 
ATOM   1561 C  CD2 . PHE A 1 193 ? 25.521  -9.732  -7.965  1.00 43.45  ? 193 PHE A CD2 1 
ATOM   1562 C  CE1 . PHE A 1 193 ? 27.979  -9.825  -9.193  1.00 44.68  ? 193 PHE A CE1 1 
ATOM   1563 C  CE2 . PHE A 1 193 ? 26.441  -8.713  -7.767  1.00 44.65  ? 193 PHE A CE2 1 
ATOM   1564 C  CZ  . PHE A 1 193 ? 27.672  -8.764  -8.375  1.00 44.24  ? 193 PHE A CZ  1 
ATOM   1565 N  N   . ALA A 1 194 ? 25.923  -14.187 -7.137  1.00 45.99  ? 194 ALA A N   1 
ATOM   1566 C  CA  . ALA A 1 194 ? 26.797  -14.679 -6.082  1.00 42.38  ? 194 ALA A CA  1 
ATOM   1567 C  C   . ALA A 1 194 ? 27.442  -16.016 -6.470  1.00 47.48  ? 194 ALA A C   1 
ATOM   1568 O  O   . ALA A 1 194 ? 28.577  -16.293 -6.055  1.00 50.84  ? 194 ALA A O   1 
ATOM   1569 C  CB  . ALA A 1 194 ? 26.011  -14.795 -4.793  1.00 39.14  ? 194 ALA A CB  1 
ATOM   1570 N  N   . GLU A 1 195 ? 26.695  -16.846 -7.226  1.00 47.80  ? 195 GLU A N   1 
ATOM   1571 C  CA  . GLU A 1 195 ? 27.142  -18.154 -7.710  1.00 47.94  ? 195 GLU A CA  1 
ATOM   1572 C  C   . GLU A 1 195 ? 28.215  -18.035 -8.798  1.00 48.05  ? 195 GLU A C   1 
ATOM   1573 O  O   . GLU A 1 195 ? 29.065  -18.906 -8.923  1.00 53.43  ? 195 GLU A O   1 
ATOM   1574 C  CB  . GLU A 1 195 ? 25.956  -18.948 -8.268  1.00 46.82  ? 195 GLU A CB  1 
ATOM   1575 C  CG  . GLU A 1 195 ? 26.294  -20.378 -8.636  1.00 49.15  ? 195 GLU A CG  1 
ATOM   1576 C  CD  . GLU A 1 195 ? 25.131  -21.356 -8.695  1.00 55.32  ? 195 GLU A CD  1 
ATOM   1577 O  OE1 . GLU A 1 195 ? 24.015  -21.002 -8.230  1.00 56.94  ? 195 GLU A OE1 1 
ATOM   1578 O  OE2 . GLU A 1 195 ? 25.354  -22.488 -9.193  1.00 60.00  ? 195 GLU A OE2 1 
ATOM   1579 N  N   . MET A 1 196 ? 28.155  -16.985 -9.619  1.00 48.11  ? 196 MET A N   1 
ATOM   1580 C  CA  . MET A 1 196 ? 29.146  -16.762 -10.658 1.00 49.67  ? 196 MET A CA  1 
ATOM   1581 C  C   . MET A 1 196 ? 30.477  -16.391 -10.002 1.00 53.01  ? 196 MET A C   1 
ATOM   1582 O  O   . MET A 1 196 ? 31.528  -16.894 -10.401 1.00 56.03  ? 196 MET A O   1 
ATOM   1583 C  CB  . MET A 1 196 ? 28.696  -15.654 -11.622 1.00 53.07  ? 196 MET A CB  1 
ATOM   1584 C  CG  . MET A 1 196 ? 27.752  -16.145 -12.717 1.00 52.47  ? 196 MET A CG  1 
ATOM   1585 S  SD  . MET A 1 196 ? 27.322  -14.885 -13.934 1.00 55.39  ? 196 MET A SD  1 
ATOM   1586 C  CE  . MET A 1 196 ? 26.264  -13.804 -12.976 1.00 56.67  ? 196 MET A CE  1 
ATOM   1587 N  N   . VAL A 1 197 ? 30.409  -15.541 -8.971  1.00 51.63  ? 197 VAL A N   1 
ATOM   1588 C  CA  . VAL A 1 197 ? 31.576  -15.066 -8.231  1.00 51.69  ? 197 VAL A CA  1 
ATOM   1589 C  C   . VAL A 1 197 ? 32.320  -16.206 -7.504  1.00 54.22  ? 197 VAL A C   1 
ATOM   1590 O  O   . VAL A 1 197 ? 33.530  -16.348 -7.692  1.00 54.01  ? 197 VAL A O   1 
ATOM   1591 C  CB  . VAL A 1 197 ? 31.166  -13.934 -7.271  1.00 48.56  ? 197 VAL A CB  1 
ATOM   1592 C  CG1 . VAL A 1 197 ? 32.355  -13.455 -6.453  1.00 54.91  ? 197 VAL A CG1 1 
ATOM   1593 C  CG2 . VAL A 1 197 ? 30.558  -12.764 -8.028  1.00 46.15  ? 197 VAL A CG2 1 
ATOM   1594 N  N   . THR A 1 198 ? 31.599  -17.024 -6.709  1.00 56.82  ? 198 THR A N   1 
ATOM   1595 C  CA  . THR A 1 198 ? 32.161  -18.049 -5.826  1.00 56.70  ? 198 THR A CA  1 
ATOM   1596 C  C   . THR A 1 198 ? 32.218  -19.437 -6.485  1.00 60.58  ? 198 THR A C   1 
ATOM   1597 O  O   . THR A 1 198 ? 32.922  -20.306 -5.980  1.00 71.88  ? 198 THR A O   1 
ATOM   1598 C  CB  . THR A 1 198 ? 31.369  -18.145 -4.505  1.00 55.28  ? 198 THR A CB  1 
ATOM   1599 O  OG1 . THR A 1 198 ? 30.061  -18.665 -4.745  1.00 55.79  ? 198 THR A OG1 1 
ATOM   1600 C  CG2 . THR A 1 198 ? 31.212  -16.816 -3.798  1.00 56.86  ? 198 THR A CG2 1 
ATOM   1601 N  N   . ARG A 1 199 ? 31.441  -19.669 -7.558  1.00 60.96  ? 199 ARG A N   1 
ATOM   1602 C  CA  . ARG A 1 199 ? 31.345  -20.945 -8.277  1.00 65.85  ? 199 ARG A CA  1 
ATOM   1603 C  C   . ARG A 1 199 ? 30.670  -22.028 -7.432  1.00 63.77  ? 199 ARG A C   1 
ATOM   1604 O  O   . ARG A 1 199 ? 30.741  -23.207 -7.772  1.00 58.74  ? 199 ARG A O   1 
ATOM   1605 C  CB  . ARG A 1 199 ? 32.710  -21.402 -8.800  1.00 76.34  ? 199 ARG A CB  1 
ATOM   1606 C  CG  . ARG A 1 199 ? 33.395  -20.355 -9.669  1.00 90.04  ? 199 ARG A CG  1 
ATOM   1607 C  CD  . ARG A 1 199 ? 34.759  -20.779 -10.178 1.00 98.11  ? 199 ARG A CD  1 
ATOM   1608 N  NE  . ARG A 1 199 ? 35.786  -20.973 -9.154  1.00 98.18  ? 199 ARG A NE  1 
ATOM   1609 C  CZ  . ARG A 1 199 ? 36.531  -20.015 -8.605  1.00 92.99  ? 199 ARG A CZ  1 
ATOM   1610 N  NH1 . ARG A 1 199 ? 36.333  -18.744 -8.909  1.00 89.56  ? 199 ARG A NH1 1 
ATOM   1611 N  NH2 . ARG A 1 199 ? 37.479  -20.341 -7.739  1.00 91.38  ? 199 ARG A NH2 1 
ATOM   1612 N  N   . ARG A 1 200 ? 29.967  -21.605 -6.370  1.00 62.80  ? 200 ARG A N   1 
ATOM   1613 C  CA  . ARG A 1 200 ? 29.154  -22.470 -5.527  1.00 62.87  ? 200 ARG A CA  1 
ATOM   1614 C  C   . ARG A 1 200 ? 27.784  -21.826 -5.303  1.00 53.18  ? 200 ARG A C   1 
ATOM   1615 O  O   . ARG A 1 200 ? 27.675  -20.602 -5.198  1.00 48.01  ? 200 ARG A O   1 
ATOM   1616 C  CB  . ARG A 1 200 ? 29.846  -22.700 -4.180  1.00 74.00  ? 200 ARG A CB  1 
ATOM   1617 C  CG  . ARG A 1 200 ? 31.193  -23.408 -4.276  1.00 88.45  ? 200 ARG A CG  1 
ATOM   1618 C  CD  . ARG A 1 200 ? 31.407  -24.439 -3.170  1.00 95.83  ? 200 ARG A CD  1 
ATOM   1619 N  NE  . ARG A 1 200 ? 31.160  -25.806 -3.638  1.00 100.72 ? 200 ARG A NE  1 
ATOM   1620 C  CZ  . ARG A 1 200 ? 31.055  -26.882 -2.859  1.00 99.51  ? 200 ARG A CZ  1 
ATOM   1621 N  NH1 . ARG A 1 200 ? 30.815  -28.069 -3.399  1.00 95.72  ? 200 ARG A NH1 1 
ATOM   1622 N  NH2 . ARG A 1 200 ? 31.173  -26.769 -1.545  1.00 92.68  ? 200 ARG A NH2 1 
ATOM   1623 N  N   . ALA A 1 201 ? 26.743  -22.663 -5.220  1.00 49.25  ? 201 ALA A N   1 
ATOM   1624 C  CA  . ALA A 1 201 ? 25.393  -22.209 -4.920  1.00 51.41  ? 201 ALA A CA  1 
ATOM   1625 C  C   . ALA A 1 201 ? 25.418  -21.412 -3.618  1.00 50.71  ? 201 ALA A C   1 
ATOM   1626 O  O   . ALA A 1 201 ? 25.983  -21.865 -2.628  1.00 51.55  ? 201 ALA A O   1 
ATOM   1627 C  CB  . ALA A 1 201 ? 24.458  -23.397 -4.819  1.00 51.93  ? 201 ALA A CB  1 
ATOM   1628 N  N   . LEU A 1 202 ? 24.815  -20.219 -3.623  1.00 48.84  ? 202 LEU A N   1 
ATOM   1629 C  CA  . LEU A 1 202 ? 24.792  -19.381 -2.433  1.00 48.34  ? 202 LEU A CA  1 
ATOM   1630 C  C   . LEU A 1 202 ? 24.033  -20.051 -1.280  1.00 47.36  ? 202 LEU A C   1 
ATOM   1631 O  O   . LEU A 1 202 ? 24.543  -20.062 -0.163  1.00 44.99  ? 202 LEU A O   1 
ATOM   1632 C  CB  . LEU A 1 202 ? 24.176  -18.022 -2.781  1.00 47.68  ? 202 LEU A CB  1 
ATOM   1633 C  CG  . LEU A 1 202 ? 24.150  -17.022 -1.627  1.00 49.96  ? 202 LEU A CG  1 
ATOM   1634 C  CD1 . LEU A 1 202 ? 25.530  -16.880 -0.978  1.00 49.10  ? 202 LEU A CD1 1 
ATOM   1635 C  CD2 . LEU A 1 202 ? 23.636  -15.669 -2.100  1.00 48.58  ? 202 LEU A CD2 1 
ATOM   1636 N  N   . PHE A 1 203 ? 22.826  -20.590 -1.553  1.00 46.24  ? 203 PHE A N   1 
ATOM   1637 C  CA  . PHE A 1 203 ? 21.933  -21.140 -0.535  1.00 44.12  ? 203 PHE A CA  1 
ATOM   1638 C  C   . PHE A 1 203 ? 21.388  -22.511 -0.945  1.00 45.17  ? 203 PHE A C   1 
ATOM   1639 O  O   . PHE A 1 203 ? 20.205  -22.647 -1.255  1.00 45.81  ? 203 PHE A O   1 
ATOM   1640 C  CB  . PHE A 1 203 ? 20.723  -20.224 -0.296  1.00 44.23  ? 203 PHE A CB  1 
ATOM   1641 C  CG  . PHE A 1 203 ? 21.024  -18.789 0.057   1.00 42.04  ? 203 PHE A CG  1 
ATOM   1642 C  CD1 . PHE A 1 203 ? 21.836  -18.472 1.134   1.00 39.61  ? 203 PHE A CD1 1 
ATOM   1643 C  CD2 . PHE A 1 203 ? 20.461  -17.749 -0.670  1.00 39.46  ? 203 PHE A CD2 1 
ATOM   1644 C  CE1 . PHE A 1 203 ? 22.076  -17.146 1.470   1.00 40.18  ? 203 PHE A CE1 1 
ATOM   1645 C  CE2 . PHE A 1 203 ? 20.728  -16.424 -0.355  1.00 36.71  ? 203 PHE A CE2 1 
ATOM   1646 C  CZ  . PHE A 1 203 ? 21.533  -16.125 0.715   1.00 37.12  ? 203 PHE A CZ  1 
ATOM   1647 N  N   . PRO A 1 204 ? 22.189  -23.597 -0.923  1.00 46.54  ? 204 PRO A N   1 
ATOM   1648 C  CA  . PRO A 1 204 ? 21.692  -24.908 -1.354  1.00 46.03  ? 204 PRO A CA  1 
ATOM   1649 C  C   . PRO A 1 204 ? 20.928  -25.696 -0.289  1.00 45.78  ? 204 PRO A C   1 
ATOM   1650 O  O   . PRO A 1 204 ? 21.442  -26.674 0.239   1.00 50.72  ? 204 PRO A O   1 
ATOM   1651 C  CB  . PRO A 1 204 ? 22.987  -25.631 -1.774  1.00 46.44  ? 204 PRO A CB  1 
ATOM   1652 C  CG  . PRO A 1 204 ? 24.076  -25.026 -0.885  1.00 44.01  ? 204 PRO A CG  1 
ATOM   1653 C  CD  . PRO A 1 204 ? 23.621  -23.607 -0.585  1.00 46.96  ? 204 PRO A CD  1 
ATOM   1654 N  N   . GLY A 1 205 ? 19.691  -25.283 0.024   1.00 47.65  ? 205 GLY A N   1 
ATOM   1655 C  CA  . GLY A 1 205 ? 18.830  -26.043 0.927   1.00 48.77  ? 205 GLY A CA  1 
ATOM   1656 C  C   . GLY A 1 205 ? 18.456  -27.409 0.348   1.00 54.97  ? 205 GLY A C   1 
ATOM   1657 O  O   . GLY A 1 205 ? 18.574  -27.604 -0.858  1.00 60.09  ? 205 GLY A O   1 
ATOM   1658 N  N   . ASP A 1 206 ? 18.016  -28.348 1.202   1.00 60.15  ? 206 ASP A N   1 
ATOM   1659 C  CA  . ASP A 1 206 ? 17.470  -29.626 0.751   1.00 65.63  ? 206 ASP A CA  1 
ATOM   1660 C  C   . ASP A 1 206 ? 16.004  -29.765 1.186   1.00 57.20  ? 206 ASP A C   1 
ATOM   1661 O  O   . ASP A 1 206 ? 15.401  -30.810 0.967   1.00 57.35  ? 206 ASP A O   1 
ATOM   1662 C  CB  . ASP A 1 206 ? 18.347  -30.799 1.215   1.00 75.35  ? 206 ASP A CB  1 
ATOM   1663 C  CG  . ASP A 1 206 ? 18.679  -30.788 2.697   1.00 82.10  ? 206 ASP A CG  1 
ATOM   1664 O  OD1 . ASP A 1 206 ? 17.928  -30.148 3.461   1.00 85.65  ? 206 ASP A OD1 1 
ATOM   1665 O  OD2 . ASP A 1 206 ? 19.697  -31.409 3.075   1.00 89.56  ? 206 ASP A OD2 1 
ATOM   1666 N  N   . SER A 1 207 ? 15.446  -28.706 1.794   1.00 51.86  ? 207 SER A N   1 
ATOM   1667 C  CA  . SER A 1 207 ? 14.053  -28.615 2.225   1.00 52.34  ? 207 SER A CA  1 
ATOM   1668 C  C   . SER A 1 207 ? 13.715  -27.134 2.429   1.00 51.40  ? 207 SER A C   1 
ATOM   1669 O  O   . SER A 1 207 ? 14.625  -26.301 2.435   1.00 51.69  ? 207 SER A O   1 
ATOM   1670 C  CB  . SER A 1 207 ? 13.797  -29.419 3.489   1.00 51.21  ? 207 SER A CB  1 
ATOM   1671 O  OG  . SER A 1 207 ? 14.314  -28.756 4.641   1.00 54.10  ? 207 SER A OG  1 
ATOM   1672 N  N   . GLU A 1 208 ? 12.426  -26.809 2.604   1.00 50.22  ? 208 GLU A N   1 
ATOM   1673 C  CA  . GLU A 1 208 ? 11.982  -25.429 2.761   1.00 52.33  ? 208 GLU A CA  1 
ATOM   1674 C  C   . GLU A 1 208 ? 12.614  -24.803 4.002   1.00 52.03  ? 208 GLU A C   1 
ATOM   1675 O  O   . GLU A 1 208 ? 13.124  -23.691 3.933   1.00 52.02  ? 208 GLU A O   1 
ATOM   1676 C  CB  . GLU A 1 208 ? 10.454  -25.329 2.841   1.00 56.48  ? 208 GLU A CB  1 
ATOM   1677 C  CG  . GLU A 1 208 ? 9.792   -25.124 1.488   1.00 66.73  ? 208 GLU A CG  1 
ATOM   1678 C  CD  . GLU A 1 208 ? 8.302   -25.424 1.406   1.00 74.93  ? 208 GLU A CD  1 
ATOM   1679 O  OE1 . GLU A 1 208 ? 7.773   -26.093 2.322   1.00 84.63  ? 208 GLU A OE1 1 
ATOM   1680 O  OE2 . GLU A 1 208 ? 7.671   -24.989 0.421   1.00 74.96  ? 208 GLU A OE2 1 
ATOM   1681 N  N   . ILE A 1 209 ? 12.550  -25.504 5.138   1.00 56.38  ? 209 ILE A N   1 
ATOM   1682 C  CA  . ILE A 1 209 ? 13.080  -24.981 6.392   1.00 57.62  ? 209 ILE A CA  1 
ATOM   1683 C  C   . ILE A 1 209 ? 14.601  -24.849 6.277   1.00 50.15  ? 209 ILE A C   1 
ATOM   1684 O  O   . ILE A 1 209 ? 15.174  -23.814 6.609   1.00 45.97  ? 209 ILE A O   1 
ATOM   1685 C  CB  . ILE A 1 209 ? 12.637  -25.836 7.603   1.00 61.60  ? 209 ILE A CB  1 
ATOM   1686 C  CG1 . ILE A 1 209 ? 12.934  -25.117 8.918   1.00 64.56  ? 209 ILE A CG1 1 
ATOM   1687 C  CG2 . ILE A 1 209 ? 13.235  -27.242 7.585   1.00 67.05  ? 209 ILE A CG2 1 
ATOM   1688 C  CD1 . ILE A 1 209 ? 12.108  -23.871 9.133   1.00 67.34  ? 209 ILE A CD1 1 
ATOM   1689 N  N   . ASP A 1 210 ? 15.256  -25.881 5.751   1.00 45.87  ? 210 ASP A N   1 
ATOM   1690 C  CA  . ASP A 1 210 ? 16.702  -25.843 5.613   1.00 49.49  ? 210 ASP A CA  1 
ATOM   1691 C  C   . ASP A 1 210 ? 17.125  -24.665 4.730   1.00 49.70  ? 210 ASP A C   1 
ATOM   1692 O  O   . ASP A 1 210 ? 18.179  -24.069 4.967   1.00 50.34  ? 210 ASP A O   1 
ATOM   1693 C  CB  . ASP A 1 210 ? 17.232  -27.163 5.060   1.00 54.76  ? 210 ASP A CB  1 
ATOM   1694 C  CG  . ASP A 1 210 ? 18.745  -27.186 5.041   1.00 59.08  ? 210 ASP A CG  1 
ATOM   1695 O  OD1 . ASP A 1 210 ? 19.345  -26.928 6.108   1.00 63.94  ? 210 ASP A OD1 1 
ATOM   1696 O  OD2 . ASP A 1 210 ? 19.303  -27.432 3.967   1.00 62.62  ? 210 ASP A OD2 1 
ATOM   1697 N  N   . GLN A 1 211 ? 16.293  -24.332 3.723   1.00 48.51  ? 211 GLN A N   1 
ATOM   1698 C  CA  . GLN A 1 211 ? 16.546  -23.220 2.809   1.00 44.81  ? 211 GLN A CA  1 
ATOM   1699 C  C   . GLN A 1 211 ? 16.489  -21.889 3.568   1.00 43.05  ? 211 GLN A C   1 
ATOM   1700 O  O   . GLN A 1 211 ? 17.417  -21.082 3.462   1.00 45.94  ? 211 GLN A O   1 
ATOM   1701 C  CB  . GLN A 1 211 ? 15.582  -23.265 1.612   1.00 46.11  ? 211 GLN A CB  1 
ATOM   1702 C  CG  . GLN A 1 211 ? 15.823  -22.188 0.550   1.00 43.74  ? 211 GLN A CG  1 
ATOM   1703 C  CD  . GLN A 1 211 ? 17.123  -22.319 -0.214  1.00 43.35  ? 211 GLN A CD  1 
ATOM   1704 O  OE1 . GLN A 1 211 ? 17.675  -23.400 -0.392  1.00 39.17  ? 211 GLN A OE1 1 
ATOM   1705 N  NE2 . GLN A 1 211 ? 17.622  -21.198 -0.704  1.00 47.38  ? 211 GLN A NE2 1 
ATOM   1706 N  N   . LEU A 1 212 ? 15.421  -21.667 4.351   1.00 41.97  ? 212 LEU A N   1 
ATOM   1707 C  CA  . LEU A 1 212 ? 15.296  -20.466 5.172   1.00 43.67  ? 212 LEU A CA  1 
ATOM   1708 C  C   . LEU A 1 212 ? 16.546  -20.292 6.027   1.00 44.03  ? 212 LEU A C   1 
ATOM   1709 O  O   . LEU A 1 212 ? 17.106  -19.196 6.085   1.00 45.25  ? 212 LEU A O   1 
ATOM   1710 C  CB  . LEU A 1 212 ? 14.050  -20.555 6.061   1.00 45.69  ? 212 LEU A CB  1 
ATOM   1711 C  CG  . LEU A 1 212 ? 12.746  -20.109 5.403   1.00 47.75  ? 212 LEU A CG  1 
ATOM   1712 C  CD1 . LEU A 1 212 ? 11.539  -20.541 6.233   1.00 46.79  ? 212 LEU A CD1 1 
ATOM   1713 C  CD2 . LEU A 1 212 ? 12.734  -18.595 5.196   1.00 48.58  ? 212 LEU A CD2 1 
ATOM   1714 N  N   . PHE A 1 213 ? 16.968  -21.390 6.666   1.00 44.10  ? 213 PHE A N   1 
ATOM   1715 C  CA  . PHE A 1 213 ? 18.076  -21.384 7.607   1.00 44.03  ? 213 PHE A CA  1 
ATOM   1716 C  C   . PHE A 1 213 ? 19.369  -21.040 6.885   1.00 46.24  ? 213 PHE A C   1 
ATOM   1717 O  O   . PHE A 1 213 ? 20.156  -20.254 7.404   1.00 49.98  ? 213 PHE A O   1 
ATOM   1718 C  CB  . PHE A 1 213 ? 18.180  -22.718 8.351   1.00 47.80  ? 213 PHE A CB  1 
ATOM   1719 C  CG  . PHE A 1 213 ? 17.167  -22.901 9.454   1.00 49.27  ? 213 PHE A CG  1 
ATOM   1720 C  CD1 . PHE A 1 213 ? 16.144  -21.982 9.653   1.00 52.36  ? 213 PHE A CD1 1 
ATOM   1721 C  CD2 . PHE A 1 213 ? 17.247  -23.988 10.308  1.00 53.41  ? 213 PHE A CD2 1 
ATOM   1722 C  CE1 . PHE A 1 213 ? 15.214  -22.162 10.665  1.00 55.91  ? 213 PHE A CE1 1 
ATOM   1723 C  CE2 . PHE A 1 213 ? 16.321  -24.159 11.325  1.00 58.43  ? 213 PHE A CE2 1 
ATOM   1724 C  CZ  . PHE A 1 213 ? 15.302  -23.251 11.498  1.00 54.89  ? 213 PHE A CZ  1 
ATOM   1725 N  N   . ARG A 1 214 ? 19.591  -21.599 5.694   1.00 48.82  ? 214 ARG A N   1 
ATOM   1726 C  CA  . ARG A 1 214 ? 20.780  -21.222 4.935   1.00 47.42  ? 214 ARG A CA  1 
ATOM   1727 C  C   . ARG A 1 214 ? 20.774  -19.717 4.677   1.00 42.87  ? 214 ARG A C   1 
ATOM   1728 O  O   . ARG A 1 214 ? 21.797  -19.069 4.859   1.00 48.18  ? 214 ARG A O   1 
ATOM   1729 C  CB  . ARG A 1 214 ? 20.917  -22.050 3.657   1.00 48.86  ? 214 ARG A CB  1 
ATOM   1730 C  CG  . ARG A 1 214 ? 21.598  -23.378 3.931   1.00 49.21  ? 214 ARG A CG  1 
ATOM   1731 C  CD  . ARG A 1 214 ? 21.354  -24.349 2.821   1.00 54.16  ? 214 ARG A CD  1 
ATOM   1732 N  NE  . ARG A 1 214 ? 21.721  -25.686 3.237   1.00 59.69  ? 214 ARG A NE  1 
ATOM   1733 C  CZ  . ARG A 1 214 ? 22.967  -26.128 3.316   1.00 61.37  ? 214 ARG A CZ  1 
ATOM   1734 N  NH1 . ARG A 1 214 ? 23.988  -25.322 3.067   1.00 58.04  ? 214 ARG A NH1 1 
ATOM   1735 N  NH2 . ARG A 1 214 ? 23.177  -27.386 3.655   1.00 65.73  ? 214 ARG A NH2 1 
ATOM   1736 N  N   . ILE A 1 215 ? 19.614  -19.160 4.310   1.00 42.53  ? 215 ILE A N   1 
ATOM   1737 C  CA  . ILE A 1 215 ? 19.497  -17.731 4.067   1.00 41.83  ? 215 ILE A CA  1 
ATOM   1738 C  C   . ILE A 1 215 ? 19.799  -16.967 5.363   1.00 41.93  ? 215 ILE A C   1 
ATOM   1739 O  O   . ILE A 1 215 ? 20.599  -16.033 5.347   1.00 45.39  ? 215 ILE A O   1 
ATOM   1740 C  CB  . ILE A 1 215 ? 18.114  -17.377 3.472   1.00 41.16  ? 215 ILE A CB  1 
ATOM   1741 C  CG1 . ILE A 1 215 ? 17.905  -18.016 2.095   1.00 45.00  ? 215 ILE A CG1 1 
ATOM   1742 C  CG2 . ILE A 1 215 ? 17.918  -15.869 3.399   1.00 40.10  ? 215 ILE A CG2 1 
ATOM   1743 C  CD1 . ILE A 1 215 ? 16.440  -18.114 1.653   1.00 47.09  ? 215 ILE A CD1 1 
ATOM   1744 N  N   . PHE A 1 216 ? 19.161  -17.357 6.475   1.00 41.02  ? 216 PHE A N   1 
ATOM   1745 C  CA  . PHE A 1 216 ? 19.270  -16.645 7.746   1.00 42.50  ? 216 PHE A CA  1 
ATOM   1746 C  C   . PHE A 1 216 ? 20.711  -16.639 8.251   1.00 44.23  ? 216 PHE A C   1 
ATOM   1747 O  O   . PHE A 1 216 ? 21.193  -15.601 8.712   1.00 45.32  ? 216 PHE A O   1 
ATOM   1748 C  CB  . PHE A 1 216 ? 18.354  -17.255 8.812   1.00 42.81  ? 216 PHE A CB  1 
ATOM   1749 C  CG  . PHE A 1 216 ? 16.872  -17.085 8.592   1.00 43.79  ? 216 PHE A CG  1 
ATOM   1750 C  CD1 . PHE A 1 216 ? 16.375  -16.238 7.618   1.00 48.54  ? 216 PHE A CD1 1 
ATOM   1751 C  CD2 . PHE A 1 216 ? 15.966  -17.787 9.363   1.00 47.68  ? 216 PHE A CD2 1 
ATOM   1752 C  CE1 . PHE A 1 216 ? 15.015  -16.097 7.418   1.00 48.38  ? 216 PHE A CE1 1 
ATOM   1753 C  CE2 . PHE A 1 216 ? 14.603  -17.639 9.167   1.00 50.71  ? 216 PHE A CE2 1 
ATOM   1754 C  CZ  . PHE A 1 216 ? 14.132  -16.792 8.198   1.00 51.22  ? 216 PHE A CZ  1 
ATOM   1755 N  N   . ARG A 1 217 ? 21.398  -17.787 8.142   1.00 48.57  ? 217 ARG A N   1 
ATOM   1756 C  CA  . ARG A 1 217 ? 22.794  -17.920 8.561   1.00 51.83  ? 217 ARG A CA  1 
ATOM   1757 C  C   . ARG A 1 217 ? 23.642  -16.842 7.894   1.00 52.40  ? 217 ARG A C   1 
ATOM   1758 O  O   . ARG A 1 217 ? 24.613  -16.379 8.479   1.00 61.37  ? 217 ARG A O   1 
ATOM   1759 C  CB  . ARG A 1 217 ? 23.420  -19.276 8.195   1.00 58.93  ? 217 ARG A CB  1 
ATOM   1760 C  CG  . ARG A 1 217 ? 23.151  -20.411 9.173   1.00 64.66  ? 217 ARG A CG  1 
ATOM   1761 C  CD  . ARG A 1 217 ? 24.195  -21.513 9.111   1.00 70.87  ? 217 ARG A CD  1 
ATOM   1762 N  NE  . ARG A 1 217 ? 23.660  -22.754 9.653   1.00 82.71  ? 217 ARG A NE  1 
ATOM   1763 C  CZ  . ARG A 1 217 ? 22.811  -23.555 9.014   1.00 88.08  ? 217 ARG A CZ  1 
ATOM   1764 N  NH1 . ARG A 1 217 ? 22.356  -24.643 9.608   1.00 93.73  ? 217 ARG A NH1 1 
ATOM   1765 N  NH2 . ARG A 1 217 ? 22.420  -23.274 7.781   1.00 86.39  ? 217 ARG A NH2 1 
ATOM   1766 N  N   . THR A 1 218 ? 23.278  -16.459 6.665   1.00 52.03  ? 218 THR A N   1 
ATOM   1767 C  CA  . THR A 1 218 ? 24.103  -15.584 5.844   1.00 47.87  ? 218 THR A CA  1 
ATOM   1768 C  C   . THR A 1 218 ? 23.640  -14.131 5.943   1.00 48.52  ? 218 THR A C   1 
ATOM   1769 O  O   . THR A 1 218 ? 24.472  -13.241 6.055   1.00 51.51  ? 218 THR A O   1 
ATOM   1770 C  CB  . THR A 1 218 ? 24.099  -16.078 4.395   1.00 46.78  ? 218 THR A CB  1 
ATOM   1771 O  OG1 . THR A 1 218 ? 24.441  -17.467 4.394   1.00 43.97  ? 218 THR A OG1 1 
ATOM   1772 C  CG2 . THR A 1 218 ? 25.044  -15.301 3.510   1.00 47.33  ? 218 THR A CG2 1 
ATOM   1773 N  N   . LEU A 1 219 ? 22.324  -13.888 5.886   1.00 49.47  ? 219 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 219 ? 21.795  -12.535 5.746   1.00 48.42  ? 219 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 219 ? 21.300  -12.001 7.082   1.00 44.28  ? 219 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 219 ? 20.882  -10.839 7.162   1.00 46.31  ? 219 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 219 ? 20.637  -12.555 4.738   1.00 49.54  ? 219 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 219 ? 20.999  -12.787 3.271   1.00 46.41  ? 219 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 219 ? 19.820  -12.415 2.378   1.00 47.47  ? 219 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 219 ? 22.244  -11.997 2.875   1.00 43.68  ? 219 LEU A CD2 1 
ATOM   1781 N  N   . GLY A 1 220 ? 21.323  -12.875 8.096   1.00 41.63  ? 220 GLY A N   1 
ATOM   1782 C  CA  . GLY A 1 220 ? 20.747  -12.589 9.398   1.00 42.18  ? 220 GLY A CA  1 
ATOM   1783 C  C   . GLY A 1 220 ? 19.286  -13.013 9.433   1.00 43.16  ? 220 GLY A C   1 
ATOM   1784 O  O   . GLY A 1 220 ? 18.618  -12.964 8.407   1.00 44.94  ? 220 GLY A O   1 
ATOM   1785 N  N   . THR A 1 221 ? 18.805  -13.440 10.605  1.00 42.84  ? 221 THR A N   1 
ATOM   1786 C  CA  . THR A 1 221 ? 17.400  -13.771 10.772  1.00 42.36  ? 221 THR A CA  1 
ATOM   1787 C  C   . THR A 1 221 ? 16.583  -12.493 10.757  1.00 43.60  ? 221 THR A C   1 
ATOM   1788 O  O   . THR A 1 221 ? 16.838  -11.593 11.541  1.00 51.52  ? 221 THR A O   1 
ATOM   1789 C  CB  . THR A 1 221 ? 17.117  -14.521 12.070  1.00 40.58  ? 221 THR A CB  1 
ATOM   1790 O  OG1 . THR A 1 221 ? 18.087  -15.562 12.142  1.00 39.74  ? 221 THR A OG1 1 
ATOM   1791 C  CG2 . THR A 1 221 ? 15.723  -15.107 12.109  1.00 42.64  ? 221 THR A CG2 1 
ATOM   1792 N  N   . PRO A 1 222 ? 15.575  -12.378 9.871   1.00 46.37  ? 222 PRO A N   1 
ATOM   1793 C  CA  . PRO A 1 222 ? 14.777  -11.158 9.784   1.00 45.94  ? 222 PRO A CA  1 
ATOM   1794 C  C   . PRO A 1 222 ? 13.745  -11.055 10.911  1.00 46.47  ? 222 PRO A C   1 
ATOM   1795 O  O   . PRO A 1 222 ? 13.185  -12.062 11.334  1.00 42.73  ? 222 PRO A O   1 
ATOM   1796 C  CB  . PRO A 1 222 ? 14.109  -11.316 8.419   1.00 44.33  ? 222 PRO A CB  1 
ATOM   1797 C  CG  . PRO A 1 222 ? 13.885  -12.809 8.327   1.00 46.71  ? 222 PRO A CG  1 
ATOM   1798 C  CD  . PRO A 1 222 ? 15.121  -13.426 8.947   1.00 46.84  ? 222 PRO A CD  1 
ATOM   1799 N  N   . ASP A 1 223 ? 13.549  -9.816  11.384  1.00 49.87  ? 223 ASP A N   1 
ATOM   1800 C  CA  . ASP A 1 223 ? 12.622  -9.418  12.441  1.00 54.32  ? 223 ASP A CA  1 
ATOM   1801 C  C   . ASP A 1 223 ? 11.840  -8.198  11.940  1.00 48.37  ? 223 ASP A C   1 
ATOM   1802 O  O   . ASP A 1 223 ? 12.098  -7.692  10.847  1.00 48.13  ? 223 ASP A O   1 
ATOM   1803 C  CB  . ASP A 1 223 ? 13.376  -9.070  13.740  1.00 60.95  ? 223 ASP A CB  1 
ATOM   1804 C  CG  . ASP A 1 223 ? 14.431  -7.975  13.602  1.00 71.04  ? 223 ASP A CG  1 
ATOM   1805 O  OD1 . ASP A 1 223 ? 14.487  -7.329  12.529  1.00 70.08  ? 223 ASP A OD1 1 
ATOM   1806 O  OD2 . ASP A 1 223 ? 15.216  -7.781  14.563  1.00 81.12  ? 223 ASP A OD2 1 
ATOM   1807 N  N   . GLU A 1 224 ? 10.931  -7.687  12.772  1.00 47.55  ? 224 GLU A N   1 
ATOM   1808 C  CA  . GLU A 1 224 ? 10.152  -6.492  12.486  1.00 48.02  ? 224 GLU A CA  1 
ATOM   1809 C  C   . GLU A 1 224 ? 11.026  -5.299  12.085  1.00 47.88  ? 224 GLU A C   1 
ATOM   1810 O  O   . GLU A 1 224 ? 10.519  -4.395  11.427  1.00 58.01  ? 224 GLU A O   1 
ATOM   1811 C  CB  . GLU A 1 224 ? 9.292   -6.140  13.706  1.00 51.75  ? 224 GLU A CB  1 
ATOM   1812 C  CG  . GLU A 1 224 ? 8.111   -7.074  13.913  1.00 54.05  ? 224 GLU A CG  1 
ATOM   1813 C  CD  . GLU A 1 224 ? 7.044   -7.031  12.831  1.00 55.02  ? 224 GLU A CD  1 
ATOM   1814 O  OE1 . GLU A 1 224 ? 6.748   -5.924  12.328  1.00 52.80  ? 224 GLU A OE1 1 
ATOM   1815 O  OE2 . GLU A 1 224 ? 6.500   -8.108  12.506  1.00 64.67  ? 224 GLU A OE2 1 
ATOM   1816 N  N   . VAL A 1 225 ? 12.302  -5.267  12.492  1.00 45.11  ? 225 VAL A N   1 
ATOM   1817 C  CA  . VAL A 1 225 ? 13.183  -4.126  12.234  1.00 50.41  ? 225 VAL A CA  1 
ATOM   1818 C  C   . VAL A 1 225 ? 13.486  -3.980  10.730  1.00 51.34  ? 225 VAL A C   1 
ATOM   1819 O  O   . VAL A 1 225 ? 13.330  -2.886  10.184  1.00 55.13  ? 225 VAL A O   1 
ATOM   1820 C  CB  . VAL A 1 225 ? 14.482  -4.239  13.065  1.00 55.57  ? 225 VAL A CB  1 
ATOM   1821 C  CG1 . VAL A 1 225 ? 15.533  -3.218  12.655  1.00 55.10  ? 225 VAL A CG1 1 
ATOM   1822 C  CG2 . VAL A 1 225 ? 14.214  -4.152  14.562  1.00 58.51  ? 225 VAL A CG2 1 
ATOM   1823 N  N   . VAL A 1 226 ? 13.953  -5.066  10.081  1.00 46.84  ? 226 VAL A N   1 
ATOM   1824 C  CA  . VAL A 1 226 ? 14.399  -5.061  8.685   1.00 54.39  ? 226 VAL A CA  1 
ATOM   1825 C  C   . VAL A 1 226 ? 13.279  -5.528  7.748   1.00 53.89  ? 226 VAL A C   1 
ATOM   1826 O  O   . VAL A 1 226 ? 13.407  -5.356  6.541   1.00 55.17  ? 226 VAL A O   1 
ATOM   1827 C  CB  . VAL A 1 226 ? 15.690  -5.891  8.439   1.00 56.69  ? 226 VAL A CB  1 
ATOM   1828 C  CG1 . VAL A 1 226 ? 16.873  -5.378  9.245   1.00 58.57  ? 226 VAL A CG1 1 
ATOM   1829 C  CG2 . VAL A 1 226 ? 15.519  -7.381  8.688   1.00 54.18  ? 226 VAL A CG2 1 
ATOM   1830 N  N   . TRP A 1 227 ? 12.187  -6.100  8.282   1.00 52.09  ? 227 TRP A N   1 
ATOM   1831 C  CA  . TRP A 1 227 ? 11.079  -6.578  7.460   1.00 46.90  ? 227 TRP A CA  1 
ATOM   1832 C  C   . TRP A 1 227 ? 9.738   -6.478  8.211   1.00 43.75  ? 227 TRP A C   1 
ATOM   1833 O  O   . TRP A 1 227 ? 9.238   -7.439  8.791   1.00 35.35  ? 227 TRP A O   1 
ATOM   1834 C  CB  . TRP A 1 227 ? 11.413  -7.998  6.989   1.00 44.21  ? 227 TRP A CB  1 
ATOM   1835 C  CG  . TRP A 1 227 ? 10.530  -8.529  5.905   1.00 43.44  ? 227 TRP A CG  1 
ATOM   1836 C  CD1 . TRP A 1 227 ? 9.496   -7.895  5.270   1.00 46.11  ? 227 TRP A CD1 1 
ATOM   1837 C  CD2 . TRP A 1 227 ? 10.592  -9.849  5.350   1.00 41.16  ? 227 TRP A CD2 1 
ATOM   1838 N  NE1 . TRP A 1 227 ? 8.900   -8.735  4.373   1.00 40.89  ? 227 TRP A NE1 1 
ATOM   1839 C  CE2 . TRP A 1 227 ? 9.556   -9.941  4.398   1.00 43.08  ? 227 TRP A CE2 1 
ATOM   1840 C  CE3 . TRP A 1 227 ? 11.405  -10.966 5.585   1.00 39.90  ? 227 TRP A CE3 1 
ATOM   1841 C  CZ2 . TRP A 1 227 ? 9.349   -11.103 3.655   1.00 41.51  ? 227 TRP A CZ2 1 
ATOM   1842 C  CZ3 . TRP A 1 227 ? 11.190  -12.116 4.861   1.00 40.89  ? 227 TRP A CZ3 1 
ATOM   1843 C  CH2 . TRP A 1 227 ? 10.168  -12.181 3.912   1.00 42.65  ? 227 TRP A CH2 1 
ATOM   1844 N  N   . PRO A 1 228 ? 9.091   -5.293  8.241   1.00 43.10  ? 228 PRO A N   1 
ATOM   1845 C  CA  . PRO A 1 228 ? 7.869   -5.118  9.016   1.00 44.48  ? 228 PRO A CA  1 
ATOM   1846 C  C   . PRO A 1 228 ? 6.833   -6.103  8.488   1.00 48.59  ? 228 PRO A C   1 
ATOM   1847 O  O   . PRO A 1 228 ? 6.811   -6.380  7.298   1.00 52.08  ? 228 PRO A O   1 
ATOM   1848 C  CB  . PRO A 1 228 ? 7.480   -3.658  8.753   1.00 44.43  ? 228 PRO A CB  1 
ATOM   1849 C  CG  . PRO A 1 228 ? 8.774   -2.998  8.345   1.00 43.95  ? 228 PRO A CG  1 
ATOM   1850 C  CD  . PRO A 1 228 ? 9.498   -4.060  7.550   1.00 46.11  ? 228 PRO A CD  1 
ATOM   1851 N  N   . GLY A 1 229 ? 6.012   -6.651  9.384   1.00 46.34  ? 229 GLY A N   1 
ATOM   1852 C  CA  . GLY A 1 229 ? 4.993   -7.614  9.008   1.00 44.82  ? 229 GLY A CA  1 
ATOM   1853 C  C   . GLY A 1 229 ? 5.494   -9.054  9.020   1.00 45.88  ? 229 GLY A C   1 
ATOM   1854 O  O   . GLY A 1 229 ? 4.667   -9.958  8.945   1.00 49.46  ? 229 GLY A O   1 
ATOM   1855 N  N   . VAL A 1 230 ? 6.817   -9.271  9.122   1.00 45.14  ? 230 VAL A N   1 
ATOM   1856 C  CA  . VAL A 1 230 ? 7.401   -10.596 8.901   1.00 46.22  ? 230 VAL A CA  1 
ATOM   1857 C  C   . VAL A 1 230 ? 6.983   -11.562 10.009  1.00 47.75  ? 230 VAL A C   1 
ATOM   1858 O  O   . VAL A 1 230 ? 6.795   -12.742 9.733   1.00 45.76  ? 230 VAL A O   1 
ATOM   1859 C  CB  . VAL A 1 230 ? 8.939   -10.585 8.741   1.00 47.25  ? 230 VAL A CB  1 
ATOM   1860 C  CG1 . VAL A 1 230 ? 9.682   -10.264 10.020  1.00 46.94  ? 230 VAL A CG1 1 
ATOM   1861 C  CG2 . VAL A 1 230 ? 9.445   -11.915 8.212   1.00 52.59  ? 230 VAL A CG2 1 
ATOM   1862 N  N   . THR A 1 231 ? 6.856   -11.071 11.251  1.00 55.72  ? 231 THR A N   1 
ATOM   1863 C  CA  . THR A 1 231 ? 6.585   -11.925 12.405  1.00 60.83  ? 231 THR A CA  1 
ATOM   1864 C  C   . THR A 1 231 ? 5.110   -12.345 12.421  1.00 62.66  ? 231 THR A C   1 
ATOM   1865 O  O   . THR A 1 231 ? 4.772   -13.331 13.068  1.00 63.06  ? 231 THR A O   1 
ATOM   1866 C  CB  . THR A 1 231 ? 7.052   -11.261 13.709  1.00 61.77  ? 231 THR A CB  1 
ATOM   1867 O  OG1 . THR A 1 231 ? 6.320   -10.058 13.941  1.00 63.48  ? 231 THR A OG1 1 
ATOM   1868 C  CG2 . THR A 1 231 ? 8.530   -10.942 13.687  1.00 61.31  ? 231 THR A CG2 1 
ATOM   1869 N  N   . SER A 1 232 ? 4.262   -11.609 11.678  1.00 71.89  ? 232 SER A N   1 
ATOM   1870 C  CA  . SER A 1 232 ? 2.836   -11.881 11.498  1.00 75.46  ? 232 SER A CA  1 
ATOM   1871 C  C   . SER A 1 232 ? 2.574   -12.972 10.450  1.00 74.96  ? 232 SER A C   1 
ATOM   1872 O  O   . SER A 1 232 ? 1.434   -13.399 10.307  1.00 82.87  ? 232 SER A O   1 
ATOM   1873 C  CB  . SER A 1 232 ? 2.074   -10.615 11.090  1.00 81.44  ? 232 SER A CB  1 
ATOM   1874 O  OG  . SER A 1 232 ? 2.075   -9.621  12.107  1.00 88.13  ? 232 SER A OG  1 
ATOM   1875 N  N   . MET A 1 233 ? 3.600   -13.424 9.712   1.00 74.50  ? 233 MET A N   1 
ATOM   1876 C  CA  . MET A 1 233 ? 3.403   -14.194 8.484   1.00 72.08  ? 233 MET A CA  1 
ATOM   1877 C  C   . MET A 1 233 ? 2.952   -15.620 8.780   1.00 71.85  ? 233 MET A C   1 
ATOM   1878 O  O   . MET A 1 233 ? 3.171   -16.124 9.879   1.00 67.41  ? 233 MET A O   1 
ATOM   1879 C  CB  . MET A 1 233 ? 4.684   -14.267 7.646   1.00 67.01  ? 233 MET A CB  1 
ATOM   1880 C  CG  . MET A 1 233 ? 4.886   -13.035 6.826   1.00 70.58  ? 233 MET A CG  1 
ATOM   1881 S  SD  . MET A 1 233 ? 5.971   -13.238 5.403   1.00 80.06  ? 233 MET A SD  1 
ATOM   1882 C  CE  . MET A 1 233 ? 5.899   -11.536 4.837   1.00 84.46  ? 233 MET A CE  1 
ATOM   1883 N  N   . PRO A 1 234 ? 2.333   -16.317 7.793   1.00 75.28  ? 234 PRO A N   1 
ATOM   1884 C  CA  . PRO A 1 234 ? 1.886   -17.697 7.985   1.00 76.23  ? 234 PRO A CA  1 
ATOM   1885 C  C   . PRO A 1 234 ? 2.932   -18.594 8.648   1.00 72.19  ? 234 PRO A C   1 
ATOM   1886 O  O   . PRO A 1 234 ? 2.723   -19.059 9.770   1.00 59.63  ? 234 PRO A O   1 
ATOM   1887 C  CB  . PRO A 1 234 ? 1.581   -18.143 6.546   1.00 76.34  ? 234 PRO A CB  1 
ATOM   1888 C  CG  . PRO A 1 234 ? 1.094   -16.877 5.876   1.00 73.46  ? 234 PRO A CG  1 
ATOM   1889 C  CD  . PRO A 1 234 ? 1.988   -15.801 6.453   1.00 71.02  ? 234 PRO A CD  1 
ATOM   1890 N  N   . ASP A 1 235 ? 4.077   -18.753 7.966   1.00 71.64  ? 235 ASP A N   1 
ATOM   1891 C  CA  . ASP A 1 235 ? 5.054   -19.801 8.239   1.00 68.23  ? 235 ASP A CA  1 
ATOM   1892 C  C   . ASP A 1 235 ? 6.267   -19.295 9.046   1.00 61.14  ? 235 ASP A C   1 
ATOM   1893 O  O   . ASP A 1 235 ? 7.221   -20.049 9.241   1.00 54.45  ? 235 ASP A O   1 
ATOM   1894 C  CB  . ASP A 1 235 ? 5.443   -20.469 6.912   1.00 72.00  ? 235 ASP A CB  1 
ATOM   1895 C  CG  . ASP A 1 235 ? 4.299   -21.230 6.256   1.00 76.45  ? 235 ASP A CG  1 
ATOM   1896 O  OD1 . ASP A 1 235 ? 3.768   -22.155 6.899   1.00 74.78  ? 235 ASP A OD1 1 
ATOM   1897 O  OD2 . ASP A 1 235 ? 3.951   -20.897 5.103   1.00 78.11  ? 235 ASP A OD2 1 
ATOM   1898 N  N   . TYR A 1 236 ? 6.228   -18.046 9.551   1.00 56.70  ? 236 TYR A N   1 
ATOM   1899 C  CA  . TYR A 1 236 ? 7.209   -17.533 10.508  1.00 60.35  ? 236 TYR A CA  1 
ATOM   1900 C  C   . TYR A 1 236 ? 6.972   -18.159 11.884  1.00 61.67  ? 236 TYR A C   1 
ATOM   1901 O  O   . TYR A 1 236 ? 5.825   -18.254 12.330  1.00 66.26  ? 236 TYR A O   1 
ATOM   1902 C  CB  . TYR A 1 236 ? 7.130   -16.006 10.643  1.00 66.14  ? 236 TYR A CB  1 
ATOM   1903 C  CG  . TYR A 1 236 ? 8.174   -15.383 11.541  1.00 72.46  ? 236 TYR A CG  1 
ATOM   1904 C  CD1 . TYR A 1 236 ? 9.421   -15.036 11.046  1.00 77.44  ? 236 TYR A CD1 1 
ATOM   1905 C  CD2 . TYR A 1 236 ? 7.928   -15.153 12.890  1.00 78.26  ? 236 TYR A CD2 1 
ATOM   1906 C  CE1 . TYR A 1 236 ? 10.388  -14.461 11.856  1.00 83.79  ? 236 TYR A CE1 1 
ATOM   1907 C  CE2 . TYR A 1 236 ? 8.886   -14.585 13.717  1.00 82.86  ? 236 TYR A CE2 1 
ATOM   1908 C  CZ  . TYR A 1 236 ? 10.121  -14.239 13.195  1.00 86.59  ? 236 TYR A CZ  1 
ATOM   1909 O  OH  . TYR A 1 236 ? 11.084  -13.671 13.986  1.00 93.60  ? 236 TYR A OH  1 
ATOM   1910 N  N   . LYS A 1 237 ? 8.071   -18.554 12.549  1.00 59.55  ? 237 LYS A N   1 
ATOM   1911 C  CA  . LYS A 1 237 ? 8.050   -19.116 13.896  1.00 64.66  ? 237 LYS A CA  1 
ATOM   1912 C  C   . LYS A 1 237 ? 8.951   -18.301 14.817  1.00 60.02  ? 237 LYS A C   1 
ATOM   1913 O  O   . LYS A 1 237 ? 10.117  -18.056 14.504  1.00 57.81  ? 237 LYS A O   1 
ATOM   1914 C  CB  . LYS A 1 237 ? 8.470   -20.589 13.863  1.00 72.58  ? 237 LYS A CB  1 
ATOM   1915 C  CG  . LYS A 1 237 ? 7.351   -21.526 13.428  1.00 77.41  ? 237 LYS A CG  1 
ATOM   1916 C  CD  . LYS A 1 237 ? 7.796   -22.616 12.498  1.00 83.08  ? 237 LYS A CD  1 
ATOM   1917 C  CE  . LYS A 1 237 ? 8.744   -23.592 13.154  1.00 89.18  ? 237 LYS A CE  1 
ATOM   1918 N  NZ  . LYS A 1 237 ? 9.134   -24.655 12.201  1.00 94.86  ? 237 LYS A NZ  1 
ATOM   1919 N  N   . PRO A 1 238 ? 8.429   -17.862 15.986  1.00 60.04  ? 238 PRO A N   1 
ATOM   1920 C  CA  . PRO A 1 238 ? 9.237   -17.129 16.966  1.00 59.26  ? 238 PRO A CA  1 
ATOM   1921 C  C   . PRO A 1 238 ? 10.501  -17.858 17.442  1.00 53.38  ? 238 PRO A C   1 
ATOM   1922 O  O   . PRO A 1 238 ? 11.449  -17.208 17.874  1.00 53.85  ? 238 PRO A O   1 
ATOM   1923 C  CB  . PRO A 1 238 ? 8.291   -16.919 18.159  1.00 58.61  ? 238 PRO A CB  1 
ATOM   1924 C  CG  . PRO A 1 238 ? 6.895   -17.132 17.604  1.00 62.18  ? 238 PRO A CG  1 
ATOM   1925 C  CD  . PRO A 1 238 ? 7.037   -18.060 16.418  1.00 60.18  ? 238 PRO A CD  1 
ATOM   1926 N  N   . SER A 1 239 ? 10.513  -19.197 17.335  1.00 49.13  ? 239 SER A N   1 
ATOM   1927 C  CA  . SER A 1 239 ? 11.620  -20.045 17.775  1.00 53.80  ? 239 SER A CA  1 
ATOM   1928 C  C   . SER A 1 239 ? 12.789  -20.064 16.782  1.00 54.06  ? 239 SER A C   1 
ATOM   1929 O  O   . SER A 1 239 ? 13.799  -20.720 17.025  1.00 55.62  ? 239 SER A O   1 
ATOM   1930 C  CB  . SER A 1 239 ? 11.131  -21.458 18.058  1.00 54.05  ? 239 SER A CB  1 
ATOM   1931 O  OG  . SER A 1 239 ? 10.609  -22.086 16.894  1.00 53.92  ? 239 SER A OG  1 
ATOM   1932 N  N   . PHE A 1 240 ? 12.663  -19.373 15.646  1.00 57.51  ? 240 PHE A N   1 
ATOM   1933 C  CA  . PHE A 1 240 ? 13.730  -19.343 14.655  1.00 57.54  ? 240 PHE A CA  1 
ATOM   1934 C  C   . PHE A 1 240 ? 15.019  -18.880 15.333  1.00 49.87  ? 240 PHE A C   1 
ATOM   1935 O  O   . PHE A 1 240 ? 15.006  -17.882 16.047  1.00 48.19  ? 240 PHE A O   1 
ATOM   1936 C  CB  . PHE A 1 240 ? 13.362  -18.421 13.483  1.00 59.73  ? 240 PHE A CB  1 
ATOM   1937 C  CG  . PHE A 1 240 ? 12.459  -18.991 12.411  1.00 64.75  ? 240 PHE A CG  1 
ATOM   1938 C  CD1 . PHE A 1 240 ? 12.285  -20.360 12.249  1.00 65.26  ? 240 PHE A CD1 1 
ATOM   1939 C  CD2 . PHE A 1 240 ? 11.789  -18.140 11.538  1.00 65.52  ? 240 PHE A CD2 1 
ATOM   1940 C  CE1 . PHE A 1 240 ? 11.461  -20.856 11.250  1.00 66.23  ? 240 PHE A CE1 1 
ATOM   1941 C  CE2 . PHE A 1 240 ? 10.967  -18.639 10.539  1.00 60.23  ? 240 PHE A CE2 1 
ATOM   1942 C  CZ  . PHE A 1 240 ? 10.803  -19.996 10.400  1.00 63.76  ? 240 PHE A CZ  1 
ATOM   1943 N  N   . PRO A 1 241 ? 16.162  -19.575 15.127  1.00 50.63  ? 241 PRO A N   1 
ATOM   1944 C  CA  . PRO A 1 241 ? 17.457  -19.120 15.642  1.00 49.59  ? 241 PRO A CA  1 
ATOM   1945 C  C   . PRO A 1 241 ? 17.766  -17.707 15.173  1.00 54.11  ? 241 PRO A C   1 
ATOM   1946 O  O   . PRO A 1 241 ? 17.465  -17.395 14.027  1.00 65.52  ? 241 PRO A O   1 
ATOM   1947 C  CB  . PRO A 1 241 ? 18.477  -20.072 15.020  1.00 45.95  ? 241 PRO A CB  1 
ATOM   1948 C  CG  . PRO A 1 241 ? 17.681  -21.316 14.700  1.00 50.94  ? 241 PRO A CG  1 
ATOM   1949 C  CD  . PRO A 1 241 ? 16.273  -20.843 14.394  1.00 53.98  ? 241 PRO A CD  1 
ATOM   1950 N  N   . LYS A 1 242 ? 18.348  -16.872 16.047  1.00 59.27  ? 242 LYS A N   1 
ATOM   1951 C  CA  . LYS A 1 242 ? 18.603  -15.468 15.740  1.00 65.51  ? 242 LYS A CA  1 
ATOM   1952 C  C   . LYS A 1 242 ? 20.087  -15.324 15.410  1.00 67.43  ? 242 LYS A C   1 
ATOM   1953 O  O   . LYS A 1 242 ? 20.908  -15.066 16.292  1.00 75.71  ? 242 LYS A O   1 
ATOM   1954 C  CB  . LYS A 1 242 ? 18.157  -14.551 16.887  1.00 73.11  ? 242 LYS A CB  1 
ATOM   1955 C  CG  . LYS A 1 242 ? 16.683  -14.653 17.282  1.00 86.38  ? 242 LYS A CG  1 
ATOM   1956 C  CD  . LYS A 1 242 ? 15.753  -13.566 16.745  1.00 94.56  ? 242 LYS A CD  1 
ATOM   1957 C  CE  . LYS A 1 242 ? 14.579  -13.292 17.668  1.00 98.66  ? 242 LYS A CE  1 
ATOM   1958 N  NZ  . LYS A 1 242 ? 13.814  -14.524 17.983  1.00 101.71 ? 242 LYS A NZ  1 
ATOM   1959 N  N   . TRP A 1 243 ? 20.399  -15.549 14.127  1.00 56.68  ? 243 TRP A N   1 
ATOM   1960 C  CA  . TRP A 1 243 ? 21.732  -15.397 13.558  1.00 52.31  ? 243 TRP A CA  1 
ATOM   1961 C  C   . TRP A 1 243 ? 21.949  -13.945 13.144  1.00 50.23  ? 243 TRP A C   1 
ATOM   1962 O  O   . TRP A 1 243 ? 20.984  -13.235 12.865  1.00 45.87  ? 243 TRP A O   1 
ATOM   1963 C  CB  . TRP A 1 243 ? 21.900  -16.310 12.341  1.00 47.10  ? 243 TRP A CB  1 
ATOM   1964 C  CG  . TRP A 1 243 ? 22.102  -17.765 12.623  1.00 51.10  ? 243 TRP A CG  1 
ATOM   1965 C  CD1 . TRP A 1 243 ? 23.198  -18.340 13.200  1.00 53.57  ? 243 TRP A CD1 1 
ATOM   1966 C  CD2 . TRP A 1 243 ? 21.225  -18.853 12.267  1.00 52.42  ? 243 TRP A CD2 1 
ATOM   1967 N  NE1 . TRP A 1 243 ? 23.060  -19.704 13.234  1.00 55.61  ? 243 TRP A NE1 1 
ATOM   1968 C  CE2 . TRP A 1 243 ? 21.858  -20.048 12.675  1.00 53.64  ? 243 TRP A CE2 1 
ATOM   1969 C  CE3 . TRP A 1 243 ? 19.965  -18.942 11.664  1.00 53.45  ? 243 TRP A CE3 1 
ATOM   1970 C  CZ2 . TRP A 1 243 ? 21.284  -21.301 12.481  1.00 51.48  ? 243 TRP A CZ2 1 
ATOM   1971 C  CZ3 . TRP A 1 243 ? 19.397  -20.182 11.474  1.00 50.25  ? 243 TRP A CZ3 1 
ATOM   1972 C  CH2 . TRP A 1 243 ? 20.049  -21.344 11.880  1.00 50.28  ? 243 TRP A CH2 1 
ATOM   1973 N  N   . ALA A 1 244 ? 23.226  -13.543 13.094  1.00 51.94  ? 244 ALA A N   1 
ATOM   1974 C  CA  . ALA A 1 244 ? 23.655  -12.213 12.678  1.00 54.15  ? 244 ALA A CA  1 
ATOM   1975 C  C   . ALA A 1 244 ? 24.003  -12.219 11.186  1.00 54.18  ? 244 ALA A C   1 
ATOM   1976 O  O   . ALA A 1 244 ? 24.518  -13.211 10.667  1.00 61.15  ? 244 ALA A O   1 
ATOM   1977 C  CB  . ALA A 1 244 ? 24.851  -11.781 13.503  1.00 54.04  ? 244 ALA A CB  1 
ATOM   1978 N  N   A ARG A 1 245 ? 23.692  -11.108 10.502  0.50 54.10  ? 245 ARG A N   1 
ATOM   1979 N  N   B ARG A 1 245 ? 23.691  -11.110 10.504  0.50 52.10  ? 245 ARG A N   1 
ATOM   1980 C  CA  A ARG A 1 245 ? 24.146  -10.856 9.139   0.50 52.70  ? 245 ARG A CA  1 
ATOM   1981 C  CA  B ARG A 1 245 ? 24.144  -10.854 9.142   0.50 49.44  ? 245 ARG A CA  1 
ATOM   1982 C  C   A ARG A 1 245 ? 25.672  -10.990 9.090   0.50 53.30  ? 245 ARG A C   1 
ATOM   1983 C  C   B ARG A 1 245 ? 25.671  -10.984 9.087   0.50 51.49  ? 245 ARG A C   1 
ATOM   1984 O  O   A ARG A 1 245 ? 26.368  -10.372 9.892   0.50 51.36  ? 245 ARG A O   1 
ATOM   1985 O  O   B ARG A 1 245 ? 26.368  -10.362 9.885   0.50 49.70  ? 245 ARG A O   1 
ATOM   1986 C  CB  A ARG A 1 245 ? 23.679  -9.464  8.685   0.50 51.28  ? 245 ARG A CB  1 
ATOM   1987 C  CB  B ARG A 1 245 ? 23.642  -9.467  8.709   0.50 45.70  ? 245 ARG A CB  1 
ATOM   1988 C  CG  A ARG A 1 245 ? 24.219  -9.017  7.331   0.50 56.13  ? 245 ARG A CG  1 
ATOM   1989 C  CG  B ARG A 1 245 ? 24.340  -8.875  7.492   0.50 48.19  ? 245 ARG A CG  1 
ATOM   1990 C  CD  A ARG A 1 245 ? 23.856  -7.588  6.956   0.50 59.17  ? 245 ARG A CD  1 
ATOM   1991 C  CD  B ARG A 1 245 ? 23.492  -7.825  6.792   0.50 49.12  ? 245 ARG A CD  1 
ATOM   1992 N  NE  A ARG A 1 245 ? 24.063  -7.304  5.538   0.50 60.85  ? 245 ARG A NE  1 
ATOM   1993 N  NE  B ARG A 1 245 ? 22.188  -8.370  6.428   0.50 48.90  ? 245 ARG A NE  1 
ATOM   1994 C  CZ  A ARG A 1 245 ? 23.169  -7.550  4.585   0.50 62.54  ? 245 ARG A CZ  1 
ATOM   1995 C  CZ  B ARG A 1 245 ? 21.710  -8.457  5.195   0.50 45.41  ? 245 ARG A CZ  1 
ATOM   1996 N  NH1 A ARG A 1 245 ? 23.453  -7.257  3.328   0.50 59.00  ? 245 ARG A NH1 1 
ATOM   1997 N  NH1 B ARG A 1 245 ? 22.392  -7.967  4.175   0.50 50.26  ? 245 ARG A NH1 1 
ATOM   1998 N  NH2 A ARG A 1 245 ? 21.994  -8.078  4.897   0.50 60.89  ? 245 ARG A NH2 1 
ATOM   1999 N  NH2 B ARG A 1 245 ? 20.533  -9.022  4.998   0.50 43.95  ? 245 ARG A NH2 1 
ATOM   2000 N  N   . GLN A 1 246 ? 26.178  -11.830 8.174   1.00 53.86  ? 246 GLN A N   1 
ATOM   2001 C  CA  . GLN A 1 246 ? 27.611  -11.971 7.906   1.00 55.61  ? 246 GLN A CA  1 
ATOM   2002 C  C   . GLN A 1 246 ? 28.115  -10.751 7.129   1.00 61.32  ? 246 GLN A C   1 
ATOM   2003 O  O   . GLN A 1 246 ? 27.319  -10.069 6.488   1.00 69.03  ? 246 GLN A O   1 
ATOM   2004 C  CB  . GLN A 1 246 ? 27.883  -13.217 7.055   1.00 54.19  ? 246 GLN A CB  1 
ATOM   2005 C  CG  . GLN A 1 246 ? 27.970  -14.532 7.823   1.00 59.93  ? 246 GLN A CG  1 
ATOM   2006 C  CD  . GLN A 1 246 ? 28.400  -15.667 6.913   1.00 67.75  ? 246 GLN A CD  1 
ATOM   2007 O  OE1 . GLN A 1 246 ? 29.259  -15.503 6.047   1.00 66.97  ? 246 GLN A OE1 1 
ATOM   2008 N  NE2 . GLN A 1 246 ? 27.788  -16.832 7.075   1.00 70.17  ? 246 GLN A NE2 1 
ATOM   2009 N  N   . ASP A 1 247 ? 29.434  -10.493 7.157   1.00 65.69  ? 247 ASP A N   1 
ATOM   2010 C  CA  . ASP A 1 247 ? 30.037  -9.429  6.357   1.00 65.39  ? 247 ASP A CA  1 
ATOM   2011 C  C   . ASP A 1 247 ? 30.132  -9.909  4.905   1.00 60.86  ? 247 ASP A C   1 
ATOM   2012 O  O   . ASP A 1 247 ? 30.566  -11.029 4.636   1.00 57.11  ? 247 ASP A O   1 
ATOM   2013 C  CB  . ASP A 1 247 ? 31.390  -8.990  6.937   1.00 71.98  ? 247 ASP A CB  1 
ATOM   2014 C  CG  . ASP A 1 247 ? 31.846  -7.610  6.484   1.00 76.54  ? 247 ASP A CG  1 
ATOM   2015 O  OD1 . ASP A 1 247 ? 32.421  -7.512  5.385   1.00 69.69  ? 247 ASP A OD1 1 
ATOM   2016 O  OD2 . ASP A 1 247 ? 31.600  -6.638  7.228   1.00 88.25  ? 247 ASP A OD2 1 
ATOM   2017 N  N   . PHE A 1 248 ? 29.715  -9.058  3.962   1.00 59.71  ? 248 PHE A N   1 
ATOM   2018 C  CA  . PHE A 1 248 ? 29.668  -9.433  2.550   1.00 68.45  ? 248 PHE A CA  1 
ATOM   2019 C  C   . PHE A 1 248 ? 31.075  -9.627  1.971   1.00 70.39  ? 248 PHE A C   1 
ATOM   2020 O  O   . PHE A 1 248 ? 31.241  -10.372 1.005   1.00 66.24  ? 248 PHE A O   1 
ATOM   2021 C  CB  . PHE A 1 248 ? 28.806  -8.440  1.760   1.00 73.58  ? 248 PHE A CB  1 
ATOM   2022 C  CG  . PHE A 1 248 ? 27.368  -8.874  1.635   1.00 77.80  ? 248 PHE A CG  1 
ATOM   2023 C  CD1 . PHE A 1 248 ? 26.674  -9.342  2.742   1.00 83.44  ? 248 PHE A CD1 1 
ATOM   2024 C  CD2 . PHE A 1 248 ? 26.716  -8.845  0.414   1.00 80.12  ? 248 PHE A CD2 1 
ATOM   2025 C  CE1 . PHE A 1 248 ? 25.359  -9.761  2.631   1.00 80.36  ? 248 PHE A CE1 1 
ATOM   2026 C  CE2 . PHE A 1 248 ? 25.398  -9.267  0.306   1.00 79.71  ? 248 PHE A CE2 1 
ATOM   2027 C  CZ  . PHE A 1 248 ? 24.723  -9.721  1.413   1.00 75.89  ? 248 PHE A CZ  1 
ATOM   2028 N  N   A SER A 1 249 ? 32.072  -8.963  2.572   0.50 72.91  ? 249 SER A N   1 
ATOM   2029 N  N   B SER A 1 249 ? 32.073  -8.956  2.567   0.50 71.57  ? 249 SER A N   1 
ATOM   2030 C  CA  A SER A 1 249 ? 33.472  -9.134  2.205   0.50 72.51  ? 249 SER A CA  1 
ATOM   2031 C  CA  B SER A 1 249 ? 33.475  -9.129  2.203   0.50 70.22  ? 249 SER A CA  1 
ATOM   2032 C  C   A SER A 1 249 ? 33.905  -10.588 2.401   0.50 71.28  ? 249 SER A C   1 
ATOM   2033 C  C   B SER A 1 249 ? 33.911  -10.582 2.409   0.50 70.01  ? 249 SER A C   1 
ATOM   2034 O  O   A SER A 1 249 ? 34.870  -11.024 1.778   0.50 73.69  ? 249 SER A O   1 
ATOM   2035 O  O   B SER A 1 249 ? 34.884  -11.015 1.796   0.50 72.41  ? 249 SER A O   1 
ATOM   2036 C  CB  A SER A 1 249 ? 34.359  -8.200  2.992   0.50 72.53  ? 249 SER A CB  1 
ATOM   2037 C  CB  B SER A 1 249 ? 34.375  -8.177  2.969   0.50 68.75  ? 249 SER A CB  1 
ATOM   2038 O  OG  A SER A 1 249 ? 34.587  -8.706  4.299   0.50 71.18  ? 249 SER A OG  1 
ATOM   2039 O  OG  B SER A 1 249 ? 34.099  -6.820  2.642   0.50 64.96  ? 249 SER A OG  1 
ATOM   2040 N  N   . LYS A 1 250 ? 33.189  -11.329 3.261   1.00 67.94  ? 250 LYS A N   1 
ATOM   2041 C  CA  . LYS A 1 250 ? 33.496  -12.735 3.539   1.00 73.27  ? 250 LYS A CA  1 
ATOM   2042 C  C   . LYS A 1 250 ? 32.642  -13.676 2.685   1.00 66.47  ? 250 LYS A C   1 
ATOM   2043 O  O   . LYS A 1 250 ? 33.124  -14.733 2.302   1.00 62.22  ? 250 LYS A O   1 
ATOM   2044 C  CB  . LYS A 1 250 ? 33.290  -13.082 5.022   1.00 82.39  ? 250 LYS A CB  1 
ATOM   2045 C  CG  . LYS A 1 250 ? 34.028  -12.188 6.012   1.00 95.20  ? 250 LYS A CG  1 
ATOM   2046 C  CD  . LYS A 1 250 ? 35.547  -12.149 5.853   1.00 99.82  ? 250 LYS A CD  1 
ATOM   2047 C  CE  . LYS A 1 250 ? 36.169  -10.863 6.364   1.00 105.48 ? 250 LYS A CE  1 
ATOM   2048 N  NZ  . LYS A 1 250 ? 35.612  -10.446 7.675   1.00 111.65 ? 250 LYS A NZ  1 
ATOM   2049 N  N   . VAL A 1 251 ? 31.388  -13.292 2.398   1.00 65.52  ? 251 VAL A N   1 
ATOM   2050 C  CA  . VAL A 1 251 ? 30.428  -14.104 1.653   1.00 60.38  ? 251 VAL A CA  1 
ATOM   2051 C  C   . VAL A 1 251 ? 30.800  -14.195 0.169   1.00 57.63  ? 251 VAL A C   1 
ATOM   2052 O  O   . VAL A 1 251 ? 30.599  -15.238 -0.453  1.00 56.91  ? 251 VAL A O   1 
ATOM   2053 C  CB  . VAL A 1 251 ? 29.007  -13.531 1.804   1.00 63.62  ? 251 VAL A CB  1 
ATOM   2054 C  CG1 . VAL A 1 251 ? 28.004  -14.230 0.895   1.00 65.86  ? 251 VAL A CG1 1 
ATOM   2055 C  CG2 . VAL A 1 251 ? 28.536  -13.574 3.246   1.00 65.68  ? 251 VAL A CG2 1 
ATOM   2056 N  N   . VAL A 1 252 ? 31.280  -13.074 -0.389  1.00 55.57  ? 252 VAL A N   1 
ATOM   2057 C  CA  . VAL A 1 252 ? 31.680  -12.949 -1.785  1.00 58.71  ? 252 VAL A CA  1 
ATOM   2058 C  C   . VAL A 1 252 ? 32.988  -12.156 -1.852  1.00 60.57  ? 252 VAL A C   1 
ATOM   2059 O  O   . VAL A 1 252 ? 33.005  -11.004 -2.292  1.00 62.01  ? 252 VAL A O   1 
ATOM   2060 C  CB  . VAL A 1 252 ? 30.581  -12.280 -2.635  1.00 62.19  ? 252 VAL A CB  1 
ATOM   2061 C  CG1 . VAL A 1 252 ? 29.381  -13.202 -2.815  1.00 59.25  ? 252 VAL A CG1 1 
ATOM   2062 C  CG2 . VAL A 1 252 ? 30.159  -10.922 -2.067  1.00 59.60  ? 252 VAL A CG2 1 
ATOM   2063 N  N   . PRO A 1 253 ? 34.128  -12.776 -1.457  1.00 57.96  ? 253 PRO A N   1 
ATOM   2064 C  CA  . PRO A 1 253 ? 35.430  -12.097 -1.443  1.00 54.77  ? 253 PRO A CA  1 
ATOM   2065 C  C   . PRO A 1 253 ? 35.814  -11.315 -2.705  1.00 53.99  ? 253 PRO A C   1 
ATOM   2066 O  O   . PRO A 1 253 ? 36.193  -10.146 -2.611  1.00 54.86  ? 253 PRO A O   1 
ATOM   2067 C  CB  . PRO A 1 253 ? 36.424  -13.244 -1.188  1.00 56.68  ? 253 PRO A CB  1 
ATOM   2068 C  CG  . PRO A 1 253 ? 35.613  -14.315 -0.474  1.00 57.05  ? 253 PRO A CG  1 
ATOM   2069 C  CD  . PRO A 1 253 ? 34.206  -14.180 -1.014  1.00 55.60  ? 253 PRO A CD  1 
ATOM   2070 N  N   . PRO A 1 254 ? 35.730  -11.875 -3.935  1.00 51.88  ? 254 PRO A N   1 
ATOM   2071 C  CA  . PRO A 1 254 ? 36.258  -11.164 -5.108  1.00 54.96  ? 254 PRO A CA  1 
ATOM   2072 C  C   . PRO A 1 254 ? 35.647  -9.790  -5.436  1.00 56.79  ? 254 PRO A C   1 
ATOM   2073 O  O   . PRO A 1 254 ? 36.200  -9.066  -6.261  1.00 53.16  ? 254 PRO A O   1 
ATOM   2074 C  CB  . PRO A 1 254 ? 36.021  -12.145 -6.274  1.00 54.22  ? 254 PRO A CB  1 
ATOM   2075 C  CG  . PRO A 1 254 ? 35.801  -13.508 -5.622  1.00 56.18  ? 254 PRO A CG  1 
ATOM   2076 C  CD  . PRO A 1 254 ? 35.200  -13.210 -4.262  1.00 54.43  ? 254 PRO A CD  1 
ATOM   2077 N  N   . LEU A 1 255 ? 34.543  -9.407  -4.772  1.00 57.31  ? 255 LEU A N   1 
ATOM   2078 C  CA  . LEU A 1 255 ? 33.697  -8.290  -5.195  1.00 57.17  ? 255 LEU A CA  1 
ATOM   2079 C  C   . LEU A 1 255 ? 34.174  -6.959  -4.603  1.00 55.62  ? 255 LEU A C   1 
ATOM   2080 O  O   . LEU A 1 255 ? 34.488  -6.882  -3.424  1.00 52.27  ? 255 LEU A O   1 
ATOM   2081 C  CB  . LEU A 1 255 ? 32.268  -8.601  -4.732  1.00 61.07  ? 255 LEU A CB  1 
ATOM   2082 C  CG  . LEU A 1 255 ? 31.167  -8.454  -5.779  1.00 64.52  ? 255 LEU A CG  1 
ATOM   2083 C  CD1 . LEU A 1 255 ? 31.439  -9.302  -7.013  1.00 62.80  ? 255 LEU A CD1 1 
ATOM   2084 C  CD2 . LEU A 1 255 ? 29.827  -8.841  -5.183  1.00 67.98  ? 255 LEU A CD2 1 
ATOM   2085 N  N   . ASP A 1 256 ? 34.155  -5.891  -5.411  1.00 56.68  ? 256 ASP A N   1 
ATOM   2086 C  CA  . ASP A 1 256 ? 34.500  -4.553  -4.940  1.00 59.87  ? 256 ASP A CA  1 
ATOM   2087 C  C   . ASP A 1 256 ? 33.307  -3.938  -4.191  1.00 58.33  ? 256 ASP A C   1 
ATOM   2088 O  O   . ASP A 1 256 ? 32.224  -4.519  -4.131  1.00 60.50  ? 256 ASP A O   1 
ATOM   2089 C  CB  . ASP A 1 256 ? 35.015  -3.687  -6.101  1.00 67.23  ? 256 ASP A CB  1 
ATOM   2090 C  CG  . ASP A 1 256 ? 33.993  -3.359  -7.182  1.00 76.35  ? 256 ASP A CG  1 
ATOM   2091 O  OD1 . ASP A 1 256 ? 33.264  -4.284  -7.610  1.00 78.28  ? 256 ASP A OD1 1 
ATOM   2092 O  OD2 . ASP A 1 256 ? 33.954  -2.183  -7.613  1.00 77.22  ? 256 ASP A OD2 1 
ATOM   2093 N  N   . GLU A 1 257 ? 33.524  -2.760  -3.594  1.00 52.47  ? 257 GLU A N   1 
ATOM   2094 C  CA  . GLU A 1 257 ? 32.493  -2.017  -2.890  1.00 51.86  ? 257 GLU A CA  1 
ATOM   2095 C  C   . GLU A 1 257 ? 31.188  -1.956  -3.690  1.00 52.31  ? 257 GLU A C   1 
ATOM   2096 O  O   . GLU A 1 257 ? 30.112  -2.149  -3.120  1.00 44.31  ? 257 GLU A O   1 
ATOM   2097 C  CB  . GLU A 1 257 ? 32.962  -0.589  -2.605  1.00 57.11  ? 257 GLU A CB  1 
ATOM   2098 C  CG  . GLU A 1 257 ? 31.976  0.184   -1.744  1.00 63.21  ? 257 GLU A CG  1 
ATOM   2099 C  CD  . GLU A 1 257 ? 32.289  1.653   -1.560  1.00 68.17  ? 257 GLU A CD  1 
ATOM   2100 O  OE1 . GLU A 1 257 ? 31.409  2.383   -1.059  1.00 59.86  ? 257 GLU A OE1 1 
ATOM   2101 O  OE2 . GLU A 1 257 ? 33.426  2.053   -1.894  1.00 81.60  ? 257 GLU A OE2 1 
ATOM   2102 N  N   . ASP A 1 258 ? 31.289  -1.611  -4.984  1.00 51.47  ? 258 ASP A N   1 
ATOM   2103 C  CA  . ASP A 1 258 ? 30.121  -1.417  -5.839  1.00 53.12  ? 258 ASP A CA  1 
ATOM   2104 C  C   . ASP A 1 258 ? 29.339  -2.726  -5.974  1.00 51.23  ? 258 ASP A C   1 
ATOM   2105 O  O   . ASP A 1 258 ? 28.116  -2.712  -5.942  1.00 49.94  ? 258 ASP A O   1 
ATOM   2106 C  CB  . ASP A 1 258 ? 30.499  -0.872  -7.221  1.00 56.19  ? 258 ASP A CB  1 
ATOM   2107 C  CG  . ASP A 1 258 ? 30.800  0.621   -7.301  1.00 62.33  ? 258 ASP A CG  1 
ATOM   2108 O  OD1 . ASP A 1 258 ? 30.531  1.350   -6.317  1.00 56.99  ? 258 ASP A OD1 1 
ATOM   2109 O  OD2 . ASP A 1 258 ? 31.307  1.052   -8.372  1.00 72.67  ? 258 ASP A OD2 1 
ATOM   2110 N  N   . GLY A 1 259 ? 30.046  -3.856  -6.106  1.00 48.79  ? 259 GLY A N   1 
ATOM   2111 C  CA  . GLY A 1 259 ? 29.418  -5.153  -6.318  1.00 45.49  ? 259 GLY A CA  1 
ATOM   2112 C  C   . GLY A 1 259 ? 28.621  -5.596  -5.097  1.00 47.57  ? 259 GLY A C   1 
ATOM   2113 O  O   . GLY A 1 259 ? 27.462  -5.961  -5.219  1.00 49.78  ? 259 GLY A O   1 
ATOM   2114 N  N   . ARG A 1 260 ? 29.256  -5.524  -3.923  1.00 48.93  ? 260 ARG A N   1 
ATOM   2115 C  CA  . ARG A 1 260 ? 28.640  -5.845  -2.644  1.00 47.28  ? 260 ARG A CA  1 
ATOM   2116 C  C   . ARG A 1 260 ? 27.339  -5.057  -2.461  1.00 48.53  ? 260 ARG A C   1 
ATOM   2117 O  O   . ARG A 1 260 ? 26.311  -5.634  -2.104  1.00 51.00  ? 260 ARG A O   1 
ATOM   2118 C  CB  . ARG A 1 260 ? 29.618  -5.546  -1.501  1.00 47.73  ? 260 ARG A CB  1 
ATOM   2119 C  CG  . ARG A 1 260 ? 30.722  -6.586  -1.318  1.00 51.33  ? 260 ARG A CG  1 
ATOM   2120 C  CD  . ARG A 1 260 ? 31.408  -6.492  0.034   1.00 52.60  ? 260 ARG A CD  1 
ATOM   2121 N  NE  . ARG A 1 260 ? 32.225  -5.291  0.187   1.00 53.71  ? 260 ARG A NE  1 
ATOM   2122 C  CZ  . ARG A 1 260 ? 33.465  -5.157  -0.280  1.00 54.28  ? 260 ARG A CZ  1 
ATOM   2123 N  NH1 . ARG A 1 260 ? 34.043  -6.156  -0.925  1.00 54.93  ? 260 ARG A NH1 1 
ATOM   2124 N  NH2 . ARG A 1 260 ? 34.129  -4.027  -0.098  1.00 51.18  ? 260 ARG A NH2 1 
ATOM   2125 N  N   . SER A 1 261 ? 27.408  -3.737  -2.693  1.00 42.62  ? 261 SER A N   1 
ATOM   2126 C  CA  . SER A 1 261 ? 26.275  -2.834  -2.535  1.00 43.88  ? 261 SER A CA  1 
ATOM   2127 C  C   . SER A 1 261 ? 25.104  -3.304  -3.397  1.00 47.51  ? 261 SER A C   1 
ATOM   2128 O  O   . SER A 1 261 ? 23.995  -3.467  -2.896  1.00 48.60  ? 261 SER A O   1 
ATOM   2129 C  CB  . SER A 1 261 ? 26.659  -1.417  -2.857  1.00 42.66  ? 261 SER A CB  1 
ATOM   2130 O  OG  . SER A 1 261 ? 25.545  -0.710  -3.351  1.00 41.08  ? 261 SER A OG  1 
ATOM   2131 N  N   . LEU A 1 262 ? 25.378  -3.568  -4.678  1.00 42.81  ? 262 LEU A N   1 
ATOM   2132 C  CA  . LEU A 1 262 ? 24.369  -4.111  -5.566  1.00 45.16  ? 262 LEU A CA  1 
ATOM   2133 C  C   . LEU A 1 262 ? 23.884  -5.465  -5.052  1.00 45.35  ? 262 LEU A C   1 
ATOM   2134 O  O   . LEU A 1 262 ? 22.676  -5.727  -5.025  1.00 45.14  ? 262 LEU A O   1 
ATOM   2135 C  CB  . LEU A 1 262 ? 24.920  -4.256  -6.988  1.00 48.34  ? 262 LEU A CB  1 
ATOM   2136 C  CG  . LEU A 1 262 ? 23.999  -5.001  -7.955  1.00 45.30  ? 262 LEU A CG  1 
ATOM   2137 C  CD1 . LEU A 1 262 ? 22.700  -4.232  -8.134  1.00 42.88  ? 262 LEU A CD1 1 
ATOM   2138 C  CD2 . LEU A 1 262 ? 24.679  -5.226  -9.298  1.00 47.17  ? 262 LEU A CD2 1 
ATOM   2139 N  N   . LEU A 1 263 ? 24.807  -6.365  -4.709  1.00 39.27  ? 263 LEU A N   1 
ATOM   2140 C  CA  . LEU A 1 263 ? 24.358  -7.703  -4.367  1.00 39.62  ? 263 LEU A CA  1 
ATOM   2141 C  C   . LEU A 1 263 ? 23.422  -7.636  -3.150  1.00 42.60  ? 263 LEU A C   1 
ATOM   2142 O  O   . LEU A 1 263 ? 22.401  -8.303  -3.139  1.00 43.82  ? 263 LEU A O   1 
ATOM   2143 C  CB  . LEU A 1 263 ? 25.559  -8.616  -4.125  1.00 37.10  ? 263 LEU A CB  1 
ATOM   2144 C  CG  . LEU A 1 263 ? 25.191  -10.011 -3.636  1.00 38.16  ? 263 LEU A CG  1 
ATOM   2145 C  CD1 . LEU A 1 263 ? 24.416  -10.768 -4.704  1.00 40.08  ? 263 LEU A CD1 1 
ATOM   2146 C  CD2 . LEU A 1 263 ? 26.435  -10.777 -3.236  1.00 38.93  ? 263 LEU A CD2 1 
ATOM   2147 N  N   . SER A 1 264 ? 23.733  -6.795  -2.150  1.00 44.43  ? 264 SER A N   1 
ATOM   2148 C  CA  . SER A 1 264 ? 22.935  -6.704  -0.928  1.00 46.43  ? 264 SER A CA  1 
ATOM   2149 C  C   . SER A 1 264 ? 21.547  -6.106  -1.205  1.00 47.45  ? 264 SER A C   1 
ATOM   2150 O  O   . SER A 1 264 ? 20.575  -6.447  -0.529  1.00 48.99  ? 264 SER A O   1 
ATOM   2151 C  CB  . SER A 1 264 ? 23.678  -5.944  0.171   1.00 46.21  ? 264 SER A CB  1 
ATOM   2152 O  OG  . SER A 1 264 ? 23.512  -4.545  0.041   1.00 45.15  ? 264 SER A OG  1 
ATOM   2153 N  N   . GLN A 1 265 ? 21.470  -5.212  -2.200  1.00 42.95  ? 265 GLN A N   1 
ATOM   2154 C  CA  . GLN A 1 265 ? 20.228  -4.625  -2.680  1.00 41.17  ? 265 GLN A CA  1 
ATOM   2155 C  C   . GLN A 1 265 ? 19.352  -5.657  -3.402  1.00 40.78  ? 265 GLN A C   1 
ATOM   2156 O  O   . GLN A 1 265 ? 18.123  -5.531  -3.397  1.00 40.24  ? 265 GLN A O   1 
ATOM   2157 C  CB  . GLN A 1 265 ? 20.537  -3.414  -3.564  1.00 41.66  ? 265 GLN A CB  1 
ATOM   2158 C  CG  . GLN A 1 265 ? 20.909  -2.181  -2.746  1.00 43.97  ? 265 GLN A CG  1 
ATOM   2159 C  CD  . GLN A 1 265 ? 21.190  -1.001  -3.639  1.00 47.92  ? 265 GLN A CD  1 
ATOM   2160 O  OE1 . GLN A 1 265 ? 20.279  -0.390  -4.195  1.00 53.16  ? 265 GLN A OE1 1 
ATOM   2161 N  NE2 . GLN A 1 265 ? 22.466  -0.690  -3.805  1.00 51.14  ? 265 GLN A NE2 1 
ATOM   2162 N  N   . MET A 1 266 ? 19.962  -6.667  -4.035  1.00 38.02  ? 266 MET A N   1 
ATOM   2163 C  CA  . MET A 1 266 ? 19.192  -7.684  -4.729  1.00 37.64  ? 266 MET A CA  1 
ATOM   2164 C  C   . MET A 1 266 ? 18.691  -8.707  -3.712  1.00 40.01  ? 266 MET A C   1 
ATOM   2165 O  O   . MET A 1 266 ? 17.737  -9.427  -4.003  1.00 38.83  ? 266 MET A O   1 
ATOM   2166 C  CB  . MET A 1 266 ? 20.007  -8.376  -5.830  1.00 38.99  ? 266 MET A CB  1 
ATOM   2167 C  CG  . MET A 1 266 ? 20.425  -7.417  -6.938  1.00 43.03  ? 266 MET A CG  1 
ATOM   2168 S  SD  . MET A 1 266 ? 21.528  -8.135  -8.186  1.00 48.39  ? 266 MET A SD  1 
ATOM   2169 C  CE  . MET A 1 266 ? 20.422  -9.321  -8.953  1.00 51.35  ? 266 MET A CE  1 
ATOM   2170 N  N   . LEU A 1 267 ? 19.311  -8.742  -2.520  1.00 41.11  ? 267 LEU A N   1 
ATOM   2171 C  CA  . LEU A 1 267 ? 19.001  -9.752  -1.517  1.00 42.15  ? 267 LEU A CA  1 
ATOM   2172 C  C   . LEU A 1 267 ? 18.339  -9.163  -0.259  1.00 40.31  ? 267 LEU A C   1 
ATOM   2173 O  O   . LEU A 1 267 ? 18.206  -9.881  0.726   1.00 37.22  ? 267 LEU A O   1 
ATOM   2174 C  CB  . LEU A 1 267 ? 20.289  -10.519 -1.184  1.00 44.69  ? 267 LEU A CB  1 
ATOM   2175 C  CG  . LEU A 1 267 ? 20.826  -11.462 -2.266  1.00 44.29  ? 267 LEU A CG  1 
ATOM   2176 C  CD1 . LEU A 1 267 ? 22.006  -12.256 -1.737  1.00 45.52  ? 267 LEU A CD1 1 
ATOM   2177 C  CD2 . LEU A 1 267 ? 19.759  -12.427 -2.752  1.00 45.13  ? 267 LEU A CD2 1 
ATOM   2178 N  N   . HIS A 1 268 ? 17.825  -7.923  -0.305  1.00 39.04  ? 268 HIS A N   1 
ATOM   2179 C  CA  . HIS A 1 268 ? 16.951  -7.413  0.755   1.00 46.49  ? 268 HIS A CA  1 
ATOM   2180 C  C   . HIS A 1 268 ? 15.821  -8.396  1.050   1.00 43.61  ? 268 HIS A C   1 
ATOM   2181 O  O   . HIS A 1 268 ? 15.228  -8.954  0.141   1.00 45.43  ? 268 HIS A O   1 
ATOM   2182 C  CB  . HIS A 1 268 ? 16.310  -6.069  0.397   1.00 52.29  ? 268 HIS A CB  1 
ATOM   2183 C  CG  . HIS A 1 268 ? 17.042  -4.870  0.888   1.00 64.81  ? 268 HIS A CG  1 
ATOM   2184 N  ND1 . HIS A 1 268 ? 17.915  -4.160  0.089   1.00 74.65  ? 268 HIS A ND1 1 
ATOM   2185 C  CD2 . HIS A 1 268 ? 17.021  -4.247  2.070   1.00 73.36  ? 268 HIS A CD2 1 
ATOM   2186 C  CE1 . HIS A 1 268 ? 18.416  -3.145  0.773   1.00 76.08  ? 268 HIS A CE1 1 
ATOM   2187 N  NE2 . HIS A 1 268 ? 17.883  -3.177  1.978   1.00 86.00  ? 268 HIS A NE2 1 
ATOM   2188 N  N   . TYR A 1 269 ? 15.503  -8.578  2.332   1.00 46.10  ? 269 TYR A N   1 
ATOM   2189 C  CA  . TYR A 1 269 ? 14.407  -9.443  2.758   1.00 43.16  ? 269 TYR A CA  1 
ATOM   2190 C  C   . TYR A 1 269 ? 13.050  -8.866  2.349   1.00 44.09  ? 269 TYR A C   1 
ATOM   2191 O  O   . TYR A 1 269 ? 12.207  -9.589  1.806   1.00 46.22  ? 269 TYR A O   1 
ATOM   2192 C  CB  . TYR A 1 269 ? 14.446  -9.627  4.276   1.00 42.24  ? 269 TYR A CB  1 
ATOM   2193 C  CG  . TYR A 1 269 ? 15.400  -10.680 4.764   1.00 42.30  ? 269 TYR A CG  1 
ATOM   2194 C  CD1 . TYR A 1 269 ? 15.258  -11.990 4.349   1.00 42.49  ? 269 TYR A CD1 1 
ATOM   2195 C  CD2 . TYR A 1 269 ? 16.420  -10.380 5.655   1.00 43.04  ? 269 TYR A CD2 1 
ATOM   2196 C  CE1 . TYR A 1 269 ? 16.114  -12.980 4.796   1.00 44.99  ? 269 TYR A CE1 1 
ATOM   2197 C  CE2 . TYR A 1 269 ? 17.284  -11.360 6.117   1.00 41.08  ? 269 TYR A CE2 1 
ATOM   2198 C  CZ  . TYR A 1 269 ? 17.121  -12.664 5.687   1.00 42.99  ? 269 TYR A CZ  1 
ATOM   2199 O  OH  . TYR A 1 269 ? 17.939  -13.657 6.126   1.00 49.85  ? 269 TYR A OH  1 
ATOM   2200 N  N   . ASP A 1 270 ? 12.837  -7.576  2.653   1.00 42.64  ? 270 ASP A N   1 
ATOM   2201 C  CA  . ASP A 1 270 ? 11.566  -6.913  2.396   1.00 45.11  ? 270 ASP A CA  1 
ATOM   2202 C  C   . ASP A 1 270 ? 11.474  -6.698  0.888   1.00 44.78  ? 270 ASP A C   1 
ATOM   2203 O  O   . ASP A 1 270 ? 12.276  -5.939  0.347   1.00 43.42  ? 270 ASP A O   1 
ATOM   2204 C  CB  . ASP A 1 270 ? 11.412  -5.600  3.184   1.00 43.92  ? 270 ASP A CB  1 
ATOM   2205 C  CG  . ASP A 1 270 ? 10.048  -4.932  3.023   1.00 48.24  ? 270 ASP A CG  1 
ATOM   2206 O  OD1 . ASP A 1 270 ? 9.282   -5.389  2.154   1.00 47.63  ? 270 ASP A OD1 1 
ATOM   2207 O  OD2 . ASP A 1 270 ? 9.750   -3.951  3.759   1.00 49.83  ? 270 ASP A OD2 1 
ATOM   2208 N  N   . PRO A 1 271 ? 10.510  -7.327  0.165   1.00 41.21  ? 271 PRO A N   1 
ATOM   2209 C  CA  . PRO A 1 271 ? 10.401  -7.143  -1.280  1.00 40.01  ? 271 PRO A CA  1 
ATOM   2210 C  C   . PRO A 1 271 ? 10.256  -5.695  -1.750  1.00 43.29  ? 271 PRO A C   1 
ATOM   2211 O  O   . PRO A 1 271 ? 10.635  -5.403  -2.875  1.00 48.03  ? 271 PRO A O   1 
ATOM   2212 C  CB  . PRO A 1 271 ? 9.147   -7.936  -1.665  1.00 37.12  ? 271 PRO A CB  1 
ATOM   2213 C  CG  . PRO A 1 271 ? 9.002   -8.957  -0.565  1.00 39.49  ? 271 PRO A CG  1 
ATOM   2214 C  CD  . PRO A 1 271 ? 9.465   -8.230  0.679   1.00 39.28  ? 271 PRO A CD  1 
ATOM   2215 N  N   . ASN A 1 272 ? 9.745   -4.799  -0.893  1.00 44.11  ? 272 ASN A N   1 
ATOM   2216 C  CA  . ASN A 1 272 ? 9.616   -3.379  -1.209  1.00 51.89  ? 272 ASN A CA  1 
ATOM   2217 C  C   . ASN A 1 272 ? 10.967  -2.662  -1.257  1.00 47.44  ? 272 ASN A C   1 
ATOM   2218 O  O   . ASN A 1 272 ? 11.112  -1.682  -1.978  1.00 57.14  ? 272 ASN A O   1 
ATOM   2219 C  CB  . ASN A 1 272 ? 8.707   -2.647  -0.213  1.00 64.53  ? 272 ASN A CB  1 
ATOM   2220 C  CG  . ASN A 1 272 ? 7.264   -3.110  -0.258  1.00 71.47  ? 272 ASN A CG  1 
ATOM   2221 O  OD1 . ASN A 1 272 ? 6.857   -3.847  -1.158  1.00 68.18  ? 272 ASN A OD1 1 
ATOM   2222 N  ND2 . ASN A 1 272 ? 6.486   -2.686  0.725   1.00 76.51  ? 272 ASN A ND2 1 
ATOM   2223 N  N   . LYS A 1 273 ? 11.955  -3.113  -0.486  1.00 47.12  ? 273 LYS A N   1 
ATOM   2224 C  CA  . LYS A 1 273 ? 13.257  -2.453  -0.460  1.00 49.55  ? 273 LYS A CA  1 
ATOM   2225 C  C   . LYS A 1 273 ? 14.146  -2.994  -1.590  1.00 45.44  ? 273 LYS A C   1 
ATOM   2226 O  O   . LYS A 1 273 ? 15.097  -2.338  -2.003  1.00 43.54  ? 273 LYS A O   1 
ATOM   2227 C  CB  . LYS A 1 273 ? 13.902  -2.654  0.916   1.00 57.06  ? 273 LYS A CB  1 
ATOM   2228 C  CG  . LYS A 1 273 ? 12.981  -2.427  2.109   1.00 58.69  ? 273 LYS A CG  1 
ATOM   2229 C  CD  . LYS A 1 273 ? 13.135  -1.103  2.786   1.00 64.33  ? 273 LYS A CD  1 
ATOM   2230 C  CE  . LYS A 1 273 ? 12.255  -1.024  4.014   1.00 69.43  ? 273 LYS A CE  1 
ATOM   2231 N  NZ  . LYS A 1 273 ? 12.159  0.367   4.511   1.00 74.60  ? 273 LYS A NZ  1 
ATOM   2232 N  N   . ARG A 1 274 ? 13.804  -4.183  -2.103  1.00 39.58  ? 274 ARG A N   1 
ATOM   2233 C  CA  . ARG A 1 274 ? 14.656  -4.964  -2.989  1.00 40.31  ? 274 ARG A CA  1 
ATOM   2234 C  C   . ARG A 1 274 ? 14.696  -4.251  -4.344  1.00 42.31  ? 274 ARG A C   1 
ATOM   2235 O  O   . ARG A 1 274 ? 13.680  -3.726  -4.786  1.00 48.96  ? 274 ARG A O   1 
ATOM   2236 C  CB  . ARG A 1 274 ? 14.124  -6.407  -3.007  1.00 36.14  ? 274 ARG A CB  1 
ATOM   2237 C  CG  . ARG A 1 274 ? 15.083  -7.425  -3.601  1.00 35.98  ? 274 ARG A CG  1 
ATOM   2238 C  CD  . ARG A 1 274 ? 14.466  -8.808  -3.730  1.00 36.00  ? 274 ARG A CD  1 
ATOM   2239 N  NE  . ARG A 1 274 ? 14.133  -9.404  -2.450  1.00 38.01  ? 274 ARG A NE  1 
ATOM   2240 C  CZ  . ARG A 1 274 ? 13.218  -10.347 -2.250  1.00 40.26  ? 274 ARG A CZ  1 
ATOM   2241 N  NH1 . ARG A 1 274 ? 12.545  -10.870 -3.257  1.00 43.35  ? 274 ARG A NH1 1 
ATOM   2242 N  NH2 . ARG A 1 274 ? 12.948  -10.743 -1.019  1.00 44.69  ? 274 ARG A NH2 1 
ATOM   2243 N  N   . ILE A 1 275 ? 15.878  -4.179  -4.974  1.00 42.09  ? 275 ILE A N   1 
ATOM   2244 C  CA  . ILE A 1 275 ? 16.104  -3.331  -6.149  1.00 38.04  ? 275 ILE A CA  1 
ATOM   2245 C  C   . ILE A 1 275 ? 15.364  -3.924  -7.346  1.00 37.38  ? 275 ILE A C   1 
ATOM   2246 O  O   . ILE A 1 275 ? 15.217  -5.144  -7.428  1.00 40.50  ? 275 ILE A O   1 
ATOM   2247 C  CB  . ILE A 1 275 ? 17.620  -3.154  -6.424  1.00 38.14  ? 275 ILE A CB  1 
ATOM   2248 C  CG1 . ILE A 1 275 ? 17.903  -1.952  -7.327  1.00 40.62  ? 275 ILE A CG1 1 
ATOM   2249 C  CG2 . ILE A 1 275 ? 18.260  -4.423  -6.972  1.00 34.00  ? 275 ILE A CG2 1 
ATOM   2250 C  CD1 . ILE A 1 275 ? 19.338  -1.516  -7.339  1.00 43.42  ? 275 ILE A CD1 1 
ATOM   2251 N  N   . SER A 1 276 ? 14.866  -3.052  -8.239  1.00 37.74  ? 276 SER A N   1 
ATOM   2252 C  CA  . SER A 1 276 ? 14.255  -3.445  -9.507  1.00 39.79  ? 276 SER A CA  1 
ATOM   2253 C  C   . SER A 1 276 ? 15.356  -3.716  -10.536 1.00 41.39  ? 276 SER A C   1 
ATOM   2254 O  O   . SER A 1 276 ? 16.462  -3.194  -10.406 1.00 45.25  ? 276 SER A O   1 
ATOM   2255 C  CB  . SER A 1 276 ? 13.286  -2.377  -10.010 1.00 40.02  ? 276 SER A CB  1 
ATOM   2256 O  OG  . SER A 1 276 ? 13.971  -1.250  -10.537 1.00 44.29  ? 276 SER A OG  1 
ATOM   2257 N  N   . ALA A 1 277 ? 15.051  -4.524  -11.555 1.00 39.24  ? 277 ALA A N   1 
ATOM   2258 C  CA  . ALA A 1 277 ? 15.961  -4.775  -12.668 1.00 40.28  ? 277 ALA A CA  1 
ATOM   2259 C  C   . ALA A 1 277 ? 16.387  -3.461  -13.323 1.00 41.16  ? 277 ALA A C   1 
ATOM   2260 O  O   . ALA A 1 277 ? 17.557  -3.297  -13.643 1.00 41.76  ? 277 ALA A O   1 
ATOM   2261 C  CB  . ALA A 1 277 ? 15.314  -5.696  -13.676 1.00 39.58  ? 277 ALA A CB  1 
ATOM   2262 N  N   . LYS A 1 278 ? 15.440  -2.539  -13.520 1.00 40.08  ? 278 LYS A N   1 
ATOM   2263 C  CA  . LYS A 1 278 ? 15.692  -1.260  -14.170 1.00 45.26  ? 278 LYS A CA  1 
ATOM   2264 C  C   . LYS A 1 278 ? 16.615  -0.369  -13.310 1.00 44.56  ? 278 LYS A C   1 
ATOM   2265 O  O   . LYS A 1 278 ? 17.547  0.232   -13.840 1.00 44.51  ? 278 LYS A O   1 
ATOM   2266 C  CB  . LYS A 1 278 ? 14.337  -0.628  -14.522 1.00 55.93  ? 278 LYS A CB  1 
ATOM   2267 C  CG  . LYS A 1 278 ? 14.338  0.298   -15.734 1.00 69.12  ? 278 LYS A CG  1 
ATOM   2268 C  CD  . LYS A 1 278 ? 12.990  0.458   -16.439 1.00 79.23  ? 278 LYS A CD  1 
ATOM   2269 C  CE  . LYS A 1 278 ? 12.822  -0.470  -17.629 1.00 85.38  ? 278 LYS A CE  1 
ATOM   2270 N  NZ  . LYS A 1 278 ? 11.713  -0.064  -18.530 1.00 80.93  ? 278 LYS A NZ  1 
ATOM   2271 N  N   . ALA A 1 279 ? 16.385  -0.286  -11.987 1.00 45.95  ? 279 ALA A N   1 
ATOM   2272 C  CA  . ALA A 1 279 ? 17.202  0.537   -11.086 1.00 46.26  ? 279 ALA A CA  1 
ATOM   2273 C  C   . ALA A 1 279 ? 18.622  -0.012  -10.978 1.00 43.09  ? 279 ALA A C   1 
ATOM   2274 O  O   . ALA A 1 279 ? 19.569  0.750   -10.755 1.00 44.58  ? 279 ALA A O   1 
ATOM   2275 C  CB  . ALA A 1 279 ? 16.583  0.626   -9.708  1.00 44.26  ? 279 ALA A CB  1 
ATOM   2276 N  N   . ALA A 1 280 ? 18.732  -1.339  -11.118 1.00 36.24  ? 280 ALA A N   1 
ATOM   2277 C  CA  . ALA A 1 280 ? 19.978  -2.071  -10.976 1.00 37.89  ? 280 ALA A CA  1 
ATOM   2278 C  C   . ALA A 1 280 ? 20.902  -1.777  -12.153 1.00 39.33  ? 280 ALA A C   1 
ATOM   2279 O  O   . ALA A 1 280 ? 22.114  -1.705  -11.951 1.00 43.35  ? 280 ALA A O   1 
ATOM   2280 C  CB  . ALA A 1 280 ? 19.710  -3.552  -10.847 1.00 37.47  ? 280 ALA A CB  1 
ATOM   2281 N  N   . LEU A 1 281 ? 20.316  -1.598  -13.349 1.00 39.49  ? 281 LEU A N   1 
ATOM   2282 C  CA  . LEU A 1 281 ? 21.055  -1.246  -14.550 1.00 41.10  ? 281 LEU A CA  1 
ATOM   2283 C  C   . LEU A 1 281 ? 21.760  0.098   -14.363 1.00 46.66  ? 281 LEU A C   1 
ATOM   2284 O  O   . LEU A 1 281 ? 22.874  0.267   -14.851 1.00 51.54  ? 281 LEU A O   1 
ATOM   2285 C  CB  . LEU A 1 281 ? 20.104  -1.206  -15.747 1.00 41.84  ? 281 LEU A CB  1 
ATOM   2286 C  CG  . LEU A 1 281 ? 19.568  -2.553  -16.228 1.00 42.40  ? 281 LEU A CG  1 
ATOM   2287 C  CD1 . LEU A 1 281 ? 18.480  -2.353  -17.287 1.00 40.78  ? 281 LEU A CD1 1 
ATOM   2288 C  CD2 . LEU A 1 281 ? 20.681  -3.444  -16.757 1.00 42.69  ? 281 LEU A CD2 1 
ATOM   2289 N  N   . ALA A 1 282 ? 21.141  1.038   -13.636 1.00 45.48  ? 282 ALA A N   1 
ATOM   2290 C  CA  . ALA A 1 282 ? 21.755  2.339   -13.361 1.00 46.35  ? 282 ALA A CA  1 
ATOM   2291 C  C   . ALA A 1 282 ? 22.719  2.323   -12.158 1.00 43.68  ? 282 ALA A C   1 
ATOM   2292 O  O   . ALA A 1 282 ? 23.145  3.384   -11.712 1.00 48.75  ? 282 ALA A O   1 
ATOM   2293 C  CB  . ALA A 1 282 ? 20.663  3.365   -13.150 1.00 45.05  ? 282 ALA A CB  1 
ATOM   2294 N  N   . HIS A 1 283 ? 23.058  1.148   -11.605 1.00 40.15  ? 283 HIS A N   1 
ATOM   2295 C  CA  . HIS A 1 283 ? 23.924  1.060   -10.427 1.00 45.10  ? 283 HIS A CA  1 
ATOM   2296 C  C   . HIS A 1 283 ? 25.382  1.302   -10.821 1.00 44.30  ? 283 HIS A C   1 
ATOM   2297 O  O   . HIS A 1 283 ? 25.824  0.841   -11.867 1.00 40.66  ? 283 HIS A O   1 
ATOM   2298 C  CB  . HIS A 1 283 ? 23.756  -0.301  -9.738  1.00 44.77  ? 283 HIS A CB  1 
ATOM   2299 C  CG  . HIS A 1 283 ? 24.459  -0.460  -8.429  1.00 44.47  ? 283 HIS A CG  1 
ATOM   2300 N  ND1 . HIS A 1 283 ? 25.797  -0.758  -8.353  1.00 42.31  ? 283 HIS A ND1 1 
ATOM   2301 C  CD2 . HIS A 1 283 ? 24.016  -0.443  -7.153  1.00 45.62  ? 283 HIS A CD2 1 
ATOM   2302 C  CE1 . HIS A 1 283 ? 26.151  -0.895  -7.083  1.00 40.66  ? 283 HIS A CE1 1 
ATOM   2303 N  NE2 . HIS A 1 283 ? 25.091  -0.696  -6.330  1.00 42.69  ? 283 HIS A NE2 1 
ATOM   2304 N  N   . PRO A 1 284 ? 26.170  2.049   -10.019 1.00 47.16  ? 284 PRO A N   1 
ATOM   2305 C  CA  . PRO A 1 284 ? 27.582  2.322   -10.333 1.00 51.78  ? 284 PRO A CA  1 
ATOM   2306 C  C   . PRO A 1 284 ? 28.469  1.129   -10.713 1.00 47.51  ? 284 PRO A C   1 
ATOM   2307 O  O   . PRO A 1 284 ? 29.402  1.279   -11.491 1.00 52.69  ? 284 PRO A O   1 
ATOM   2308 C  CB  . PRO A 1 284 ? 28.138  2.921   -9.028  1.00 51.80  ? 284 PRO A CB  1 
ATOM   2309 C  CG  . PRO A 1 284 ? 26.930  3.511   -8.327  1.00 53.65  ? 284 PRO A CG  1 
ATOM   2310 C  CD  . PRO A 1 284 ? 25.737  2.686   -8.771  1.00 48.70  ? 284 PRO A CD  1 
ATOM   2311 N  N   . PHE A 1 285 ? 28.171  -0.053  -10.165 1.00 43.29  ? 285 PHE A N   1 
ATOM   2312 C  CA  . PHE A 1 285 ? 28.798  -1.311  -10.552 1.00 45.72  ? 285 PHE A CA  1 
ATOM   2313 C  C   . PHE A 1 285 ? 28.955  -1.516  -12.064 1.00 46.54  ? 285 PHE A C   1 
ATOM   2314 O  O   . PHE A 1 285 ? 29.850  -2.250  -12.473 1.00 51.64  ? 285 PHE A O   1 
ATOM   2315 C  CB  . PHE A 1 285 ? 27.976  -2.491  -10.041 1.00 44.31  ? 285 PHE A CB  1 
ATOM   2316 C  CG  . PHE A 1 285 ? 28.621  -3.837  -10.244 1.00 44.58  ? 285 PHE A CG  1 
ATOM   2317 C  CD1 . PHE A 1 285 ? 29.889  -4.091  -9.747  1.00 44.02  ? 285 PHE A CD1 1 
ATOM   2318 C  CD2 . PHE A 1 285 ? 27.953  -4.850  -10.907 1.00 46.18  ? 285 PHE A CD2 1 
ATOM   2319 C  CE1 . PHE A 1 285 ? 30.463  -5.342  -9.887  1.00 47.15  ? 285 PHE A CE1 1 
ATOM   2320 C  CE2 . PHE A 1 285 ? 28.532  -6.099  -11.060 1.00 48.93  ? 285 PHE A CE2 1 
ATOM   2321 C  CZ  . PHE A 1 285 ? 29.785  -6.342  -10.546 1.00 49.62  ? 285 PHE A CZ  1 
ATOM   2322 N  N   . PHE A 1 286 ? 28.081  -0.907  -12.876 1.00 43.83  ? 286 PHE A N   1 
ATOM   2323 C  CA  . PHE A 1 286 ? 28.042  -1.089  -14.324 1.00 44.58  ? 286 PHE A CA  1 
ATOM   2324 C  C   . PHE A 1 286 ? 28.519  0.158   -15.090 1.00 49.19  ? 286 PHE A C   1 
ATOM   2325 O  O   . PHE A 1 286 ? 28.292  0.254   -16.301 1.00 46.83  ? 286 PHE A O   1 
ATOM   2326 C  CB  . PHE A 1 286 ? 26.601  -1.397  -14.760 1.00 41.60  ? 286 PHE A CB  1 
ATOM   2327 C  CG  . PHE A 1 286 ? 26.025  -2.685  -14.235 1.00 38.38  ? 286 PHE A CG  1 
ATOM   2328 C  CD1 . PHE A 1 286 ? 26.551  -3.902  -14.626 1.00 39.02  ? 286 PHE A CD1 1 
ATOM   2329 C  CD2 . PHE A 1 286 ? 24.937  -2.685  -13.378 1.00 37.34  ? 286 PHE A CD2 1 
ATOM   2330 C  CE1 . PHE A 1 286 ? 26.031  -5.087  -14.129 1.00 36.67  ? 286 PHE A CE1 1 
ATOM   2331 C  CE2 . PHE A 1 286 ? 24.410  -3.872  -12.898 1.00 35.83  ? 286 PHE A CE2 1 
ATOM   2332 C  CZ  . PHE A 1 286 ? 24.961  -5.070  -13.271 1.00 34.38  ? 286 PHE A CZ  1 
ATOM   2333 N  N   . GLN A 1 287 ? 29.182  1.119   -14.424 1.00 54.82  ? 287 GLN A N   1 
ATOM   2334 C  CA  . GLN A 1 287 ? 29.646  2.326   -15.110 1.00 64.12  ? 287 GLN A CA  1 
ATOM   2335 C  C   . GLN A 1 287 ? 30.688  1.971   -16.182 1.00 65.52  ? 287 GLN A C   1 
ATOM   2336 O  O   . GLN A 1 287 ? 30.814  2.711   -17.157 1.00 68.62  ? 287 GLN A O   1 
ATOM   2337 C  CB  . GLN A 1 287 ? 30.150  3.391   -14.123 1.00 68.84  ? 287 GLN A CB  1 
ATOM   2338 C  CG  . GLN A 1 287 ? 31.386  3.001   -13.321 1.00 77.94  ? 287 GLN A CG  1 
ATOM   2339 C  CD  . GLN A 1 287 ? 31.447  3.753   -12.009 1.00 85.54  ? 287 GLN A CD  1 
ATOM   2340 O  OE1 . GLN A 1 287 ? 31.053  4.917   -11.932 1.00 88.99  ? 287 GLN A OE1 1 
ATOM   2341 N  NE2 . GLN A 1 287 ? 31.898  3.083   -10.956 1.00 76.57  ? 287 GLN A NE2 1 
ATOM   2342 N  N   . ASP A 1 288 ? 31.390  0.832   -16.030 1.00 60.74  ? 288 ASP A N   1 
ATOM   2343 C  CA  . ASP A 1 288 ? 32.442  0.409   -16.953 1.00 67.27  ? 288 ASP A CA  1 
ATOM   2344 C  C   . ASP A 1 288 ? 32.139  -0.954  -17.590 1.00 66.60  ? 288 ASP A C   1 
ATOM   2345 O  O   . ASP A 1 288 ? 33.067  -1.694  -17.914 1.00 71.32  ? 288 ASP A O   1 
ATOM   2346 C  CB  . ASP A 1 288 ? 33.802  0.330   -16.240 1.00 73.95  ? 288 ASP A CB  1 
ATOM   2347 C  CG  . ASP A 1 288 ? 33.829  -0.569  -15.007 1.00 80.10  ? 288 ASP A CG  1 
ATOM   2348 O  OD1 . ASP A 1 288 ? 32.747  -0.778  -14.405 1.00 79.63  ? 288 ASP A OD1 1 
ATOM   2349 O  OD2 . ASP A 1 288 ? 34.933  -1.072  -14.659 1.00 73.80  ? 288 ASP A OD2 1 
ATOM   2350 N  N   . VAL A 1 289 ? 30.856  -1.302  -17.780 1.00 60.94  ? 289 VAL A N   1 
ATOM   2351 C  CA  . VAL A 1 289 ? 30.491  -2.605  -18.339 1.00 54.89  ? 289 VAL A CA  1 
ATOM   2352 C  C   . VAL A 1 289 ? 30.812  -2.592  -19.834 1.00 51.83  ? 289 VAL A C   1 
ATOM   2353 O  O   . VAL A 1 289 ? 30.735  -1.534  -20.443 1.00 53.58  ? 289 VAL A O   1 
ATOM   2354 C  CB  . VAL A 1 289 ? 29.012  -2.977  -18.070 1.00 50.42  ? 289 VAL A CB  1 
ATOM   2355 C  CG1 . VAL A 1 289 ? 28.027  -2.141  -18.871 1.00 49.26  ? 289 VAL A CG1 1 
ATOM   2356 C  CG2 . VAL A 1 289 ? 28.750  -4.463  -18.298 1.00 48.33  ? 289 VAL A CG2 1 
ATOM   2357 N  N   . THR A 1 290 ? 31.162  -3.756  -20.408 1.00 52.56  ? 290 THR A N   1 
ATOM   2358 C  CA  . THR A 1 290 ? 31.505  -3.900  -21.823 1.00 60.32  ? 290 THR A CA  1 
ATOM   2359 C  C   . THR A 1 290 ? 30.444  -4.721  -22.565 1.00 67.98  ? 290 THR A C   1 
ATOM   2360 O  O   . THR A 1 290 ? 29.686  -5.461  -21.943 1.00 72.74  ? 290 THR A O   1 
ATOM   2361 C  CB  . THR A 1 290 ? 32.862  -4.596  -22.020 1.00 61.97  ? 290 THR A CB  1 
ATOM   2362 O  OG1 . THR A 1 290 ? 32.816  -5.845  -21.324 1.00 60.82  ? 290 THR A OG1 1 
ATOM   2363 C  CG2 . THR A 1 290 ? 34.037  -3.765  -21.545 1.00 62.93  ? 290 THR A CG2 1 
ATOM   2364 N  N   . LYS A 1 291 ? 30.455  -4.629  -23.906 1.00 74.37  ? 291 LYS A N   1 
ATOM   2365 C  CA  . LYS A 1 291 ? 29.447  -5.229  -24.774 1.00 79.84  ? 291 LYS A CA  1 
ATOM   2366 C  C   . LYS A 1 291 ? 29.627  -6.747  -24.830 1.00 80.25  ? 291 LYS A C   1 
ATOM   2367 O  O   . LYS A 1 291 ? 30.670  -7.267  -24.433 1.00 78.10  ? 291 LYS A O   1 
ATOM   2368 C  CB  . LYS A 1 291 ? 29.519  -4.612  -26.178 1.00 87.65  ? 291 LYS A CB  1 
ATOM   2369 C  CG  . LYS A 1 291 ? 29.258  -3.108  -26.263 1.00 95.08  ? 291 LYS A CG  1 
ATOM   2370 C  CD  . LYS A 1 291 ? 28.021  -2.618  -25.503 1.00 104.47 ? 291 LYS A CD  1 
ATOM   2371 C  CE  . LYS A 1 291 ? 28.327  -2.042  -24.130 1.00 106.95 ? 291 LYS A CE  1 
ATOM   2372 N  NZ  . LYS A 1 291 ? 27.116  -1.872  -23.284 1.00 99.99  ? 291 LYS A NZ  1 
ATOM   2373 N  N   . PRO A 1 292 ? 28.597  -7.510  -25.279 1.00 82.48  ? 292 PRO A N   1 
ATOM   2374 C  CA  . PRO A 1 292 ? 28.774  -8.925  -25.634 1.00 86.99  ? 292 PRO A CA  1 
ATOM   2375 C  C   . PRO A 1 292 ? 29.782  -9.098  -26.780 1.00 91.11  ? 292 PRO A C   1 
ATOM   2376 O  O   . PRO A 1 292 ? 29.706  -8.364  -27.766 1.00 91.26  ? 292 PRO A O   1 
ATOM   2377 C  CB  . PRO A 1 292 ? 27.361  -9.397  -26.037 1.00 81.50  ? 292 PRO A CB  1 
ATOM   2378 C  CG  . PRO A 1 292 ? 26.413  -8.359  -25.455 1.00 79.94  ? 292 PRO A CG  1 
ATOM   2379 C  CD  . PRO A 1 292 ? 27.199  -7.066  -25.402 1.00 80.17  ? 292 PRO A CD  1 
ATOM   2380 N  N   . VAL A 1 293 ? 30.742  -10.034 -26.621 1.00 92.30  ? 293 VAL A N   1 
ATOM   2381 C  CA  . VAL A 1 293 ? 31.806  -10.317 -27.590 1.00 94.44  ? 293 VAL A CA  1 
ATOM   2382 C  C   . VAL A 1 293 ? 32.090  -11.824 -27.569 1.00 92.93  ? 293 VAL A C   1 
ATOM   2383 O  O   . VAL A 1 293 ? 32.104  -12.417 -26.494 1.00 98.15  ? 293 VAL A O   1 
ATOM   2384 C  CB  . VAL A 1 293 ? 33.087  -9.499  -27.291 1.00 95.99  ? 293 VAL A CB  1 
ATOM   2385 C  CG1 . VAL A 1 293 ? 34.237  -9.817  -28.246 1.00 98.08  ? 293 VAL A CG1 1 
ATOM   2386 C  CG2 . VAL A 1 293 ? 32.826  -7.998  -27.287 1.00 96.49  ? 293 VAL A CG2 1 
ATOM   2387 N  N   . PRO A 1 294 ? 32.306  -12.505 -28.726 1.00 93.76  ? 294 PRO A N   1 
ATOM   2388 C  CA  . PRO A 1 294 ? 32.478  -13.968 -28.754 1.00 93.08  ? 294 PRO A CA  1 
ATOM   2389 C  C   . PRO A 1 294 ? 33.552  -14.625 -27.862 1.00 87.84  ? 294 PRO A C   1 
ATOM   2390 O  O   . PRO A 1 294 ? 34.497  -13.974 -27.443 1.00 81.11  ? 294 PRO A O   1 
ATOM   2391 C  CB  . PRO A 1 294 ? 32.791  -14.282 -30.234 1.00 90.86  ? 294 PRO A CB  1 
ATOM   2392 C  CG  . PRO A 1 294 ? 33.059  -12.942 -30.893 1.00 92.53  ? 294 PRO A CG  1 
ATOM   2393 C  CD  . PRO A 1 294 ? 32.282  -11.929 -30.082 1.00 91.08  ? 294 PRO A CD  1 
ATOM   2394 N  N   . VAL B 2 1   ? 1.860   2.584   -5.631  1.00 65.01  ? 175 VAL B N   1 
ATOM   2395 C  CA  . VAL B 2 1   ? 2.374   2.714   -7.034  1.00 66.03  ? 175 VAL B CA  1 
ATOM   2396 C  C   . VAL B 2 1   ? 3.524   1.723   -7.231  1.00 62.38  ? 175 VAL B C   1 
ATOM   2397 O  O   . VAL B 2 1   ? 4.596   1.927   -6.670  1.00 58.18  ? 175 VAL B O   1 
ATOM   2398 C  CB  . VAL B 2 1   ? 2.838   4.151   -7.346  1.00 72.09  ? 175 VAL B CB  1 
ATOM   2399 C  CG1 . VAL B 2 1   ? 3.368   4.252   -8.765  1.00 70.21  ? 175 VAL B CG1 1 
ATOM   2400 C  CG2 . VAL B 2 1   ? 1.752   5.196   -7.114  1.00 76.22  ? 175 VAL B CG2 1 
ATOM   2401 N  N   . PRO B 2 2   ? 3.347   0.616   -7.998  1.00 59.36  ? 176 PRO B N   1 
ATOM   2402 C  CA  . PRO B 2 2   ? 4.410   -0.376  -8.190  1.00 56.19  ? 176 PRO B CA  1 
ATOM   2403 C  C   . PRO B 2 2   ? 5.436   0.010   -9.253  1.00 61.21  ? 176 PRO B C   1 
ATOM   2404 O  O   . PRO B 2 2   ? 5.235   0.974   -9.992  1.00 55.36  ? 176 PRO B O   1 
ATOM   2405 C  CB  . PRO B 2 2   ? 3.656   -1.630  -8.654  1.00 55.92  ? 176 PRO B CB  1 
ATOM   2406 C  CG  . PRO B 2 2   ? 2.445   -1.080  -9.379  1.00 57.00  ? 176 PRO B CG  1 
ATOM   2407 C  CD  . PRO B 2 2   ? 2.099   0.222   -8.676  1.00 58.87  ? 176 PRO B CD  1 
ATOM   2408 N  N   . ASP B 2 3   ? 6.526   -0.770  -9.320  1.00 63.09  ? 177 ASP B N   1 
ATOM   2409 C  CA  . ASP B 2 3   ? 7.574   -0.592  -10.319 1.00 64.07  ? 177 ASP B CA  1 
ATOM   2410 C  C   . ASP B 2 3   ? 7.022   -0.920  -11.705 1.00 61.01  ? 177 ASP B C   1 
ATOM   2411 O  O   . ASP B 2 3   ? 6.283   -1.895  -11.856 1.00 55.34  ? 177 ASP B O   1 
ATOM   2412 C  CB  . ASP B 2 3   ? 8.766   -1.523  -10.072 1.00 66.48  ? 177 ASP B CB  1 
ATOM   2413 C  CG  . ASP B 2 3   ? 9.616   -1.187  -8.861  1.00 72.56  ? 177 ASP B CG  1 
ATOM   2414 O  OD1 . ASP B 2 3   ? 9.864   0.024   -8.632  1.00 77.42  ? 177 ASP B OD1 1 
ATOM   2415 O  OD2 . ASP B 2 3   ? 10.060  -2.150  -8.181  1.00 74.03  ? 177 ASP B OD2 1 
ATOM   2416 N  N   . TYR B 2 4   ? 7.420   -0.112  -12.698 1.00 56.76  ? 178 TYR B N   1 
ATOM   2417 C  CA  . TYR B 2 4   ? 7.078   -0.315  -14.100 1.00 52.70  ? 178 TYR B CA  1 
ATOM   2418 C  C   . TYR B 2 4   ? 5.617   0.035   -14.410 1.00 52.39  ? 178 TYR B C   1 
ATOM   2419 O  O   . TYR B 2 4   ? 5.145   -0.267  -15.502 1.00 50.66  ? 178 TYR B O   1 
ATOM   2420 C  CB  . TYR B 2 4   ? 7.324   -1.767  -14.517 1.00 50.21  ? 178 TYR B CB  1 
ATOM   2421 C  CG  . TYR B 2 4   ? 8.692   -2.299  -14.191 1.00 52.91  ? 178 TYR B CG  1 
ATOM   2422 C  CD1 . TYR B 2 4   ? 9.798   -1.927  -14.939 1.00 54.01  ? 178 TYR B CD1 1 
ATOM   2423 C  CD2 . TYR B 2 4   ? 8.879   -3.207  -13.160 1.00 49.81  ? 178 TYR B CD2 1 
ATOM   2424 C  CE1 . TYR B 2 4   ? 11.061  -2.422  -14.653 1.00 52.44  ? 178 TYR B CE1 1 
ATOM   2425 C  CE2 . TYR B 2 4   ? 10.135  -3.709  -12.861 1.00 50.17  ? 178 TYR B CE2 1 
ATOM   2426 C  CZ  . TYR B 2 4   ? 11.230  -3.312  -13.608 1.00 51.51  ? 178 TYR B CZ  1 
ATOM   2427 O  OH  . TYR B 2 4   ? 12.469  -3.805  -13.315 1.00 48.68  ? 178 TYR B OH  1 
ATOM   2428 N  N   . HIS B 2 5   ? 4.897   0.694   -13.495 1.00 52.19  ? 179 HIS B N   1 
ATOM   2429 C  CA  . HIS B 2 5   ? 3.478   0.946   -13.711 1.00 55.46  ? 179 HIS B CA  1 
ATOM   2430 C  C   . HIS B 2 5   ? 3.274   1.772   -14.986 1.00 52.05  ? 179 HIS B C   1 
ATOM   2431 O  O   . HIS B 2 5   ? 2.379   1.447   -15.759 1.00 53.40  ? 179 HIS B O   1 
ATOM   2432 C  CB  . HIS B 2 5   ? 2.802   1.521   -12.459 1.00 57.64  ? 179 HIS B CB  1 
ATOM   2433 C  CG  . HIS B 2 5   ? 2.797   3.012   -12.367 1.00 69.46  ? 179 HIS B CG  1 
ATOM   2434 N  ND1 . HIS B 2 5   ? 1.705   3.776   -12.729 1.00 79.35  ? 179 HIS B ND1 1 
ATOM   2435 C  CD2 . HIS B 2 5   ? 3.744   3.882   -11.973 1.00 77.86  ? 179 HIS B CD2 1 
ATOM   2436 C  CE1 . HIS B 2 5   ? 1.987   5.062   -12.546 1.00 87.00  ? 179 HIS B CE1 1 
ATOM   2437 N  NE2 . HIS B 2 5   ? 3.219   5.149   -12.079 1.00 83.95  ? 179 HIS B NE2 1 
ATOM   2438 N  N   . GLU B 2 6   ? 4.116   2.794   -15.228 1.00 48.95  ? 180 GLU B N   1 
ATOM   2439 C  CA  . GLU B 2 6   ? 3.994   3.641   -16.411 1.00 56.44  ? 180 GLU B CA  1 
ATOM   2440 C  C   . GLU B 2 6   ? 4.426   2.891   -17.671 1.00 53.97  ? 180 GLU B C   1 
ATOM   2441 O  O   . GLU B 2 6   ? 3.823   3.087   -18.721 1.00 61.22  ? 180 GLU B O   1 
ATOM   2442 C  CB  . GLU B 2 6   ? 4.797   4.939   -16.282 1.00 69.61  ? 180 GLU B CB  1 
ATOM   2443 C  CG  . GLU B 2 6   ? 4.240   5.914   -15.250 1.00 84.41  ? 180 GLU B CG  1 
ATOM   2444 C  CD  . GLU B 2 6   ? 2.878   6.538   -15.531 1.00 94.61  ? 180 GLU B CD  1 
ATOM   2445 O  OE1 . GLU B 2 6   ? 1.878   5.789   -15.592 1.00 97.52  ? 180 GLU B OE1 1 
ATOM   2446 O  OE2 . GLU B 2 6   ? 2.816   7.783   -15.667 1.00 103.03 ? 180 GLU B OE2 1 
ATOM   2447 N  N   . ASP B 2 7   ? 5.461   2.048   -17.574 1.00 47.91  ? 181 ASP B N   1 
ATOM   2448 C  CA  . ASP B 2 7   ? 5.901   1.201   -18.681 1.00 44.81  ? 181 ASP B CA  1 
ATOM   2449 C  C   . ASP B 2 7   ? 4.834   0.199   -19.111 1.00 40.08  ? 181 ASP B C   1 
ATOM   2450 O  O   . ASP B 2 7   ? 4.635   -0.025  -20.305 1.00 38.81  ? 181 ASP B O   1 
ATOM   2451 C  CB  . ASP B 2 7   ? 7.129   0.366   -18.309 1.00 47.46  ? 181 ASP B CB  1 
ATOM   2452 C  CG  . ASP B 2 7   ? 8.386   1.201   -18.172 1.00 51.41  ? 181 ASP B CG  1 
ATOM   2453 O  OD1 . ASP B 2 7   ? 8.453   2.293   -18.808 1.00 49.22  ? 181 ASP B OD1 1 
ATOM   2454 O  OD2 . ASP B 2 7   ? 9.263   0.780   -17.396 1.00 54.79  ? 181 ASP B OD2 1 
ATOM   2455 N  N   . ILE B 2 8   ? 4.232   -0.485  -18.135 1.00 39.71  ? 182 ILE B N   1 
ATOM   2456 C  CA  . ILE B 2 8   ? 3.233   -1.496  -18.426 1.00 36.43  ? 182 ILE B CA  1 
ATOM   2457 C  C   . ILE B 2 8   ? 2.054   -0.811  -19.122 1.00 36.94  ? 182 ILE B C   1 
ATOM   2458 O  O   . ILE B 2 8   ? 1.567   -1.324  -20.132 1.00 36.71  ? 182 ILE B O   1 
ATOM   2459 C  CB  . ILE B 2 8   ? 2.866   -2.272  -17.148 1.00 36.29  ? 182 ILE B CB  1 
ATOM   2460 C  CG1 . ILE B 2 8   ? 4.060   -3.113  -16.678 1.00 38.80  ? 182 ILE B CG1 1 
ATOM   2461 C  CG2 . ILE B 2 8   ? 1.632   -3.139  -17.372 1.00 38.51  ? 182 ILE B CG2 1 
ATOM   2462 C  CD1 . ILE B 2 8   ? 3.887   -3.790  -15.329 1.00 36.92  ? 182 ILE B CD1 1 
ATOM   2463 N  N   . HIS B 2 9   ? 1.653   0.374   -18.628 1.00 35.96  ? 183 HIS B N   1 
ATOM   2464 C  CA  . HIS B 2 9   ? 0.514   1.113   -19.174 1.00 39.93  ? 183 HIS B CA  1 
ATOM   2465 C  C   . HIS B 2 9   ? 0.772   1.476   -20.639 1.00 42.72  ? 183 HIS B C   1 
ATOM   2466 O  O   . HIS B 2 9   ? -0.099  1.289   -21.499 1.00 46.62  ? 183 HIS B O   1 
ATOM   2467 C  CB  . HIS B 2 9   ? 0.199   2.358   -18.331 1.00 41.41  ? 183 HIS B CB  1 
ATOM   2468 C  CG  . HIS B 2 9   ? -0.955  3.150   -18.848 1.00 44.25  ? 183 HIS B CG  1 
ATOM   2469 N  ND1 . HIS B 2 9   ? -0.804  4.378   -19.452 1.00 43.76  ? 183 HIS B ND1 1 
ATOM   2470 C  CD2 . HIS B 2 9   ? -2.270  2.883   -18.879 1.00 48.80  ? 183 HIS B CD2 1 
ATOM   2471 C  CE1 . HIS B 2 9   ? -1.995  4.834   -19.818 1.00 48.64  ? 183 HIS B CE1 1 
ATOM   2472 N  NE2 . HIS B 2 9   ? -2.902  3.945   -19.479 1.00 48.13  ? 183 HIS B NE2 1 
ATOM   2473 N  N   . THR B 2 10  ? 1.995   1.952   -20.920 1.00 42.80  ? 184 THR B N   1 
ATOM   2474 C  CA  . THR B 2 10  ? 2.423   2.260   -22.278 1.00 40.12  ? 184 THR B CA  1 
ATOM   2475 C  C   . THR B 2 10  ? 2.348   1.010   -23.150 1.00 35.59  ? 184 THR B C   1 
ATOM   2476 O  O   . THR B 2 10  ? 1.861   1.085   -24.270 1.00 37.18  ? 184 THR B O   1 
ATOM   2477 C  CB  . THR B 2 10  ? 3.828   2.874   -22.295 1.00 37.82  ? 184 THR B CB  1 
ATOM   2478 O  OG1 . THR B 2 10  ? 3.756   4.043   -21.486 1.00 38.41  ? 184 THR B OG1 1 
ATOM   2479 C  CG2 . THR B 2 10  ? 4.307   3.247   -23.682 1.00 39.72  ? 184 THR B CG2 1 
ATOM   2480 N  N   . TYR B 2 11  ? 2.830   -0.127  -22.635 1.00 36.33  ? 185 TYR B N   1 
ATOM   2481 C  CA  . TYR B 2 11  ? 2.797   -1.383  -23.376 1.00 37.28  ? 185 TYR B CA  1 
ATOM   2482 C  C   . TYR B 2 11  ? 1.346   -1.765  -23.663 1.00 36.66  ? 185 TYR B C   1 
ATOM   2483 O  O   . TYR B 2 11  ? 0.996   -2.040  -24.799 1.00 38.22  ? 185 TYR B O   1 
ATOM   2484 C  CB  . TYR B 2 11  ? 3.511   -2.504  -22.616 1.00 38.60  ? 185 TYR B CB  1 
ATOM   2485 C  CG  . TYR B 2 11  ? 3.522   -3.835  -23.329 1.00 42.96  ? 185 TYR B CG  1 
ATOM   2486 C  CD1 . TYR B 2 11  ? 4.119   -3.975  -24.573 1.00 44.01  ? 185 TYR B CD1 1 
ATOM   2487 C  CD2 . TYR B 2 11  ? 2.939   -4.960  -22.765 1.00 46.75  ? 185 TYR B CD2 1 
ATOM   2488 C  CE1 . TYR B 2 11  ? 4.146   -5.195  -25.230 1.00 46.82  ? 185 TYR B CE1 1 
ATOM   2489 C  CE2 . TYR B 2 11  ? 2.949   -6.187  -23.416 1.00 48.97  ? 185 TYR B CE2 1 
ATOM   2490 C  CZ  . TYR B 2 11  ? 3.566   -6.307  -24.646 1.00 48.60  ? 185 TYR B CZ  1 
ATOM   2491 O  OH  . TYR B 2 11  ? 3.571   -7.509  -25.309 1.00 61.88  ? 185 TYR B OH  1 
ATOM   2492 N  N   . LEU B 2 12  ? 0.492   -1.767  -22.631 1.00 43.92  ? 186 LEU B N   1 
ATOM   2493 C  CA  . LEU B 2 12  ? -0.922  -2.109  -22.784 1.00 43.44  ? 186 LEU B CA  1 
ATOM   2494 C  C   . LEU B 2 12  ? -1.579  -1.224  -23.864 1.00 42.61  ? 186 LEU B C   1 
ATOM   2495 O  O   . LEU B 2 12  ? -2.385  -1.729  -24.654 1.00 37.17  ? 186 LEU B O   1 
ATOM   2496 C  CB  . LEU B 2 12  ? -1.626  -2.040  -21.412 1.00 43.38  ? 186 LEU B CB  1 
ATOM   2497 C  CG  . LEU B 2 12  ? -1.121  -3.016  -20.334 1.00 46.06  ? 186 LEU B CG  1 
ATOM   2498 C  CD1 . LEU B 2 12  ? -2.022  -3.042  -19.102 1.00 45.99  ? 186 LEU B CD1 1 
ATOM   2499 C  CD2 . LEU B 2 12  ? -0.966  -4.423  -20.883 1.00 48.69  ? 186 LEU B CD2 1 
ATOM   2500 N  N   . ARG B 2 13  ? -1.199  0.064   -23.961 1.00 38.39  ? 187 ARG B N   1 
ATOM   2501 C  CA  . ARG B 2 13  ? -1.796  0.969   -24.943 1.00 40.39  ? 187 ARG B CA  1 
ATOM   2502 C  C   . ARG B 2 13  ? -1.375  0.603   -26.368 1.00 44.74  ? 187 ARG B C   1 
ATOM   2503 O  O   . ARG B 2 13  ? -2.144  0.834   -27.304 1.00 47.31  ? 187 ARG B O   1 
ATOM   2504 C  CB  . ARG B 2 13  ? -1.492  2.445   -24.648 1.00 38.17  ? 187 ARG B CB  1 
ATOM   2505 C  CG  . ARG B 2 13  ? -2.291  3.002   -23.476 1.00 39.90  ? 187 ARG B CG  1 
ATOM   2506 C  CD  . ARG B 2 13  ? -3.771  3.139   -23.784 1.00 40.91  ? 187 ARG B CD  1 
ATOM   2507 N  NE  . ARG B 2 13  ? -3.953  4.223   -24.736 1.00 42.65  ? 187 ARG B NE  1 
ATOM   2508 C  CZ  . ARG B 2 13  ? -4.038  5.509   -24.413 1.00 42.22  ? 187 ARG B CZ  1 
ATOM   2509 N  NH1 . ARG B 2 13  ? -4.197  5.884   -23.153 1.00 40.70  ? 187 ARG B NH1 1 
ATOM   2510 N  NH2 . ARG B 2 13  ? -4.009  6.418   -25.373 1.00 41.17  ? 187 ARG B NH2 1 
ATOM   2511 N  N   . GLU B 2 14  ? -0.171  0.042   -26.538 1.00 46.74  ? 188 GLU B N   1 
ATOM   2512 C  CA  . GLU B 2 14  ? 0.270   -0.453  -27.836 1.00 49.13  ? 188 GLU B CA  1 
ATOM   2513 C  C   . GLU B 2 14  ? -0.506  -1.722  -28.190 1.00 45.45  ? 188 GLU B C   1 
ATOM   2514 O  O   . GLU B 2 14  ? -0.973  -1.880  -29.314 1.00 46.06  ? 188 GLU B O   1 
ATOM   2515 C  CB  . GLU B 2 14  ? 1.773   -0.748  -27.859 1.00 56.19  ? 188 GLU B CB  1 
ATOM   2516 C  CG  . GLU B 2 14  ? 2.642   0.481   -27.617 1.00 70.66  ? 188 GLU B CG  1 
ATOM   2517 C  CD  . GLU B 2 14  ? 4.145   0.302   -27.813 1.00 80.07  ? 188 GLU B CD  1 
ATOM   2518 O  OE1 . GLU B 2 14  ? 4.873   1.309   -27.688 1.00 78.17  ? 188 GLU B OE1 1 
ATOM   2519 O  OE2 . GLU B 2 14  ? 4.587   -0.837  -28.100 1.00 82.34  ? 188 GLU B OE2 1 
ATOM   2520 N  N   . MET B 2 15  ? -0.652  -2.627  -27.223 1.00 42.25  ? 189 MET B N   1 
ATOM   2521 C  CA  . MET B 2 15  ? -1.147  -3.960  -27.524 1.00 45.50  ? 189 MET B CA  1 
ATOM   2522 C  C   . MET B 2 15  ? -2.662  -3.970  -27.750 1.00 45.00  ? 189 MET B C   1 
ATOM   2523 O  O   . MET B 2 15  ? -3.166  -4.935  -28.319 1.00 48.31  ? 189 MET B O   1 
ATOM   2524 C  CB  . MET B 2 15  ? -0.774  -4.937  -26.402 1.00 46.80  ? 189 MET B CB  1 
ATOM   2525 C  CG  . MET B 2 15  ? 0.739   -5.176  -26.323 1.00 58.21  ? 189 MET B CG  1 
ATOM   2526 S  SD  . MET B 2 15  ? 1.543   -5.635  -27.913 1.00 60.65  ? 189 MET B SD  1 
ATOM   2527 C  CE  . MET B 2 15  ? 1.071   -7.359  -28.065 1.00 63.49  ? 189 MET B CE  1 
ATOM   2528 N  N   . GLU B 2 16  ? -3.388  -2.933  -27.305 1.00 42.24  ? 190 GLU B N   1 
ATOM   2529 C  CA  . GLU B 2 16  ? -4.848  -2.941  -27.365 1.00 43.84  ? 190 GLU B CA  1 
ATOM   2530 C  C   . GLU B 2 16  ? -5.301  -2.582  -28.780 1.00 50.55  ? 190 GLU B C   1 
ATOM   2531 O  O   . GLU B 2 16  ? -6.440  -2.891  -29.136 1.00 54.13  ? 190 GLU B O   1 
ATOM   2532 C  CB  . GLU B 2 16  ? -5.485  -2.036  -26.302 1.00 41.32  ? 190 GLU B CB  1 
ATOM   2533 C  CG  . GLU B 2 16  ? -5.334  -0.534  -26.518 1.00 41.64  ? 190 GLU B CG  1 
ATOM   2534 C  CD  . GLU B 2 16  ? -6.207  0.312   -25.597 1.00 46.15  ? 190 GLU B CD  1 
ATOM   2535 O  OE1 . GLU B 2 16  ? -7.113  -0.269  -24.947 1.00 48.10  ? 190 GLU B OE1 1 
ATOM   2536 O  OE2 . GLU B 2 16  ? -5.977  1.551   -25.504 1.00 46.91  ? 190 GLU B OE2 1 
ATOM   2537 N  N   . VAL B 2 17  ? -4.406  -1.942  -29.562 1.00 51.84  ? 191 VAL B N   1 
ATOM   2538 C  CA  . VAL B 2 17  ? -4.644  -1.592  -30.959 1.00 51.48  ? 191 VAL B CA  1 
ATOM   2539 C  C   . VAL B 2 17  ? -4.491  -2.849  -31.815 1.00 53.28  ? 191 VAL B C   1 
ATOM   2540 O  O   . VAL B 2 17  ? -5.325  -3.123  -32.671 1.00 58.65  ? 191 VAL B O   1 
ATOM   2541 C  CB  . VAL B 2 17  ? -3.690  -0.487  -31.454 1.00 57.34  ? 191 VAL B CB  1 
ATOM   2542 C  CG1 . VAL B 2 17  ? -3.945  -0.142  -32.918 1.00 57.47  ? 191 VAL B CG1 1 
ATOM   2543 C  CG2 . VAL B 2 17  ? -3.761  0.764   -30.590 1.00 55.51  ? 191 VAL B CG2 1 
ATOM   2544 N  N   . LYS B 2 18  ? -3.433  -3.617  -31.542 1.00 54.29  ? 192 LYS B N   1 
ATOM   2545 C  CA  . LYS B 2 18  ? -3.107  -4.843  -32.262 1.00 56.85  ? 192 LYS B CA  1 
ATOM   2546 C  C   . LYS B 2 18  ? -4.061  -5.987  -31.913 1.00 50.46  ? 192 LYS B C   1 
ATOM   2547 O  O   . LYS B 2 18  ? -4.261  -6.867  -32.741 1.00 53.83  ? 192 LYS B O   1 
ATOM   2548 C  CB  . LYS B 2 18  ? -1.661  -5.265  -31.958 1.00 61.56  ? 192 LYS B CB  1 
ATOM   2549 C  CG  . LYS B 2 18  ? -0.607  -4.224  -32.317 1.00 68.05  ? 192 LYS B CG  1 
ATOM   2550 C  CD  . LYS B 2 18  ? 0.815   -4.613  -31.972 1.00 76.65  ? 192 LYS B CD  1 
ATOM   2551 C  CE  . LYS B 2 18  ? 1.752   -3.422  -32.024 1.00 83.60  ? 192 LYS B CE  1 
ATOM   2552 N  NZ  . LYS B 2 18  ? 3.142   -3.799  -31.673 1.00 84.90  ? 192 LYS B NZ  1 
ATOM   2553 N  N   . CYS B 2 19  ? -4.656  -5.973  -30.708 1.00 55.72  ? 193 CYS B N   1 
ATOM   2554 C  CA  . CYS B 2 19  ? -5.475  -7.075  -30.200 1.00 59.61  ? 193 CYS B CA  1 
ATOM   2555 C  C   . CYS B 2 19  ? -6.969  -6.840  -30.464 1.00 59.33  ? 193 CYS B C   1 
ATOM   2556 O  O   . CYS B 2 19  ? -7.788  -7.677  -30.092 1.00 63.89  ? 193 CYS B O   1 
ATOM   2557 C  CB  . CYS B 2 19  ? -5.240  -7.296  -28.701 1.00 65.97  ? 193 CYS B CB  1 
ATOM   2558 S  SG  . CYS B 2 19  ? -3.746  -8.254  -28.298 1.00 72.36  ? 193 CYS B SG  1 
ATOM   2559 N  N   . LYS B 2 20  ? -7.310  -5.714  -31.114 1.00 55.58  ? 194 LYS B N   1 
ATOM   2560 C  CA  . LYS B 2 20  ? -8.683  -5.289  -31.389 1.00 60.52  ? 194 LYS B CA  1 
ATOM   2561 C  C   . LYS B 2 20  ? -9.332  -6.211  -32.428 1.00 56.29  ? 194 LYS B C   1 
ATOM   2562 O  O   . LYS B 2 20  ? -8.672  -6.630  -33.374 1.00 56.46  ? 194 LYS B O   1 
ATOM   2563 C  CB  . LYS B 2 20  ? -8.671  -3.833  -31.875 1.00 66.76  ? 194 LYS B CB  1 
ATOM   2564 C  CG  . LYS B 2 20  ? -9.987  -3.293  -32.412 1.00 76.86  ? 194 LYS B CG  1 
ATOM   2565 C  CD  . LYS B 2 20  ? -9.898  -1.831  -32.811 1.00 87.27  ? 194 LYS B CD  1 
ATOM   2566 C  CE  . LYS B 2 20  ? -11.249 -1.196  -33.066 1.00 88.74  ? 194 LYS B CE  1 
ATOM   2567 N  NZ  . LYS B 2 20  ? -11.312 0.176   -32.508 1.00 87.60  ? 194 LYS B NZ  1 
ATOM   2568 N  N   . PRO B 2 21  ? -10.626 -6.590  -32.289 1.00 55.34  ? 195 PRO B N   1 
ATOM   2569 C  CA  . PRO B 2 21  ? -11.334 -7.317  -33.346 1.00 57.68  ? 195 PRO B CA  1 
ATOM   2570 C  C   . PRO B 2 21  ? -11.816 -6.371  -34.447 1.00 56.86  ? 195 PRO B C   1 
ATOM   2571 O  O   . PRO B 2 21  ? -11.871 -5.160  -34.230 1.00 60.65  ? 195 PRO B O   1 
ATOM   2572 C  CB  . PRO B 2 21  ? -12.540 -7.957  -32.641 1.00 57.83  ? 195 PRO B CB  1 
ATOM   2573 C  CG  . PRO B 2 21  ? -12.407 -7.579  -31.171 1.00 56.44  ? 195 PRO B CG  1 
ATOM   2574 C  CD  . PRO B 2 21  ? -11.483 -6.380  -31.114 1.00 56.04  ? 195 PRO B CD  1 
ATOM   2575 N  N   . LYS B 2 22  ? -12.160 -6.926  -35.619 1.00 62.19  ? 196 LYS B N   1 
ATOM   2576 C  CA  . LYS B 2 22  ? -12.729 -6.150  -36.719 1.00 71.36  ? 196 LYS B CA  1 
ATOM   2577 C  C   . LYS B 2 22  ? -14.077 -5.567  -36.274 1.00 72.76  ? 196 LYS B C   1 
ATOM   2578 O  O   . LYS B 2 22  ? -14.983 -6.311  -35.916 1.00 71.90  ? 196 LYS B O   1 
ATOM   2579 C  CB  . LYS B 2 22  ? -12.868 -7.013  -37.981 1.00 76.40  ? 196 LYS B CB  1 
ATOM   2580 C  CG  . LYS B 2 22  ? -11.556 -7.529  -38.560 1.00 83.41  ? 196 LYS B CG  1 
ATOM   2581 C  CD  . LYS B 2 22  ? -11.604 -7.836  -40.051 1.00 94.98  ? 196 LYS B CD  1 
ATOM   2582 C  CE  . LYS B 2 22  ? -10.232 -8.088  -40.648 1.00 101.24 ? 196 LYS B CE  1 
ATOM   2583 N  NZ  . LYS B 2 22  ? -9.642  -9.359  -40.161 1.00 103.77 ? 196 LYS B NZ  1 
ATOM   2584 N  N   . VAL B 2 23  ? -14.201 -4.232  -36.304 1.00 77.50  ? 197 VAL B N   1 
ATOM   2585 C  CA  . VAL B 2 23  ? -15.346 -3.511  -35.750 1.00 80.53  ? 197 VAL B CA  1 
ATOM   2586 C  C   . VAL B 2 23  ? -16.682 -4.003  -36.329 1.00 78.35  ? 197 VAL B C   1 
ATOM   2587 O  O   . VAL B 2 23  ? -17.667 -4.074  -35.596 1.00 83.33  ? 197 VAL B O   1 
ATOM   2588 C  CB  . VAL B 2 23  ? -15.181 -1.988  -35.950 1.00 80.61  ? 197 VAL B CB  1 
ATOM   2589 C  CG1 . VAL B 2 23  ? -15.208 -1.597  -37.425 1.00 82.85  ? 197 VAL B CG1 1 
ATOM   2590 C  CG2 . VAL B 2 23  ? -16.214 -1.197  -35.161 1.00 78.22  ? 197 VAL B CG2 1 
ATOM   2591 N  N   . GLY B 2 24  ? -16.737 -4.320  -37.630 1.00 69.24  ? 198 GLY B N   1 
ATOM   2592 C  CA  . GLY B 2 24  ? -18.014 -4.567  -38.292 1.00 73.13  ? 198 GLY B CA  1 
ATOM   2593 C  C   . GLY B 2 24  ? -18.279 -6.040  -38.610 1.00 70.39  ? 198 GLY B C   1 
ATOM   2594 O  O   . GLY B 2 24  ? -18.958 -6.343  -39.591 1.00 71.42  ? 198 GLY B O   1 
ATOM   2595 N  N   . TYR B 2 25  ? -17.779 -6.953  -37.768 1.00 63.25  ? 199 TYR B N   1 
ATOM   2596 C  CA  . TYR B 2 25  ? -17.639 -8.355  -38.154 1.00 60.24  ? 199 TYR B CA  1 
ATOM   2597 C  C   . TYR B 2 25  ? -19.000 -9.069  -38.147 1.00 54.87  ? 199 TYR B C   1 
ATOM   2598 O  O   . TYR B 2 25  ? -19.220 -9.995  -38.930 1.00 53.49  ? 199 TYR B O   1 
ATOM   2599 C  CB  . TYR B 2 25  ? -16.571 -9.046  -37.289 1.00 59.18  ? 199 TYR B CB  1 
ATOM   2600 C  CG  . TYR B 2 25  ? -17.010 -9.481  -35.910 1.00 55.03  ? 199 TYR B CG  1 
ATOM   2601 C  CD1 . TYR B 2 25  ? -17.875 -10.553 -35.740 1.00 52.62  ? 199 TYR B CD1 1 
ATOM   2602 C  CD2 . TYR B 2 25  ? -16.545 -8.841  -34.769 1.00 50.84  ? 199 TYR B CD2 1 
ATOM   2603 C  CE1 . TYR B 2 25  ? -18.297 -10.953 -34.483 1.00 48.74  ? 199 TYR B CE1 1 
ATOM   2604 C  CE2 . TYR B 2 25  ? -16.949 -9.235  -33.502 1.00 51.49  ? 199 TYR B CE2 1 
ATOM   2605 C  CZ  . TYR B 2 25  ? -17.833 -10.291 -33.359 1.00 49.70  ? 199 TYR B CZ  1 
ATOM   2606 O  OH  . TYR B 2 25  ? -18.242 -10.702 -32.114 1.00 53.71  ? 199 TYR B OH  1 
ATOM   2607 N  N   . MET B 2 26  ? -19.913 -8.668  -37.257 1.00 54.41  ? 200 MET B N   1 
ATOM   2608 C  CA  . MET B 2 26  ? -21.184 -9.371  -37.101 1.00 57.69  ? 200 MET B CA  1 
ATOM   2609 C  C   . MET B 2 26  ? -22.037 -9.223  -38.372 1.00 60.26  ? 200 MET B C   1 
ATOM   2610 O  O   . MET B 2 26  ? -22.781 -10.141 -38.721 1.00 55.28  ? 200 MET B O   1 
ATOM   2611 C  CB  . MET B 2 26  ? -21.949 -8.862  -35.873 1.00 54.55  ? 200 MET B CB  1 
ATOM   2612 C  CG  . MET B 2 26  ? -23.036 -9.802  -35.373 1.00 56.67  ? 200 MET B CG  1 
ATOM   2613 S  SD  . MET B 2 26  ? -22.418 -11.407 -34.750 1.00 63.75  ? 200 MET B SD  1 
ATOM   2614 C  CE  . MET B 2 26  ? -21.745 -10.868 -33.179 1.00 72.05  ? 200 MET B CE  1 
ATOM   2615 N  N   . LYS B 2 27  ? -21.890 -8.085  -39.076 1.00 64.15  ? 201 LYS B N   1 
ATOM   2616 C  CA  . LYS B 2 27  ? -22.542 -7.824  -40.361 1.00 69.32  ? 201 LYS B CA  1 
ATOM   2617 C  C   . LYS B 2 27  ? -22.181 -8.916  -41.369 1.00 68.35  ? 201 LYS B C   1 
ATOM   2618 O  O   . LYS B 2 27  ? -23.060 -9.391  -42.079 1.00 62.71  ? 201 LYS B O   1 
ATOM   2619 C  CB  . LYS B 2 27  ? -22.153 -6.452  -40.933 1.00 74.62  ? 201 LYS B CB  1 
ATOM   2620 C  CG  . LYS B 2 27  ? -22.004 -5.349  -39.893 1.00 86.60  ? 201 LYS B CG  1 
ATOM   2621 C  CD  . LYS B 2 27  ? -22.055 -3.940  -40.432 1.00 93.45  ? 201 LYS B CD  1 
ATOM   2622 C  CE  . LYS B 2 27  ? -22.306 -2.936  -39.326 1.00 99.03  ? 201 LYS B CE  1 
ATOM   2623 N  NZ  . LYS B 2 27  ? -22.606 -1.591  -39.867 1.00 103.76 ? 201 LYS B NZ  1 
ATOM   2624 N  N   . LYS B 2 28  ? -20.900 -9.324  -41.397 1.00 67.00  ? 202 LYS B N   1 
ATOM   2625 C  CA  . LYS B 2 28  ? -20.376 -10.307 -42.345 1.00 65.76  ? 202 LYS B CA  1 
ATOM   2626 C  C   . LYS B 2 28  ? -20.590 -11.755 -41.885 1.00 57.20  ? 202 LYS B C   1 
ATOM   2627 O  O   . LYS B 2 28  ? -20.111 -12.667 -42.552 1.00 56.16  ? 202 LYS B O   1 
ATOM   2628 C  CB  . LYS B 2 28  ? -18.883 -10.041 -42.596 1.00 76.89  ? 202 LYS B CB  1 
ATOM   2629 C  CG  . LYS B 2 28  ? -18.602 -8.885  -43.549 1.00 86.16  ? 202 LYS B CG  1 
ATOM   2630 C  CD  . LYS B 2 28  ? -17.256 -8.222  -43.362 1.00 95.79  ? 202 LYS B CD  1 
ATOM   2631 C  CE  . LYS B 2 28  ? -17.100 -6.995  -44.243 1.00 102.59 ? 202 LYS B CE  1 
ATOM   2632 N  NZ  . LYS B 2 28  ? -16.227 -5.962  -43.631 1.00 98.85  ? 202 LYS B NZ  1 
ATOM   2633 N  N   . GLN B 2 29  ? -21.303 -11.981 -40.767 1.00 54.51  ? 203 GLN B N   1 
ATOM   2634 C  CA  . GLN B 2 29  ? -21.562 -13.320 -40.244 1.00 48.43  ? 203 GLN B CA  1 
ATOM   2635 C  C   . GLN B 2 29  ? -22.943 -13.748 -40.722 1.00 49.91  ? 203 GLN B C   1 
ATOM   2636 O  O   . GLN B 2 29  ? -23.940 -13.119 -40.381 1.00 46.08  ? 203 GLN B O   1 
ATOM   2637 C  CB  . GLN B 2 29  ? -21.474 -13.363 -38.712 1.00 51.12  ? 203 GLN B CB  1 
ATOM   2638 C  CG  . GLN B 2 29  ? -20.049 -13.365 -38.158 1.00 48.32  ? 203 GLN B CG  1 
ATOM   2639 C  CD  . GLN B 2 29  ? -19.441 -14.740 -37.999 1.00 45.89  ? 203 GLN B CD  1 
ATOM   2640 O  OE1 . GLN B 2 29  ? -20.114 -15.759 -38.116 1.00 48.63  ? 203 GLN B OE1 1 
ATOM   2641 N  NE2 . GLN B 2 29  ? -18.147 -14.787 -37.723 1.00 43.55  ? 203 GLN B NE2 1 
ATOM   2642 N  N   . PRO B 2 30  ? -23.044 -14.808 -41.548 1.00 56.17  ? 204 PRO B N   1 
ATOM   2643 C  CA  . PRO B 2 30  ? -24.326 -15.190 -42.140 1.00 59.18  ? 204 PRO B CA  1 
ATOM   2644 C  C   . PRO B 2 30  ? -25.388 -15.598 -41.114 1.00 60.08  ? 204 PRO B C   1 
ATOM   2645 O  O   . PRO B 2 30  ? -26.549 -15.219 -41.269 1.00 61.33  ? 204 PRO B O   1 
ATOM   2646 C  CB  . PRO B 2 30  ? -23.966 -16.359 -43.083 1.00 59.50  ? 204 PRO B CB  1 
ATOM   2647 C  CG  . PRO B 2 30  ? -22.632 -16.885 -42.574 1.00 59.89  ? 204 PRO B CG  1 
ATOM   2648 C  CD  . PRO B 2 30  ? -21.936 -15.678 -41.976 1.00 58.70  ? 204 PRO B CD  1 
ATOM   2649 N  N   . ASP B 2 31  ? -24.984 -16.323 -40.050 1.00 59.27  ? 205 ASP B N   1 
ATOM   2650 C  CA  . ASP B 2 31  ? -25.928 -17.049 -39.199 1.00 59.85  ? 205 ASP B CA  1 
ATOM   2651 C  C   . ASP B 2 31  ? -26.107 -16.468 -37.787 1.00 59.61  ? 205 ASP B C   1 
ATOM   2652 O  O   . ASP B 2 31  ? -27.103 -16.801 -37.139 1.00 58.19  ? 205 ASP B O   1 
ATOM   2653 C  CB  . ASP B 2 31  ? -25.579 -18.537 -39.092 1.00 59.57  ? 205 ASP B CB  1 
ATOM   2654 C  CG  . ASP B 2 31  ? -26.777 -19.379 -38.670 1.00 65.10  ? 205 ASP B CG  1 
ATOM   2655 O  OD1 . ASP B 2 31  ? -27.899 -19.118 -39.174 1.00 69.57  ? 205 ASP B OD1 1 
ATOM   2656 O  OD2 . ASP B 2 31  ? -26.590 -20.291 -37.852 1.00 69.57  ? 205 ASP B OD2 1 
ATOM   2657 N  N   . ILE B 2 32  ? -25.181 -15.627 -37.290 1.00 55.45  ? 206 ILE B N   1 
ATOM   2658 C  CA  . ILE B 2 32  ? -25.237 -15.160 -35.903 1.00 55.52  ? 206 ILE B CA  1 
ATOM   2659 C  C   . ILE B 2 32  ? -25.356 -13.636 -35.877 1.00 50.87  ? 206 ILE B C   1 
ATOM   2660 O  O   . ILE B 2 32  ? -25.030 -12.989 -36.868 1.00 52.07  ? 206 ILE B O   1 
ATOM   2661 C  CB  . ILE B 2 32  ? -24.020 -15.643 -35.079 1.00 60.74  ? 206 ILE B CB  1 
ATOM   2662 C  CG1 . ILE B 2 32  ? -22.705 -15.070 -35.610 1.00 62.60  ? 206 ILE B CG1 1 
ATOM   2663 C  CG2 . ILE B 2 32  ? -23.978 -17.166 -34.993 1.00 60.58  ? 206 ILE B CG2 1 
ATOM   2664 C  CD1 . ILE B 2 32  ? -21.516 -15.371 -34.740 1.00 65.89  ? 206 ILE B CD1 1 
ATOM   2665 N  N   . THR B 2 33  ? -25.756 -13.096 -34.710 1.00 50.67  ? 207 THR B N   1 
ATOM   2666 C  CA  . THR B 2 33  ? -26.179 -11.709 -34.517 1.00 53.76  ? 207 THR B CA  1 
ATOM   2667 C  C   . THR B 2 33  ? -25.678 -11.183 -33.163 1.00 51.06  ? 207 THR B C   1 
ATOM   2668 O  O   . THR B 2 33  ? -25.378 -11.979 -32.266 1.00 47.12  ? 207 THR B O   1 
ATOM   2669 C  CB  . THR B 2 33  ? -27.718 -11.579 -34.558 1.00 57.41  ? 207 THR B CB  1 
ATOM   2670 O  OG1 . THR B 2 33  ? -28.295 -12.534 -33.664 1.00 61.13  ? 207 THR B OG1 1 
ATOM   2671 C  CG2 . THR B 2 33  ? -28.320 -11.791 -35.932 1.00 54.22  ? 207 THR B CG2 1 
ATOM   2672 N  N   . ASN B 2 34  ? -25.651 -9.844  -33.008 1.00 44.88  ? 208 ASN B N   1 
ATOM   2673 C  CA  . ASN B 2 34  ? -25.323 -9.183  -31.749 1.00 42.27  ? 208 ASN B CA  1 
ATOM   2674 C  C   . ASN B 2 34  ? -26.139 -9.768  -30.601 1.00 40.45  ? 208 ASN B C   1 
ATOM   2675 O  O   . ASN B 2 34  ? -25.640 -9.912  -29.491 1.00 41.77  ? 208 ASN B O   1 
ATOM   2676 C  CB  . ASN B 2 34  ? -25.579 -7.677  -31.781 1.00 46.60  ? 208 ASN B CB  1 
ATOM   2677 C  CG  . ASN B 2 34  ? -24.688 -6.904  -32.730 1.00 49.19  ? 208 ASN B CG  1 
ATOM   2678 O  OD1 . ASN B 2 34  ? -23.595 -7.343  -33.089 1.00 54.67  ? 208 ASN B OD1 1 
ATOM   2679 N  ND2 . ASN B 2 34  ? -25.133 -5.710  -33.088 1.00 52.82  ? 208 ASN B ND2 1 
ATOM   2680 N  N   . SER B 2 35  ? -27.398 -10.104 -30.874 1.00 44.67  ? 209 SER B N   1 
ATOM   2681 C  CA  A SER B 2 35  ? -28.299 -10.603 -29.844 0.50 44.31  ? 209 SER B CA  1 
ATOM   2682 C  CA  B SER B 2 35  ? -28.315 -10.618 -29.868 0.50 47.33  ? 209 SER B CA  1 
ATOM   2683 C  C   . SER B 2 35  ? -27.849 -11.995 -29.392 1.00 46.53  ? 209 SER B C   1 
ATOM   2684 O  O   . SER B 2 35  ? -27.902 -12.308 -28.208 1.00 52.55  ? 209 SER B O   1 
ATOM   2685 C  CB  A SER B 2 35  ? -29.749 -10.567 -30.312 0.50 42.81  ? 209 SER B CB  1 
ATOM   2686 C  CB  B SER B 2 35  ? -29.734 -10.650 -30.413 0.50 49.36  ? 209 SER B CB  1 
ATOM   2687 O  OG  A SER B 2 35  ? -30.552 -11.486 -29.583 0.50 38.17  ? 209 SER B OG  1 
ATOM   2688 O  OG  B SER B 2 35  ? -29.779 -11.288 -31.687 0.50 50.53  ? 209 SER B OG  1 
ATOM   2689 N  N   . MET B 2 36  ? -27.383 -12.826 -30.326 1.00 48.62  ? 210 MET B N   1 
ATOM   2690 C  CA  . MET B 2 36  ? -26.902 -14.161 -29.994 1.00 50.21  ? 210 MET B CA  1 
ATOM   2691 C  C   . MET B 2 36  ? -25.585 -14.091 -29.214 1.00 48.58  ? 210 MET B C   1 
ATOM   2692 O  O   . MET B 2 36  ? -25.321 -14.946 -28.375 1.00 44.45  ? 210 MET B O   1 
ATOM   2693 C  CB  . MET B 2 36  ? -26.647 -14.964 -31.271 1.00 52.94  ? 210 MET B CB  1 
ATOM   2694 C  CG  . MET B 2 36  ? -27.880 -15.197 -32.091 1.00 52.38  ? 210 MET B CG  1 
ATOM   2695 S  SD  . MET B 2 36  ? -27.543 -16.464 -33.321 1.00 57.52  ? 210 MET B SD  1 
ATOM   2696 C  CE  . MET B 2 36  ? -29.058 -16.336 -34.269 1.00 65.94  ? 210 MET B CE  1 
ATOM   2697 N  N   . ARG B 2 37  ? -24.735 -13.111 -29.549 1.00 47.38  ? 211 ARG B N   1 
ATOM   2698 C  CA  . ARG B 2 37  ? -23.491 -12.868 -28.837 1.00 50.54  ? 211 ARG B CA  1 
ATOM   2699 C  C   . ARG B 2 37  ? -23.813 -12.504 -27.383 1.00 50.64  ? 211 ARG B C   1 
ATOM   2700 O  O   . ARG B 2 37  ? -23.239 -13.077 -26.456 1.00 48.67  ? 211 ARG B O   1 
ATOM   2701 C  CB  . ARG B 2 37  ? -22.705 -11.766 -29.554 1.00 50.15  ? 211 ARG B CB  1 
ATOM   2702 C  CG  . ARG B 2 37  ? -21.254 -11.621 -29.111 1.00 51.76  ? 211 ARG B CG  1 
ATOM   2703 C  CD  . ARG B 2 37  ? -20.615 -10.411 -29.765 1.00 49.95  ? 211 ARG B CD  1 
ATOM   2704 N  NE  . ARG B 2 37  ? -19.507 -9.909  -28.974 1.00 54.09  ? 211 ARG B NE  1 
ATOM   2705 C  CZ  . ARG B 2 37  ? -19.617 -9.269  -27.815 1.00 54.31  ? 211 ARG B CZ  1 
ATOM   2706 N  NH1 . ARG B 2 37  ? -20.803 -9.005  -27.297 1.00 54.28  ? 211 ARG B NH1 1 
ATOM   2707 N  NH2 . ARG B 2 37  ? -18.526 -8.896  -27.169 1.00 54.15  ? 211 ARG B NH2 1 
ATOM   2708 N  N   . ALA B 2 38  ? -24.760 -11.573 -27.190 1.00 47.00  ? 212 ALA B N   1 
ATOM   2709 C  CA  . ALA B 2 38  ? -25.216 -11.164 -25.862 1.00 47.02  ? 212 ALA B CA  1 
ATOM   2710 C  C   . ALA B 2 38  ? -25.604 -12.365 -25.001 1.00 41.42  ? 212 ALA B C   1 
ATOM   2711 O  O   . ALA B 2 38  ? -25.238 -12.426 -23.832 1.00 40.54  ? 212 ALA B O   1 
ATOM   2712 C  CB  . ALA B 2 38  ? -26.379 -10.205 -25.963 1.00 48.30  ? 212 ALA B CB  1 
ATOM   2713 N  N   . ILE B 2 39  ? -26.375 -13.299 -25.560 1.00 39.23  ? 213 ILE B N   1 
ATOM   2714 C  CA  . ILE B 2 39  ? -26.807 -14.466 -24.805 1.00 40.63  ? 213 ILE B CA  1 
ATOM   2715 C  C   . ILE B 2 39  ? -25.571 -15.261 -24.373 1.00 39.06  ? 213 ILE B C   1 
ATOM   2716 O  O   . ILE B 2 39  ? -25.467 -15.632 -23.204 1.00 38.72  ? 213 ILE B O   1 
ATOM   2717 C  CB  . ILE B 2 39  ? -27.820 -15.295 -25.619 1.00 43.19  ? 213 ILE B CB  1 
ATOM   2718 C  CG1 . ILE B 2 39  ? -29.169 -14.582 -25.717 1.00 45.57  ? 213 ILE B CG1 1 
ATOM   2719 C  CG2 . ILE B 2 39  ? -27.976 -16.706 -25.062 1.00 45.35  ? 213 ILE B CG2 1 
ATOM   2720 C  CD1 . ILE B 2 39  ? -30.073 -15.113 -26.833 1.00 50.59  ? 213 ILE B CD1 1 
ATOM   2721 N  N   . LEU B 2 40  ? -24.632 -15.484 -25.306 1.00 40.78  ? 214 LEU B N   1 
ATOM   2722 C  CA  . LEU B 2 40  ? -23.370 -16.170 -25.032 1.00 40.97  ? 214 LEU B CA  1 
ATOM   2723 C  C   . LEU B 2 40  ? -22.601 -15.525 -23.864 1.00 38.87  ? 214 LEU B C   1 
ATOM   2724 O  O   . LEU B 2 40  ? -22.272 -16.191 -22.884 1.00 42.05  ? 214 LEU B O   1 
ATOM   2725 C  CB  . LEU B 2 40  ? -22.523 -16.204 -26.315 1.00 40.91  ? 214 LEU B CB  1 
ATOM   2726 C  CG  . LEU B 2 40  ? -21.233 -17.017 -26.220 1.00 39.81  ? 214 LEU B CG  1 
ATOM   2727 C  CD1 . LEU B 2 40  ? -21.524 -18.496 -25.986 1.00 40.15  ? 214 LEU B CD1 1 
ATOM   2728 C  CD2 . LEU B 2 40  ? -20.372 -16.831 -27.449 1.00 39.45  ? 214 LEU B CD2 1 
ATOM   2729 N  N   . VAL B 2 41  ? -22.290 -14.232 -23.950 1.00 38.00  ? 215 VAL B N   1 
ATOM   2730 C  CA  . VAL B 2 41  ? -21.453 -13.573 -22.950 1.00 40.20  ? 215 VAL B CA  1 
ATOM   2731 C  C   . VAL B 2 41  ? -22.108 -13.633 -21.571 1.00 41.91  ? 215 VAL B C   1 
ATOM   2732 O  O   . VAL B 2 41  ? -21.481 -13.994 -20.575 1.00 40.14  ? 215 VAL B O   1 
ATOM   2733 C  CB  . VAL B 2 41  ? -21.167 -12.114 -23.342 1.00 42.89  ? 215 VAL B CB  1 
ATOM   2734 C  CG1 . VAL B 2 41  ? -20.438 -11.383 -22.220 1.00 45.77  ? 215 VAL B CG1 1 
ATOM   2735 C  CG2 . VAL B 2 41  ? -20.389 -12.021 -24.650 1.00 42.40  ? 215 VAL B CG2 1 
ATOM   2736 N  N   . ASP B 2 42  ? -23.374 -13.221 -21.532 1.00 43.69  ? 216 ASP B N   1 
ATOM   2737 C  CA  . ASP B 2 42  ? -24.226 -13.395 -20.373 1.00 39.74  ? 216 ASP B CA  1 
ATOM   2738 C  C   . ASP B 2 42  ? -24.105 -14.815 -19.810 1.00 38.98  ? 216 ASP B C   1 
ATOM   2739 O  O   . ASP B 2 42  ? -23.930 -14.992 -18.602 1.00 43.61  ? 216 ASP B O   1 
ATOM   2740 C  CB  . ASP B 2 42  ? -25.670 -13.042 -20.714 1.00 42.39  ? 216 ASP B CB  1 
ATOM   2741 C  CG  . ASP B 2 42  ? -26.576 -13.235 -19.511 1.00 45.40  ? 216 ASP B CG  1 
ATOM   2742 O  OD1 . ASP B 2 42  ? -26.663 -12.297 -18.683 1.00 41.65  ? 216 ASP B OD1 1 
ATOM   2743 O  OD2 . ASP B 2 42  ? -27.091 -14.365 -19.358 1.00 49.08  ? 216 ASP B OD2 1 
ATOM   2744 N  N   . TRP B 2 43  ? -24.203 -15.844 -20.652 1.00 34.17  ? 217 TRP B N   1 
ATOM   2745 C  CA  . TRP B 2 43  ? -24.036 -17.205 -20.150 1.00 35.59  ? 217 TRP B CA  1 
ATOM   2746 C  C   . TRP B 2 43  ? -22.631 -17.382 -19.567 1.00 41.17  ? 217 TRP B C   1 
ATOM   2747 O  O   . TRP B 2 43  ? -22.463 -17.991 -18.510 1.00 45.75  ? 217 TRP B O   1 
ATOM   2748 C  CB  . TRP B 2 43  ? -24.349 -18.245 -21.229 1.00 34.57  ? 217 TRP B CB  1 
ATOM   2749 C  CG  . TRP B 2 43  ? -23.958 -19.643 -20.867 1.00 40.18  ? 217 TRP B CG  1 
ATOM   2750 C  CD1 . TRP B 2 43  ? -24.574 -20.490 -19.990 1.00 42.90  ? 217 TRP B CD1 1 
ATOM   2751 C  CD2 . TRP B 2 43  ? -22.811 -20.355 -21.369 1.00 44.48  ? 217 TRP B CD2 1 
ATOM   2752 N  NE1 . TRP B 2 43  ? -23.894 -21.682 -19.922 1.00 42.53  ? 217 TRP B NE1 1 
ATOM   2753 C  CE2 . TRP B 2 43  ? -22.830 -21.639 -20.781 1.00 41.43  ? 217 TRP B CE2 1 
ATOM   2754 C  CE3 . TRP B 2 43  ? -21.800 -20.042 -22.289 1.00 43.51  ? 217 TRP B CE3 1 
ATOM   2755 C  CZ2 . TRP B 2 43  ? -21.859 -22.595 -21.061 1.00 44.85  ? 217 TRP B CZ2 1 
ATOM   2756 C  CZ3 . TRP B 2 43  ? -20.842 -20.992 -22.568 1.00 45.09  ? 217 TRP B CZ3 1 
ATOM   2757 C  CH2 . TRP B 2 43  ? -20.873 -22.247 -21.957 1.00 46.25  ? 217 TRP B CH2 1 
ATOM   2758 N  N   . LEU B 2 44  ? -21.614 -16.831 -20.241 1.00 41.61  ? 218 LEU B N   1 
ATOM   2759 C  CA  . LEU B 2 44  ? -20.248 -16.928 -19.737 1.00 44.25  ? 218 LEU B CA  1 
ATOM   2760 C  C   . LEU B 2 44  ? -20.117 -16.265 -18.366 1.00 42.60  ? 218 LEU B C   1 
ATOM   2761 O  O   . LEU B 2 44  ? -19.308 -16.709 -17.555 1.00 42.31  ? 218 LEU B O   1 
ATOM   2762 C  CB  . LEU B 2 44  ? -19.246 -16.338 -20.740 1.00 45.45  ? 218 LEU B CB  1 
ATOM   2763 C  CG  . LEU B 2 44  ? -19.068 -17.150 -22.020 1.00 50.64  ? 218 LEU B CG  1 
ATOM   2764 C  CD1 . LEU B 2 44  ? -18.178 -16.417 -23.015 1.00 53.35  ? 218 LEU B CD1 1 
ATOM   2765 C  CD2 . LEU B 2 44  ? -18.520 -18.545 -21.729 1.00 54.34  ? 218 LEU B CD2 1 
ATOM   2766 N  N   . VAL B 2 45  ? -20.903 -15.219 -18.086 1.00 43.08  ? 219 VAL B N   1 
ATOM   2767 C  CA  . VAL B 2 45  ? -20.856 -14.595 -16.765 1.00 42.27  ? 219 VAL B CA  1 
ATOM   2768 C  C   . VAL B 2 45  ? -21.314 -15.599 -15.706 1.00 41.62  ? 219 VAL B C   1 
ATOM   2769 O  O   . VAL B 2 45  ? -20.661 -15.731 -14.680 1.00 44.39  ? 219 VAL B O   1 
ATOM   2770 C  CB  . VAL B 2 45  ? -21.689 -13.304 -16.720 1.00 41.71  ? 219 VAL B CB  1 
ATOM   2771 C  CG1 . VAL B 2 45  ? -21.855 -12.778 -15.302 1.00 44.83  ? 219 VAL B CG1 1 
ATOM   2772 C  CG2 . VAL B 2 45  ? -21.090 -12.249 -17.635 1.00 40.15  ? 219 VAL B CG2 1 
ATOM   2773 N  N   . GLU B 2 46  ? -22.394 -16.337 -15.988 1.00 45.18  ? 220 GLU B N   1 
ATOM   2774 C  CA  . GLU B 2 46  ? -22.938 -17.349 -15.087 1.00 49.63  ? 220 GLU B CA  1 
ATOM   2775 C  C   . GLU B 2 46  ? -21.880 -18.430 -14.847 1.00 45.54  ? 220 GLU B C   1 
ATOM   2776 O  O   . GLU B 2 46  ? -21.746 -18.889 -13.718 1.00 43.92  ? 220 GLU B O   1 
ATOM   2777 C  CB  . GLU B 2 46  ? -24.244 -17.961 -15.621 1.00 58.74  ? 220 GLU B CB  1 
ATOM   2778 C  CG  . GLU B 2 46  ? -25.423 -16.982 -15.691 1.00 73.65  ? 220 GLU B CG  1 
ATOM   2779 C  CD  . GLU B 2 46  ? -26.623 -17.358 -16.565 1.00 84.75  ? 220 GLU B CD  1 
ATOM   2780 O  OE1 . GLU B 2 46  ? -26.458 -17.493 -17.807 1.00 84.95  ? 220 GLU B OE1 1 
ATOM   2781 O  OE2 . GLU B 2 46  ? -27.745 -17.473 -16.011 1.00 86.92  ? 220 GLU B OE2 1 
ATOM   2782 N  N   . VAL B 2 47  ? -21.151 -18.847 -15.899 1.00 43.60  ? 221 VAL B N   1 
ATOM   2783 C  CA  . VAL B 2 47  ? -20.102 -19.862 -15.781 1.00 42.50  ? 221 VAL B CA  1 
ATOM   2784 C  C   . VAL B 2 47  ? -19.012 -19.373 -14.820 1.00 42.98  ? 221 VAL B C   1 
ATOM   2785 O  O   . VAL B 2 47  ? -18.523 -20.137 -13.988 1.00 41.59  ? 221 VAL B O   1 
ATOM   2786 C  CB  . VAL B 2 47  ? -19.506 -20.232 -17.156 1.00 45.12  ? 221 VAL B CB  1 
ATOM   2787 C  CG1 . VAL B 2 47  ? -18.221 -21.052 -17.052 1.00 44.32  ? 221 VAL B CG1 1 
ATOM   2788 C  CG2 . VAL B 2 47  ? -20.527 -20.954 -18.022 1.00 47.90  ? 221 VAL B CG2 1 
ATOM   2789 N  N   . GLY B 2 48  ? -18.641 -18.094 -14.926 1.00 43.78  ? 222 GLY B N   1 
ATOM   2790 C  CA  . GLY B 2 48  ? -17.639 -17.497 -14.055 1.00 47.57  ? 222 GLY B CA  1 
ATOM   2791 C  C   . GLY B 2 48  ? -18.051 -17.526 -12.585 1.00 50.59  ? 222 GLY B C   1 
ATOM   2792 O  O   . GLY B 2 48  ? -17.241 -17.870 -11.724 1.00 53.37  ? 222 GLY B O   1 
ATOM   2793 N  N   . GLU B 2 49  ? -19.306 -17.151 -12.308 1.00 49.66  ? 223 GLU B N   1 
ATOM   2794 C  CA  . GLU B 2 49  ? -19.861 -17.196 -10.962 1.00 52.02  ? 223 GLU B CA  1 
ATOM   2795 C  C   . GLU B 2 49  ? -19.871 -18.621 -10.410 1.00 51.88  ? 223 GLU B C   1 
ATOM   2796 O  O   . GLU B 2 49  ? -19.439 -18.827 -9.279  1.00 60.09  ? 223 GLU B O   1 
ATOM   2797 C  CB  . GLU B 2 49  ? -21.265 -16.592 -10.952 1.00 62.05  ? 223 GLU B CB  1 
ATOM   2798 C  CG  . GLU B 2 49  ? -21.253 -15.092 -11.162 1.00 65.64  ? 223 GLU B CG  1 
ATOM   2799 C  CD  . GLU B 2 49  ? -20.185 -14.416 -10.320 1.00 77.42  ? 223 GLU B CD  1 
ATOM   2800 O  OE1 . GLU B 2 49  ? -20.429 -14.193 -9.108  1.00 83.81  ? 223 GLU B OE1 1 
ATOM   2801 O  OE2 . GLU B 2 49  ? -19.081 -14.177 -10.868 1.00 83.70  ? 223 GLU B OE2 1 
ATOM   2802 N  N   . GLU B 2 50  ? -20.360 -19.598 -11.187 1.00 48.91  ? 224 GLU B N   1 
ATOM   2803 C  CA  . GLU B 2 50  ? -20.460 -20.972 -10.699 1.00 53.46  ? 224 GLU B CA  1 
ATOM   2804 C  C   . GLU B 2 50  ? -19.078 -21.509 -10.308 1.00 53.17  ? 224 GLU B C   1 
ATOM   2805 O  O   . GLU B 2 50  ? -18.988 -22.195 -9.295  1.00 52.39  ? 224 GLU B O   1 
ATOM   2806 C  CB  . GLU B 2 50  ? -21.155 -21.906 -11.701 1.00 56.00  ? 224 GLU B CB  1 
ATOM   2807 C  CG  . GLU B 2 50  ? -21.650 -23.229 -11.091 1.00 66.04  ? 224 GLU B CG  1 
ATOM   2808 C  CD  . GLU B 2 50  ? -22.773 -23.170 -10.053 1.00 78.21  ? 224 GLU B CD  1 
ATOM   2809 O  OE1 . GLU B 2 50  ? -23.537 -22.169 -10.046 1.00 72.16  ? 224 GLU B OE1 1 
ATOM   2810 O  OE2 . GLU B 2 50  ? -22.883 -24.129 -9.232  1.00 85.65  ? 224 GLU B OE2 1 
ATOM   2811 N  N   . TYR B 2 51  ? -18.021 -21.190 -11.085 1.00 50.45  ? 225 TYR B N   1 
ATOM   2812 C  CA  . TYR B 2 51  ? -16.677 -21.745 -10.904 1.00 52.16  ? 225 TYR B CA  1 
ATOM   2813 C  C   . TYR B 2 51  ? -15.711 -20.775 -10.221 1.00 50.25  ? 225 TYR B C   1 
ATOM   2814 O  O   . TYR B 2 51  ? -14.514 -21.054 -10.150 1.00 50.54  ? 225 TYR B O   1 
ATOM   2815 C  CB  . TYR B 2 51  ? -16.097 -22.206 -12.244 1.00 53.48  ? 225 TYR B CB  1 
ATOM   2816 C  CG  . TYR B 2 51  ? -16.711 -23.503 -12.686 1.00 56.60  ? 225 TYR B CG  1 
ATOM   2817 C  CD1 . TYR B 2 51  ? -16.423 -24.680 -12.016 1.00 56.77  ? 225 TYR B CD1 1 
ATOM   2818 C  CD2 . TYR B 2 51  ? -17.644 -23.535 -13.702 1.00 59.64  ? 225 TYR B CD2 1 
ATOM   2819 C  CE1 . TYR B 2 51  ? -17.021 -25.873 -12.371 1.00 61.88  ? 225 TYR B CE1 1 
ATOM   2820 C  CE2 . TYR B 2 51  ? -18.248 -24.721 -14.076 1.00 64.23  ? 225 TYR B CE2 1 
ATOM   2821 C  CZ  . TYR B 2 51  ? -17.944 -25.889 -13.402 1.00 63.92  ? 225 TYR B CZ  1 
ATOM   2822 O  OH  . TYR B 2 51  ? -18.553 -27.051 -13.791 1.00 67.61  ? 225 TYR B OH  1 
ATOM   2823 N  N   . LYS B 2 52  ? -16.237 -19.652 -9.719  1.00 50.50  ? 226 LYS B N   1 
ATOM   2824 C  CA  . LYS B 2 52  ? -15.474 -18.690 -8.931  1.00 54.59  ? 226 LYS B CA  1 
ATOM   2825 C  C   . LYS B 2 52  ? -14.197 -18.281 -9.669  1.00 46.22  ? 226 LYS B C   1 
ATOM   2826 O  O   . LYS B 2 52  ? -13.149 -18.170 -9.053  1.00 50.43  ? 226 LYS B O   1 
ATOM   2827 C  CB  . LYS B 2 52  ? -15.210 -19.246 -7.524  1.00 58.31  ? 226 LYS B CB  1 
ATOM   2828 C  CG  . LYS B 2 52  ? -16.411 -19.157 -6.587  1.00 66.91  ? 226 LYS B CG  1 
ATOM   2829 C  CD  . LYS B 2 52  ? -16.449 -20.196 -5.481  1.00 76.36  ? 226 LYS B CD  1 
ATOM   2830 C  CE  . LYS B 2 52  ? -17.836 -20.367 -4.894  1.00 86.84  ? 226 LYS B CE  1 
ATOM   2831 N  NZ  . LYS B 2 52  ? -17.798 -20.998 -3.554  1.00 91.57  ? 226 LYS B NZ  1 
ATOM   2832 N  N   . LEU B 2 53  ? -14.322 -17.991 -10.967 1.00 42.01  ? 227 LEU B N   1 
ATOM   2833 C  CA  . LEU B 2 53  ? -13.231 -17.504 -11.807 1.00 44.53  ? 227 LEU B CA  1 
ATOM   2834 C  C   . LEU B 2 53  ? -13.126 -15.985 -11.697 1.00 44.12  ? 227 LEU B C   1 
ATOM   2835 O  O   . LEU B 2 53  ? -14.127 -15.329 -11.433 1.00 47.88  ? 227 LEU B O   1 
ATOM   2836 C  CB  . LEU B 2 53  ? -13.508 -17.878 -13.267 1.00 45.75  ? 227 LEU B CB  1 
ATOM   2837 C  CG  . LEU B 2 53  ? -13.837 -19.342 -13.537 1.00 46.41  ? 227 LEU B CG  1 
ATOM   2838 C  CD1 . LEU B 2 53  ? -14.067 -19.552 -15.024 1.00 50.29  ? 227 LEU B CD1 1 
ATOM   2839 C  CD2 . LEU B 2 53  ? -12.740 -20.263 -13.020 1.00 45.09  ? 227 LEU B CD2 1 
ATOM   2840 N  N   . GLN B 2 54  ? -11.926 -15.445 -11.963 1.00 46.22  ? 228 GLN B N   1 
ATOM   2841 C  CA  . GLN B 2 54  ? -11.639 -14.011 -11.931 1.00 44.54  ? 228 GLN B CA  1 
ATOM   2842 C  C   . GLN B 2 54  ? -12.420 -13.254 -13.006 1.00 42.10  ? 228 GLN B C   1 
ATOM   2843 O  O   . GLN B 2 54  ? -12.678 -13.791 -14.079 1.00 43.05  ? 228 GLN B O   1 
ATOM   2844 C  CB  . GLN B 2 54  ? -10.153 -13.762 -12.224 1.00 51.29  ? 228 GLN B CB  1 
ATOM   2845 C  CG  . GLN B 2 54  ? -9.188  -14.427 -11.256 1.00 51.65  ? 228 GLN B CG  1 
ATOM   2846 C  CD  . GLN B 2 54  ? -9.377  -13.901 -9.855  1.00 51.06  ? 228 GLN B CD  1 
ATOM   2847 O  OE1 . GLN B 2 54  ? -9.314  -12.697 -9.609  1.00 48.76  ? 228 GLN B OE1 1 
ATOM   2848 N  NE2 . GLN B 2 54  ? -9.654  -14.807 -8.932  1.00 54.27  ? 228 GLN B NE2 1 
ATOM   2849 N  N   . ASN B 2 55  ? -12.733 -11.982 -12.734 1.00 45.17  ? 229 ASN B N   1 
ATOM   2850 C  CA  . ASN B 2 55  ? -13.252 -11.045 -13.726 1.00 48.29  ? 229 ASN B CA  1 
ATOM   2851 C  C   . ASN B 2 55  ? -12.385 -11.091 -14.990 1.00 49.12  ? 229 ASN B C   1 
ATOM   2852 O  O   . ASN B 2 55  ? -12.925 -11.164 -16.088 1.00 53.37  ? 229 ASN B O   1 
ATOM   2853 C  CB  . ASN B 2 55  ? -13.371 -9.608  -13.177 1.00 58.08  ? 229 ASN B CB  1 
ATOM   2854 C  CG  . ASN B 2 55  ? -14.547 -9.373  -12.239 1.00 67.42  ? 229 ASN B CG  1 
ATOM   2855 O  OD1 . ASN B 2 55  ? -15.361 -10.270 -12.011 1.00 63.79  ? 229 ASN B OD1 1 
ATOM   2856 N  ND2 . ASN B 2 55  ? -14.632 -8.178  -11.666 1.00 73.41  ? 229 ASN B ND2 1 
ATOM   2857 N  N   . GLU B 2 56  ? -11.050 -11.043 -14.844 1.00 47.75  ? 230 GLU B N   1 
ATOM   2858 C  CA  . GLU B 2 56  ? -10.121 -11.010 -15.975 1.00 45.45  ? 230 GLU B CA  1 
ATOM   2859 C  C   . GLU B 2 56  ? -10.386 -12.153 -16.970 1.00 40.29  ? 230 GLU B C   1 
ATOM   2860 O  O   . GLU B 2 56  ? -10.402 -11.946 -18.184 1.00 40.96  ? 230 GLU B O   1 
ATOM   2861 C  CB  . GLU B 2 56  ? -8.667  -11.062 -15.481 1.00 47.88  ? 230 GLU B CB  1 
ATOM   2862 C  CG  . GLU B 2 56  ? -7.619  -10.975 -16.590 1.00 48.61  ? 230 GLU B CG  1 
ATOM   2863 C  CD  . GLU B 2 56  ? -7.534  -9.658  -17.353 1.00 55.32  ? 230 GLU B CD  1 
ATOM   2864 O  OE1 . GLU B 2 56  ? -8.332  -8.738  -17.072 1.00 53.48  ? 230 GLU B OE1 1 
ATOM   2865 O  OE2 . GLU B 2 56  ? -6.645  -9.547  -18.223 1.00 71.08  ? 230 GLU B OE2 1 
ATOM   2866 N  N   . THR B 2 57  ? -10.559 -13.373 -16.462 1.00 36.77  ? 231 THR B N   1 
ATOM   2867 C  CA  . THR B 2 57  ? -10.787 -14.549 -17.288 1.00 35.78  ? 231 THR B CA  1 
ATOM   2868 C  C   . THR B 2 57  ? -11.970 -14.336 -18.226 1.00 34.74  ? 231 THR B C   1 
ATOM   2869 O  O   . THR B 2 57  ? -11.930 -14.743 -19.378 1.00 42.58  ? 231 THR B O   1 
ATOM   2870 C  CB  . THR B 2 57  ? -11.027 -15.775 -16.404 1.00 37.32  ? 231 THR B CB  1 
ATOM   2871 O  OG1 . THR B 2 57  ? -9.916  -15.848 -15.504 1.00 38.57  ? 231 THR B OG1 1 
ATOM   2872 C  CG2 . THR B 2 57  ? -11.206 -17.057 -17.190 1.00 36.86  ? 231 THR B CG2 1 
ATOM   2873 N  N   . LEU B 2 58  ? -13.026 -13.701 -17.734 1.00 39.78  ? 232 LEU B N   1 
ATOM   2874 C  CA  . LEU B 2 58  ? -14.227 -13.470 -18.526 1.00 40.20  ? 232 LEU B CA  1 
ATOM   2875 C  C   . LEU B 2 58  ? -13.934 -12.447 -19.623 1.00 38.14  ? 232 LEU B C   1 
ATOM   2876 O  O   . LEU B 2 58  ? -14.334 -12.658 -20.758 1.00 39.12  ? 232 LEU B O   1 
ATOM   2877 C  CB  . LEU B 2 58  ? -15.357 -13.012 -17.593 1.00 46.16  ? 232 LEU B CB  1 
ATOM   2878 C  CG  . LEU B 2 58  ? -16.579 -12.375 -18.256 1.00 49.33  ? 232 LEU B CG  1 
ATOM   2879 C  CD1 . LEU B 2 58  ? -17.432 -13.423 -18.962 1.00 47.93  ? 232 LEU B CD1 1 
ATOM   2880 C  CD2 . LEU B 2 58  ? -17.393 -11.621 -17.211 1.00 50.48  ? 232 LEU B CD2 1 
ATOM   2881 N  N   . HIS B 2 59  ? -13.242 -11.343 -19.295 1.00 38.83  ? 233 HIS B N   1 
ATOM   2882 C  CA  . HIS B 2 59  ? -12.892 -10.321 -20.277 1.00 37.27  ? 233 HIS B CA  1 
ATOM   2883 C  C   . HIS B 2 59  ? -11.975 -10.885 -21.371 1.00 36.11  ? 233 HIS B C   1 
ATOM   2884 O  O   . HIS B 2 59  ? -12.127 -10.531 -22.528 1.00 39.23  ? 233 HIS B O   1 
ATOM   2885 C  CB  . HIS B 2 59  ? -12.247 -9.101  -19.613 1.00 36.87  ? 233 HIS B CB  1 
ATOM   2886 C  CG  . HIS B 2 59  ? -13.171 -8.240  -18.834 1.00 39.60  ? 233 HIS B CG  1 
ATOM   2887 N  ND1 . HIS B 2 59  ? -13.380 -6.917  -19.156 1.00 40.95  ? 233 HIS B ND1 1 
ATOM   2888 C  CD2 . HIS B 2 59  ? -13.896 -8.479  -17.725 1.00 43.33  ? 233 HIS B CD2 1 
ATOM   2889 C  CE1 . HIS B 2 59  ? -14.221 -6.387  -18.275 1.00 41.36  ? 233 HIS B CE1 1 
ATOM   2890 N  NE2 . HIS B 2 59  ? -14.552 -7.323  -17.404 1.00 44.09  ? 233 HIS B NE2 1 
ATOM   2891 N  N   . LEU B 2 60  ? -11.034 -11.775 -21.033 1.00 39.03  ? 234 LEU B N   1 
ATOM   2892 C  CA  . LEU B 2 60  ? -10.165 -12.386 -22.041 1.00 37.76  ? 234 LEU B CA  1 
ATOM   2893 C  C   . LEU B 2 60  ? -10.969 -13.296 -22.975 1.00 36.84  ? 234 LEU B C   1 
ATOM   2894 O  O   . LEU B 2 60  ? -10.738 -13.284 -24.183 1.00 38.49  ? 234 LEU B O   1 
ATOM   2895 C  CB  . LEU B 2 60  ? -9.037  -13.193 -21.385 1.00 37.82  ? 234 LEU B CB  1 
ATOM   2896 C  CG  . LEU B 2 60  ? -7.884  -12.404 -20.754 1.00 40.12  ? 234 LEU B CG  1 
ATOM   2897 C  CD1 . LEU B 2 60  ? -7.046  -13.316 -19.868 1.00 40.36  ? 234 LEU B CD1 1 
ATOM   2898 C  CD2 . LEU B 2 60  ? -6.996  -11.755 -21.803 1.00 39.65  ? 234 LEU B CD2 1 
ATOM   2899 N  N   . ALA B 2 61  ? -11.847 -14.132 -22.409 1.00 35.34  ? 235 ALA B N   1 
ATOM   2900 C  CA  . ALA B 2 61  ? -12.654 -15.062 -23.186 1.00 36.78  ? 235 ALA B CA  1 
ATOM   2901 C  C   . ALA B 2 61  ? -13.406 -14.293 -24.265 1.00 35.02  ? 235 ALA B C   1 
ATOM   2902 O  O   . ALA B 2 61  ? -13.421 -14.669 -25.439 1.00 33.19  ? 235 ALA B O   1 
ATOM   2903 C  CB  . ALA B 2 61  ? -13.621 -15.777 -22.282 1.00 39.58  ? 235 ALA B CB  1 
ATOM   2904 N  N   . VAL B 2 62  ? -13.984 -13.175 -23.843 1.00 33.73  ? 236 VAL B N   1 
ATOM   2905 C  CA  . VAL B 2 62  ? -14.757 -12.339 -24.745 1.00 38.97  ? 236 VAL B CA  1 
ATOM   2906 C  C   . VAL B 2 62  ? -13.850 -11.780 -25.844 1.00 37.54  ? 236 VAL B C   1 
ATOM   2907 O  O   . VAL B 2 62  ? -14.246 -11.747 -26.995 1.00 41.62  ? 236 VAL B O   1 
ATOM   2908 C  CB  . VAL B 2 62  ? -15.488 -11.244 -23.949 1.00 38.53  ? 236 VAL B CB  1 
ATOM   2909 C  CG1 . VAL B 2 62  ? -16.079 -10.166 -24.841 1.00 40.79  ? 236 VAL B CG1 1 
ATOM   2910 C  CG2 . VAL B 2 62  ? -16.555 -11.869 -23.067 1.00 38.91  ? 236 VAL B CG2 1 
ATOM   2911 N  N   . ASN B 2 63  ? -12.648 -11.316 -25.498 1.00 39.64  ? 237 ASN B N   1 
ATOM   2912 C  CA  . ASN B 2 63  ? -11.718 -10.810 -26.500 1.00 40.50  ? 237 ASN B CA  1 
ATOM   2913 C  C   . ASN B 2 63  ? -11.365 -11.926 -27.493 1.00 42.39  ? 237 ASN B C   1 
ATOM   2914 O  O   . ASN B 2 63  ? -11.268 -11.655 -28.690 1.00 39.84  ? 237 ASN B O   1 
ATOM   2915 C  CB  . ASN B 2 63  ? -10.478 -10.185 -25.859 1.00 44.11  ? 237 ASN B CB  1 
ATOM   2916 C  CG  . ASN B 2 63  ? -9.404  -9.846  -26.868 1.00 44.42  ? 237 ASN B CG  1 
ATOM   2917 O  OD1 . ASN B 2 63  ? -8.470  -10.614 -27.051 1.00 40.25  ? 237 ASN B OD1 1 
ATOM   2918 N  ND2 . ASN B 2 63  ? -9.568  -8.742  -27.578 1.00 50.15  ? 237 ASN B ND2 1 
ATOM   2919 N  N   . TYR B 2 64  ? -11.187 -13.172 -27.008 1.00 40.23  ? 238 TYR B N   1 
ATOM   2920 C  CA  . TYR B 2 64  ? -10.855 -14.301 -27.872 1.00 39.98  ? 238 TYR B CA  1 
ATOM   2921 C  C   . TYR B 2 64  ? -12.014 -14.609 -28.826 1.00 42.27  ? 238 TYR B C   1 
ATOM   2922 O  O   . TYR B 2 64  ? -11.802 -14.803 -30.021 1.00 38.45  ? 238 TYR B O   1 
ATOM   2923 C  CB  . TYR B 2 64  ? -10.570 -15.584 -27.082 1.00 36.94  ? 238 TYR B CB  1 
ATOM   2924 C  CG  . TYR B 2 64  ? -9.422  -15.532 -26.115 1.00 35.56  ? 238 TYR B CG  1 
ATOM   2925 C  CD1 . TYR B 2 64  ? -8.495  -14.506 -26.147 1.00 37.83  ? 238 TYR B CD1 1 
ATOM   2926 C  CD2 . TYR B 2 64  ? -9.288  -16.502 -25.134 1.00 33.02  ? 238 TYR B CD2 1 
ATOM   2927 C  CE1 . TYR B 2 64  ? -7.448  -14.461 -25.241 1.00 37.45  ? 238 TYR B CE1 1 
ATOM   2928 C  CE2 . TYR B 2 64  ? -8.259  -16.456 -24.212 1.00 32.15  ? 238 TYR B CE2 1 
ATOM   2929 C  CZ  . TYR B 2 64  ? -7.326  -15.442 -24.281 1.00 31.33  ? 238 TYR B CZ  1 
ATOM   2930 O  OH  . TYR B 2 64  ? -6.319  -15.358 -23.368 1.00 36.94  ? 238 TYR B OH  1 
ATOM   2931 N  N   . ILE B 2 65  ? -13.226 -14.707 -28.270 1.00 39.58  ? 239 ILE B N   1 
ATOM   2932 C  CA  . ILE B 2 65  ? -14.424 -14.959 -29.054 1.00 41.61  ? 239 ILE B CA  1 
ATOM   2933 C  C   . ILE B 2 65  ? -14.535 -13.929 -30.179 1.00 41.72  ? 239 ILE B C   1 
ATOM   2934 O  O   . ILE B 2 65  ? -14.792 -14.315 -31.315 1.00 43.05  ? 239 ILE B O   1 
ATOM   2935 C  CB  . ILE B 2 65  ? -15.695 -14.970 -28.179 1.00 41.34  ? 239 ILE B CB  1 
ATOM   2936 C  CG1 . ILE B 2 65  ? -15.719 -16.154 -27.210 1.00 41.67  ? 239 ILE B CG1 1 
ATOM   2937 C  CG2 . ILE B 2 65  ? -16.951 -14.948 -29.039 1.00 42.36  ? 239 ILE B CG2 1 
ATOM   2938 C  CD1 . ILE B 2 65  ? -16.607 -15.916 -26.002 1.00 41.70  ? 239 ILE B CD1 1 
ATOM   2939 N  N   . ASP B 2 66  ? -14.392 -12.633 -29.867 1.00 37.33  ? 240 ASP B N   1 
ATOM   2940 C  CA  . ASP B 2 66  ? -14.633 -11.589 -30.856 1.00 36.98  ? 240 ASP B CA  1 
ATOM   2941 C  C   . ASP B 2 66  ? -13.559 -11.626 -31.954 1.00 38.52  ? 240 ASP B C   1 
ATOM   2942 O  O   . ASP B 2 66  ? -13.861 -11.399 -33.119 1.00 41.00  ? 240 ASP B O   1 
ATOM   2943 C  CB  . ASP B 2 66  ? -14.748 -10.208 -30.195 1.00 42.79  ? 240 ASP B CB  1 
ATOM   2944 C  CG  . ASP B 2 66  ? -16.045 -9.952  -29.430 1.00 47.82  ? 240 ASP B CG  1 
ATOM   2945 O  OD1 . ASP B 2 66  ? -17.103 -10.463 -29.851 1.00 50.19  ? 240 ASP B OD1 1 
ATOM   2946 O  OD2 . ASP B 2 66  ? -15.998 -9.212  -28.433 1.00 45.12  ? 240 ASP B OD2 1 
ATOM   2947 N  N   . ARG B 2 67  ? -12.300 -11.900 -31.593 1.00 40.13  ? 241 ARG B N   1 
ATOM   2948 C  CA  . ARG B 2 67  ? -11.214 -12.010 -32.561 1.00 41.95  ? 241 ARG B CA  1 
ATOM   2949 C  C   . ARG B 2 67  ? -11.434 -13.244 -33.429 1.00 40.29  ? 241 ARG B C   1 
ATOM   2950 O  O   . ARG B 2 67  ? -11.188 -13.214 -34.625 1.00 44.07  ? 241 ARG B O   1 
ATOM   2951 C  CB  . ARG B 2 67  ? -9.844  -12.066 -31.873 1.00 43.42  ? 241 ARG B CB  1 
ATOM   2952 C  CG  . ARG B 2 67  ? -9.353  -10.702 -31.408 1.00 46.11  ? 241 ARG B CG  1 
ATOM   2953 C  CD  . ARG B 2 67  ? -8.359  -10.817 -30.277 1.00 48.89  ? 241 ARG B CD  1 
ATOM   2954 N  NE  . ARG B 2 67  ? -7.197  -11.582 -30.667 1.00 49.94  ? 241 ARG B NE  1 
ATOM   2955 C  CZ  . ARG B 2 67  ? -6.356  -12.180 -29.831 1.00 51.92  ? 241 ARG B CZ  1 
ATOM   2956 N  NH1 . ARG B 2 67  ? -6.552  -12.161 -28.521 1.00 48.50  ? 241 ARG B NH1 1 
ATOM   2957 N  NH2 . ARG B 2 67  ? -5.319  -12.826 -30.332 1.00 54.02  ? 241 ARG B NH2 1 
ATOM   2958 N  N   . PHE B 2 68  ? -11.898 -14.335 -32.827 1.00 37.92  ? 242 PHE B N   1 
ATOM   2959 C  CA  . PHE B 2 68  ? -12.162 -15.548 -33.583 1.00 39.58  ? 242 PHE B CA  1 
ATOM   2960 C  C   . PHE B 2 68  ? -13.267 -15.301 -34.619 1.00 42.94  ? 242 PHE B C   1 
ATOM   2961 O  O   . PHE B 2 68  ? -13.096 -15.668 -35.779 1.00 45.94  ? 242 PHE B O   1 
ATOM   2962 C  CB  . PHE B 2 68  ? -12.507 -16.692 -32.635 1.00 37.32  ? 242 PHE B CB  1 
ATOM   2963 C  CG  . PHE B 2 68  ? -12.758 -18.006 -33.324 1.00 36.24  ? 242 PHE B CG  1 
ATOM   2964 C  CD1 . PHE B 2 68  ? -11.717 -18.868 -33.615 1.00 38.23  ? 242 PHE B CD1 1 
ATOM   2965 C  CD2 . PHE B 2 68  ? -14.045 -18.395 -33.635 1.00 37.16  ? 242 PHE B CD2 1 
ATOM   2966 C  CE1 . PHE B 2 68  ? -11.962 -20.104 -34.200 1.00 41.89  ? 242 PHE B CE1 1 
ATOM   2967 C  CE2 . PHE B 2 68  ? -14.287 -19.622 -34.231 1.00 37.86  ? 242 PHE B CE2 1 
ATOM   2968 C  CZ  . PHE B 2 68  ? -13.248 -20.469 -34.533 1.00 38.22  ? 242 PHE B CZ  1 
ATOM   2969 N  N   . LEU B 2 69  ? -14.382 -14.671 -34.212 1.00 44.32  ? 243 LEU B N   1 
ATOM   2970 C  CA  . LEU B 2 69  ? -15.537 -14.481 -35.089 1.00 42.28  ? 243 LEU B CA  1 
ATOM   2971 C  C   . LEU B 2 69  ? -15.244 -13.443 -36.173 1.00 46.15  ? 243 LEU B C   1 
ATOM   2972 O  O   . LEU B 2 69  ? -15.963 -13.389 -37.166 1.00 50.80  ? 243 LEU B O   1 
ATOM   2973 C  CB  . LEU B 2 69  ? -16.755 -14.053 -34.266 1.00 38.86  ? 243 LEU B CB  1 
ATOM   2974 C  CG  . LEU B 2 69  ? -17.293 -15.075 -33.262 1.00 40.89  ? 243 LEU B CG  1 
ATOM   2975 C  CD1 . LEU B 2 69  ? -18.514 -14.521 -32.546 1.00 43.60  ? 243 LEU B CD1 1 
ATOM   2976 C  CD2 . LEU B 2 69  ? -17.620 -16.414 -33.907 1.00 38.95  ? 243 LEU B CD2 1 
ATOM   2977 N  N   . SER B 2 70  ? -14.201 -12.624 -35.968 1.00 47.48  ? 244 SER B N   1 
ATOM   2978 C  CA  . SER B 2 70  ? -13.645 -11.742 -36.989 1.00 46.40  ? 244 SER B CA  1 
ATOM   2979 C  C   . SER B 2 70  ? -13.076 -12.511 -38.184 1.00 47.06  ? 244 SER B C   1 
ATOM   2980 O  O   . SER B 2 70  ? -12.940 -11.933 -39.254 1.00 50.12  ? 244 SER B O   1 
ATOM   2981 C  CB  . SER B 2 70  ? -12.561 -10.857 -36.417 1.00 44.25  ? 244 SER B CB  1 
ATOM   2982 O  OG  . SER B 2 70  ? -13.093 -9.941  -35.474 1.00 44.03  ? 244 SER B OG  1 
ATOM   2983 N  N   . SER B 2 71  ? -12.681 -13.777 -38.002 1.00 48.35  ? 245 SER B N   1 
ATOM   2984 C  CA  . SER B 2 71  ? -11.924 -14.517 -39.013 1.00 51.89  ? 245 SER B CA  1 
ATOM   2985 C  C   . SER B 2 71  ? -12.728 -15.691 -39.563 1.00 52.50  ? 245 SER B C   1 
ATOM   2986 O  O   . SER B 2 71  ? -12.501 -16.096 -40.693 1.00 61.14  ? 245 SER B O   1 
ATOM   2987 C  CB  . SER B 2 71  ? -10.603 -15.047 -38.466 1.00 53.38  ? 245 SER B CB  1 
ATOM   2988 O  OG  . SER B 2 71  ? -9.862  -14.046 -37.774 1.00 57.95  ? 245 SER B OG  1 
ATOM   2989 N  N   . MET B 2 72  ? -13.603 -16.278 -38.738 1.00 49.66  ? 246 MET B N   1 
ATOM   2990 C  CA  . MET B 2 72  ? -14.277 -17.525 -39.058 1.00 50.03  ? 246 MET B CA  1 
ATOM   2991 C  C   . MET B 2 72  ? -15.789 -17.308 -39.015 1.00 49.87  ? 246 MET B C   1 
ATOM   2992 O  O   . MET B 2 72  ? -16.283 -16.546 -38.185 1.00 53.10  ? 246 MET B O   1 
ATOM   2993 C  CB  . MET B 2 72  ? -13.919 -18.611 -38.041 1.00 51.14  ? 246 MET B CB  1 
ATOM   2994 C  CG  . MET B 2 72  ? -12.443 -18.831 -37.911 1.00 53.86  ? 246 MET B CG  1 
ATOM   2995 S  SD  . MET B 2 72  ? -11.791 -19.952 -39.160 1.00 55.23  ? 246 MET B SD  1 
ATOM   2996 C  CE  . MET B 2 72  ? -12.223 -21.566 -38.508 1.00 50.57  ? 246 MET B CE  1 
ATOM   2997 N  N   . SER B 2 73  ? -16.495 -17.995 -39.921 1.00 45.63  ? 247 SER B N   1 
ATOM   2998 C  CA  . SER B 2 73  ? -17.946 -18.056 -39.944 1.00 46.37  ? 247 SER B CA  1 
ATOM   2999 C  C   . SER B 2 73  ? -18.378 -19.214 -39.059 1.00 44.32  ? 247 SER B C   1 
ATOM   3000 O  O   . SER B 2 73  ? -17.784 -20.283 -39.121 1.00 43.25  ? 247 SER B O   1 
ATOM   3001 C  CB  . SER B 2 73  ? -18.471 -18.207 -41.349 1.00 49.64  ? 247 SER B CB  1 
ATOM   3002 O  OG  . SER B 2 73  ? -18.268 -17.000 -42.072 1.00 56.34  ? 247 SER B OG  1 
ATOM   3003 N  N   . VAL B 2 74  ? -19.378 -18.963 -38.211 1.00 45.13  ? 248 VAL B N   1 
ATOM   3004 C  CA  . VAL B 2 74  ? -19.844 -19.937 -37.232 1.00 47.06  ? 248 VAL B CA  1 
ATOM   3005 C  C   . VAL B 2 74  ? -21.370 -19.978 -37.318 1.00 46.28  ? 248 VAL B C   1 
ATOM   3006 O  O   . VAL B 2 74  ? -22.003 -18.927 -37.439 1.00 45.79  ? 248 VAL B O   1 
ATOM   3007 C  CB  . VAL B 2 74  ? -19.343 -19.579 -35.813 1.00 41.69  ? 248 VAL B CB  1 
ATOM   3008 C  CG1 . VAL B 2 74  ? -19.840 -20.553 -34.763 1.00 40.64  ? 248 VAL B CG1 1 
ATOM   3009 C  CG2 . VAL B 2 74  ? -17.816 -19.500 -35.750 1.00 46.07  ? 248 VAL B CG2 1 
ATOM   3010 N  N   . LEU B 2 75  ? -21.938 -21.190 -37.300 1.00 45.55  ? 249 LEU B N   1 
ATOM   3011 C  CA  . LEU B 2 75  ? -23.381 -21.386 -37.232 1.00 47.82  ? 249 LEU B CA  1 
ATOM   3012 C  C   . LEU B 2 75  ? -23.830 -21.268 -35.777 1.00 50.74  ? 249 LEU B C   1 
ATOM   3013 O  O   . LEU B 2 75  ? -23.115 -21.723 -34.885 1.00 52.85  ? 249 LEU B O   1 
ATOM   3014 C  CB  . LEU B 2 75  ? -23.731 -22.783 -37.765 1.00 52.87  ? 249 LEU B CB  1 
ATOM   3015 C  CG  . LEU B 2 75  ? -23.440 -23.093 -39.235 1.00 52.00  ? 249 LEU B CG  1 
ATOM   3016 C  CD1 . LEU B 2 75  ? -24.290 -24.278 -39.680 1.00 50.02  ? 249 LEU B CD1 1 
ATOM   3017 C  CD2 . LEU B 2 75  ? -23.679 -21.892 -40.152 1.00 54.85  ? 249 LEU B CD2 1 
ATOM   3018 N  N   . ARG B 2 76  ? -25.034 -20.719 -35.547 1.00 50.15  ? 250 ARG B N   1 
ATOM   3019 C  CA  . ARG B 2 76  ? -25.568 -20.510 -34.205 1.00 49.17  ? 250 ARG B CA  1 
ATOM   3020 C  C   . ARG B 2 76  ? -25.438 -21.786 -33.368 1.00 45.81  ? 250 ARG B C   1 
ATOM   3021 O  O   . ARG B 2 76  ? -25.170 -21.696 -32.175 1.00 46.18  ? 250 ARG B O   1 
ATOM   3022 C  CB  . ARG B 2 76  ? -27.026 -20.040 -34.247 1.00 55.65  ? 250 ARG B CB  1 
ATOM   3023 C  CG  . ARG B 2 76  ? -28.018 -21.137 -34.601 1.00 60.90  ? 250 ARG B CG  1 
ATOM   3024 C  CD  . ARG B 2 76  ? -29.403 -20.576 -34.826 1.00 67.40  ? 250 ARG B CD  1 
ATOM   3025 N  NE  . ARG B 2 76  ? -29.423 -19.716 -35.998 1.00 77.29  ? 250 ARG B NE  1 
ATOM   3026 C  CZ  . ARG B 2 76  ? -30.479 -19.035 -36.433 1.00 74.40  ? 250 ARG B CZ  1 
ATOM   3027 N  NH1 . ARG B 2 76  ? -31.636 -19.103 -35.797 1.00 66.50  ? 250 ARG B NH1 1 
ATOM   3028 N  NH2 . ARG B 2 76  ? -30.364 -18.282 -37.514 1.00 72.12  ? 250 ARG B NH2 1 
ATOM   3029 N  N   . GLY B 2 77  ? -25.616 -22.973 -33.967 1.00 41.02  ? 251 GLY B N   1 
ATOM   3030 C  CA  . GLY B 2 77  ? -25.508 -24.227 -33.217 1.00 41.13  ? 251 GLY B CA  1 
ATOM   3031 C  C   . GLY B 2 77  ? -24.118 -24.501 -32.613 1.00 42.20  ? 251 GLY B C   1 
ATOM   3032 O  O   . GLY B 2 77  ? -23.964 -25.391 -31.772 1.00 42.77  ? 251 GLY B O   1 
ATOM   3033 N  N   . LYS B 2 78  ? -23.097 -23.760 -33.073 1.00 39.71  ? 252 LYS B N   1 
ATOM   3034 C  CA  . LYS B 2 78  ? -21.699 -23.999 -32.734 1.00 39.67  ? 252 LYS B CA  1 
ATOM   3035 C  C   . LYS B 2 78  ? -21.106 -22.811 -31.961 1.00 40.08  ? 252 LYS B C   1 
ATOM   3036 O  O   . LYS B 2 78  ? -19.953 -22.855 -31.543 1.00 39.92  ? 252 LYS B O   1 
ATOM   3037 C  CB  . LYS B 2 78  ? -20.924 -24.269 -34.031 1.00 38.29  ? 252 LYS B CB  1 
ATOM   3038 C  CG  . LYS B 2 78  ? -21.111 -25.651 -34.638 1.00 40.78  ? 252 LYS B CG  1 
ATOM   3039 C  CD  . LYS B 2 78  ? -20.730 -26.763 -33.698 1.00 45.20  ? 252 LYS B CD  1 
ATOM   3040 C  CE  . LYS B 2 78  ? -20.625 -28.103 -34.390 1.00 50.36  ? 252 LYS B CE  1 
ATOM   3041 N  NZ  . LYS B 2 78  ? -21.887 -28.861 -34.265 1.00 54.91  ? 252 LYS B NZ  1 
ATOM   3042 N  N   . LEU B 2 79  ? -21.890 -21.749 -31.765 1.00 39.30  ? 253 LEU B N   1 
ATOM   3043 C  CA  . LEU B 2 79  ? -21.422 -20.522 -31.143 1.00 41.31  ? 253 LEU B CA  1 
ATOM   3044 C  C   . LEU B 2 79  ? -21.054 -20.767 -29.684 1.00 47.71  ? 253 LEU B C   1 
ATOM   3045 O  O   . LEU B 2 79  ? -20.118 -20.151 -29.172 1.00 51.04  ? 253 LEU B O   1 
ATOM   3046 C  CB  . LEU B 2 79  ? -22.520 -19.462 -31.232 1.00 40.57  ? 253 LEU B CB  1 
ATOM   3047 C  CG  . LEU B 2 79  ? -22.123 -18.113 -30.658 1.00 41.06  ? 253 LEU B CG  1 
ATOM   3048 C  CD1 . LEU B 2 79  ? -21.034 -17.488 -31.509 1.00 43.92  ? 253 LEU B CD1 1 
ATOM   3049 C  CD2 . LEU B 2 79  ? -23.321 -17.194 -30.555 1.00 45.64  ? 253 LEU B CD2 1 
ATOM   3050 N  N   . GLN B 2 80  ? -21.796 -21.663 -29.021 1.00 48.22  ? 254 GLN B N   1 
ATOM   3051 C  CA  . GLN B 2 80  ? -21.560 -21.935 -27.616 1.00 49.28  ? 254 GLN B CA  1 
ATOM   3052 C  C   . GLN B 2 80  ? -20.251 -22.708 -27.455 1.00 49.35  ? 254 GLN B C   1 
ATOM   3053 O  O   . GLN B 2 80  ? -19.593 -22.571 -26.426 1.00 49.87  ? 254 GLN B O   1 
ATOM   3054 C  CB  . GLN B 2 80  ? -22.730 -22.706 -27.012 1.00 51.61  ? 254 GLN B CB  1 
ATOM   3055 C  CG  . GLN B 2 80  ? -22.675 -22.784 -25.494 1.00 53.88  ? 254 GLN B CG  1 
ATOM   3056 C  CD  . GLN B 2 80  ? -23.824 -23.577 -24.925 1.00 53.02  ? 254 GLN B CD  1 
ATOM   3057 O  OE1 . GLN B 2 80  ? -24.572 -24.234 -25.645 1.00 53.93  ? 254 GLN B OE1 1 
ATOM   3058 N  NE2 . GLN B 2 80  ? -23.940 -23.554 -23.610 1.00 52.62  ? 254 GLN B NE2 1 
ATOM   3059 N  N   . LEU B 2 81  ? -19.903 -23.533 -28.456 1.00 49.66  ? 255 LEU B N   1 
ATOM   3060 C  CA  . LEU B 2 81  ? -18.687 -24.342 -28.438 1.00 45.21  ? 255 LEU B CA  1 
ATOM   3061 C  C   . LEU B 2 81  ? -17.454 -23.437 -28.528 1.00 46.53  ? 255 LEU B C   1 
ATOM   3062 O  O   . LEU B 2 81  ? -16.441 -23.727 -27.891 1.00 51.25  ? 255 LEU B O   1 
ATOM   3063 C  CB  . LEU B 2 81  ? -18.724 -25.363 -29.583 1.00 43.58  ? 255 LEU B CB  1 
ATOM   3064 C  CG  . LEU B 2 81  ? -17.519 -26.302 -29.691 1.00 43.35  ? 255 LEU B CG  1 
ATOM   3065 C  CD1 . LEU B 2 81  ? -17.275 -27.067 -28.403 1.00 43.28  ? 255 LEU B CD1 1 
ATOM   3066 C  CD2 . LEU B 2 81  ? -17.710 -27.290 -30.816 1.00 44.26  ? 255 LEU B CD2 1 
ATOM   3067 N  N   . VAL B 2 82  ? -17.547 -22.343 -29.302 1.00 42.83  ? 256 VAL B N   1 
ATOM   3068 C  CA  . VAL B 2 82  ? -16.471 -21.360 -29.413 1.00 44.96  ? 256 VAL B CA  1 
ATOM   3069 C  C   . VAL B 2 82  ? -16.244 -20.677 -28.059 1.00 41.04  ? 256 VAL B C   1 
ATOM   3070 O  O   . VAL B 2 82  ? -15.104 -20.407 -27.683 1.00 43.75  ? 256 VAL B O   1 
ATOM   3071 C  CB  . VAL B 2 82  ? -16.757 -20.323 -30.525 1.00 48.36  ? 256 VAL B CB  1 
ATOM   3072 C  CG1 . VAL B 2 82  ? -15.787 -19.144 -30.479 1.00 47.48  ? 256 VAL B CG1 1 
ATOM   3073 C  CG2 . VAL B 2 82  ? -16.758 -20.958 -31.915 1.00 48.25  ? 256 VAL B CG2 1 
ATOM   3074 N  N   . GLY B 2 83  ? -17.337 -20.335 -27.367 1.00 39.63  ? 257 GLY B N   1 
ATOM   3075 C  CA  . GLY B 2 83  ? -17.299 -19.725 -26.045 1.00 38.58  ? 257 GLY B CA  1 
ATOM   3076 C  C   . GLY B 2 83  ? -16.723 -20.651 -24.969 1.00 35.67  ? 257 GLY B C   1 
ATOM   3077 O  O   . GLY B 2 83  ? -15.979 -20.198 -24.116 1.00 38.31  ? 257 GLY B O   1 
ATOM   3078 N  N   . THR B 2 84  ? -17.087 -21.934 -24.998 1.00 34.56  ? 258 THR B N   1 
ATOM   3079 C  CA  . THR B 2 84  ? -16.571 -22.942 -24.083 1.00 37.33  ? 258 THR B CA  1 
ATOM   3080 C  C   . THR B 2 84  ? -15.050 -23.041 -24.218 1.00 39.50  ? 258 THR B C   1 
ATOM   3081 O  O   . THR B 2 84  ? -14.333 -23.012 -23.213 1.00 36.02  ? 258 THR B O   1 
ATOM   3082 C  CB  . THR B 2 84  ? -17.236 -24.303 -24.337 1.00 39.84  ? 258 THR B CB  1 
ATOM   3083 O  OG1 . THR B 2 84  ? -18.644 -24.141 -24.207 1.00 42.38  ? 258 THR B OG1 1 
ATOM   3084 C  CG2 . THR B 2 84  ? -16.828 -25.386 -23.365 1.00 42.50  ? 258 THR B CG2 1 
ATOM   3085 N  N   . ALA B 2 85  ? -14.562 -23.155 -25.463 1.00 41.28  ? 259 ALA B N   1 
ATOM   3086 C  CA  . ALA B 2 85  ? -13.134 -23.258 -25.720 1.00 39.89  ? 259 ALA B CA  1 
ATOM   3087 C  C   . ALA B 2 85  ? -12.458 -21.934 -25.377 1.00 41.10  ? 259 ALA B C   1 
ATOM   3088 O  O   . ALA B 2 85  ? -11.346 -21.935 -24.882 1.00 43.81  ? 259 ALA B O   1 
ATOM   3089 C  CB  . ALA B 2 85  ? -12.872 -23.660 -27.144 1.00 42.36  ? 259 ALA B CB  1 
ATOM   3090 N  N   . ALA B 2 86  ? -13.123 -20.799 -25.599 1.00 39.38  ? 260 ALA B N   1 
ATOM   3091 C  CA  . ALA B 2 86  ? -12.480 -19.531 -25.296 1.00 41.23  ? 260 ALA B CA  1 
ATOM   3092 C  C   . ALA B 2 86  ? -12.324 -19.441 -23.779 1.00 44.10  ? 260 ALA B C   1 
ATOM   3093 O  O   . ALA B 2 86  ? -11.297 -18.983 -23.293 1.00 39.99  ? 260 ALA B O   1 
ATOM   3094 C  CB  . ALA B 2 86  ? -13.257 -18.369 -25.870 1.00 42.49  ? 260 ALA B CB  1 
ATOM   3095 N  N   . MET B 2 87  ? -13.335 -19.931 -23.047 1.00 44.66  ? 261 MET B N   1 
ATOM   3096 C  CA  . MET B 2 87  ? -13.368 -19.847 -21.595 1.00 44.71  ? 261 MET B CA  1 
ATOM   3097 C  C   . MET B 2 87  ? -12.310 -20.792 -21.014 1.00 39.43  ? 261 MET B C   1 
ATOM   3098 O  O   . MET B 2 87  ? -11.645 -20.415 -20.064 1.00 39.07  ? 261 MET B O   1 
ATOM   3099 C  CB  . MET B 2 87  ? -14.761 -20.179 -21.039 1.00 46.85  ? 261 MET B CB  1 
ATOM   3100 C  CG  . MET B 2 87  ? -14.996 -19.666 -19.623 1.00 54.52  ? 261 MET B CG  1 
ATOM   3101 S  SD  . MET B 2 87  ? -14.751 -17.860 -19.512 1.00 67.67  ? 261 MET B SD  1 
ATOM   3102 C  CE  . MET B 2 87  ? -15.947 -17.410 -18.255 1.00 70.89  ? 261 MET B CE  1 
ATOM   3103 N  N   . LEU B 2 88  ? -12.145 -21.987 -21.604 1.00 38.27  ? 262 LEU B N   1 
ATOM   3104 C  CA  . LEU B 2 88  ? -11.101 -22.947 -21.244 1.00 40.89  ? 262 LEU B CA  1 
ATOM   3105 C  C   . LEU B 2 88  ? -9.696  -22.334 -21.403 1.00 41.37  ? 262 LEU B C   1 
ATOM   3106 O  O   . LEU B 2 88  ? -8.863  -22.472 -20.509 1.00 41.80  ? 262 LEU B O   1 
ATOM   3107 C  CB  . LEU B 2 88  ? -11.290 -24.215 -22.100 1.00 40.22  ? 262 LEU B CB  1 
ATOM   3108 C  CG  . LEU B 2 88  ? -10.289 -25.363 -21.911 1.00 43.56  ? 262 LEU B CG  1 
ATOM   3109 C  CD1 . LEU B 2 88  ? -10.355 -25.980 -20.517 1.00 46.65  ? 262 LEU B CD1 1 
ATOM   3110 C  CD2 . LEU B 2 88  ? -10.533 -26.453 -22.941 1.00 43.01  ? 262 LEU B CD2 1 
ATOM   3111 N  N   . LEU B 2 89  ? -9.441  -21.655 -22.530 1.00 40.46  ? 263 LEU B N   1 
ATOM   3112 C  CA  . LEU B 2 89  ? -8.142  -21.062 -22.841 1.00 42.15  ? 263 LEU B CA  1 
ATOM   3113 C  C   . LEU B 2 89  ? -7.853  -19.897 -21.896 1.00 41.50  ? 263 LEU B C   1 
ATOM   3114 O  O   . LEU B 2 89  ? -6.760  -19.814 -21.339 1.00 33.91  ? 263 LEU B O   1 
ATOM   3115 C  CB  . LEU B 2 89  ? -8.115  -20.591 -24.302 1.00 43.13  ? 263 LEU B CB  1 
ATOM   3116 C  CG  . LEU B 2 89  ? -7.927  -21.699 -25.340 1.00 46.07  ? 263 LEU B CG  1 
ATOM   3117 C  CD1 . LEU B 2 89  ? -8.111  -21.157 -26.743 1.00 45.12  ? 263 LEU B CD1 1 
ATOM   3118 C  CD2 . LEU B 2 89  ? -6.560  -22.359 -25.205 1.00 48.58  ? 263 LEU B CD2 1 
ATOM   3119 N  N   . ALA B 2 90  ? -8.843  -19.010 -21.720 1.00 43.78  ? 264 ALA B N   1 
ATOM   3120 C  CA  . ALA B 2 90  ? -8.726  -17.876 -20.808 1.00 39.76  ? 264 ALA B CA  1 
ATOM   3121 C  C   . ALA B 2 90  ? -8.403  -18.396 -19.405 1.00 38.31  ? 264 ALA B C   1 
ATOM   3122 O  O   . ALA B 2 90  ? -7.492  -17.905 -18.758 1.00 43.83  ? 264 ALA B O   1 
ATOM   3123 C  CB  . ALA B 2 90  ? -9.985  -17.031 -20.843 1.00 36.71  ? 264 ALA B CB  1 
ATOM   3124 N  N   . SER B 2 91  ? -9.098  -19.446 -18.969 1.00 36.94  ? 265 SER B N   1 
ATOM   3125 C  CA  . SER B 2 91  ? -8.882  -20.046 -17.667 1.00 36.21  ? 265 SER B CA  1 
ATOM   3126 C  C   . SER B 2 91  ? -7.463  -20.604 -17.553 1.00 37.63  ? 265 SER B C   1 
ATOM   3127 O  O   . SER B 2 91  ? -6.799  -20.423 -16.533 1.00 37.71  ? 265 SER B O   1 
ATOM   3128 C  CB  . SER B 2 91  ? -9.917  -21.110 -17.418 1.00 39.25  ? 265 SER B CB  1 
ATOM   3129 O  OG  . SER B 2 91  ? -11.210 -20.529 -17.364 1.00 43.33  ? 265 SER B OG  1 
ATOM   3130 N  N   . LYS B 2 92  ? -6.996  -21.318 -18.583 1.00 38.41  ? 266 LYS B N   1 
ATOM   3131 C  CA  . LYS B 2 92  ? -5.653  -21.872 -18.543 1.00 37.09  ? 266 LYS B CA  1 
ATOM   3132 C  C   . LYS B 2 92  ? -4.656  -20.725 -18.418 1.00 36.75  ? 266 LYS B C   1 
ATOM   3133 O  O   . LYS B 2 92  ? -3.677  -20.834 -17.697 1.00 36.48  ? 266 LYS B O   1 
ATOM   3134 C  CB  . LYS B 2 92  ? -5.389  -22.762 -19.756 1.00 37.25  ? 266 LYS B CB  1 
ATOM   3135 C  CG  . LYS B 2 92  ? -5.982  -24.159 -19.637 1.00 38.06  ? 266 LYS B CG  1 
ATOM   3136 C  CD  . LYS B 2 92  ? -5.932  -24.992 -20.903 1.00 39.23  ? 266 LYS B CD  1 
ATOM   3137 C  CE  . LYS B 2 92  ? -6.461  -26.389 -20.664 1.00 45.58  ? 266 LYS B CE  1 
ATOM   3138 N  NZ  . LYS B 2 92  ? -6.065  -27.317 -21.743 1.00 52.38  ? 266 LYS B NZ  1 
ATOM   3139 N  N   . PHE B 2 93  ? -4.918  -19.616 -19.102 1.00 35.80  ? 267 PHE B N   1 
ATOM   3140 C  CA  . PHE B 2 93  ? -3.945  -18.536 -19.146 1.00 38.87  ? 267 PHE B CA  1 
ATOM   3141 C  C   . PHE B 2 93  ? -3.859  -17.845 -17.782 1.00 40.00  ? 267 PHE B C   1 
ATOM   3142 O  O   . PHE B 2 93  ? -2.761  -17.525 -17.332 1.00 44.61  ? 267 PHE B O   1 
ATOM   3143 C  CB  . PHE B 2 93  ? -4.273  -17.563 -20.285 1.00 37.58  ? 267 PHE B CB  1 
ATOM   3144 C  CG  . PHE B 2 93  ? -3.284  -16.439 -20.479 1.00 38.67  ? 267 PHE B CG  1 
ATOM   3145 C  CD1 . PHE B 2 93  ? -2.108  -16.635 -21.188 1.00 38.45  ? 267 PHE B CD1 1 
ATOM   3146 C  CD2 . PHE B 2 93  ? -3.519  -15.186 -19.936 1.00 39.49  ? 267 PHE B CD2 1 
ATOM   3147 C  CE1 . PHE B 2 93  ? -1.202  -15.599 -21.364 1.00 40.42  ? 267 PHE B CE1 1 
ATOM   3148 C  CE2 . PHE B 2 93  ? -2.612  -14.150 -20.111 1.00 40.33  ? 267 PHE B CE2 1 
ATOM   3149 C  CZ  . PHE B 2 93  ? -1.457  -14.355 -20.834 1.00 40.14  ? 267 PHE B CZ  1 
ATOM   3150 N  N   . GLU B 2 94  ? -5.003  -17.645 -17.116 1.00 41.80  ? 268 GLU B N   1 
ATOM   3151 C  CA  . GLU B 2 94  ? -5.128  -16.655 -16.046 1.00 43.41  ? 268 GLU B CA  1 
ATOM   3152 C  C   . GLU B 2 94  ? -5.358  -17.309 -14.674 1.00 40.24  ? 268 GLU B C   1 
ATOM   3153 O  O   . GLU B 2 94  ? -4.891  -16.789 -13.677 1.00 38.46  ? 268 GLU B O   1 
ATOM   3154 C  CB  . GLU B 2 94  ? -6.239  -15.650 -16.379 1.00 47.03  ? 268 GLU B CB  1 
ATOM   3155 C  CG  . GLU B 2 94  ? -6.216  -14.382 -15.521 1.00 54.96  ? 268 GLU B CG  1 
ATOM   3156 C  CD  . GLU B 2 94  ? -5.085  -13.379 -15.752 1.00 62.37  ? 268 GLU B CD  1 
ATOM   3157 O  OE1 . GLU B 2 94  ? -4.499  -13.375 -16.862 1.00 53.89  ? 268 GLU B OE1 1 
ATOM   3158 O  OE2 . GLU B 2 94  ? -4.793  -12.582 -14.811 1.00 65.28  ? 268 GLU B OE2 1 
ATOM   3159 N  N   . GLU B 2 95  ? -6.093  -18.420 -14.588 1.00 37.69  ? 269 GLU B N   1 
ATOM   3160 C  CA  . GLU B 2 95  ? -6.443  -19.004 -13.296 1.00 39.82  ? 269 GLU B CA  1 
ATOM   3161 C  C   . GLU B 2 95  ? -5.286  -19.834 -12.721 1.00 39.02  ? 269 GLU B C   1 
ATOM   3162 O  O   . GLU B 2 95  ? -4.551  -20.476 -13.455 1.00 41.81  ? 269 GLU B O   1 
ATOM   3163 C  CB  . GLU B 2 95  ? -7.674  -19.909 -13.433 1.00 40.28  ? 269 GLU B CB  1 
ATOM   3164 C  CG  . GLU B 2 95  ? -8.932  -19.179 -13.854 1.00 43.85  ? 269 GLU B CG  1 
ATOM   3165 C  CD  . GLU B 2 95  ? -9.464  -18.182 -12.844 1.00 50.03  ? 269 GLU B CD  1 
ATOM   3166 O  OE1 . GLU B 2 95  ? -9.116  -18.335 -11.640 1.00 53.02  ? 269 GLU B OE1 1 
ATOM   3167 O  OE2 . GLU B 2 95  ? -10.213 -17.248 -13.266 1.00 45.28  ? 269 GLU B OE2 1 
ATOM   3168 N  N   . ILE B 2 96  ? -5.180  -19.885 -11.389 1.00 43.57  ? 270 ILE B N   1 
ATOM   3169 C  CA  . ILE B 2 96  ? -4.338  -20.853 -10.689 1.00 45.53  ? 270 ILE B CA  1 
ATOM   3170 C  C   . ILE B 2 96  ? -4.925  -22.260 -10.866 1.00 46.00  ? 270 ILE B C   1 
ATOM   3171 O  O   . ILE B 2 96  ? -4.194  -23.188 -11.216 1.00 41.49  ? 270 ILE B O   1 
ATOM   3172 C  CB  . ILE B 2 96  ? -4.201  -20.460 -9.199  1.00 47.41  ? 270 ILE B CB  1 
ATOM   3173 C  CG1 . ILE B 2 96  ? -3.544  -19.085 -9.022  1.00 48.58  ? 270 ILE B CG1 1 
ATOM   3174 C  CG2 . ILE B 2 96  ? -3.456  -21.530 -8.413  1.00 50.57  ? 270 ILE B CG2 1 
ATOM   3175 C  CD1 . ILE B 2 96  ? -3.710  -18.492 -7.631  1.00 49.30  ? 270 ILE B CD1 1 
ATOM   3176 N  N   . TYR B 2 97  ? -6.249  -22.392 -10.633 1.00 47.34  ? 271 TYR B N   1 
ATOM   3177 C  CA  . TYR B 2 97  ? -6.967  -23.665 -10.665 1.00 52.26  ? 271 TYR B CA  1 
ATOM   3178 C  C   . TYR B 2 97  ? -8.091  -23.599 -11.692 1.00 55.55  ? 271 TYR B C   1 
ATOM   3179 O  O   . TYR B 2 97  ? -9.242  -23.339 -11.350 1.00 60.59  ? 271 TYR B O   1 
ATOM   3180 C  CB  . TYR B 2 97  ? -7.495  -24.037 -9.279  1.00 55.20  ? 271 TYR B CB  1 
ATOM   3181 C  CG  . TYR B 2 97  ? -6.395  -24.461 -8.342  1.00 62.75  ? 271 TYR B CG  1 
ATOM   3182 C  CD1 . TYR B 2 97  ? -5.595  -25.549 -8.653  1.00 66.89  ? 271 TYR B CD1 1 
ATOM   3183 C  CD2 . TYR B 2 97  ? -6.112  -23.748 -7.184  1.00 61.79  ? 271 TYR B CD2 1 
ATOM   3184 C  CE1 . TYR B 2 97  ? -4.554  -25.935 -7.825  1.00 74.14  ? 271 TYR B CE1 1 
ATOM   3185 C  CE2 . TYR B 2 97  ? -5.073  -24.119 -6.343  1.00 63.71  ? 271 TYR B CE2 1 
ATOM   3186 C  CZ  . TYR B 2 97  ? -4.294  -25.221 -6.665  1.00 74.64  ? 271 TYR B CZ  1 
ATOM   3187 O  OH  . TYR B 2 97  ? -3.260  -25.625 -5.850  1.00 79.56  ? 271 TYR B OH  1 
ATOM   3188 N  N   . PRO B 2 98  ? -7.779  -23.816 -12.988 1.00 52.72  ? 272 PRO B N   1 
ATOM   3189 C  CA  . PRO B 2 98  ? -8.788  -23.759 -14.040 1.00 52.87  ? 272 PRO B CA  1 
ATOM   3190 C  C   . PRO B 2 98  ? -9.715  -24.965 -13.976 1.00 51.85  ? 272 PRO B C   1 
ATOM   3191 O  O   . PRO B 2 98  ? -9.274  -26.061 -13.646 1.00 49.48  ? 272 PRO B O   1 
ATOM   3192 C  CB  . PRO B 2 98  ? -7.968  -23.757 -15.339 1.00 49.72  ? 272 PRO B CB  1 
ATOM   3193 C  CG  . PRO B 2 98  ? -6.663  -24.406 -14.968 1.00 48.49  ? 272 PRO B CG  1 
ATOM   3194 C  CD  . PRO B 2 98  ? -6.431  -24.063 -13.517 1.00 48.18  ? 272 PRO B CD  1 
ATOM   3195 N  N   . PRO B 2 99  ? -11.015 -24.825 -14.312 1.00 46.49  ? 273 PRO B N   1 
ATOM   3196 C  CA  . PRO B 2 99  ? -11.881 -25.993 -14.380 1.00 43.65  ? 273 PRO B CA  1 
ATOM   3197 C  C   . PRO B 2 99  ? -11.247 -26.963 -15.368 1.00 45.18  ? 273 PRO B C   1 
ATOM   3198 O  O   . PRO B 2 99  ? -10.511 -26.542 -16.257 1.00 49.67  ? 273 PRO B O   1 
ATOM   3199 C  CB  . PRO B 2 99  ? -13.228 -25.422 -14.830 1.00 42.36  ? 273 PRO B CB  1 
ATOM   3200 C  CG  . PRO B 2 99  ? -13.153 -23.959 -14.411 1.00 44.46  ? 273 PRO B CG  1 
ATOM   3201 C  CD  . PRO B 2 99  ? -11.708 -23.578 -14.668 1.00 45.20  ? 273 PRO B CD  1 
ATOM   3202 N  N   . GLU B 2 100 ? -11.477 -28.263 -15.171 1.00 45.75  ? 274 GLU B N   1 
ATOM   3203 C  CA  . GLU B 2 100 ? -11.050 -29.247 -16.151 1.00 46.46  ? 274 GLU B CA  1 
ATOM   3204 C  C   . GLU B 2 100 ? -12.118 -29.299 -17.243 1.00 48.33  ? 274 GLU B C   1 
ATOM   3205 O  O   . GLU B 2 100 ? -13.204 -28.724 -17.094 1.00 44.70  ? 274 GLU B O   1 
ATOM   3206 C  CB  . GLU B 2 100 ? -10.666 -30.613 -15.549 1.00 53.04  ? 274 GLU B CB  1 
ATOM   3207 C  CG  . GLU B 2 100 ? -11.383 -31.068 -14.293 1.00 62.28  ? 274 GLU B CG  1 
ATOM   3208 C  CD  . GLU B 2 100 ? -11.022 -32.486 -13.857 1.00 66.53  ? 274 GLU B CD  1 
ATOM   3209 O  OE1 . GLU B 2 100 ? -11.134 -33.398 -14.698 1.00 73.77  ? 274 GLU B OE1 1 
ATOM   3210 O  OE2 . GLU B 2 100 ? -10.641 -32.689 -12.677 1.00 68.71  ? 274 GLU B OE2 1 
ATOM   3211 N  N   . VAL B 2 101 ? -11.758 -29.935 -18.366 1.00 46.82  ? 275 VAL B N   1 
ATOM   3212 C  CA  . VAL B 2 101 ? -12.566 -29.931 -19.577 1.00 50.67  ? 275 VAL B CA  1 
ATOM   3213 C  C   . VAL B 2 101 ? -13.900 -30.637 -19.318 1.00 49.50  ? 275 VAL B C   1 
ATOM   3214 O  O   . VAL B 2 101 ? -14.943 -30.148 -19.737 1.00 52.75  ? 275 VAL B O   1 
ATOM   3215 C  CB  . VAL B 2 101 ? -11.800 -30.580 -20.743 1.00 50.46  ? 275 VAL B CB  1 
ATOM   3216 C  CG1 . VAL B 2 101 ? -12.681 -30.722 -21.969 1.00 50.76  ? 275 VAL B CG1 1 
ATOM   3217 C  CG2 . VAL B 2 101 ? -10.538 -29.803 -21.079 1.00 55.68  ? 275 VAL B CG2 1 
ATOM   3218 N  N   . ALA B 2 102 ? -13.842 -31.789 -18.638 1.00 51.53  ? 276 ALA B N   1 
ATOM   3219 C  CA  . ALA B 2 102 ? -15.005 -32.558 -18.205 1.00 50.60  ? 276 ALA B CA  1 
ATOM   3220 C  C   . ALA B 2 102 ? -16.075 -31.666 -17.567 1.00 46.26  ? 276 ALA B C   1 
ATOM   3221 O  O   . ALA B 2 102 ? -17.260 -31.932 -17.732 1.00 49.95  ? 276 ALA B O   1 
ATOM   3222 C  CB  . ALA B 2 102 ? -14.548 -33.650 -17.255 1.00 49.94  ? 276 ALA B CB  1 
ATOM   3223 N  N   . GLU B 2 103 ? -15.652 -30.626 -16.833 1.00 46.66  ? 277 GLU B N   1 
ATOM   3224 C  CA  . GLU B 2 103 ? -16.550 -29.693 -16.155 1.00 50.68  ? 277 GLU B CA  1 
ATOM   3225 C  C   . GLU B 2 103 ? -17.087 -28.625 -17.110 1.00 50.20  ? 277 GLU B C   1 
ATOM   3226 O  O   . GLU B 2 103 ? -18.184 -28.114 -16.905 1.00 56.10  ? 277 GLU B O   1 
ATOM   3227 C  CB  . GLU B 2 103 ? -15.831 -28.987 -15.001 1.00 53.67  ? 277 GLU B CB  1 
ATOM   3228 C  CG  . GLU B 2 103 ? -15.390 -29.915 -13.879 1.00 59.62  ? 277 GLU B CG  1 
ATOM   3229 C  CD  . GLU B 2 103 ? -14.645 -29.197 -12.767 1.00 63.38  ? 277 GLU B CD  1 
ATOM   3230 O  OE1 . GLU B 2 103 ? -15.239 -28.988 -11.686 1.00 79.00  ? 277 GLU B OE1 1 
ATOM   3231 O  OE2 . GLU B 2 103 ? -13.472 -28.838 -12.992 1.00 62.70  ? 277 GLU B OE2 1 
ATOM   3232 N  N   . PHE B 2 104 ? -16.290 -28.241 -18.116 1.00 53.28  ? 278 PHE B N   1 
ATOM   3233 C  CA  . PHE B 2 104 ? -16.743 -27.352 -19.177 1.00 47.68  ? 278 PHE B CA  1 
ATOM   3234 C  C   . PHE B 2 104 ? -17.828 -28.050 -20.001 1.00 46.68  ? 278 PHE B C   1 
ATOM   3235 O  O   . PHE B 2 104 ? -18.803 -27.424 -20.385 1.00 49.36  ? 278 PHE B O   1 
ATOM   3236 C  CB  . PHE B 2 104 ? -15.554 -26.876 -20.018 1.00 49.75  ? 278 PHE B CB  1 
ATOM   3237 C  CG  . PHE B 2 104 ? -14.800 -25.731 -19.396 1.00 49.69  ? 278 PHE B CG  1 
ATOM   3238 C  CD1 . PHE B 2 104 ? -15.360 -24.466 -19.355 1.00 50.96  ? 278 PHE B CD1 1 
ATOM   3239 C  CD2 . PHE B 2 104 ? -13.560 -25.926 -18.811 1.00 47.86  ? 278 PHE B CD2 1 
ATOM   3240 C  CE1 . PHE B 2 104 ? -14.686 -23.410 -18.761 1.00 52.82  ? 278 PHE B CE1 1 
ATOM   3241 C  CE2 . PHE B 2 104 ? -12.881 -24.866 -18.230 1.00 49.49  ? 278 PHE B CE2 1 
ATOM   3242 C  CZ  . PHE B 2 104 ? -13.451 -23.613 -18.193 1.00 50.09  ? 278 PHE B CZ  1 
ATOM   3243 N  N   . VAL B 2 105 ? -17.659 -29.349 -20.270 1.00 41.55  ? 279 VAL B N   1 
ATOM   3244 C  CA  . VAL B 2 105 ? -18.684 -30.144 -20.928 1.00 41.48  ? 279 VAL B CA  1 
ATOM   3245 C  C   . VAL B 2 105 ? -19.966 -30.182 -20.087 1.00 44.39  ? 279 VAL B C   1 
ATOM   3246 O  O   . VAL B 2 105 ? -21.057 -30.127 -20.637 1.00 48.04  ? 279 VAL B O   1 
ATOM   3247 C  CB  . VAL B 2 105 ? -18.163 -31.563 -21.198 1.00 41.84  ? 279 VAL B CB  1 
ATOM   3248 C  CG1 . VAL B 2 105 ? -19.291 -32.494 -21.615 1.00 41.84  ? 279 VAL B CG1 1 
ATOM   3249 C  CG2 . VAL B 2 105 ? -17.058 -31.554 -22.240 1.00 41.39  ? 279 VAL B CG2 1 
ATOM   3250 N  N   . TYR B 2 106 ? -19.837 -30.314 -18.761 1.00 45.63  ? 280 TYR B N   1 
ATOM   3251 C  CA  . TYR B 2 106 ? -20.979 -30.419 -17.857 1.00 46.95  ? 280 TYR B CA  1 
ATOM   3252 C  C   . TYR B 2 106 ? -21.790 -29.124 -17.908 1.00 46.50  ? 280 TYR B C   1 
ATOM   3253 O  O   . TYR B 2 106 ? -23.019 -29.152 -17.984 1.00 46.99  ? 280 TYR B O   1 
ATOM   3254 C  CB  . TYR B 2 106 ? -20.522 -30.804 -16.443 1.00 46.97  ? 280 TYR B CB  1 
ATOM   3255 C  CG  . TYR B 2 106 ? -21.494 -30.408 -15.363 1.00 50.39  ? 280 TYR B CG  1 
ATOM   3256 C  CD1 . TYR B 2 106 ? -22.647 -31.133 -15.104 1.00 55.32  ? 280 TYR B CD1 1 
ATOM   3257 C  CD2 . TYR B 2 106 ? -21.291 -29.247 -14.646 1.00 52.42  ? 280 TYR B CD2 1 
ATOM   3258 C  CE1 . TYR B 2 106 ? -23.555 -30.731 -14.133 1.00 53.75  ? 280 TYR B CE1 1 
ATOM   3259 C  CE2 . TYR B 2 106 ? -22.184 -28.829 -13.675 1.00 55.84  ? 280 TYR B CE2 1 
ATOM   3260 C  CZ  . TYR B 2 106 ? -23.322 -29.569 -13.415 1.00 58.17  ? 280 TYR B CZ  1 
ATOM   3261 O  OH  . TYR B 2 106 ? -24.162 -29.093 -12.430 1.00 59.06  ? 280 TYR B OH  1 
ATOM   3262 N  N   . ILE B 2 107 ? -21.090 -27.986 -17.937 1.00 48.59  ? 281 ILE B N   1 
ATOM   3263 C  CA  . ILE B 2 107 ? -21.739 -26.683 -17.849 1.00 49.37  ? 281 ILE B CA  1 
ATOM   3264 C  C   . ILE B 2 107 ? -22.484 -26.357 -19.153 1.00 49.73  ? 281 ILE B C   1 
ATOM   3265 O  O   . ILE B 2 107 ? -23.380 -25.514 -19.143 1.00 51.72  ? 281 ILE B O   1 
ATOM   3266 C  CB  . ILE B 2 107 ? -20.721 -25.596 -17.424 1.00 49.37  ? 281 ILE B CB  1 
ATOM   3267 C  CG1 . ILE B 2 107 ? -21.419 -24.407 -16.755 1.00 56.83  ? 281 ILE B CG1 1 
ATOM   3268 C  CG2 . ILE B 2 107 ? -19.818 -25.151 -18.574 1.00 47.21  ? 281 ILE B CG2 1 
ATOM   3269 C  CD1 . ILE B 2 107 ? -21.998 -24.690 -15.373 1.00 61.32  ? 281 ILE B CD1 1 
ATOM   3270 N  N   . THR B 2 108 ? -22.122 -27.018 -20.269 1.00 50.88  ? 282 THR B N   1 
ATOM   3271 C  CA  . THR B 2 108 ? -22.837 -26.905 -21.542 1.00 54.14  ? 282 THR B CA  1 
ATOM   3272 C  C   . THR B 2 108 ? -24.057 -27.827 -21.580 1.00 55.17  ? 282 THR B C   1 
ATOM   3273 O  O   . THR B 2 108 ? -24.841 -27.750 -22.518 1.00 63.35  ? 282 THR B O   1 
ATOM   3274 C  CB  . THR B 2 108 ? -21.995 -27.312 -22.764 1.00 54.77  ? 282 THR B CB  1 
ATOM   3275 O  OG1 . THR B 2 108 ? -21.837 -28.733 -22.757 1.00 49.21  ? 282 THR B OG1 1 
ATOM   3276 C  CG2 . THR B 2 108 ? -20.632 -26.654 -22.839 1.00 58.87  ? 282 THR B CG2 1 
ATOM   3277 N  N   . ASP B 2 109 ? -24.142 -28.759 -20.621 1.00 60.46  ? 283 ASP B N   1 
ATOM   3278 C  CA  . ASP B 2 109 ? -25.224 -29.730 -20.501 1.00 61.03  ? 283 ASP B CA  1 
ATOM   3279 C  C   . ASP B 2 109 ? -25.089 -30.905 -21.484 1.00 57.56  ? 283 ASP B C   1 
ATOM   3280 O  O   . ASP B 2 109 ? -26.102 -31.507 -21.814 1.00 52.09  ? 283 ASP B O   1 
ATOM   3281 C  CB  . ASP B 2 109 ? -26.585 -29.044 -20.667 1.00 69.13  ? 283 ASP B CB  1 
ATOM   3282 C  CG  . ASP B 2 109 ? -27.756 -29.762 -20.013 1.00 81.45  ? 283 ASP B CG  1 
ATOM   3283 O  OD1 . ASP B 2 109 ? -27.510 -30.715 -19.230 1.00 82.64  ? 283 ASP B OD1 1 
ATOM   3284 O  OD2 . ASP B 2 109 ? -28.913 -29.367 -20.301 1.00 91.27  ? 283 ASP B OD2 1 
ATOM   3285 N  N   . ASP B 2 110 ? -23.864 -31.281 -21.903 1.00 58.37  ? 284 ASP B N   1 
ATOM   3286 C  CA  . ASP B 2 110 ? -23.614 -32.331 -22.904 1.00 60.91  ? 284 ASP B CA  1 
ATOM   3287 C  C   . ASP B 2 110 ? -24.127 -31.954 -24.307 1.00 54.88  ? 284 ASP B C   1 
ATOM   3288 O  O   . ASP B 2 110 ? -24.404 -32.829 -25.139 1.00 50.85  ? 284 ASP B O   1 
ATOM   3289 C  CB  . ASP B 2 110 ? -24.197 -33.690 -22.488 1.00 69.32  ? 284 ASP B CB  1 
ATOM   3290 C  CG  . ASP B 2 110 ? -23.343 -34.489 -21.521 1.00 77.52  ? 284 ASP B CG  1 
ATOM   3291 O  OD1 . ASP B 2 110 ? -22.400 -33.909 -20.944 1.00 86.25  ? 284 ASP B OD1 1 
ATOM   3292 O  OD2 . ASP B 2 110 ? -23.627 -35.696 -21.363 1.00 85.93  ? 284 ASP B OD2 1 
ATOM   3293 N  N   . THR B 2 111 ? -24.239 -30.645 -24.578 1.00 48.40  ? 285 THR B N   1 
ATOM   3294 C  CA  . THR B 2 111 ? -24.498 -30.124 -25.912 1.00 48.05  ? 285 THR B CA  1 
ATOM   3295 C  C   . THR B 2 111 ? -23.356 -30.548 -26.843 1.00 48.96  ? 285 THR B C   1 
ATOM   3296 O  O   . THR B 2 111 ? -23.610 -30.787 -28.020 1.00 53.69  ? 285 THR B O   1 
ATOM   3297 C  CB  . THR B 2 111 ? -24.717 -28.602 -25.870 1.00 53.00  ? 285 THR B CB  1 
ATOM   3298 O  OG1 . THR B 2 111 ? -25.802 -28.281 -24.998 1.00 48.87  ? 285 THR B OG1 1 
ATOM   3299 C  CG2 . THR B 2 111 ? -25.025 -27.997 -27.221 1.00 56.91  ? 285 THR B CG2 1 
ATOM   3300 N  N   . TYR B 2 112 ? -22.119 -30.647 -26.305 1.00 43.19  ? 286 TYR B N   1 
ATOM   3301 C  CA  . TYR B 2 112 ? -20.908 -31.064 -27.020 1.00 43.24  ? 286 TYR B CA  1 
ATOM   3302 C  C   . TYR B 2 112 ? -20.138 -32.132 -26.236 1.00 43.36  ? 286 TYR B C   1 
ATOM   3303 O  O   . TYR B 2 112 ? -20.380 -32.317 -25.051 1.00 52.75  ? 286 TYR B O   1 
ATOM   3304 C  CB  . TYR B 2 112 ? -19.965 -29.879 -27.248 1.00 43.41  ? 286 TYR B CB  1 
ATOM   3305 C  CG  . TYR B 2 112 ? -20.665 -28.654 -27.768 1.00 44.25  ? 286 TYR B CG  1 
ATOM   3306 C  CD1 . TYR B 2 112 ? -21.153 -28.610 -29.066 1.00 44.94  ? 286 TYR B CD1 1 
ATOM   3307 C  CD2 . TYR B 2 112 ? -20.882 -27.558 -26.947 1.00 45.52  ? 286 TYR B CD2 1 
ATOM   3308 C  CE1 . TYR B 2 112 ? -21.835 -27.501 -29.541 1.00 46.78  ? 286 TYR B CE1 1 
ATOM   3309 C  CE2 . TYR B 2 112 ? -21.545 -26.432 -27.414 1.00 46.53  ? 286 TYR B CE2 1 
ATOM   3310 C  CZ  . TYR B 2 112 ? -22.034 -26.412 -28.709 1.00 43.95  ? 286 TYR B CZ  1 
ATOM   3311 O  OH  . TYR B 2 112 ? -22.693 -25.304 -29.162 1.00 43.78  ? 286 TYR B OH  1 
ATOM   3312 N  N   . THR B 2 113 ? -19.199 -32.820 -26.902 1.00 43.49  ? 287 THR B N   1 
ATOM   3313 C  CA  . THR B 2 113 ? -18.402 -33.886 -26.306 1.00 47.25  ? 287 THR B CA  1 
ATOM   3314 C  C   . THR B 2 113 ? -17.027 -33.352 -25.901 1.00 48.43  ? 287 THR B C   1 
ATOM   3315 O  O   . THR B 2 113 ? -16.610 -32.292 -26.360 1.00 42.04  ? 287 THR B O   1 
ATOM   3316 C  CB  . THR B 2 113 ? -18.233 -35.066 -27.272 1.00 50.39  ? 287 THR B CB  1 
ATOM   3317 O  OG1 . THR B 2 113 ? -17.585 -34.606 -28.461 1.00 53.68  ? 287 THR B OG1 1 
ATOM   3318 C  CG2 . THR B 2 113 ? -19.556 -35.708 -27.619 1.00 53.92  ? 287 THR B CG2 1 
ATOM   3319 N  N   . LYS B 2 114 ? -16.327 -34.114 -25.053 1.00 49.95  ? 288 LYS B N   1 
ATOM   3320 C  CA  . LYS B 2 114 ? -14.969 -33.785 -24.646 1.00 57.97  ? 288 LYS B CA  1 
ATOM   3321 C  C   . LYS B 2 114 ? -14.120 -33.612 -25.905 1.00 51.48  ? 288 LYS B C   1 
ATOM   3322 O  O   . LYS B 2 114 ? -13.347 -32.661 -26.007 1.00 48.72  ? 288 LYS B O   1 
ATOM   3323 C  CB  . LYS B 2 114 ? -14.413 -34.851 -23.692 1.00 63.12  ? 288 LYS B CB  1 
ATOM   3324 C  CG  . LYS B 2 114 ? -13.164 -34.428 -22.935 1.00 70.19  ? 288 LYS B CG  1 
ATOM   3325 C  CD  . LYS B 2 114 ? -12.532 -35.502 -22.089 1.00 74.87  ? 288 LYS B CD  1 
ATOM   3326 C  CE  . LYS B 2 114 ? -11.082 -35.173 -21.814 1.00 82.29  ? 288 LYS B CE  1 
ATOM   3327 N  NZ  . LYS B 2 114 ? -10.437 -36.183 -20.947 1.00 93.83  ? 288 LYS B NZ  1 
ATOM   3328 N  N   . LYS B 2 115 ? -14.340 -34.501 -26.880 1.00 54.56  ? 289 LYS B N   1 
ATOM   3329 C  CA  . LYS B 2 115 ? -13.644 -34.496 -28.163 1.00 62.21  ? 289 LYS B CA  1 
ATOM   3330 C  C   . LYS B 2 115 ? -13.820 -33.147 -28.880 1.00 54.98  ? 289 LYS B C   1 
ATOM   3331 O  O   . LYS B 2 115 ? -12.835 -32.546 -29.303 1.00 50.34  ? 289 LYS B O   1 
ATOM   3332 C  CB  . LYS B 2 115 ? -14.106 -35.699 -28.998 1.00 77.26  ? 289 LYS B CB  1 
ATOM   3333 C  CG  . LYS B 2 115 ? -13.711 -37.061 -28.430 1.00 102.96 ? 289 LYS B CG  1 
ATOM   3334 C  CD  . LYS B 2 115 ? -14.224 -38.258 -29.228 1.00 126.69 ? 289 LYS B CD  1 
ATOM   3335 C  CE  . LYS B 2 115 ? -13.794 -39.596 -28.651 1.00 128.90 ? 289 LYS B CE  1 
ATOM   3336 N  NZ  . LYS B 2 115 ? -14.328 -40.725 -29.452 1.00 129.80 ? 289 LYS B NZ  1 
ATOM   3337 N  N   . GLN B 2 116 ? -15.058 -32.645 -28.999 1.00 50.31  ? 290 GLN B N   1 
ATOM   3338 C  CA  . GLN B 2 116 ? -15.321 -31.413 -29.740 1.00 49.26  ? 290 GLN B CA  1 
ATOM   3339 C  C   . GLN B 2 116 ? -14.647 -30.213 -29.072 1.00 45.97  ? 290 GLN B C   1 
ATOM   3340 O  O   . GLN B 2 116 ? -14.030 -29.383 -29.739 1.00 45.15  ? 290 GLN B O   1 
ATOM   3341 C  CB  . GLN B 2 116 ? -16.826 -31.165 -29.857 1.00 49.56  ? 290 GLN B CB  1 
ATOM   3342 C  CG  . GLN B 2 116 ? -17.541 -32.152 -30.772 1.00 51.11  ? 290 GLN B CG  1 
ATOM   3343 C  CD  . GLN B 2 116 ? -19.038 -31.956 -30.734 1.00 52.55  ? 290 GLN B CD  1 
ATOM   3344 O  OE1 . GLN B 2 116 ? -19.661 -32.064 -29.681 1.00 51.56  ? 290 GLN B OE1 1 
ATOM   3345 N  NE2 . GLN B 2 116 ? -19.628 -31.643 -31.879 1.00 50.81  ? 290 GLN B NE2 1 
ATOM   3346 N  N   . VAL B 2 117 ? -14.786 -30.122 -27.748 1.00 47.40  ? 291 VAL B N   1 
ATOM   3347 C  CA  . VAL B 2 117 ? -14.241 -29.024 -26.957 1.00 44.98  ? 291 VAL B CA  1 
ATOM   3348 C  C   . VAL B 2 117 ? -12.714 -28.945 -27.082 1.00 41.78  ? 291 VAL B C   1 
ATOM   3349 O  O   . VAL B 2 117 ? -12.177 -27.846 -27.214 1.00 39.51  ? 291 VAL B O   1 
ATOM   3350 C  CB  . VAL B 2 117 ? -14.685 -29.132 -25.485 1.00 46.75  ? 291 VAL B CB  1 
ATOM   3351 C  CG1 . VAL B 2 117 ? -13.973 -28.108 -24.607 1.00 48.05  ? 291 VAL B CG1 1 
ATOM   3352 C  CG2 . VAL B 2 117 ? -16.196 -28.998 -25.346 1.00 46.48  ? 291 VAL B CG2 1 
ATOM   3353 N  N   . LEU B 2 118 ? -12.012 -30.084 -27.017 1.00 41.08  ? 292 LEU B N   1 
ATOM   3354 C  CA  . LEU B 2 118 ? -10.554 -30.110 -27.148 1.00 46.08  ? 292 LEU B CA  1 
ATOM   3355 C  C   . LEU B 2 118 ? -10.112 -29.656 -28.542 1.00 45.43  ? 292 LEU B C   1 
ATOM   3356 O  O   . LEU B 2 118 ? -9.175  -28.873 -28.678 1.00 45.50  ? 292 LEU B O   1 
ATOM   3357 C  CB  . LEU B 2 118 ? -10.056 -31.530 -26.869 1.00 51.14  ? 292 LEU B CB  1 
ATOM   3358 C  CG  . LEU B 2 118 ? -10.182 -31.981 -25.418 1.00 55.73  ? 292 LEU B CG  1 
ATOM   3359 C  CD1 . LEU B 2 118 ? -9.855  -33.459 -25.275 1.00 64.11  ? 292 LEU B CD1 1 
ATOM   3360 C  CD2 . LEU B 2 118 ? -9.272  -31.153 -24.541 1.00 55.62  ? 292 LEU B CD2 1 
ATOM   3361 N  N   . ARG B 2 119 ? -10.815 -30.146 -29.569 1.00 46.29  ? 293 ARG B N   1 
ATOM   3362 C  CA  . ARG B 2 119 ? -10.551 -29.813 -30.963 1.00 47.61  ? 293 ARG B CA  1 
ATOM   3363 C  C   . ARG B 2 119 ? -10.819 -28.335 -31.241 1.00 38.57  ? 293 ARG B C   1 
ATOM   3364 O  O   . ARG B 2 119 ? -10.127 -27.728 -32.048 1.00 38.09  ? 293 ARG B O   1 
ATOM   3365 C  CB  . ARG B 2 119 ? -11.384 -30.709 -31.887 1.00 52.54  ? 293 ARG B CB  1 
ATOM   3366 C  CG  . ARG B 2 119 ? -10.640 -31.948 -32.361 1.00 58.91  ? 293 ARG B CG  1 
ATOM   3367 C  CD  . ARG B 2 119 ? -11.538 -33.131 -32.650 1.00 68.29  ? 293 ARG B CD  1 
ATOM   3368 N  NE  . ARG B 2 119 ? -10.972 -33.970 -33.700 1.00 80.90  ? 293 ARG B NE  1 
ATOM   3369 C  CZ  . ARG B 2 119 ? -11.267 -35.251 -33.895 1.00 88.93  ? 293 ARG B CZ  1 
ATOM   3370 N  NH1 . ARG B 2 119 ? -12.112 -35.879 -33.092 1.00 88.69  ? 293 ARG B NH1 1 
ATOM   3371 N  NH2 . ARG B 2 119 ? -10.699 -35.907 -34.894 1.00 90.39  ? 293 ARG B NH2 1 
ATOM   3372 N  N   . MET B 2 120 ? -11.810 -27.755 -30.569 1.00 35.80  ? 294 MET B N   1 
ATOM   3373 C  CA  . MET B 2 120 ? -12.143 -26.351 -30.775 1.00 38.36  ? 294 MET B CA  1 
ATOM   3374 C  C   . MET B 2 120 ? -11.060 -25.498 -30.108 1.00 38.13  ? 294 MET B C   1 
ATOM   3375 O  O   . MET B 2 120 ? -10.673 -24.451 -30.629 1.00 40.77  ? 294 MET B O   1 
ATOM   3376 C  CB  . MET B 2 120 ? -13.538 -26.005 -30.228 1.00 42.22  ? 294 MET B CB  1 
ATOM   3377 C  CG  . MET B 2 120 ? -13.889 -24.512 -30.327 1.00 45.98  ? 294 MET B CG  1 
ATOM   3378 S  SD  . MET B 2 120 ? -13.970 -23.891 -32.035 1.00 47.80  ? 294 MET B SD  1 
ATOM   3379 C  CE  . MET B 2 120 ? -15.657 -24.339 -32.452 1.00 50.40  ? 294 MET B CE  1 
ATOM   3380 N  N   . GLU B 2 121 ? -10.543 -25.962 -28.966 1.00 39.37  ? 295 GLU B N   1 
ATOM   3381 C  CA  . GLU B 2 121 ? -9.361  -25.361 -28.365 1.00 44.14  ? 295 GLU B CA  1 
ATOM   3382 C  C   . GLU B 2 121 ? -8.247  -25.258 -29.418 1.00 42.30  ? 295 GLU B C   1 
ATOM   3383 O  O   . GLU B 2 121 ? -7.700  -24.176 -29.619 1.00 39.15  ? 295 GLU B O   1 
ATOM   3384 C  CB  . GLU B 2 121 ? -8.913  -26.155 -27.133 1.00 50.48  ? 295 GLU B CB  1 
ATOM   3385 C  CG  . GLU B 2 121 ? -7.914  -25.406 -26.265 1.00 58.52  ? 295 GLU B CG  1 
ATOM   3386 C  CD  . GLU B 2 121 ? -7.309  -26.201 -25.119 1.00 61.09  ? 295 GLU B CD  1 
ATOM   3387 O  OE1 . GLU B 2 121 ? -6.868  -27.350 -25.363 1.00 60.57  ? 295 GLU B OE1 1 
ATOM   3388 O  OE2 . GLU B 2 121 ? -7.276  -25.668 -23.987 1.00 66.21  ? 295 GLU B OE2 1 
ATOM   3389 N  N   A HIS B 2 122 ? -7.929  -26.384 -30.082 0.50 40.63  ? 296 HIS B N   1 
ATOM   3390 N  N   B HIS B 2 122 ? -7.959  -26.370 -30.105 0.50 41.80  ? 296 HIS B N   1 
ATOM   3391 C  CA  A HIS B 2 122 ? -6.921  -26.444 -31.136 0.50 41.07  ? 296 HIS B CA  1 
ATOM   3392 C  CA  B HIS B 2 122 ? -6.909  -26.411 -31.112 0.50 43.15  ? 296 HIS B CA  1 
ATOM   3393 C  C   A HIS B 2 122 ? -7.173  -25.347 -32.172 0.50 41.46  ? 296 HIS B C   1 
ATOM   3394 C  C   B HIS B 2 122 ? -7.170  -25.342 -32.175 0.50 42.52  ? 296 HIS B C   1 
ATOM   3395 O  O   A HIS B 2 122 ? -6.273  -24.571 -32.488 0.50 41.45  ? 296 HIS B O   1 
ATOM   3396 O  O   B HIS B 2 122 ? -6.277  -24.559 -32.498 0.50 42.36  ? 296 HIS B O   1 
ATOM   3397 C  CB  A HIS B 2 122 ? -6.863  -27.842 -31.777 0.50 42.37  ? 296 HIS B CB  1 
ATOM   3398 C  CB  B HIS B 2 122 ? -6.743  -27.837 -31.658 0.50 46.39  ? 296 HIS B CB  1 
ATOM   3399 C  CG  A HIS B 2 122 ? -5.901  -27.972 -32.928 0.50 44.11  ? 296 HIS B CG  1 
ATOM   3400 C  CG  B HIS B 2 122 ? -5.816  -28.698 -30.849 0.50 49.53  ? 296 HIS B CG  1 
ATOM   3401 N  ND1 A HIS B 2 122 ? -4.711  -28.664 -32.837 0.50 41.19  ? 296 HIS B ND1 1 
ATOM   3402 N  ND1 B HIS B 2 122 ? -4.653  -28.223 -30.282 0.50 50.58  ? 296 HIS B ND1 1 
ATOM   3403 C  CD2 A HIS B 2 122 ? -5.953  -27.501 -34.188 0.50 45.62  ? 296 HIS B CD2 1 
ATOM   3404 C  CD2 B HIS B 2 122 ? -5.883  -29.987 -30.497 0.50 52.84  ? 296 HIS B CD2 1 
ATOM   3405 C  CE1 A HIS B 2 122 ? -4.071  -28.593 -33.997 0.50 43.45  ? 296 HIS B CE1 1 
ATOM   3406 C  CE1 B HIS B 2 122 ? -4.042  -29.203 -29.632 0.50 50.71  ? 296 HIS B CE1 1 
ATOM   3407 N  NE2 A HIS B 2 122 ? -4.803  -27.893 -34.832 0.50 44.08  ? 296 HIS B NE2 1 
ATOM   3408 N  NE2 B HIS B 2 122 ? -4.777  -30.284 -29.742 0.50 50.58  ? 296 HIS B NE2 1 
ATOM   3409 N  N   . LEU B 2 123 ? -8.408  -25.277 -32.682 1.00 38.55  ? 297 LEU B N   1 
ATOM   3410 C  CA  . LEU B 2 123 ? -8.750  -24.331 -33.736 1.00 39.05  ? 297 LEU B CA  1 
ATOM   3411 C  C   . LEU B 2 123 ? -8.694  -22.875 -33.257 1.00 36.75  ? 297 LEU B C   1 
ATOM   3412 O  O   . LEU B 2 123 ? -8.333  -21.999 -34.036 1.00 41.60  ? 297 LEU B O   1 
ATOM   3413 C  CB  . LEU B 2 123 ? -10.133 -24.691 -34.302 1.00 42.31  ? 297 LEU B CB  1 
ATOM   3414 C  CG  . LEU B 2 123 ? -10.621 -23.847 -35.476 1.00 41.06  ? 297 LEU B CG  1 
ATOM   3415 C  CD1 . LEU B 2 123 ? -9.679  -24.005 -36.651 1.00 42.39  ? 297 LEU B CD1 1 
ATOM   3416 C  CD2 . LEU B 2 123 ? -12.051 -24.220 -35.878 1.00 42.69  ? 297 LEU B CD2 1 
ATOM   3417 N  N   . VAL B 2 124 ? -9.098  -22.586 -32.013 1.00 40.44  ? 298 VAL B N   1 
ATOM   3418 C  CA  . VAL B 2 124 ? -9.071  -21.213 -31.516 1.00 39.29  ? 298 VAL B CA  1 
ATOM   3419 C  C   . VAL B 2 124 ? -7.616  -20.752 -31.416 1.00 38.18  ? 298 VAL B C   1 
ATOM   3420 O  O   . VAL B 2 124 ? -7.300  -19.607 -31.731 1.00 36.13  ? 298 VAL B O   1 
ATOM   3421 C  CB  . VAL B 2 124 ? -9.802  -21.052 -30.167 1.00 38.98  ? 298 VAL B CB  1 
ATOM   3422 C  CG1 . VAL B 2 124 ? -9.631  -19.650 -29.595 1.00 41.40  ? 298 VAL B CG1 1 
ATOM   3423 C  CG2 . VAL B 2 124 ? -11.282 -21.389 -30.251 1.00 41.17  ? 298 VAL B CG2 1 
ATOM   3424 N  N   . LEU B 2 125 ? -6.737  -21.646 -30.949 1.00 39.03  ? 299 LEU B N   1 
ATOM   3425 C  CA  . LEU B 2 125 ? -5.320  -21.331 -30.793 1.00 41.10  ? 299 LEU B CA  1 
ATOM   3426 C  C   . LEU B 2 125 ? -4.705  -21.009 -32.154 1.00 41.63  ? 299 LEU B C   1 
ATOM   3427 O  O   . LEU B 2 125 ? -4.008  -20.003 -32.286 1.00 42.02  ? 299 LEU B O   1 
ATOM   3428 C  CB  . LEU B 2 125 ? -4.601  -22.502 -30.116 1.00 40.52  ? 299 LEU B CB  1 
ATOM   3429 C  CG  . LEU B 2 125 ? -4.728  -22.540 -28.598 1.00 41.50  ? 299 LEU B CG  1 
ATOM   3430 C  CD1 . LEU B 2 125 ? -4.354  -23.919 -28.072 1.00 43.32  ? 299 LEU B CD1 1 
ATOM   3431 C  CD2 . LEU B 2 125 ? -3.866  -21.466 -27.968 1.00 42.73  ? 299 LEU B CD2 1 
ATOM   3432 N  N   . LYS B 2 126 ? -4.998  -21.843 -33.160 1.00 40.01  ? 300 LYS B N   1 
ATOM   3433 C  CA  . LYS B 2 126 ? -4.569  -21.583 -34.526 1.00 43.13  ? 300 LYS B CA  1 
ATOM   3434 C  C   . LYS B 2 126 ? -5.069  -20.221 -35.007 1.00 42.61  ? 300 LYS B C   1 
ATOM   3435 O  O   . LYS B 2 126 ? -4.305  -19.423 -35.539 1.00 44.55  ? 300 LYS B O   1 
ATOM   3436 C  CB  . LYS B 2 126 ? -5.058  -22.687 -35.458 1.00 48.88  ? 300 LYS B CB  1 
ATOM   3437 C  CG  . LYS B 2 126 ? -4.590  -22.543 -36.896 1.00 58.74  ? 300 LYS B CG  1 
ATOM   3438 C  CD  . LYS B 2 126 ? -5.153  -23.598 -37.808 1.00 70.06  ? 300 LYS B CD  1 
ATOM   3439 C  CE  . LYS B 2 126 ? -4.975  -24.996 -37.255 1.00 76.98  ? 300 LYS B CE  1 
ATOM   3440 N  NZ  . LYS B 2 126 ? -5.154  -26.010 -38.319 1.00 82.11  ? 300 LYS B NZ  1 
ATOM   3441 N  N   . VAL B 2 127 ? -6.357  -19.939 -34.821 1.00 42.77  ? 301 VAL B N   1 
ATOM   3442 C  CA  . VAL B 2 127 ? -6.932  -18.722 -35.367 1.00 42.99  ? 301 VAL B CA  1 
ATOM   3443 C  C   . VAL B 2 127 ? -6.319  -17.506 -34.683 1.00 44.30  ? 301 VAL B C   1 
ATOM   3444 O  O   . VAL B 2 127 ? -6.129  -16.483 -35.342 1.00 50.73  ? 301 VAL B O   1 
ATOM   3445 C  CB  . VAL B 2 127 ? -8.467  -18.737 -35.287 1.00 43.10  ? 301 VAL B CB  1 
ATOM   3446 C  CG1 . VAL B 2 127 ? -9.080  -17.373 -35.577 1.00 40.53  ? 301 VAL B CG1 1 
ATOM   3447 C  CG2 . VAL B 2 127 ? -9.015  -19.789 -36.235 1.00 42.82  ? 301 VAL B CG2 1 
ATOM   3448 N  N   . LEU B 2 128 ? -6.005  -17.621 -33.383 1.00 44.88  ? 302 LEU B N   1 
ATOM   3449 C  CA  . LEU B 2 128 ? -5.465  -16.499 -32.622 1.00 43.09  ? 302 LEU B CA  1 
ATOM   3450 C  C   . LEU B 2 128 ? -3.933  -16.481 -32.703 1.00 40.48  ? 302 LEU B C   1 
ATOM   3451 O  O   . LEU B 2 128 ? -3.303  -15.615 -32.107 1.00 43.25  ? 302 LEU B O   1 
ATOM   3452 C  CB  . LEU B 2 128 ? -5.957  -16.584 -31.169 1.00 45.56  ? 302 LEU B CB  1 
ATOM   3453 C  CG  . LEU B 2 128 ? -7.468  -16.470 -30.937 1.00 49.10  ? 302 LEU B CG  1 
ATOM   3454 C  CD1 . LEU B 2 128 ? -7.778  -16.491 -29.457 1.00 47.97  ? 302 LEU B CD1 1 
ATOM   3455 C  CD2 . LEU B 2 128 ? -8.061  -15.208 -31.538 1.00 53.47  ? 302 LEU B CD2 1 
ATOM   3456 N  N   . THR B 2 129 ? -3.345  -17.421 -33.461 1.00 45.59  ? 303 THR B N   1 
ATOM   3457 C  CA  . THR B 2 129 ? -1.899  -17.639 -33.566 1.00 51.09  ? 303 THR B CA  1 
ATOM   3458 C  C   . THR B 2 129 ? -1.236  -17.647 -32.183 1.00 50.03  ? 303 THR B C   1 
ATOM   3459 O  O   . THR B 2 129 ? -0.125  -17.146 -32.029 1.00 51.83  ? 303 THR B O   1 
ATOM   3460 C  CB  . THR B 2 129 ? -1.217  -16.600 -34.471 1.00 54.79  ? 303 THR B CB  1 
ATOM   3461 O  OG1 . THR B 2 129 ? -1.366  -15.324 -33.846 1.00 54.26  ? 303 THR B OG1 1 
ATOM   3462 C  CG2 . THR B 2 129 ? -1.759  -16.583 -35.885 1.00 55.60  ? 303 THR B CG2 1 
ATOM   3463 N  N   . PHE B 2 130 ? -1.952  -18.183 -31.183 1.00 45.38  ? 304 PHE B N   1 
ATOM   3464 C  CA  . PHE B 2 130 ? -1.497  -18.319 -29.809 1.00 45.27  ? 304 PHE B CA  1 
ATOM   3465 C  C   . PHE B 2 130 ? -1.262  -16.968 -29.123 1.00 44.07  ? 304 PHE B C   1 
ATOM   3466 O  O   . PHE B 2 130 ? -0.532  -16.930 -28.140 1.00 42.22  ? 304 PHE B O   1 
ATOM   3467 C  CB  . PHE B 2 130 ? -0.231  -19.177 -29.738 1.00 46.54  ? 304 PHE B CB  1 
ATOM   3468 C  CG  . PHE B 2 130 ? -0.405  -20.658 -29.970 1.00 47.96  ? 304 PHE B CG  1 
ATOM   3469 C  CD1 . PHE B 2 130 ? -0.545  -21.167 -31.253 1.00 54.57  ? 304 PHE B CD1 1 
ATOM   3470 C  CD2 . PHE B 2 130 ? -0.355  -21.554 -28.910 1.00 52.00  ? 304 PHE B CD2 1 
ATOM   3471 C  CE1 . PHE B 2 130 ? -0.660  -22.534 -31.472 1.00 54.78  ? 304 PHE B CE1 1 
ATOM   3472 C  CE2 . PHE B 2 130 ? -0.484  -22.920 -29.126 1.00 55.82  ? 304 PHE B CE2 1 
ATOM   3473 C  CZ  . PHE B 2 130 ? -0.630  -23.410 -30.409 1.00 53.87  ? 304 PHE B CZ  1 
ATOM   3474 N  N   . ASP B 2 131 ? -1.906  -15.884 -29.585 1.00 42.23  ? 305 ASP B N   1 
ATOM   3475 C  CA  . ASP B 2 131 ? -1.753  -14.572 -28.964 1.00 45.78  ? 305 ASP B CA  1 
ATOM   3476 C  C   . ASP B 2 131 ? -2.863  -14.344 -27.944 1.00 46.87  ? 305 ASP B C   1 
ATOM   3477 O  O   . ASP B 2 131 ? -3.866  -13.714 -28.254 1.00 54.95  ? 305 ASP B O   1 
ATOM   3478 C  CB  . ASP B 2 131 ? -1.791  -13.431 -29.982 1.00 50.20  ? 305 ASP B CB  1 
ATOM   3479 C  CG  . ASP B 2 131 ? -0.690  -13.494 -31.023 1.00 57.27  ? 305 ASP B CG  1 
ATOM   3480 O  OD1 . ASP B 2 131 ? 0.467   -13.755 -30.624 1.00 63.56  ? 305 ASP B OD1 1 
ATOM   3481 O  OD2 . ASP B 2 131 ? -1.005  -13.281 -32.220 1.00 57.18  ? 305 ASP B OD2 1 
ATOM   3482 N  N   . LEU B 2 132 ? -2.650  -14.795 -26.708 1.00 44.94  ? 306 LEU B N   1 
ATOM   3483 C  CA  . LEU B 2 132 ? -3.697  -14.826 -25.697 1.00 41.02  ? 306 LEU B CA  1 
ATOM   3484 C  C   . LEU B 2 132 ? -3.577  -13.721 -24.654 1.00 38.92  ? 306 LEU B C   1 
ATOM   3485 O  O   . LEU B 2 132 ? -4.508  -13.518 -23.875 1.00 45.80  ? 306 LEU B O   1 
ATOM   3486 C  CB  . LEU B 2 132 ? -3.611  -16.189 -25.027 1.00 41.44  ? 306 LEU B CB  1 
ATOM   3487 C  CG  . LEU B 2 132 ? -3.798  -17.342 -25.998 1.00 45.61  ? 306 LEU B CG  1 
ATOM   3488 C  CD1 . LEU B 2 132 ? -3.537  -18.644 -25.289 1.00 53.36  ? 306 LEU B CD1 1 
ATOM   3489 C  CD2 . LEU B 2 132 ? -5.192  -17.322 -26.595 1.00 47.87  ? 306 LEU B CD2 1 
ATOM   3490 N  N   . ALA B 2 133 ? -2.460  -12.999 -24.642 1.00 40.97  ? 307 ALA B N   1 
ATOM   3491 C  CA  . ALA B 2 133 ? -2.187  -12.025 -23.595 1.00 47.03  ? 307 ALA B CA  1 
ATOM   3492 C  C   . ALA B 2 133 ? -2.733  -10.655 -23.999 1.00 47.34  ? 307 ALA B C   1 
ATOM   3493 O  O   . ALA B 2 133 ? -1.957  -9.723  -24.173 1.00 58.08  ? 307 ALA B O   1 
ATOM   3494 C  CB  . ALA B 2 133 ? -0.694  -11.969 -23.337 1.00 47.84  ? 307 ALA B CB  1 
ATOM   3495 N  N   . ALA B 2 134 ? -4.060  -10.518 -24.107 1.00 46.85  ? 308 ALA B N   1 
ATOM   3496 C  CA  . ALA B 2 134 ? -4.668  -9.288  -24.615 1.00 46.03  ? 308 ALA B CA  1 
ATOM   3497 C  C   . ALA B 2 134 ? -4.970  -8.342  -23.463 1.00 42.67  ? 308 ALA B C   1 
ATOM   3498 O  O   . ALA B 2 134 ? -5.367  -8.810  -22.405 1.00 43.98  ? 308 ALA B O   1 
ATOM   3499 C  CB  . ALA B 2 134 ? -5.939  -9.588  -25.370 1.00 46.26  ? 308 ALA B CB  1 
ATOM   3500 N  N   . PRO B 2 135 ? -4.787  -7.010  -23.632 1.00 40.46  ? 309 PRO B N   1 
ATOM   3501 C  CA  . PRO B 2 135 ? -5.287  -6.027  -22.668 1.00 42.31  ? 309 PRO B CA  1 
ATOM   3502 C  C   . PRO B 2 135 ? -6.812  -5.990  -22.583 1.00 40.53  ? 309 PRO B C   1 
ATOM   3503 O  O   . PRO B 2 135 ? -7.485  -6.098  -23.591 1.00 42.01  ? 309 PRO B O   1 
ATOM   3504 C  CB  . PRO B 2 135 ? -4.783  -4.675  -23.204 1.00 45.44  ? 309 PRO B CB  1 
ATOM   3505 C  CG  . PRO B 2 135 ? -3.629  -5.055  -24.113 1.00 47.11  ? 309 PRO B CG  1 
ATOM   3506 C  CD  . PRO B 2 135 ? -4.031  -6.382  -24.727 1.00 42.70  ? 309 PRO B CD  1 
ATOM   3507 N  N   . THR B 2 136 ? -7.342  -5.811  -21.372 1.00 41.49  ? 310 THR B N   1 
ATOM   3508 C  CA  . THR B 2 136 ? -8.777  -5.807  -21.118 1.00 43.23  ? 310 THR B CA  1 
ATOM   3509 C  C   . THR B 2 136 ? -9.139  -4.513  -20.404 1.00 42.15  ? 310 THR B C   1 
ATOM   3510 O  O   . THR B 2 136 ? -8.258  -3.894  -19.807 1.00 40.01  ? 310 THR B O   1 
ATOM   3511 C  CB  . THR B 2 136 ? -9.210  -7.003  -20.254 1.00 44.27  ? 310 THR B CB  1 
ATOM   3512 O  OG1 . THR B 2 136 ? -8.548  -6.906  -18.988 1.00 43.04  ? 310 THR B OG1 1 
ATOM   3513 C  CG2 . THR B 2 136 ? -8.907  -8.334  -20.910 1.00 43.70  ? 310 THR B CG2 1 
ATOM   3514 N  N   . VAL B 2 137 ? -10.426 -4.141  -20.476 1.00 40.92  ? 311 VAL B N   1 
ATOM   3515 C  CA  . VAL B 2 137 ? -11.023 -3.067  -19.683 1.00 42.39  ? 311 VAL B CA  1 
ATOM   3516 C  C   . VAL B 2 137 ? -10.595 -3.244  -18.225 1.00 42.23  ? 311 VAL B C   1 
ATOM   3517 O  O   . VAL B 2 137 ? -10.245 -2.286  -17.546 1.00 48.98  ? 311 VAL B O   1 
ATOM   3518 C  CB  . VAL B 2 137 ? -12.564 -3.061  -19.831 1.00 42.40  ? 311 VAL B CB  1 
ATOM   3519 C  CG1 . VAL B 2 137 ? -13.271 -2.114  -18.861 1.00 40.87  ? 311 VAL B CG1 1 
ATOM   3520 C  CG2 . VAL B 2 137 ? -12.974 -2.756  -21.260 1.00 42.98  ? 311 VAL B CG2 1 
ATOM   3521 N  N   . ASN B 2 138 ? -10.632 -4.487  -17.759 1.00 45.08  ? 312 ASN B N   1 
ATOM   3522 C  CA  . ASN B 2 138 ? -10.186 -4.874  -16.428 1.00 46.68  ? 312 ASN B CA  1 
ATOM   3523 C  C   . ASN B 2 138 ? -8.783  -4.350  -16.097 1.00 46.25  ? 312 ASN B C   1 
ATOM   3524 O  O   . ASN B 2 138 ? -8.582  -3.674  -15.078 1.00 44.74  ? 312 ASN B O   1 
ATOM   3525 C  CB  . ASN B 2 138 ? -10.175 -6.395  -16.322 1.00 53.21  ? 312 ASN B CB  1 
ATOM   3526 C  CG  . ASN B 2 138 ? -10.487 -6.871  -14.930 1.00 61.26  ? 312 ASN B CG  1 
ATOM   3527 O  OD1 . ASN B 2 138 ? -11.648 -6.850  -14.533 1.00 78.10  ? 312 ASN B OD1 1 
ATOM   3528 N  ND2 . ASN B 2 138 ? -9.469  -7.310  -14.206 1.00 65.95  ? 312 ASN B ND2 1 
ATOM   3529 N  N   . GLN B 2 139 ? -7.802  -4.704  -16.941 1.00 45.47  ? 313 GLN B N   1 
ATOM   3530 C  CA  . GLN B 2 139 ? -6.415  -4.319  -16.713 1.00 40.18  ? 313 GLN B CA  1 
ATOM   3531 C  C   . GLN B 2 139 ? -6.304  -2.802  -16.656 1.00 39.93  ? 313 GLN B C   1 
ATOM   3532 O  O   . GLN B 2 139 ? -5.522  -2.291  -15.856 1.00 44.60  ? 313 GLN B O   1 
ATOM   3533 C  CB  . GLN B 2 139 ? -5.479  -4.871  -17.785 1.00 41.10  ? 313 GLN B CB  1 
ATOM   3534 C  CG  . GLN B 2 139 ? -5.246  -6.372  -17.683 1.00 46.88  ? 313 GLN B CG  1 
ATOM   3535 C  CD  . GLN B 2 139 ? -4.633  -6.905  -18.956 1.00 51.72  ? 313 GLN B CD  1 
ATOM   3536 O  OE1 . GLN B 2 139 ? -3.494  -6.598  -19.293 1.00 61.42  ? 313 GLN B OE1 1 
ATOM   3537 N  NE2 . GLN B 2 139 ? -5.387  -7.715  -19.680 1.00 52.42  ? 313 GLN B NE2 1 
ATOM   3538 N  N   . PHE B 2 140 ? -7.093  -2.076  -17.468 1.00 37.55  ? 314 PHE B N   1 
ATOM   3539 C  CA  . PHE B 2 140 ? -7.035  -0.615  -17.454 1.00 36.12  ? 314 PHE B CA  1 
ATOM   3540 C  C   . PHE B 2 140 ? -7.713  -0.059  -16.206 1.00 37.23  ? 314 PHE B C   1 
ATOM   3541 O  O   . PHE B 2 140 ? -7.230  0.906   -15.625 1.00 42.45  ? 314 PHE B O   1 
ATOM   3542 C  CB  . PHE B 2 140 ? -7.589  -0.010  -18.743 1.00 36.01  ? 314 PHE B CB  1 
ATOM   3543 C  CG  . PHE B 2 140 ? -6.651  -0.147  -19.910 1.00 33.80  ? 314 PHE B CG  1 
ATOM   3544 C  CD1 . PHE B 2 140 ? -5.511  0.626   -19.989 1.00 38.25  ? 314 PHE B CD1 1 
ATOM   3545 C  CD2 . PHE B 2 140 ? -6.893  -1.062  -20.915 1.00 35.55  ? 314 PHE B CD2 1 
ATOM   3546 C  CE1 . PHE B 2 140 ? -4.640  0.496   -21.060 1.00 39.35  ? 314 PHE B CE1 1 
ATOM   3547 C  CE2 . PHE B 2 140 ? -6.017  -1.202  -21.979 1.00 36.65  ? 314 PHE B CE2 1 
ATOM   3548 C  CZ  . PHE B 2 140 ? -4.889  -0.426  -22.047 1.00 37.69  ? 314 PHE B CZ  1 
ATOM   3549 N  N   . LEU B 2 141 ? -8.809  -0.675  -15.767 1.00 40.83  ? 315 LEU B N   1 
ATOM   3550 C  CA  . LEU B 2 141 ? -9.487  -0.198  -14.575 1.00 39.92  ? 315 LEU B CA  1 
ATOM   3551 C  C   . LEU B 2 141 ? -8.561  -0.295  -13.365 1.00 43.16  ? 315 LEU B C   1 
ATOM   3552 O  O   . LEU B 2 141 ? -8.433  0.690   -12.644 1.00 44.61  ? 315 LEU B O   1 
ATOM   3553 C  CB  . LEU B 2 141 ? -10.784 -0.979  -14.373 1.00 42.60  ? 315 LEU B CB  1 
ATOM   3554 C  CG  . LEU B 2 141 ? -11.998 -0.391  -15.091 1.00 43.05  ? 315 LEU B CG  1 
ATOM   3555 C  CD1 . LEU B 2 141 ? -13.247 -1.189  -14.774 1.00 44.77  ? 315 LEU B CD1 1 
ATOM   3556 C  CD2 . LEU B 2 141 ? -12.224 1.062   -14.707 1.00 42.69  ? 315 LEU B CD2 1 
ATOM   3557 N  N   . THR B 2 142 ? -7.891  -1.444  -13.178 1.00 39.37  ? 316 THR B N   1 
ATOM   3558 C  CA  . THR B 2 142 ? -7.026  -1.635  -12.022 1.00 41.26  ? 316 THR B CA  1 
ATOM   3559 C  C   . THR B 2 142 ? -5.869  -0.626  -12.071 1.00 44.66  ? 316 THR B C   1 
ATOM   3560 O  O   . THR B 2 142 ? -5.512  -0.078  -11.027 1.00 47.31  ? 316 THR B O   1 
ATOM   3561 C  CB  . THR B 2 142 ? -6.615  -3.109  -11.836 1.00 41.73  ? 316 THR B CB  1 
ATOM   3562 O  OG1 . THR B 2 142 ? -5.698  -3.504  -12.853 1.00 39.43  ? 316 THR B OG1 1 
ATOM   3563 C  CG2 . THR B 2 142 ? -7.799  -4.059  -11.808 1.00 39.04  ? 316 THR B CG2 1 
ATOM   3564 N  N   . GLN B 2 143 ? -5.334  -0.326  -13.269 1.00 48.39  ? 317 GLN B N   1 
ATOM   3565 C  CA  . GLN B 2 143 ? -4.347  0.742   -13.441 1.00 50.05  ? 317 GLN B CA  1 
ATOM   3566 C  C   . GLN B 2 143 ? -4.925  2.070   -12.954 1.00 52.55  ? 317 GLN B C   1 
ATOM   3567 O  O   . GLN B 2 143 ? -4.241  2.816   -12.257 1.00 61.45  ? 317 GLN B O   1 
ATOM   3568 C  CB  . GLN B 2 143 ? -3.893  0.952   -14.892 1.00 53.11  ? 317 GLN B CB  1 
ATOM   3569 C  CG  . GLN B 2 143 ? -3.088  -0.195  -15.490 1.00 58.23  ? 317 GLN B CG  1 
ATOM   3570 C  CD  . GLN B 2 143 ? -1.597  0.032   -15.533 1.00 65.65  ? 317 GLN B CD  1 
ATOM   3571 O  OE1 . GLN B 2 143 ? -1.075  1.092   -15.185 1.00 64.94  ? 317 GLN B OE1 1 
ATOM   3572 N  NE2 . GLN B 2 143 ? -0.893  -0.991  -15.987 1.00 72.66  ? 317 GLN B NE2 1 
ATOM   3573 N  N   . TYR B 2 144 ? -6.165  2.389   -13.346 1.00 47.32  ? 318 TYR B N   1 
ATOM   3574 C  CA  . TYR B 2 144 ? -6.708  3.708   -13.053 1.00 45.09  ? 318 TYR B CA  1 
ATOM   3575 C  C   . TYR B 2 144 ? -7.004  3.832   -11.554 1.00 44.81  ? 318 TYR B C   1 
ATOM   3576 O  O   . TYR B 2 144 ? -6.819  4.909   -11.007 1.00 48.17  ? 318 TYR B O   1 
ATOM   3577 C  CB  . TYR B 2 144 ? -7.955  4.033   -13.882 1.00 42.53  ? 318 TYR B CB  1 
ATOM   3578 C  CG  . TYR B 2 144 ? -7.812  4.055   -15.387 1.00 44.61  ? 318 TYR B CG  1 
ATOM   3579 C  CD1 . TYR B 2 144 ? -6.578  4.055   -16.029 1.00 43.74  ? 318 TYR B CD1 1 
ATOM   3580 C  CD2 . TYR B 2 144 ? -8.950  4.084   -16.186 1.00 45.96  ? 318 TYR B CD2 1 
ATOM   3581 C  CE1 . TYR B 2 144 ? -6.480  4.099   -17.413 1.00 39.37  ? 318 TYR B CE1 1 
ATOM   3582 C  CE2 . TYR B 2 144 ? -8.870  4.102   -17.568 1.00 45.33  ? 318 TYR B CE2 1 
ATOM   3583 C  CZ  . TYR B 2 144 ? -7.629  4.109   -18.186 1.00 44.39  ? 318 TYR B CZ  1 
ATOM   3584 O  OH  . TYR B 2 144 ? -7.572  4.114   -19.561 1.00 46.26  ? 318 TYR B OH  1 
ATOM   3585 N  N   . PHE B 2 145 ? -7.473  2.754   -10.898 1.00 42.24  ? 319 PHE B N   1 
ATOM   3586 C  CA  . PHE B 2 145 ? -7.840  2.765   -9.480  1.00 41.33  ? 319 PHE B CA  1 
ATOM   3587 C  C   . PHE B 2 145 ? -6.688  3.186   -8.562  1.00 44.61  ? 319 PHE B C   1 
ATOM   3588 O  O   . PHE B 2 145 ? -6.975  3.639   -7.462  1.00 48.05  ? 319 PHE B O   1 
ATOM   3589 C  CB  . PHE B 2 145 ? -8.310  1.396   -8.973  1.00 38.91  ? 319 PHE B CB  1 
ATOM   3590 C  CG  . PHE B 2 145 ? -9.591  0.862   -9.563  1.00 41.91  ? 319 PHE B CG  1 
ATOM   3591 C  CD1 . PHE B 2 145 ? -10.506 1.698   -10.195 1.00 45.53  ? 319 PHE B CD1 1 
ATOM   3592 C  CD2 . PHE B 2 145 ? -9.884  -0.497  -9.491  1.00 42.37  ? 319 PHE B CD2 1 
ATOM   3593 C  CE1 . PHE B 2 145 ? -11.677 1.185   -10.743 1.00 45.17  ? 319 PHE B CE1 1 
ATOM   3594 C  CE2 . PHE B 2 145 ? -11.045 -1.011  -10.057 1.00 42.87  ? 319 PHE B CE2 1 
ATOM   3595 C  CZ  . PHE B 2 145 ? -11.942 -0.169  -10.676 1.00 43.72  ? 319 PHE B CZ  1 
ATOM   3596 N  N   . LEU B 2 146 ? -5.415  3.030   -8.971  1.00 45.37  ? 320 LEU B N   1 
ATOM   3597 C  CA  . LEU B 2 146 ? -4.281  3.448   -8.150  1.00 51.02  ? 320 LEU B CA  1 
ATOM   3598 C  C   . LEU B 2 146 ? -4.211  4.972   -8.013  1.00 64.97  ? 320 LEU B C   1 
ATOM   3599 O  O   . LEU B 2 146 ? -3.493  5.468   -7.147  1.00 71.10  ? 320 LEU B O   1 
ATOM   3600 C  CB  . LEU B 2 146 ? -2.963  2.938   -8.745  1.00 53.13  ? 320 LEU B CB  1 
ATOM   3601 C  CG  . LEU B 2 146 ? -2.783  1.425   -8.834  1.00 53.33  ? 320 LEU B CG  1 
ATOM   3602 C  CD1 . LEU B 2 146 ? -1.348  1.110   -9.212  1.00 56.50  ? 320 LEU B CD1 1 
ATOM   3603 C  CD2 . LEU B 2 146 ? -3.153  0.731   -7.531  1.00 52.75  ? 320 LEU B CD2 1 
ATOM   3604 N  N   . HIS B 2 147 ? -4.940  5.707   -8.865  1.00 71.90  ? 321 HIS B N   1 
ATOM   3605 C  CA  . HIS B 2 147 ? -4.892  7.166   -8.896  1.00 73.86  ? 321 HIS B CA  1 
ATOM   3606 C  C   . HIS B 2 147 ? -6.040  7.797   -8.105  1.00 79.44  ? 321 HIS B C   1 
ATOM   3607 O  O   . HIS B 2 147 ? -6.243  9.007   -8.187  1.00 91.87  ? 321 HIS B O   1 
ATOM   3608 C  CB  . HIS B 2 147 ? -4.911  7.680   -10.340 1.00 73.88  ? 321 HIS B CB  1 
ATOM   3609 C  CG  . HIS B 2 147 ? -3.699  7.282   -11.110 1.00 70.73  ? 321 HIS B CG  1 
ATOM   3610 N  ND1 . HIS B 2 147 ? -2.892  8.203   -11.736 1.00 69.35  ? 321 HIS B ND1 1 
ATOM   3611 C  CD2 . HIS B 2 147 ? -3.142  6.083   -11.342 1.00 77.85  ? 321 HIS B CD2 1 
ATOM   3612 C  CE1 . HIS B 2 147 ? -1.884  7.572   -12.322 1.00 78.52  ? 321 HIS B CE1 1 
ATOM   3613 N  NE2 . HIS B 2 147 ? -2.015  6.282   -12.098 1.00 79.42  ? 321 HIS B NE2 1 
ATOM   3614 N  N   . GLN B 2 148 ? -6.824  6.969   -7.408  1.00 81.72  ? 322 GLN B N   1 
ATOM   3615 C  CA  . GLN B 2 148 ? -7.795  7.440   -6.430  1.00 79.35  ? 322 GLN B CA  1 
ATOM   3616 C  C   . GLN B 2 148 ? -7.092  7.777   -5.118  1.00 91.67  ? 322 GLN B C   1 
ATOM   3617 O  O   . GLN B 2 148 ? -6.633  6.859   -4.433  1.00 82.07  ? 322 GLN B O   1 
ATOM   3618 C  CB  . GLN B 2 148 ? -8.778  6.326   -6.082  1.00 78.30  ? 322 GLN B CB  1 
ATOM   3619 C  CG  . GLN B 2 148 ? -10.007 6.258   -6.958  1.00 80.47  ? 322 GLN B CG  1 
ATOM   3620 C  CD  . GLN B 2 148 ? -10.986 5.286   -6.348  1.00 76.71  ? 322 GLN B CD  1 
ATOM   3621 O  OE1 . GLN B 2 148 ? -10.710 4.093   -6.221  1.00 78.67  ? 322 GLN B OE1 1 
ATOM   3622 N  NE2 . GLN B 2 148 ? -12.127 5.801   -5.927  1.00 74.23  ? 322 GLN B NE2 1 
ATOM   3623 N  N   . GLN B 2 149 ? -7.035  9.065   -4.741  1.00 110.57 ? 323 GLN B N   1 
ATOM   3624 C  CA  . GLN B 2 149 ? -6.323  9.454   -3.527  1.00 120.96 ? 323 GLN B CA  1 
ATOM   3625 C  C   . GLN B 2 149 ? -7.013  8.825   -2.312  1.00 116.82 ? 323 GLN B C   1 
ATOM   3626 O  O   . GLN B 2 149 ? -6.355  8.175   -1.500  1.00 109.27 ? 323 GLN B O   1 
ATOM   3627 C  CB  . GLN B 2 149 ? -6.152  10.977  -3.439  1.00 124.71 ? 323 GLN B CB  1 
ATOM   3628 C  CG  . GLN B 2 149 ? -4.928  11.539  -4.167  1.00 124.35 ? 323 GLN B CG  1 
ATOM   3629 C  CD  . GLN B 2 149 ? -3.893  10.520  -4.592  1.00 120.48 ? 323 GLN B CD  1 
ATOM   3630 O  OE1 . GLN B 2 149 ? -2.925  10.245  -3.882  1.00 111.30 ? 323 GLN B OE1 1 
ATOM   3631 N  NE2 . GLN B 2 149 ? -4.080  9.966   -5.781  1.00 116.83 ? 323 GLN B NE2 1 
ATOM   3632 N  N   . PRO B 2 150 ? -8.354  8.938   -2.168  1.00 111.84 ? 324 PRO B N   1 
ATOM   3633 C  CA  . PRO B 2 150 ? -9.098  8.149   -1.192  1.00 99.53  ? 324 PRO B CA  1 
ATOM   3634 C  C   . PRO B 2 150 ? -9.669  6.962   -1.973  1.00 88.30  ? 324 PRO B C   1 
ATOM   3635 O  O   . PRO B 2 150 ? -10.485 7.170   -2.875  1.00 85.92  ? 324 PRO B O   1 
ATOM   3636 C  CB  . PRO B 2 150 ? -10.155 9.183   -0.770  1.00 97.50  ? 324 PRO B CB  1 
ATOM   3637 C  CG  . PRO B 2 150 ? -10.480 9.935   -2.073  1.00 97.14  ? 324 PRO B CG  1 
ATOM   3638 C  CD  . PRO B 2 150 ? -9.266  9.773   -2.972  1.00 104.96 ? 324 PRO B CD  1 
ATOM   3639 N  N   . ALA B 2 151 ? -9.241  5.725   -1.671  1.00 79.15  ? 325 ALA B N   1 
ATOM   3640 C  CA  . ALA B 2 151 ? -9.731  4.580   -2.436  1.00 74.04  ? 325 ALA B CA  1 
ATOM   3641 C  C   . ALA B 2 151 ? -11.171 4.280   -2.015  1.00 60.95  ? 325 ALA B C   1 
ATOM   3642 O  O   . ALA B 2 151 ? -11.422 4.131   -0.826  1.00 66.05  ? 325 ALA B O   1 
ATOM   3643 C  CB  . ALA B 2 151 ? -8.842  3.371   -2.245  1.00 76.00  ? 325 ALA B CB  1 
ATOM   3644 N  N   . ASN B 2 152 ? -12.104 4.184   -2.976  1.00 55.05  ? 326 ASN B N   1 
ATOM   3645 C  CA  . ASN B 2 152 ? -13.520 3.955   -2.683  1.00 50.85  ? 326 ASN B CA  1 
ATOM   3646 C  C   . ASN B 2 152 ? -13.963 2.602   -3.260  1.00 51.05  ? 326 ASN B C   1 
ATOM   3647 O  O   . ASN B 2 152 ? -14.081 2.458   -4.470  1.00 50.69  ? 326 ASN B O   1 
ATOM   3648 C  CB  . ASN B 2 152 ? -14.392 5.087   -3.227  1.00 50.13  ? 326 ASN B CB  1 
ATOM   3649 C  CG  . ASN B 2 152 ? -15.838 5.014   -2.779  1.00 55.26  ? 326 ASN B CG  1 
ATOM   3650 O  OD1 . ASN B 2 152 ? -16.461 3.951   -2.784  1.00 52.95  ? 326 ASN B OD1 1 
ATOM   3651 N  ND2 . ASN B 2 152 ? -16.408 6.162   -2.448  1.00 57.47  ? 326 ASN B ND2 1 
ATOM   3652 N  N   A CYS B 2 153 ? -14.223 1.630   -2.375  0.50 53.15  ? 327 CYS B N   1 
ATOM   3653 N  N   B CYS B 2 153 ? -14.263 1.635   -2.381  0.50 51.87  ? 327 CYS B N   1 
ATOM   3654 C  CA  A CYS B 2 153 ? -14.514 0.252   -2.755  0.50 54.84  ? 327 CYS B CA  1 
ATOM   3655 C  CA  B CYS B 2 153 ? -14.514 0.254   -2.781  0.50 52.74  ? 327 CYS B CA  1 
ATOM   3656 C  C   A CYS B 2 153 ? -15.794 0.175   -3.598  0.50 52.04  ? 327 CYS B C   1 
ATOM   3657 C  C   B CYS B 2 153 ? -15.817 0.154   -3.581  0.50 51.04  ? 327 CYS B C   1 
ATOM   3658 O  O   A CYS B 2 153 ? -15.936 -0.738  -4.411  0.50 50.87  ? 327 CYS B O   1 
ATOM   3659 O  O   B CYS B 2 153 ? -15.992 -0.791  -4.351  0.50 50.11  ? 327 CYS B O   1 
ATOM   3660 C  CB  A CYS B 2 153 ? -14.625 -0.644  -1.519  0.50 60.29  ? 327 CYS B CB  1 
ATOM   3661 C  CB  B CYS B 2 153 ? -14.520 -0.684  -1.571  0.50 56.46  ? 327 CYS B CB  1 
ATOM   3662 S  SG  A CYS B 2 153 ? -13.043 -1.255  -0.870  0.50 63.74  ? 327 CYS B SG  1 
ATOM   3663 S  SG  B CYS B 2 153 ? -16.100 -0.799  -0.686  0.50 56.95  ? 327 CYS B SG  1 
ATOM   3664 N  N   . LYS B 2 154 ? -16.708 1.142   -3.404  1.00 51.13  ? 328 LYS B N   1 
ATOM   3665 C  CA  . LYS B 2 154 ? -17.991 1.225   -4.115  1.00 54.42  ? 328 LYS B CA  1 
ATOM   3666 C  C   . LYS B 2 154 ? -17.828 1.795   -5.532  1.00 51.15  ? 328 LYS B C   1 
ATOM   3667 O  O   . LYS B 2 154 ? -18.496 1.325   -6.447  1.00 44.37  ? 328 LYS B O   1 
ATOM   3668 C  CB  . LYS B 2 154 ? -19.002 2.103   -3.358  1.00 59.45  ? 328 LYS B CB  1 
ATOM   3669 C  CG  . LYS B 2 154 ? -20.212 1.402   -2.743  1.00 65.53  ? 328 LYS B CG  1 
ATOM   3670 C  CD  . LYS B 2 154 ? -21.302 2.399   -2.315  1.00 74.56  ? 328 LYS B CD  1 
ATOM   3671 C  CE  . LYS B 2 154 ? -22.685 1.800   -2.141  1.00 79.56  ? 328 LYS B CE  1 
ATOM   3672 N  NZ  . LYS B 2 154 ? -22.983 1.490   -0.723  1.00 83.02  ? 328 LYS B NZ  1 
ATOM   3673 N  N   . VAL B 2 155 ? -16.982 2.826   -5.707  1.00 49.68  ? 329 VAL B N   1 
ATOM   3674 C  CA  . VAL B 2 155 ? -16.615 3.340   -7.025  1.00 48.74  ? 329 VAL B CA  1 
ATOM   3675 C  C   . VAL B 2 155 ? -15.941 2.236   -7.848  1.00 49.75  ? 329 VAL B C   1 
ATOM   3676 O  O   . VAL B 2 155 ? -16.245 2.115   -9.032  1.00 49.70  ? 329 VAL B O   1 
ATOM   3677 C  CB  . VAL B 2 155 ? -15.734 4.605   -6.944  1.00 46.59  ? 329 VAL B CB  1 
ATOM   3678 C  CG1 . VAL B 2 155 ? -14.966 4.856   -8.232  1.00 47.39  ? 329 VAL B CG1 1 
ATOM   3679 C  CG2 . VAL B 2 155 ? -16.553 5.840   -6.597  1.00 48.54  ? 329 VAL B CG2 1 
ATOM   3680 N  N   . GLU B 2 156 ? -15.058 1.433   -7.219  1.00 47.75  ? 330 GLU B N   1 
ATOM   3681 C  CA  . GLU B 2 156 ? -14.300 0.376   -7.891  1.00 48.56  ? 330 GLU B CA  1 
ATOM   3682 C  C   . GLU B 2 156 ? -15.253 -0.706  -8.407  1.00 46.75  ? 330 GLU B C   1 
ATOM   3683 O  O   . GLU B 2 156 ? -15.231 -0.996  -9.595  1.00 46.31  ? 330 GLU B O   1 
ATOM   3684 C  CB  . GLU B 2 156 ? -13.201 -0.233  -7.010  1.00 47.97  ? 330 GLU B CB  1 
ATOM   3685 C  CG  . GLU B 2 156 ? -12.080 0.746   -6.675  1.00 55.34  ? 330 GLU B CG  1 
ATOM   3686 C  CD  . GLU B 2 156 ? -10.909 0.252   -5.829  1.00 61.50  ? 330 GLU B CD  1 
ATOM   3687 O  OE1 . GLU B 2 156 ? -10.652 -0.981  -5.774  1.00 64.22  ? 330 GLU B OE1 1 
ATOM   3688 O  OE2 . GLU B 2 156 ? -10.249 1.116   -5.218  1.00 67.58  ? 330 GLU B OE2 1 
ATOM   3689 N  N   . SER B 2 157 ? -16.107 -1.271  -7.546  1.00 46.93  ? 331 SER B N   1 
ATOM   3690 C  CA  . SER B 2 157 ? -17.046 -2.307  -7.968  1.00 50.52  ? 331 SER B CA  1 
ATOM   3691 C  C   . SER B 2 157 ? -17.969 -1.806  -9.087  1.00 53.24  ? 331 SER B C   1 
ATOM   3692 O  O   . SER B 2 157 ? -18.260 -2.549  -10.026 1.00 52.50  ? 331 SER B O   1 
ATOM   3693 C  CB  . SER B 2 157 ? -17.855 -2.834  -6.804  1.00 49.72  ? 331 SER B CB  1 
ATOM   3694 O  OG  . SER B 2 157 ? -17.011 -3.435  -5.841  1.00 53.31  ? 331 SER B OG  1 
ATOM   3695 N  N   . LEU B 2 158 ? -18.452 -0.561  -8.975  1.00 47.51  ? 332 LEU B N   1 
ATOM   3696 C  CA  . LEU B 2 158 ? -19.376 0.003   -9.952  1.00 47.71  ? 332 LEU B CA  1 
ATOM   3697 C  C   . LEU B 2 158 ? -18.670 0.199   -11.303 1.00 47.69  ? 332 LEU B C   1 
ATOM   3698 O  O   . LEU B 2 158 ? -19.213 -0.142  -12.353 1.00 40.73  ? 332 LEU B O   1 
ATOM   3699 C  CB  . LEU B 2 158 ? -19.933 1.325   -9.406  1.00 47.62  ? 332 LEU B CB  1 
ATOM   3700 C  CG  . LEU B 2 158 ? -20.908 2.057   -10.326 1.00 48.58  ? 332 LEU B CG  1 
ATOM   3701 C  CD1 . LEU B 2 158 ? -22.080 1.160   -10.703 1.00 48.35  ? 332 LEU B CD1 1 
ATOM   3702 C  CD2 . LEU B 2 158 ? -21.409 3.336   -9.668  1.00 52.35  ? 332 LEU B CD2 1 
ATOM   3703 N  N   . ALA B 2 159 ? -17.448 0.742   -11.277 1.00 41.63  ? 333 ALA B N   1 
ATOM   3704 C  CA  . ALA B 2 159 ? -16.623 0.850   -12.473 1.00 42.38  ? 333 ALA B CA  1 
ATOM   3705 C  C   . ALA B 2 159 ? -16.461 -0.518  -13.145 1.00 42.56  ? 333 ALA B C   1 
ATOM   3706 O  O   . ALA B 2 159 ? -16.531 -0.602  -14.368 1.00 43.40  ? 333 ALA B O   1 
ATOM   3707 C  CB  . ALA B 2 159 ? -15.277 1.458   -12.131 1.00 42.85  ? 333 ALA B CB  1 
ATOM   3708 N  N   A MET B 2 160 ? -16.192 -1.566  -12.347 0.50 42.27  ? 334 MET B N   1 
ATOM   3709 N  N   B MET B 2 160 ? -16.244 -1.564  -12.336 0.50 41.95  ? 334 MET B N   1 
ATOM   3710 C  CA  A MET B 2 160 ? -16.083 -2.935  -12.846 0.50 42.96  ? 334 MET B CA  1 
ATOM   3711 C  CA  B MET B 2 160 ? -16.108 -2.942  -12.794 0.50 42.45  ? 334 MET B CA  1 
ATOM   3712 C  C   A MET B 2 160 ? -17.418 -3.339  -13.478 0.50 43.27  ? 334 MET B C   1 
ATOM   3713 C  C   B MET B 2 160 ? -17.416 -3.462  -13.382 0.50 43.38  ? 334 MET B C   1 
ATOM   3714 O  O   A MET B 2 160 ? -17.439 -3.892  -14.577 0.50 45.25  ? 334 MET B O   1 
ATOM   3715 O  O   B MET B 2 160 ? -17.407 -4.327  -14.259 0.50 46.42  ? 334 MET B O   1 
ATOM   3716 C  CB  A MET B 2 160 ? -15.730 -3.933  -11.734 0.50 44.20  ? 334 MET B CB  1 
ATOM   3717 C  CB  B MET B 2 160 ? -15.756 -3.860  -11.622 0.50 43.11  ? 334 MET B CB  1 
ATOM   3718 C  CG  A MET B 2 160 ? -14.239 -4.153  -11.497 0.50 47.68  ? 334 MET B CG  1 
ATOM   3719 C  CG  B MET B 2 160 ? -14.627 -4.796  -11.903 0.50 46.18  ? 334 MET B CG  1 
ATOM   3720 S  SD  A MET B 2 160 ? -13.930 -5.451  -10.237 0.50 56.48  ? 334 MET B SD  1 
ATOM   3721 S  SD  B MET B 2 160 ? -13.085 -3.913  -12.125 0.50 47.43  ? 334 MET B SD  1 
ATOM   3722 C  CE  A MET B 2 160 ? -13.713 -4.464  -8.757  0.50 53.05  ? 334 MET B CE  1 
ATOM   3723 C  CE  B MET B 2 160 ? -12.825 -4.221  -13.867 0.50 49.74  ? 334 MET B CE  1 
ATOM   3724 N  N   . PHE B 2 161 ? -18.529 -3.009  -12.795 1.00 43.67  ? 335 PHE B N   1 
ATOM   3725 C  CA  . PHE B 2 161 ? -19.873 -3.386  -13.218 1.00 40.87  ? 335 PHE B CA  1 
ATOM   3726 C  C   . PHE B 2 161 ? -20.127 -2.879  -14.637 1.00 38.99  ? 335 PHE B C   1 
ATOM   3727 O  O   . PHE B 2 161 ? -20.492 -3.659  -15.514 1.00 40.94  ? 335 PHE B O   1 
ATOM   3728 C  CB  . PHE B 2 161 ? -20.910 -2.863  -12.212 1.00 42.27  ? 335 PHE B CB  1 
ATOM   3729 C  CG  . PHE B 2 161 ? -22.356 -3.023  -12.618 1.00 42.07  ? 335 PHE B CG  1 
ATOM   3730 C  CD1 . PHE B 2 161 ? -22.879 -4.265  -12.933 1.00 42.91  ? 335 PHE B CD1 1 
ATOM   3731 C  CD2 . PHE B 2 161 ? -23.199 -1.923  -12.676 1.00 45.43  ? 335 PHE B CD2 1 
ATOM   3732 C  CE1 . PHE B 2 161 ? -24.208 -4.400  -13.309 1.00 46.50  ? 335 PHE B CE1 1 
ATOM   3733 C  CE2 . PHE B 2 161 ? -24.529 -2.062  -13.040 1.00 43.10  ? 335 PHE B CE2 1 
ATOM   3734 C  CZ  . PHE B 2 161 ? -25.030 -3.300  -13.357 1.00 44.88  ? 335 PHE B CZ  1 
ATOM   3735 N  N   . LEU B 2 162 ? -19.891 -1.577  -14.838 1.00 37.04  ? 336 LEU B N   1 
ATOM   3736 C  CA  . LEU B 2 162 ? -20.099 -0.881  -16.098 1.00 37.12  ? 336 LEU B CA  1 
ATOM   3737 C  C   . LEU B 2 162 ? -19.221 -1.468  -17.198 1.00 39.41  ? 336 LEU B C   1 
ATOM   3738 O  O   . LEU B 2 162 ? -19.698 -1.635  -18.316 1.00 41.21  ? 336 LEU B O   1 
ATOM   3739 C  CB  . LEU B 2 162 ? -19.799 0.603   -15.896 1.00 39.03  ? 336 LEU B CB  1 
ATOM   3740 C  CG  . LEU B 2 162 ? -20.756 1.334   -14.956 1.00 43.73  ? 336 LEU B CG  1 
ATOM   3741 C  CD1 . LEU B 2 162 ? -20.349 2.792   -14.807 1.00 45.99  ? 336 LEU B CD1 1 
ATOM   3742 C  CD2 . LEU B 2 162 ? -22.208 1.223   -15.438 1.00 45.21  ? 336 LEU B CD2 1 
ATOM   3743 N  N   . GLY B 2 163 ? -17.957 -1.766  -16.870 1.00 35.15  ? 337 GLY B N   1 
ATOM   3744 C  CA  . GLY B 2 163 ? -17.050 -2.438  -17.780 1.00 36.60  ? 337 GLY B CA  1 
ATOM   3745 C  C   . GLY B 2 163 ? -17.567 -3.808  -18.223 1.00 37.00  ? 337 GLY B C   1 
ATOM   3746 O  O   . GLY B 2 163 ? -17.407 -4.179  -19.387 1.00 38.33  ? 337 GLY B O   1 
ATOM   3747 N  N   . GLU B 2 164 ? -18.158 -4.563  -17.290 1.00 37.31  ? 338 GLU B N   1 
ATOM   3748 C  CA  . GLU B 2 164 ? -18.737 -5.864  -17.601 1.00 40.47  ? 338 GLU B CA  1 
ATOM   3749 C  C   . GLU B 2 164 ? -19.966 -5.671  -18.504 1.00 42.83  ? 338 GLU B C   1 
ATOM   3750 O  O   . GLU B 2 164 ? -20.167 -6.450  -19.432 1.00 39.03  ? 338 GLU B O   1 
ATOM   3751 C  CB  . GLU B 2 164 ? -19.048 -6.614  -16.303 1.00 45.12  ? 338 GLU B CB  1 
ATOM   3752 C  CG  . GLU B 2 164 ? -18.601 -8.065  -16.281 1.00 51.08  ? 338 GLU B CG  1 
ATOM   3753 C  CD  . GLU B 2 164 ? -18.134 -8.566  -14.922 1.00 59.46  ? 338 GLU B CD  1 
ATOM   3754 O  OE1 . GLU B 2 164 ? -18.546 -9.680  -14.550 1.00 64.52  ? 338 GLU B OE1 1 
ATOM   3755 O  OE2 . GLU B 2 164 ? -17.342 -7.854  -14.249 1.00 61.87  ? 338 GLU B OE2 1 
ATOM   3756 N  N   . LEU B 2 165 ? -20.760 -4.605  -18.297 1.00 46.06  ? 339 LEU B N   1 
ATOM   3757 C  CA  . LEU B 2 165 ? -21.962 -4.388  -19.104 1.00 48.12  ? 339 LEU B CA  1 
ATOM   3758 C  C   . LEU B 2 165 ? -21.599 -4.161  -20.570 1.00 47.74  ? 339 LEU B C   1 
ATOM   3759 O  O   . LEU B 2 165 ? -22.355 -4.557  -21.451 1.00 49.57  ? 339 LEU B O   1 
ATOM   3760 C  CB  . LEU B 2 165 ? -22.774 -3.204  -18.562 1.00 45.03  ? 339 LEU B CB  1 
ATOM   3761 C  CG  . LEU B 2 165 ? -23.582 -3.492  -17.299 1.00 44.66  ? 339 LEU B CG  1 
ATOM   3762 C  CD1 . LEU B 2 165 ? -24.432 -2.291  -16.924 1.00 47.00  ? 339 LEU B CD1 1 
ATOM   3763 C  CD2 . LEU B 2 165 ? -24.450 -4.731  -17.465 1.00 44.19  ? 339 LEU B CD2 1 
ATOM   3764 N  N   . SER B 2 166 ? -20.451 -3.510  -20.807 1.00 46.87  ? 340 SER B N   1 
ATOM   3765 C  CA  . SER B 2 166 ? -19.942 -3.209  -22.139 1.00 42.15  ? 340 SER B CA  1 
ATOM   3766 C  C   . SER B 2 166 ? -19.574 -4.470  -22.934 1.00 45.11  ? 340 SER B C   1 
ATOM   3767 O  O   . SER B 2 166 ? -19.552 -4.423  -24.166 1.00 52.60  ? 340 SER B O   1 
ATOM   3768 C  CB  . SER B 2 166 ? -18.771 -2.270  -22.032 1.00 45.91  ? 340 SER B CB  1 
ATOM   3769 O  OG  . SER B 2 166 ? -17.610 -2.936  -21.570 1.00 44.84  ? 340 SER B OG  1 
ATOM   3770 N  N   . LEU B 2 167 ? -19.274 -5.591  -22.250 1.00 43.49  ? 341 LEU B N   1 
ATOM   3771 C  CA  . LEU B 2 167 ? -18.963 -6.868  -22.894 1.00 38.85  ? 341 LEU B CA  1 
ATOM   3772 C  C   . LEU B 2 167 ? -20.194 -7.442  -23.593 1.00 41.99  ? 341 LEU B C   1 
ATOM   3773 O  O   . LEU B 2 167 ? -20.060 -8.312  -24.450 1.00 43.52  ? 341 LEU B O   1 
ATOM   3774 C  CB  . LEU B 2 167 ? -18.511 -7.918  -21.871 1.00 41.32  ? 341 LEU B CB  1 
ATOM   3775 C  CG  . LEU B 2 167 ? -17.227 -7.679  -21.080 1.00 43.97  ? 341 LEU B CG  1 
ATOM   3776 C  CD1 . LEU B 2 167 ? -17.031 -8.839  -20.113 1.00 43.55  ? 341 LEU B CD1 1 
ATOM   3777 C  CD2 . LEU B 2 167 ? -16.004 -7.518  -21.987 1.00 45.17  ? 341 LEU B CD2 1 
ATOM   3778 N  N   . ILE B 2 168 ? -21.392 -7.034  -23.161 1.00 43.64  ? 342 ILE B N   1 
ATOM   3779 C  CA  . ILE B 2 168 ? -22.625 -7.670  -23.607 1.00 48.97  ? 342 ILE B CA  1 
ATOM   3780 C  C   . ILE B 2 168 ? -23.002 -7.175  -25.005 1.00 49.69  ? 342 ILE B C   1 
ATOM   3781 O  O   . ILE B 2 168 ? -23.345 -7.988  -25.869 1.00 47.67  ? 342 ILE B O   1 
ATOM   3782 C  CB  . ILE B 2 168 ? -23.749 -7.455  -22.572 1.00 48.82  ? 342 ILE B CB  1 
ATOM   3783 C  CG1 . ILE B 2 168 ? -23.403 -8.134  -21.244 1.00 48.60  ? 342 ILE B CG1 1 
ATOM   3784 C  CG2 . ILE B 2 168 ? -25.096 -7.923  -23.110 1.00 50.38  ? 342 ILE B CG2 1 
ATOM   3785 C  CD1 . ILE B 2 168 ? -23.474 -9.656  -21.279 1.00 49.30  ? 342 ILE B CD1 1 
ATOM   3786 N  N   . ASP B 2 169 ? -22.899 -5.853  -25.220 1.00 53.46  ? 343 ASP B N   1 
ATOM   3787 C  CA  . ASP B 2 169 ? -23.415 -5.178  -26.408 1.00 54.18  ? 343 ASP B CA  1 
ATOM   3788 C  C   . ASP B 2 169 ? -22.268 -4.808  -27.359 1.00 50.24  ? 343 ASP B C   1 
ATOM   3789 O  O   . ASP B 2 169 ? -21.622 -3.777  -27.189 1.00 48.22  ? 343 ASP B O   1 
ATOM   3790 C  CB  . ASP B 2 169 ? -24.286 -3.992  -25.966 1.00 59.68  ? 343 ASP B CB  1 
ATOM   3791 C  CG  . ASP B 2 169 ? -25.413 -4.431  -25.037 1.00 64.59  ? 343 ASP B CG  1 
ATOM   3792 O  OD1 . ASP B 2 169 ? -25.962 -5.538  -25.283 1.00 65.17  ? 343 ASP B OD1 1 
ATOM   3793 O  OD2 . ASP B 2 169 ? -25.743 -3.679  -24.076 1.00 59.33  ? 343 ASP B OD2 1 
ATOM   3794 N  N   . ALA B 2 170 ? -22.047 -5.671  -28.363 1.00 50.73  ? 344 ALA B N   1 
ATOM   3795 C  CA  . ALA B 2 170 ? -21.112 -5.481  -29.472 1.00 54.14  ? 344 ALA B CA  1 
ATOM   3796 C  C   . ALA B 2 170 ? -21.317 -4.148  -30.188 1.00 53.70  ? 344 ALA B C   1 
ATOM   3797 O  O   . ALA B 2 170 ? -20.354 -3.524  -30.643 1.00 51.37  ? 344 ALA B O   1 
ATOM   3798 C  CB  . ALA B 2 170 ? -21.282 -6.612  -30.456 1.00 55.91  ? 344 ALA B CB  1 
ATOM   3799 N  N   . ASP B 2 171 ? -22.592 -3.763  -30.334 1.00 54.11  ? 345 ASP B N   1 
ATOM   3800 C  CA  . ASP B 2 171 ? -22.972 -2.430  -30.767 1.00 57.36  ? 345 ASP B CA  1 
ATOM   3801 C  C   . ASP B 2 171 ? -23.471 -1.736  -29.507 1.00 48.26  ? 345 ASP B C   1 
ATOM   3802 O  O   . ASP B 2 171 ? -24.432 -2.213  -28.912 1.00 48.72  ? 345 ASP B O   1 
ATOM   3803 C  CB  . ASP B 2 171 ? -24.033 -2.479  -31.878 1.00 67.47  ? 345 ASP B CB  1 
ATOM   3804 C  CG  . ASP B 2 171 ? -24.576 -1.133  -32.361 1.00 76.42  ? 345 ASP B CG  1 
ATOM   3805 O  OD1 . ASP B 2 171 ? -24.140 -0.073  -31.854 1.00 70.93  ? 345 ASP B OD1 1 
ATOM   3806 O  OD2 . ASP B 2 171 ? -25.449 -1.145  -33.257 1.00 84.59  ? 345 ASP B OD2 1 
ATOM   3807 N  N   . PRO B 2 172 ? -22.846 -0.630  -29.037 1.00 45.00  ? 346 PRO B N   1 
ATOM   3808 C  CA  . PRO B 2 172 ? -21.739 0.032   -29.733 1.00 48.15  ? 346 PRO B CA  1 
ATOM   3809 C  C   . PRO B 2 172 ? -20.288 -0.248  -29.322 1.00 49.72  ? 346 PRO B C   1 
ATOM   3810 O  O   . PRO B 2 172 ? -19.380 0.392   -29.853 1.00 50.82  ? 346 PRO B O   1 
ATOM   3811 C  CB  . PRO B 2 172 ? -22.066 1.496   -29.382 1.00 45.96  ? 346 PRO B CB  1 
ATOM   3812 C  CG  . PRO B 2 172 ? -22.532 1.431   -27.948 1.00 46.84  ? 346 PRO B CG  1 
ATOM   3813 C  CD  . PRO B 2 172 ? -23.252 0.100   -27.827 1.00 45.73  ? 346 PRO B CD  1 
ATOM   3814 N  N   . TYR B 2 173 ? -20.035 -1.189  -28.397 1.00 49.92  ? 347 TYR B N   1 
ATOM   3815 C  CA  . TYR B 2 173 ? -18.788 -1.146  -27.628 1.00 51.92  ? 347 TYR B CA  1 
ATOM   3816 C  C   . TYR B 2 173 ? -17.559 -1.678  -28.389 1.00 48.35  ? 347 TYR B C   1 
ATOM   3817 O  O   . TYR B 2 173 ? -16.453 -1.405  -27.949 1.00 50.70  ? 347 TYR B O   1 
ATOM   3818 C  CB  . TYR B 2 173 ? -19.031 -1.724  -26.227 1.00 52.23  ? 347 TYR B CB  1 
ATOM   3819 C  CG  . TYR B 2 173 ? -19.956 -0.856  -25.415 1.00 50.39  ? 347 TYR B CG  1 
ATOM   3820 C  CD1 . TYR B 2 173 ? -19.605 0.446   -25.103 1.00 52.78  ? 347 TYR B CD1 1 
ATOM   3821 C  CD2 . TYR B 2 173 ? -21.210 -1.298  -25.030 1.00 48.39  ? 347 TYR B CD2 1 
ATOM   3822 C  CE1 . TYR B 2 173 ? -20.464 1.275   -24.399 1.00 55.58  ? 347 TYR B CE1 1 
ATOM   3823 C  CE2 . TYR B 2 173 ? -22.080 -0.485  -24.324 1.00 48.49  ? 347 TYR B CE2 1 
ATOM   3824 C  CZ  . TYR B 2 173 ? -21.705 0.806   -24.008 1.00 52.24  ? 347 TYR B CZ  1 
ATOM   3825 O  OH  . TYR B 2 173 ? -22.558 1.620   -23.310 1.00 51.88  ? 347 TYR B OH  1 
ATOM   3826 N  N   . LEU B 2 174 ? -17.699 -2.335  -29.554 1.00 49.84  ? 348 LEU B N   1 
ATOM   3827 C  CA  . LEU B 2 174 ? -16.533 -2.689  -30.368 1.00 51.62  ? 348 LEU B CA  1 
ATOM   3828 C  C   . LEU B 2 174 ? -15.851 -1.451  -30.961 1.00 47.58  ? 348 LEU B C   1 
ATOM   3829 O  O   . LEU B 2 174 ? -14.669 -1.497  -31.273 1.00 56.27  ? 348 LEU B O   1 
ATOM   3830 C  CB  . LEU B 2 174 ? -16.941 -3.663  -31.479 1.00 53.33  ? 348 LEU B CB  1 
ATOM   3831 C  CG  . LEU B 2 174 ? -17.330 -5.072  -31.033 1.00 57.22  ? 348 LEU B CG  1 
ATOM   3832 C  CD1 . LEU B 2 174 ? -17.568 -5.965  -32.241 1.00 63.14  ? 348 LEU B CD1 1 
ATOM   3833 C  CD2 . LEU B 2 174 ? -16.276 -5.694  -30.132 1.00 54.99  ? 348 LEU B CD2 1 
ATOM   3834 N  N   . LYS B 2 175 ? -16.588 -0.353  -31.128 1.00 49.61  ? 349 LYS B N   1 
ATOM   3835 C  CA  . LYS B 2 175 ? -16.030 0.908   -31.614 1.00 57.35  ? 349 LYS B CA  1 
ATOM   3836 C  C   . LYS B 2 175 ? -14.876 1.408   -30.733 1.00 57.96  ? 349 LYS B C   1 
ATOM   3837 O  O   . LYS B 2 175 ? -13.999 2.116   -31.231 1.00 64.36  ? 349 LYS B O   1 
ATOM   3838 C  CB  . LYS B 2 175 ? -17.118 1.991   -31.684 1.00 59.88  ? 349 LYS B CB  1 
ATOM   3839 C  CG  . LYS B 2 175 ? -18.195 1.750   -32.731 1.00 67.65  ? 349 LYS B CG  1 
ATOM   3840 C  CD  . LYS B 2 175 ? -19.059 2.959   -33.020 1.00 77.97  ? 349 LYS B CD  1 
ATOM   3841 C  CE  . LYS B 2 175 ? -20.174 3.151   -32.015 1.00 82.13  ? 349 LYS B CE  1 
ATOM   3842 N  NZ  . LYS B 2 175 ? -20.840 4.461   -32.198 1.00 87.67  ? 349 LYS B NZ  1 
ATOM   3843 N  N   . TYR B 2 176 ? -14.885 1.062   -29.433 1.00 51.21  ? 350 TYR B N   1 
ATOM   3844 C  CA  . TYR B 2 176 ? -14.037 1.720   -28.442 1.00 50.43  ? 350 TYR B CA  1 
ATOM   3845 C  C   . TYR B 2 176 ? -12.927 0.783   -27.937 1.00 49.55  ? 350 TYR B C   1 
ATOM   3846 O  O   . TYR B 2 176 ? -13.111 -0.427  -27.783 1.00 49.24  ? 350 TYR B O   1 
ATOM   3847 C  CB  . TYR B 2 176 ? -14.879 2.252   -27.273 1.00 51.88  ? 350 TYR B CB  1 
ATOM   3848 C  CG  . TYR B 2 176 ? -16.055 3.136   -27.633 1.00 51.97  ? 350 TYR B CG  1 
ATOM   3849 C  CD1 . TYR B 2 176 ? -15.895 4.457   -28.030 1.00 49.56  ? 350 TYR B CD1 1 
ATOM   3850 C  CD2 . TYR B 2 176 ? -17.349 2.646   -27.546 1.00 55.44  ? 350 TYR B CD2 1 
ATOM   3851 C  CE1 . TYR B 2 176 ? -16.988 5.251   -28.351 1.00 53.84  ? 350 TYR B CE1 1 
ATOM   3852 C  CE2 . TYR B 2 176 ? -18.452 3.428   -27.850 1.00 55.74  ? 350 TYR B CE2 1 
ATOM   3853 C  CZ  . TYR B 2 176 ? -18.270 4.732   -28.263 1.00 57.38  ? 350 TYR B CZ  1 
ATOM   3854 O  OH  . TYR B 2 176 ? -19.390 5.467   -28.547 1.00 54.73  ? 350 TYR B OH  1 
ATOM   3855 N  N   . LEU B 2 177 ? -11.760 1.375   -27.666 1.00 49.43  ? 351 LEU B N   1 
ATOM   3856 C  CA  . LEU B 2 177 ? -10.627 0.677   -27.069 1.00 50.27  ? 351 LEU B CA  1 
ATOM   3857 C  C   . LEU B 2 177 ? -10.905 0.441   -25.584 1.00 48.45  ? 351 LEU B C   1 
ATOM   3858 O  O   . LEU B 2 177 ? -11.522 1.275   -24.902 1.00 45.11  ? 351 LEU B O   1 
ATOM   3859 C  CB  . LEU B 2 177 ? -9.349  1.508   -27.268 1.00 50.34  ? 351 LEU B CB  1 
ATOM   3860 C  CG  . LEU B 2 177 ? -8.916  1.737   -28.721 1.00 55.09  ? 351 LEU B CG  1 
ATOM   3861 C  CD1 . LEU B 2 177 ? -7.788  2.763   -28.820 1.00 54.15  ? 351 LEU B CD1 1 
ATOM   3862 C  CD2 . LEU B 2 177 ? -8.491  0.431   -29.384 1.00 54.03  ? 351 LEU B CD2 1 
ATOM   3863 N  N   . PRO B 2 178 ? -10.455 -0.712  -25.035 1.00 45.55  ? 352 PRO B N   1 
ATOM   3864 C  CA  . PRO B 2 178 ? -10.572 -0.973  -23.601 1.00 41.75  ? 352 PRO B CA  1 
ATOM   3865 C  C   . PRO B 2 178 ? -10.179 0.213   -22.708 1.00 42.84  ? 352 PRO B C   1 
ATOM   3866 O  O   . PRO B 2 178 ? -10.839 0.463   -21.709 1.00 45.70  ? 352 PRO B O   1 
ATOM   3867 C  CB  . PRO B 2 178 ? -9.609  -2.157  -23.388 1.00 43.17  ? 352 PRO B CB  1 
ATOM   3868 C  CG  . PRO B 2 178 ? -9.520  -2.865  -24.721 1.00 43.96  ? 352 PRO B CG  1 
ATOM   3869 C  CD  . PRO B 2 178 ? -9.833  -1.823  -25.774 1.00 43.82  ? 352 PRO B CD  1 
ATOM   3870 N  N   . SER B 2 179 ? -9.119  0.954   -23.067 1.00 39.97  ? 353 SER B N   1 
ATOM   3871 C  CA  . SER B 2 179 ? -8.648  2.088   -22.279 1.00 41.54  ? 353 SER B CA  1 
ATOM   3872 C  C   . SER B 2 179 ? -9.680  3.221   -22.206 1.00 41.61  ? 353 SER B C   1 
ATOM   3873 O  O   . SER B 2 179 ? -9.730  3.926   -21.203 1.00 45.81  ? 353 SER B O   1 
ATOM   3874 C  CB  . SER B 2 179 ? -7.317  2.588   -22.781 1.00 41.51  ? 353 SER B CB  1 
ATOM   3875 O  OG  . SER B 2 179 ? -7.428  3.135   -24.083 1.00 43.49  ? 353 SER B OG  1 
ATOM   3876 N  N   . VAL B 2 180 ? -10.493 3.404   -23.253 1.00 39.73  ? 354 VAL B N   1 
ATOM   3877 C  CA  . VAL B 2 180 ? -11.484 4.476   -23.306 1.00 42.42  ? 354 VAL B CA  1 
ATOM   3878 C  C   . VAL B 2 180 ? -12.746 4.041   -22.564 1.00 39.04  ? 354 VAL B C   1 
ATOM   3879 O  O   . VAL B 2 180 ? -13.340 4.836   -21.833 1.00 37.72  ? 354 VAL B O   1 
ATOM   3880 C  CB  . VAL B 2 180 ? -11.814 4.865   -24.768 1.00 47.83  ? 354 VAL B CB  1 
ATOM   3881 C  CG1 . VAL B 2 180 ? -13.079 5.704   -24.887 1.00 45.63  ? 354 VAL B CG1 1 
ATOM   3882 C  CG2 . VAL B 2 180 ? -10.646 5.564   -25.455 1.00 45.77  ? 354 VAL B CG2 1 
ATOM   3883 N  N   . ILE B 2 181 ? -13.190 2.801   -22.798 1.00 38.12  ? 355 ILE B N   1 
ATOM   3884 C  CA  . ILE B 2 181 ? -14.302 2.237   -22.035 1.00 41.01  ? 355 ILE B CA  1 
ATOM   3885 C  C   . ILE B 2 181 ? -14.000 2.344   -20.537 1.00 42.06  ? 355 ILE B C   1 
ATOM   3886 O  O   . ILE B 2 181 ? -14.837 2.820   -19.781 1.00 45.20  ? 355 ILE B O   1 
ATOM   3887 C  CB  . ILE B 2 181 ? -14.626 0.787   -22.458 1.00 41.18  ? 355 ILE B CB  1 
ATOM   3888 C  CG1 . ILE B 2 181 ? -15.144 0.731   -23.903 1.00 43.32  ? 355 ILE B CG1 1 
ATOM   3889 C  CG2 . ILE B 2 181 ? -15.595 0.153   -21.463 1.00 37.24  ? 355 ILE B CG2 1 
ATOM   3890 C  CD1 . ILE B 2 181 ? -15.377 -0.674  -24.460 1.00 45.29  ? 355 ILE B CD1 1 
ATOM   3891 N  N   . ALA B 2 182 ? -12.808 1.897   -20.117 1.00 40.48  ? 356 ALA B N   1 
ATOM   3892 C  CA  . ALA B 2 182 ? -12.352 1.996   -18.734 1.00 37.54  ? 356 ALA B CA  1 
ATOM   3893 C  C   . ALA B 2 182 ? -12.404 3.439   -18.238 1.00 36.09  ? 356 ALA B C   1 
ATOM   3894 O  O   . ALA B 2 182 ? -12.852 3.677   -17.125 1.00 41.79  ? 356 ALA B O   1 
ATOM   3895 C  CB  . ALA B 2 182 ? -10.947 1.455   -18.608 1.00 41.03  ? 356 ALA B CB  1 
ATOM   3896 N  N   . GLY B 2 183 ? -11.912 4.387   -19.049 1.00 36.98  ? 357 GLY B N   1 
ATOM   3897 C  CA  . GLY B 2 183 ? -11.996 5.808   -18.738 1.00 37.62  ? 357 GLY B CA  1 
ATOM   3898 C  C   . GLY B 2 183 ? -13.441 6.232   -18.465 1.00 41.16  ? 357 GLY B C   1 
ATOM   3899 O  O   . GLY B 2 183 ? -13.733 6.856   -17.445 1.00 45.07  ? 357 GLY B O   1 
ATOM   3900 N  N   . ALA B 2 184 ? -14.341 5.833   -19.366 1.00 41.87  ? 358 ALA B N   1 
ATOM   3901 C  CA  . ALA B 2 184 ? -15.764 6.127   -19.257 1.00 43.16  ? 358 ALA B CA  1 
ATOM   3902 C  C   . ALA B 2 184 ? -16.318 5.538   -17.965 1.00 42.22  ? 358 ALA B C   1 
ATOM   3903 O  O   . ALA B 2 184 ? -16.978 6.237   -17.191 1.00 42.98  ? 358 ALA B O   1 
ATOM   3904 C  CB  . ALA B 2 184 ? -16.517 5.592   -20.462 1.00 41.79  ? 358 ALA B CB  1 
ATOM   3905 N  N   . ALA B 2 185 ? -16.028 4.250   -17.760 1.00 43.71  ? 359 ALA B N   1 
ATOM   3906 C  CA  . ALA B 2 185 ? -16.517 3.479   -16.623 1.00 42.55  ? 359 ALA B CA  1 
ATOM   3907 C  C   . ALA B 2 185 ? -16.106 4.145   -15.316 1.00 42.19  ? 359 ALA B C   1 
ATOM   3908 O  O   . ALA B 2 185 ? -16.922 4.254   -14.398 1.00 44.17  ? 359 ALA B O   1 
ATOM   3909 C  CB  . ALA B 2 185 ? -15.989 2.068   -16.688 1.00 43.76  ? 359 ALA B CB  1 
ATOM   3910 N  N   . PHE B 2 186 ? -14.841 4.576   -15.239 1.00 43.81  ? 360 PHE B N   1 
ATOM   3911 C  CA  . PHE B 2 186 ? -14.286 5.074   -13.992 1.00 42.40  ? 360 PHE B CA  1 
ATOM   3912 C  C   . PHE B 2 186 ? -14.954 6.398   -13.642 1.00 44.05  ? 360 PHE B C   1 
ATOM   3913 O  O   . PHE B 2 186 ? -15.381 6.603   -12.496 1.00 42.07  ? 360 PHE B O   1 
ATOM   3914 C  CB  . PHE B 2 186 ? -12.768 5.236   -14.064 1.00 45.50  ? 360 PHE B CB  1 
ATOM   3915 C  CG  . PHE B 2 186 ? -12.170 5.673   -12.752 1.00 51.20  ? 360 PHE B CG  1 
ATOM   3916 C  CD1 . PHE B 2 186 ? -12.330 4.898   -11.613 1.00 55.27  ? 360 PHE B CD1 1 
ATOM   3917 C  CD2 . PHE B 2 186 ? -11.503 6.884   -12.638 1.00 57.71  ? 360 PHE B CD2 1 
ATOM   3918 C  CE1 . PHE B 2 186 ? -11.808 5.314   -10.398 1.00 58.57  ? 360 PHE B CE1 1 
ATOM   3919 C  CE2 . PHE B 2 186 ? -10.977 7.296   -11.422 1.00 58.19  ? 360 PHE B CE2 1 
ATOM   3920 C  CZ  . PHE B 2 186 ? -11.138 6.514   -10.303 1.00 58.91  ? 360 PHE B CZ  1 
ATOM   3921 N  N   . HIS B 2 187 ? -15.039 7.281   -14.647 1.00 46.10  ? 361 HIS B N   1 
ATOM   3922 C  CA  . HIS B 2 187 ? -15.695 8.570   -14.479 1.00 45.92  ? 361 HIS B CA  1 
ATOM   3923 C  C   . HIS B 2 187 ? -17.160 8.378   -14.090 1.00 43.92  ? 361 HIS B C   1 
ATOM   3924 O  O   . HIS B 2 187 ? -17.637 8.995   -13.153 1.00 49.51  ? 361 HIS B O   1 
ATOM   3925 C  CB  . HIS B 2 187 ? -15.599 9.433   -15.738 1.00 45.72  ? 361 HIS B CB  1 
ATOM   3926 C  CG  . HIS B 2 187 ? -16.479 10.631  -15.631 1.00 47.46  ? 361 HIS B CG  1 
ATOM   3927 N  ND1 . HIS B 2 187 ? -16.068 11.792  -15.022 1.00 44.78  ? 361 HIS B ND1 1 
ATOM   3928 C  CD2 . HIS B 2 187 ? -17.746 10.847  -16.031 1.00 49.04  ? 361 HIS B CD2 1 
ATOM   3929 C  CE1 . HIS B 2 187 ? -17.058 12.672  -15.045 1.00 50.64  ? 361 HIS B CE1 1 
ATOM   3930 N  NE2 . HIS B 2 187 ? -18.090 12.118  -15.643 1.00 50.89  ? 361 HIS B NE2 1 
ATOM   3931 N  N   . LEU B 2 188 ? -17.885 7.531   -14.815 1.00 47.16  ? 362 LEU B N   1 
ATOM   3932 C  CA  . LEU B 2 188 ? -19.303 7.346   -14.546 1.00 50.62  ? 362 LEU B CA  1 
ATOM   3933 C  C   . LEU B 2 188 ? -19.479 6.822   -13.121 1.00 47.16  ? 362 LEU B C   1 
ATOM   3934 O  O   . LEU B 2 188 ? -20.389 7.255   -12.428 1.00 47.81  ? 362 LEU B O   1 
ATOM   3935 C  CB  . LEU B 2 188 ? -19.931 6.412   -15.598 1.00 55.75  ? 362 LEU B CB  1 
ATOM   3936 C  CG  . LEU B 2 188 ? -21.462 6.291   -15.592 1.00 62.17  ? 362 LEU B CG  1 
ATOM   3937 C  CD1 . LEU B 2 188 ? -22.143 7.652   -15.564 1.00 62.93  ? 362 LEU B CD1 1 
ATOM   3938 C  CD2 . LEU B 2 188 ? -21.963 5.508   -16.801 1.00 62.39  ? 362 LEU B CD2 1 
ATOM   3939 N  N   . ALA B 2 189 ? -18.619 5.888   -12.690 1.00 47.49  ? 363 ALA B N   1 
ATOM   3940 C  CA  . ALA B 2 189 ? -18.685 5.329   -11.342 1.00 46.22  ? 363 ALA B CA  1 
ATOM   3941 C  C   . ALA B 2 189 ? -18.401 6.416   -10.299 1.00 47.75  ? 363 ALA B C   1 
ATOM   3942 O  O   . ALA B 2 189 ? -19.212 6.671   -9.416  1.00 50.75  ? 363 ALA B O   1 
ATOM   3943 C  CB  . ALA B 2 189 ? -17.722 4.172   -11.220 1.00 43.86  ? 363 ALA B CB  1 
ATOM   3944 N  N   . LEU B 2 190 ? -17.244 7.062   -10.413 1.00 44.11  ? 364 LEU B N   1 
ATOM   3945 C  CA  . LEU B 2 190 ? -16.895 8.212   -9.596  1.00 47.33  ? 364 LEU B CA  1 
ATOM   3946 C  C   . LEU B 2 190 ? -18.074 9.177   -9.458  1.00 48.38  ? 364 LEU B C   1 
ATOM   3947 O  O   . LEU B 2 190 ? -18.475 9.501   -8.355  1.00 52.46  ? 364 LEU B O   1 
ATOM   3948 C  CB  . LEU B 2 190 ? -15.709 8.889   -10.285 1.00 52.86  ? 364 LEU B CB  1 
ATOM   3949 C  CG  . LEU B 2 190 ? -14.676 9.579   -9.406  1.00 57.75  ? 364 LEU B CG  1 
ATOM   3950 C  CD1 . LEU B 2 190 ? -14.398 8.809   -8.120  1.00 61.92  ? 364 LEU B CD1 1 
ATOM   3951 C  CD2 . LEU B 2 190 ? -13.390 9.738   -10.206 1.00 62.36  ? 364 LEU B CD2 1 
ATOM   3952 N  N   . TYR B 2 191 ? -18.613 9.658   -10.579 1.00 52.76  ? 365 TYR B N   1 
ATOM   3953 C  CA  . TYR B 2 191 ? -19.608 10.719  -10.577 1.00 52.70  ? 365 TYR B CA  1 
ATOM   3954 C  C   . TYR B 2 191 ? -20.882 10.268  -9.866  1.00 51.37  ? 365 TYR B C   1 
ATOM   3955 O  O   . TYR B 2 191 ? -21.474 11.041  -9.110  1.00 52.96  ? 365 TYR B O   1 
ATOM   3956 C  CB  . TYR B 2 191 ? -19.953 11.165  -12.000 1.00 56.65  ? 365 TYR B CB  1 
ATOM   3957 C  CG  . TYR B 2 191 ? -20.895 12.342  -12.047 1.00 63.19  ? 365 TYR B CG  1 
ATOM   3958 C  CD1 . TYR B 2 191 ? -20.433 13.633  -11.843 1.00 66.55  ? 365 TYR B CD1 1 
ATOM   3959 C  CD2 . TYR B 2 191 ? -22.257 12.164  -12.239 1.00 71.07  ? 365 TYR B CD2 1 
ATOM   3960 C  CE1 . TYR B 2 191 ? -21.290 14.722  -11.877 1.00 77.16  ? 365 TYR B CE1 1 
ATOM   3961 C  CE2 . TYR B 2 191 ? -23.130 13.241  -12.270 1.00 81.79  ? 365 TYR B CE2 1 
ATOM   3962 C  CZ  . TYR B 2 191 ? -22.645 14.528  -12.088 1.00 83.86  ? 365 TYR B CZ  1 
ATOM   3963 O  OH  . TYR B 2 191 ? -23.497 15.611  -12.118 1.00 82.41  ? 365 TYR B OH  1 
ATOM   3964 N  N   . THR B 2 192 ? -21.299 9.029   -10.148 1.00 47.48  ? 366 THR B N   1 
ATOM   3965 C  CA  . THR B 2 192 ? -22.499 8.420   -9.590  1.00 51.17  ? 366 THR B CA  1 
ATOM   3966 C  C   . THR B 2 192 ? -22.455 8.419   -8.062  1.00 55.15  ? 366 THR B C   1 
ATOM   3967 O  O   . THR B 2 192 ? -23.456 8.742   -7.425  1.00 65.45  ? 366 THR B O   1 
ATOM   3968 C  CB  . THR B 2 192 ? -22.685 6.987   -10.112 1.00 51.60  ? 366 THR B CB  1 
ATOM   3969 O  OG1 . THR B 2 192 ? -22.699 7.053   -11.535 1.00 54.58  ? 366 THR B OG1 1 
ATOM   3970 C  CG2 . THR B 2 192 ? -23.960 6.319   -9.642  1.00 53.97  ? 366 THR B CG2 1 
ATOM   3971 N  N   . VAL B 2 193 ? -21.300 8.043   -7.496  1.00 51.53  ? 367 VAL B N   1 
ATOM   3972 C  CA  . VAL B 2 193 ? -21.167 7.677   -6.090  1.00 54.62  ? 367 VAL B CA  1 
ATOM   3973 C  C   . VAL B 2 193 ? -20.783 8.895   -5.250  1.00 53.97  ? 367 VAL B C   1 
ATOM   3974 O  O   . VAL B 2 193 ? -21.298 9.055   -4.145  1.00 61.49  ? 367 VAL B O   1 
ATOM   3975 C  CB  . VAL B 2 193 ? -20.141 6.535   -5.925  1.00 59.50  ? 367 VAL B CB  1 
ATOM   3976 C  CG1 . VAL B 2 193 ? -19.778 6.259   -4.471  1.00 60.85  ? 367 VAL B CG1 1 
ATOM   3977 C  CG2 . VAL B 2 193 ? -20.635 5.260   -6.588  1.00 57.45  ? 367 VAL B CG2 1 
ATOM   3978 N  N   . THR B 2 194 ? -19.869 9.725   -5.772  1.00 51.17  ? 368 THR B N   1 
ATOM   3979 C  CA  . THR B 2 194 ? -19.245 10.806  -5.017  1.00 53.28  ? 368 THR B CA  1 
ATOM   3980 C  C   . THR B 2 194 ? -19.437 12.177  -5.677  1.00 54.56  ? 368 THR B C   1 
ATOM   3981 O  O   . THR B 2 194 ? -19.133 13.189  -5.055  1.00 59.86  ? 368 THR B O   1 
ATOM   3982 C  CB  . THR B 2 194 ? -17.737 10.564  -4.868  1.00 49.81  ? 368 THR B CB  1 
ATOM   3983 O  OG1 . THR B 2 194 ? -17.166 10.866  -6.141  1.00 54.23  ? 368 THR B OG1 1 
ATOM   3984 C  CG2 . THR B 2 194 ? -17.373 9.156   -4.441  1.00 50.02  ? 368 THR B CG2 1 
ATOM   3985 N  N   . GLY B 2 195 ? -19.874 12.224  -6.941  1.00 51.93  ? 369 GLY B N   1 
ATOM   3986 C  CA  . GLY B 2 195 ? -20.042 13.482  -7.656  1.00 54.36  ? 369 GLY B CA  1 
ATOM   3987 C  C   . GLY B 2 195 ? -18.740 14.033  -8.242  1.00 57.24  ? 369 GLY B C   1 
ATOM   3988 O  O   . GLY B 2 195 ? -18.761 15.022  -8.971  1.00 62.03  ? 369 GLY B O   1 
ATOM   3989 N  N   . GLN B 2 196 ? -17.606 13.386  -7.951  1.00 59.46  ? 370 GLN B N   1 
ATOM   3990 C  CA  . GLN B 2 196 ? -16.324 13.770  -8.531  1.00 59.16  ? 370 GLN B CA  1 
ATOM   3991 C  C   . GLN B 2 196 ? -16.242 13.376  -10.016 1.00 60.36  ? 370 GLN B C   1 
ATOM   3992 O  O   . GLN B 2 196 ? -17.093 12.641  -10.534 1.00 59.11  ? 370 GLN B O   1 
ATOM   3993 C  CB  . GLN B 2 196 ? -15.188 13.132  -7.726  1.00 59.85  ? 370 GLN B CB  1 
ATOM   3994 C  CG  . GLN B 2 196 ? -15.103 13.587  -6.274  1.00 59.82  ? 370 GLN B CG  1 
ATOM   3995 C  CD  . GLN B 2 196 ? -14.168 12.697  -5.486  1.00 70.74  ? 370 GLN B CD  1 
ATOM   3996 O  OE1 . GLN B 2 196 ? -14.593 11.811  -4.744  1.00 74.44  ? 370 GLN B OE1 1 
ATOM   3997 N  NE2 . GLN B 2 196 ? -12.870 12.900  -5.665  1.00 75.68  ? 370 GLN B NE2 1 
ATOM   3998 N  N   . SER B 2 197 ? -15.183 13.869  -10.688 1.00 59.36  ? 371 SER B N   1 
ATOM   3999 C  CA  . SER B 2 197 ? -14.958 13.688  -12.124 1.00 62.38  ? 371 SER B CA  1 
ATOM   4000 C  C   . SER B 2 197 ? -13.527 13.219  -12.443 1.00 63.16  ? 371 SER B C   1 
ATOM   4001 O  O   . SER B 2 197 ? -12.563 13.644  -11.807 1.00 62.36  ? 371 SER B O   1 
ATOM   4002 C  CB  . SER B 2 197 ? -15.274 14.969  -12.874 1.00 64.29  ? 371 SER B CB  1 
ATOM   4003 O  OG  . SER B 2 197 ? -16.661 15.274  -12.800 1.00 69.42  ? 371 SER B OG  1 
ATOM   4004 N  N   . TRP B 2 198 ? -13.412 12.338  -13.455 1.00 65.09  ? 372 TRP B N   1 
ATOM   4005 C  CA  . TRP B 2 198 ? -12.166 11.984  -14.136 1.00 63.53  ? 372 TRP B CA  1 
ATOM   4006 C  C   . TRP B 2 198 ? -11.027 12.873  -13.629 1.00 63.76  ? 372 TRP B C   1 
ATOM   4007 O  O   . TRP B 2 198 ? -10.947 14.057  -13.960 1.00 64.25  ? 372 TRP B O   1 
ATOM   4008 C  CB  . TRP B 2 198 ? -12.363 12.069  -15.663 1.00 56.21  ? 372 TRP B CB  1 
ATOM   4009 C  CG  . TRP B 2 198 ? -11.244 11.531  -16.504 1.00 52.13  ? 372 TRP B CG  1 
ATOM   4010 C  CD1 . TRP B 2 198 ? -10.492 12.232  -17.398 1.00 51.39  ? 372 TRP B CD1 1 
ATOM   4011 C  CD2 . TRP B 2 198 ? -10.774 10.171  -16.580 1.00 50.92  ? 372 TRP B CD2 1 
ATOM   4012 N  NE1 . TRP B 2 198 ? -9.574  11.413  -18.000 1.00 49.45  ? 372 TRP B NE1 1 
ATOM   4013 C  CE2 . TRP B 2 198 ? -9.725  10.146  -17.520 1.00 47.72  ? 372 TRP B CE2 1 
ATOM   4014 C  CE3 . TRP B 2 198 ? -11.128 8.978   -15.942 1.00 52.76  ? 372 TRP B CE3 1 
ATOM   4015 C  CZ2 . TRP B 2 198 ? -9.033  8.984   -17.837 1.00 51.91  ? 372 TRP B CZ2 1 
ATOM   4016 C  CZ3 . TRP B 2 198 ? -10.439 7.828   -16.247 1.00 52.12  ? 372 TRP B CZ3 1 
ATOM   4017 C  CH2 . TRP B 2 198 ? -9.406  7.832   -17.184 1.00 55.01  ? 372 TRP B CH2 1 
ATOM   4018 N  N   . PRO B 2 199 ? -10.166 12.354  -12.730 1.00 60.73  ? 373 PRO B N   1 
ATOM   4019 C  CA  . PRO B 2 199 ? -9.117  13.171  -12.116 1.00 60.34  ? 373 PRO B CA  1 
ATOM   4020 C  C   . PRO B 2 199 ? -8.099  13.784  -13.083 1.00 58.53  ? 373 PRO B C   1 
ATOM   4021 O  O   . PRO B 2 199 ? -7.862  13.253  -14.164 1.00 54.17  ? 373 PRO B O   1 
ATOM   4022 C  CB  . PRO B 2 199 ? -8.407  12.166  -11.191 1.00 64.82  ? 373 PRO B CB  1 
ATOM   4023 C  CG  . PRO B 2 199 ? -9.457  11.108  -10.893 1.00 65.86  ? 373 PRO B CG  1 
ATOM   4024 C  CD  . PRO B 2 199 ? -10.229 10.985  -12.187 1.00 63.64  ? 373 PRO B CD  1 
ATOM   4025 N  N   . GLU B 2 200 ? -7.472  14.892  -12.656 1.00 61.85  ? 374 GLU B N   1 
ATOM   4026 C  CA  . GLU B 2 200 ? -6.393  15.537  -13.397 1.00 66.85  ? 374 GLU B CA  1 
ATOM   4027 C  C   . GLU B 2 200 ? -5.189  14.599  -13.525 1.00 63.57  ? 374 GLU B C   1 
ATOM   4028 O  O   . GLU B 2 200 ? -4.436  14.718  -14.489 1.00 66.46  ? 374 GLU B O   1 
ATOM   4029 C  CB  . GLU B 2 200 ? -5.964  16.858  -12.746 1.00 76.57  ? 374 GLU B CB  1 
ATOM   4030 C  CG  . GLU B 2 200 ? -6.963  18.005  -12.912 1.00 86.91  ? 374 GLU B CG  1 
ATOM   4031 C  CD  . GLU B 2 200 ? -7.963  18.211  -11.780 1.00 95.05  ? 374 GLU B CD  1 
ATOM   4032 O  OE1 . GLU B 2 200 ? -8.050  17.336  -10.877 1.00 86.51  ? 374 GLU B OE1 1 
ATOM   4033 O  OE2 . GLU B 2 200 ? -8.649  19.262  -11.791 1.00 97.24  ? 374 GLU B OE2 1 
ATOM   4034 N  N   . SER B 2 201 ? -5.009  13.680  -12.563 1.00 60.20  ? 375 SER B N   1 
ATOM   4035 C  CA  . SER B 2 201 ? -3.910  12.716  -12.583 1.00 62.06  ? 375 SER B CA  1 
ATOM   4036 C  C   . SER B 2 201 ? -4.141  11.637  -13.646 1.00 58.47  ? 375 SER B C   1 
ATOM   4037 O  O   . SER B 2 201 ? -3.189  11.134  -14.238 1.00 54.08  ? 375 SER B O   1 
ATOM   4038 C  CB  . SER B 2 201 ? -3.673  12.106  -11.212 1.00 62.14  ? 375 SER B CB  1 
ATOM   4039 O  OG  . SER B 2 201 ? -4.813  11.388  -10.761 1.00 65.57  ? 375 SER B OG  1 
ATOM   4040 N  N   . LEU B 2 202 ? -5.402  11.290  -13.936 1.00 57.78  ? 376 LEU B N   1 
ATOM   4041 C  CA  . LEU B 2 202 ? -5.655  10.311  -14.987 1.00 55.50  ? 376 LEU B CA  1 
ATOM   4042 C  C   . LEU B 2 202 ? -5.624  10.966  -16.373 1.00 52.20  ? 376 LEU B C   1 
ATOM   4043 O  O   . LEU B 2 202 ? -5.195  10.331  -17.339 1.00 52.37  ? 376 LEU B O   1 
ATOM   4044 C  CB  . LEU B 2 202 ? -6.950  9.553   -14.684 1.00 55.22  ? 376 LEU B CB  1 
ATOM   4045 C  CG  . LEU B 2 202 ? -6.795  8.431   -13.656 1.00 53.00  ? 376 LEU B CG  1 
ATOM   4046 C  CD1 . LEU B 2 202 ? -8.146  7.872   -13.216 1.00 54.15  ? 376 LEU B CD1 1 
ATOM   4047 C  CD2 . LEU B 2 202 ? -5.916  7.318   -14.212 1.00 51.16  ? 376 LEU B CD2 1 
ATOM   4048 N  N   . ILE B 2 203 ? -5.987  12.254  -16.471 1.00 57.87  ? 377 ILE B N   1 
ATOM   4049 C  CA  . ILE B 2 203 ? -5.833  12.998  -17.722 1.00 58.61  ? 377 ILE B CA  1 
ATOM   4050 C  C   . ILE B 2 203 ? -4.378  12.919  -18.196 1.00 62.55  ? 377 ILE B C   1 
ATOM   4051 O  O   . ILE B 2 203 ? -4.143  12.639  -19.367 1.00 64.32  ? 377 ILE B O   1 
ATOM   4052 C  CB  . ILE B 2 203 ? -6.330  14.460  -17.610 1.00 56.77  ? 377 ILE B CB  1 
ATOM   4053 C  CG1 . ILE B 2 203 ? -7.852  14.545  -17.433 1.00 57.91  ? 377 ILE B CG1 1 
ATOM   4054 C  CG2 . ILE B 2 203 ? -5.881  15.277  -18.814 1.00 51.60  ? 377 ILE B CG2 1 
ATOM   4055 C  CD1 . ILE B 2 203 ? -8.377  15.927  -17.041 1.00 59.62  ? 377 ILE B CD1 1 
ATOM   4056 N  N   . ARG B 2 204 ? -3.418  13.160  -17.283 1.00 73.21  ? 378 ARG B N   1 
ATOM   4057 C  CA  . ARG B 2 204 ? -1.985  13.172  -17.578 1.00 74.53  ? 378 ARG B CA  1 
ATOM   4058 C  C   . ARG B 2 204 ? -1.499  11.783  -18.010 1.00 68.75  ? 378 ARG B C   1 
ATOM   4059 O  O   . ARG B 2 204 ? -0.790  11.669  -19.007 1.00 71.28  ? 378 ARG B O   1 
ATOM   4060 C  CB  . ARG B 2 204 ? -1.166  13.640  -16.362 1.00 87.16  ? 378 ARG B CB  1 
ATOM   4061 C  CG  . ARG B 2 204 ? -1.211  15.139  -16.085 1.00 99.17  ? 378 ARG B CG  1 
ATOM   4062 C  CD  . ARG B 2 204 ? -0.539  15.561  -14.782 1.00 108.26 ? 378 ARG B CD  1 
ATOM   4063 N  NE  . ARG B 2 204 ? 0.899   15.295  -14.731 1.00 110.53 ? 378 ARG B NE  1 
ATOM   4064 C  CZ  . ARG B 2 204 ? 1.743   15.794  -13.826 1.00 111.59 ? 378 ARG B CZ  1 
ATOM   4065 N  NH1 . ARG B 2 204 ? 1.319   16.624  -12.888 1.00 116.69 ? 378 ARG B NH1 1 
ATOM   4066 N  NH2 . ARG B 2 204 ? 3.026   15.473  -13.865 1.00 108.73 ? 378 ARG B NH2 1 
ATOM   4067 N  N   . LYS B 2 205 ? -1.867  10.737  -17.252 1.00 59.89  ? 379 LYS B N   1 
ATOM   4068 C  CA  . LYS B 2 205 ? -1.406  9.370   -17.490 1.00 57.21  ? 379 LYS B CA  1 
ATOM   4069 C  C   . LYS B 2 205 ? -1.878  8.860   -18.857 1.00 53.94  ? 379 LYS B C   1 
ATOM   4070 O  O   . LYS B 2 205 ? -1.071  8.313   -19.613 1.00 54.10  ? 379 LYS B O   1 
ATOM   4071 C  CB  . LYS B 2 205 ? -1.887  8.436   -16.372 1.00 58.38  ? 379 LYS B CB  1 
ATOM   4072 C  CG  . LYS B 2 205 ? -1.357  7.005   -16.414 1.00 60.79  ? 379 LYS B CG  1 
ATOM   4073 C  CD  . LYS B 2 205 ? -2.156  6.054   -15.531 1.00 61.66  ? 379 LYS B CD  1 
ATOM   4074 C  CE  . LYS B 2 205 ? -1.567  4.666   -15.395 1.00 63.86  ? 379 LYS B CE  1 
ATOM   4075 N  NZ  . LYS B 2 205 ? -0.397  4.641   -14.481 1.00 67.26  ? 379 LYS B NZ  1 
ATOM   4076 N  N   . THR B 2 206 ? -3.173  9.060   -19.168 1.00 48.73  ? 380 THR B N   1 
ATOM   4077 C  CA  . THR B 2 206 ? -3.827  8.481   -20.343 1.00 51.92  ? 380 THR B CA  1 
ATOM   4078 C  C   . THR B 2 206 ? -3.777  9.406   -21.568 1.00 52.39  ? 380 THR B C   1 
ATOM   4079 O  O   . THR B 2 206 ? -3.838  8.941   -22.712 1.00 52.13  ? 380 THR B O   1 
ATOM   4080 C  CB  . THR B 2 206 ? -5.289  8.136   -20.021 1.00 51.99  ? 380 THR B CB  1 
ATOM   4081 O  OG1 . THR B 2 206 ? -5.996  9.359   -19.796 1.00 51.79  ? 380 THR B OG1 1 
ATOM   4082 C  CG2 . THR B 2 206 ? -5.412  7.226   -18.818 1.00 50.63  ? 380 THR B CG2 1 
ATOM   4083 N  N   . GLY B 2 207 ? -3.698  10.720  -21.329 1.00 49.43  ? 381 GLY B N   1 
ATOM   4084 C  CA  . GLY B 2 207 ? -3.879  11.717  -22.373 1.00 49.86  ? 381 GLY B CA  1 
ATOM   4085 C  C   . GLY B 2 207 ? -5.341  11.865  -22.808 1.00 53.75  ? 381 GLY B C   1 
ATOM   4086 O  O   . GLY B 2 207 ? -5.587  12.532  -23.808 1.00 52.16  ? 381 GLY B O   1 
ATOM   4087 N  N   . TYR B 2 208 ? -6.293  11.263  -22.063 1.00 51.37  ? 382 TYR B N   1 
ATOM   4088 C  CA  . TYR B 2 208 ? -7.722  11.345  -22.364 1.00 52.20  ? 382 TYR B CA  1 
ATOM   4089 C  C   . TYR B 2 208 ? -8.376  12.419  -21.500 1.00 56.26  ? 382 TYR B C   1 
ATOM   4090 O  O   . TYR B 2 208 ? -8.333  12.313  -20.284 1.00 61.21  ? 382 TYR B O   1 
ATOM   4091 C  CB  . TYR B 2 208 ? -8.449  10.033  -22.052 1.00 47.59  ? 382 TYR B CB  1 
ATOM   4092 C  CG  . TYR B 2 208 ? -8.047  8.838   -22.879 1.00 45.74  ? 382 TYR B CG  1 
ATOM   4093 C  CD1 . TYR B 2 208 ? -7.482  8.968   -24.136 1.00 44.25  ? 382 TYR B CD1 1 
ATOM   4094 C  CD2 . TYR B 2 208 ? -8.230  7.561   -22.382 1.00 41.38  ? 382 TYR B CD2 1 
ATOM   4095 C  CE1 . TYR B 2 208 ? -7.142  7.854   -24.891 1.00 44.67  ? 382 TYR B CE1 1 
ATOM   4096 C  CE2 . TYR B 2 208 ? -7.892  6.441   -23.119 1.00 41.13  ? 382 TYR B CE2 1 
ATOM   4097 C  CZ  . TYR B 2 208 ? -7.337  6.586   -24.372 1.00 42.55  ? 382 TYR B CZ  1 
ATOM   4098 O  OH  . TYR B 2 208 ? -7.014  5.448   -25.057 1.00 43.07  ? 382 TYR B OH  1 
ATOM   4099 N  N   . THR B 2 209 ? -8.993  13.433  -22.121 1.00 62.63  ? 383 THR B N   1 
ATOM   4100 C  CA  . THR B 2 209 ? -9.763  14.442  -21.398 1.00 60.01  ? 383 THR B CA  1 
ATOM   4101 C  C   . THR B 2 209 ? -11.190 13.937  -21.202 1.00 59.70  ? 383 THR B C   1 
ATOM   4102 O  O   . THR B 2 209 ? -11.640 13.057  -21.933 1.00 57.78  ? 383 THR B O   1 
ATOM   4103 C  CB  . THR B 2 209 ? -9.798  15.778  -22.152 1.00 62.38  ? 383 THR B CB  1 
ATOM   4104 O  OG1 . THR B 2 209 ? -10.393 15.540  -23.431 1.00 58.99  ? 383 THR B OG1 1 
ATOM   4105 C  CG2 . THR B 2 209 ? -8.425  16.393  -22.320 1.00 61.86  ? 383 THR B CG2 1 
ATOM   4106 N  N   . LEU B 2 210 ? -11.894 14.500  -20.214 1.00 62.11  ? 384 LEU B N   1 
ATOM   4107 C  CA  . LEU B 2 210 ? -13.306 14.209  -20.009 1.00 64.56  ? 384 LEU B CA  1 
ATOM   4108 C  C   . LEU B 2 210 ? -14.039 14.423  -21.334 1.00 70.05  ? 384 LEU B C   1 
ATOM   4109 O  O   . LEU B 2 210 ? -14.925 13.648  -21.694 1.00 83.18  ? 384 LEU B O   1 
ATOM   4110 C  CB  . LEU B 2 210 ? -13.856 15.096  -18.881 1.00 62.52  ? 384 LEU B CB  1 
ATOM   4111 C  CG  . LEU B 2 210 ? -15.223 14.718  -18.311 1.00 68.83  ? 384 LEU B CG  1 
ATOM   4112 C  CD1 . LEU B 2 210 ? -15.389 13.208  -18.159 1.00 72.54  ? 384 LEU B CD1 1 
ATOM   4113 C  CD2 . LEU B 2 210 ? -15.445 15.404  -16.966 1.00 73.99  ? 384 LEU B CD2 1 
ATOM   4114 N  N   . GLU B 2 211 ? -13.598 15.434  -22.090 1.00 68.57  ? 385 GLU B N   1 
ATOM   4115 C  CA  . GLU B 2 211 ? -14.198 15.802  -23.367 1.00 71.41  ? 385 GLU B CA  1 
ATOM   4116 C  C   . GLU B 2 211 ? -13.994 14.691  -24.407 1.00 61.63  ? 385 GLU B C   1 
ATOM   4117 O  O   . GLU B 2 211 ? -14.948 14.310  -25.074 1.00 66.24  ? 385 GLU B O   1 
ATOM   4118 C  CB  . GLU B 2 211 ? -13.669 17.173  -23.815 1.00 82.27  ? 385 GLU B CB  1 
ATOM   4119 C  CG  . GLU B 2 211 ? -14.115 18.338  -22.916 1.00 84.43  ? 385 GLU B CG  1 
ATOM   4120 C  CD  . GLU B 2 211 ? -13.318 18.579  -21.636 1.00 88.63  ? 385 GLU B CD  1 
ATOM   4121 O  OE1 . GLU B 2 211 ? -12.128 18.187  -21.587 1.00 82.88  ? 385 GLU B OE1 1 
ATOM   4122 O  OE2 . GLU B 2 211 ? -13.889 19.152  -20.676 1.00 86.29  ? 385 GLU B OE2 1 
ATOM   4123 N  N   . SER B 2 212 ? -12.771 14.155  -24.537 1.00 61.30  ? 386 SER B N   1 
ATOM   4124 C  CA  . SER B 2 212 ? -12.449 13.076  -25.475 1.00 55.21  ? 386 SER B CA  1 
ATOM   4125 C  C   . SER B 2 212 ? -13.167 11.754  -25.157 1.00 54.48  ? 386 SER B C   1 
ATOM   4126 O  O   . SER B 2 212 ? -13.172 10.843  -25.987 1.00 51.92  ? 386 SER B O   1 
ATOM   4127 C  CB  . SER B 2 212 ? -10.963 12.847  -25.489 1.00 56.24  ? 386 SER B CB  1 
ATOM   4128 O  OG  . SER B 2 212 ? -10.532 12.366  -24.224 1.00 57.52  ? 386 SER B OG  1 
ATOM   4129 N  N   . LEU B 2 213 ? -13.725 11.628  -23.941 1.00 51.77  ? 387 LEU B N   1 
ATOM   4130 C  CA  . LEU B 2 213 ? -14.378 10.405  -23.482 1.00 50.63  ? 387 LEU B CA  1 
ATOM   4131 C  C   . LEU B 2 213 ? -15.892 10.477  -23.706 1.00 52.21  ? 387 LEU B C   1 
ATOM   4132 O  O   . LEU B 2 213 ? -16.580 9.493   -23.443 1.00 49.55  ? 387 LEU B O   1 
ATOM   4133 C  CB  . LEU B 2 213 ? -14.088 10.195  -21.988 1.00 48.71  ? 387 LEU B CB  1 
ATOM   4134 C  CG  . LEU B 2 213 ? -12.653 9.825   -21.612 1.00 48.67  ? 387 LEU B CG  1 
ATOM   4135 C  CD1 . LEU B 2 213 ? -12.459 9.902   -20.112 1.00 45.92  ? 387 LEU B CD1 1 
ATOM   4136 C  CD2 . LEU B 2 213 ? -12.282 8.437   -22.111 1.00 49.88  ? 387 LEU B CD2 1 
ATOM   4137 N  N   . LYS B 2 214 ? -16.394 11.629  -24.192 1.00 57.50  ? 388 LYS B N   1 
ATOM   4138 C  CA  . LYS B 2 214 ? -17.821 11.946  -24.227 1.00 60.34  ? 388 LYS B CA  1 
ATOM   4139 C  C   . LYS B 2 214 ? -18.605 10.916  -25.038 1.00 58.18  ? 388 LYS B C   1 
ATOM   4140 O  O   . LYS B 2 214 ? -19.634 10.425  -24.568 1.00 53.85  ? 388 LYS B O   1 
ATOM   4141 C  CB  . LYS B 2 214 ? -18.102 13.333  -24.818 1.00 65.98  ? 388 LYS B CB  1 
ATOM   4142 C  CG  . LYS B 2 214 ? -19.495 13.866  -24.511 1.00 71.95  ? 388 LYS B CG  1 
ATOM   4143 C  CD  . LYS B 2 214 ? -20.254 14.366  -25.710 1.00 81.32  ? 388 LYS B CD  1 
ATOM   4144 C  CE  . LYS B 2 214 ? -21.678 14.739  -25.351 1.00 90.81  ? 388 LYS B CE  1 
ATOM   4145 N  NZ  . LYS B 2 214 ? -22.363 15.446  -26.458 1.00 95.33  ? 388 LYS B NZ  1 
ATOM   4146 N  N   . PRO B 2 215 ? -18.176 10.568  -26.276 1.00 52.93  ? 389 PRO B N   1 
ATOM   4147 C  CA  . PRO B 2 215 ? -18.908 9.585   -27.073 1.00 54.10  ? 389 PRO B CA  1 
ATOM   4148 C  C   . PRO B 2 215 ? -19.165 8.308   -26.273 1.00 54.39  ? 389 PRO B C   1 
ATOM   4149 O  O   . PRO B 2 215 ? -20.317 7.902   -26.157 1.00 58.74  ? 389 PRO B O   1 
ATOM   4150 C  CB  . PRO B 2 215 ? -18.017 9.355   -28.305 1.00 49.54  ? 389 PRO B CB  1 
ATOM   4151 C  CG  . PRO B 2 215 ? -17.234 10.643  -28.409 1.00 50.41  ? 389 PRO B CG  1 
ATOM   4152 C  CD  . PRO B 2 215 ? -16.988 11.078  -26.978 1.00 47.99  ? 389 PRO B CD  1 
ATOM   4153 N  N   . CYS B 2 216 ? -18.107 7.720   -25.681 1.00 56.87  ? 390 CYS B N   1 
ATOM   4154 C  CA  . CYS B 2 216 ? -18.203 6.444   -24.970 1.00 48.87  ? 390 CYS B CA  1 
ATOM   4155 C  C   . CYS B 2 216 ? -19.085 6.610   -23.738 1.00 46.73  ? 390 CYS B C   1 
ATOM   4156 O  O   . CYS B 2 216 ? -19.835 5.706   -23.389 1.00 48.36  ? 390 CYS B O   1 
ATOM   4157 C  CB  . CYS B 2 216 ? -16.846 5.889   -24.539 1.00 50.22  ? 390 CYS B CB  1 
ATOM   4158 S  SG  . CYS B 2 216 ? -16.929 4.175   -23.932 1.00 55.97  ? 390 CYS B SG  1 
ATOM   4159 N  N   . LEU B 2 217 ? -18.994 7.779   -23.097 1.00 51.04  ? 391 LEU B N   1 
ATOM   4160 C  CA  . LEU B 2 217 ? -19.790 8.111   -21.919 1.00 52.85  ? 391 LEU B CA  1 
ATOM   4161 C  C   . LEU B 2 217 ? -21.291 8.191   -22.244 1.00 51.65  ? 391 LEU B C   1 
ATOM   4162 O  O   . LEU B 2 217 ? -22.105 7.638   -21.493 1.00 50.25  ? 391 LEU B O   1 
ATOM   4163 C  CB  . LEU B 2 217 ? -19.294 9.435   -21.327 1.00 54.28  ? 391 LEU B CB  1 
ATOM   4164 C  CG  . LEU B 2 217 ? -18.427 9.342   -20.079 1.00 60.23  ? 391 LEU B CG  1 
ATOM   4165 C  CD1 . LEU B 2 217 ? -17.958 10.736  -19.668 1.00 64.62  ? 391 LEU B CD1 1 
ATOM   4166 C  CD2 . LEU B 2 217 ? -19.176 8.651   -18.944 1.00 60.50  ? 391 LEU B CD2 1 
ATOM   4167 N  N   A MET B 2 218 ? -21.659 8.887   -23.329 0.50 49.63  ? 392 MET B N   1 
ATOM   4168 N  N   B MET B 2 218 ? -21.639 8.909   -23.326 0.50 51.19  ? 392 MET B N   1 
ATOM   4169 C  CA  A MET B 2 218 ? -23.062 8.974   -23.725 0.50 52.74  ? 392 MET B CA  1 
ATOM   4170 C  CA  B MET B 2 218 ? -23.011 8.976   -23.824 0.50 55.67  ? 392 MET B CA  1 
ATOM   4171 C  C   A MET B 2 218 ? -23.618 7.557   -23.922 0.50 49.80  ? 392 MET B C   1 
ATOM   4172 C  C   B MET B 2 218 ? -23.585 7.560   -23.898 0.50 51.35  ? 392 MET B C   1 
ATOM   4173 O  O   A MET B 2 218 ? -24.723 7.272   -23.470 0.50 50.02  ? 392 MET B O   1 
ATOM   4174 O  O   B MET B 2 218 ? -24.650 7.289   -23.350 0.50 51.16  ? 392 MET B O   1 
ATOM   4175 C  CB  A MET B 2 218 ? -23.271 9.803   -25.002 0.50 56.58  ? 392 MET B CB  1 
ATOM   4176 C  CB  B MET B 2 218 ? -23.092 9.615   -25.220 0.50 61.89  ? 392 MET B CB  1 
ATOM   4177 C  CG  A MET B 2 218 ? -23.185 11.322  -24.809 0.50 57.84  ? 392 MET B CG  1 
ATOM   4178 C  CG  B MET B 2 218 ? -23.367 11.114  -25.223 0.50 64.89  ? 392 MET B CG  1 
ATOM   4179 S  SD  A MET B 2 218 ? -23.853 11.960  -23.245 0.50 63.08  ? 392 MET B SD  1 
ATOM   4180 S  SD  B MET B 2 218 ? -23.927 11.698  -26.849 0.50 70.13  ? 392 MET B SD  1 
ATOM   4181 C  CE  A MET B 2 218 ? -22.323 12.426  -22.436 0.50 61.93  ? 392 MET B CE  1 
ATOM   4182 C  CE  B MET B 2 218 ? -25.594 11.039  -26.873 0.50 71.00  ? 392 MET B CE  1 
ATOM   4183 N  N   . ASP B 2 219 ? -22.846 6.656   -24.552 1.00 48.16  ? 393 ASP B N   1 
ATOM   4184 C  CA  . ASP B 2 219 ? -23.270 5.266   -24.708 1.00 49.06  ? 393 ASP B CA  1 
ATOM   4185 C  C   . ASP B 2 219 ? -23.403 4.543   -23.364 1.00 46.95  ? 393 ASP B C   1 
ATOM   4186 O  O   . ASP B 2 219 ? -24.377 3.820   -23.143 1.00 43.78  ? 393 ASP B O   1 
ATOM   4187 C  CB  . ASP B 2 219 ? -22.346 4.482   -25.639 1.00 50.87  ? 393 ASP B CB  1 
ATOM   4188 C  CG  . ASP B 2 219 ? -22.717 4.615   -27.107 1.00 56.54  ? 393 ASP B CG  1 
ATOM   4189 O  OD1 . ASP B 2 219 ? -23.923 4.697   -27.383 1.00 70.85  ? 393 ASP B OD1 1 
ATOM   4190 O  OD2 . ASP B 2 219 ? -21.803 4.583   -27.968 1.00 62.13  ? 393 ASP B OD2 1 
ATOM   4191 N  N   . LEU B 2 220 ? -22.422 4.733   -22.474 1.00 46.93  ? 394 LEU B N   1 
ATOM   4192 C  CA  . LEU B 2 220 ? -22.314 3.938   -21.263 1.00 45.27  ? 394 LEU B CA  1 
ATOM   4193 C  C   . LEU B 2 220 ? -23.361 4.383   -20.250 1.00 43.76  ? 394 LEU B C   1 
ATOM   4194 O  O   . LEU B 2 220 ? -23.941 3.552   -19.550 1.00 42.23  ? 394 LEU B O   1 
ATOM   4195 C  CB  . LEU B 2 220 ? -20.898 4.080   -20.704 1.00 47.25  ? 394 LEU B CB  1 
ATOM   4196 C  CG  . LEU B 2 220 ? -20.426 2.925   -19.836 1.00 52.76  ? 394 LEU B CG  1 
ATOM   4197 C  CD1 . LEU B 2 220 ? -20.434 1.629   -20.628 1.00 55.48  ? 394 LEU B CD1 1 
ATOM   4198 C  CD2 . LEU B 2 220 ? -19.030 3.200   -19.296 1.00 56.82  ? 394 LEU B CD2 1 
ATOM   4199 N  N   . HIS B 2 221 ? -23.567 5.702   -20.169 1.00 47.77  ? 395 HIS B N   1 
ATOM   4200 C  CA  . HIS B 2 221 ? -24.695 6.280   -19.452 1.00 50.09  ? 395 HIS B CA  1 
ATOM   4201 C  C   . HIS B 2 221 ? -25.994 5.573   -19.857 1.00 48.19  ? 395 HIS B C   1 
ATOM   4202 O  O   . HIS B 2 221 ? -26.741 5.121   -18.994 1.00 51.75  ? 395 HIS B O   1 
ATOM   4203 C  CB  . HIS B 2 221 ? -24.759 7.793   -19.692 1.00 55.89  ? 395 HIS B CB  1 
ATOM   4204 C  CG  . HIS B 2 221 ? -25.699 8.525   -18.787 1.00 62.60  ? 395 HIS B CG  1 
ATOM   4205 N  ND1 . HIS B 2 221 ? -26.316 9.698   -19.171 1.00 66.13  ? 395 HIS B ND1 1 
ATOM   4206 C  CD2 . HIS B 2 221 ? -26.155 8.242   -17.558 1.00 58.36  ? 395 HIS B CD2 1 
ATOM   4207 C  CE1 . HIS B 2 221 ? -27.092 10.115  -18.186 1.00 67.37  ? 395 HIS B CE1 1 
ATOM   4208 N  NE2 . HIS B 2 221 ? -27.006 9.246   -17.192 1.00 63.58  ? 395 HIS B NE2 1 
ATOM   4209 N  N   . GLN B 2 222 ? -26.267 5.482   -21.165 1.00 50.75  ? 396 GLN B N   1 
ATOM   4210 C  CA  . GLN B 2 222 ? -27.504 4.876   -21.655 1.00 54.56  ? 396 GLN B CA  1 
ATOM   4211 C  C   . GLN B 2 222 ? -27.571 3.426   -21.186 1.00 49.62  ? 396 GLN B C   1 
ATOM   4212 O  O   . GLN B 2 222 ? -28.593 2.992   -20.660 1.00 48.46  ? 396 GLN B O   1 
ATOM   4213 C  CB  . GLN B 2 222 ? -27.628 4.920   -23.185 1.00 61.40  ? 396 GLN B CB  1 
ATOM   4214 C  CG  . GLN B 2 222 ? -27.700 6.320   -23.782 1.00 68.96  ? 396 GLN B CG  1 
ATOM   4215 C  CD  . GLN B 2 222 ? -28.559 7.238   -22.951 1.00 79.74  ? 396 GLN B CD  1 
ATOM   4216 O  OE1 . GLN B 2 222 ? -29.745 6.975   -22.741 1.00 78.72  ? 396 GLN B OE1 1 
ATOM   4217 N  NE2 . GLN B 2 222 ? -27.953 8.307   -22.453 1.00 81.33  ? 396 GLN B NE2 1 
ATOM   4218 N  N   . THR B 2 223 ? -26.471 2.688   -21.363 1.00 46.65  ? 397 THR B N   1 
ATOM   4219 C  CA  . THR B 2 223 ? -26.457 1.277   -21.017 1.00 43.63  ? 397 THR B CA  1 
ATOM   4220 C  C   . THR B 2 223 ? -26.806 1.125   -19.543 1.00 43.44  ? 397 THR B C   1 
ATOM   4221 O  O   . THR B 2 223 ? -27.570 0.237   -19.172 1.00 46.38  ? 397 THR B O   1 
ATOM   4222 C  CB  . THR B 2 223 ? -25.108 0.630   -21.330 1.00 42.67  ? 397 THR B CB  1 
ATOM   4223 O  OG1 . THR B 2 223 ? -24.934 0.742   -22.739 1.00 44.46  ? 397 THR B OG1 1 
ATOM   4224 C  CG2 . THR B 2 223 ? -25.029 -0.821  -20.899 1.00 46.28  ? 397 THR B CG2 1 
ATOM   4225 N  N   . TYR B 2 224 ? -26.229 2.004   -18.716 1.00 46.90  ? 398 TYR B N   1 
ATOM   4226 C  CA  . TYR B 2 224 ? -26.459 1.998   -17.276 1.00 50.22  ? 398 TYR B CA  1 
ATOM   4227 C  C   . TYR B 2 224 ? -27.939 2.304   -16.986 1.00 54.79  ? 398 TYR B C   1 
ATOM   4228 O  O   . TYR B 2 224 ? -28.565 1.607   -16.185 1.00 59.52  ? 398 TYR B O   1 
ATOM   4229 C  CB  . TYR B 2 224 ? -25.470 2.958   -16.592 1.00 47.05  ? 398 TYR B CB  1 
ATOM   4230 C  CG  . TYR B 2 224 ? -25.402 2.935   -15.080 1.00 44.69  ? 398 TYR B CG  1 
ATOM   4231 C  CD1 . TYR B 2 224 ? -25.948 1.901   -14.335 1.00 44.69  ? 398 TYR B CD1 1 
ATOM   4232 C  CD2 . TYR B 2 224 ? -24.762 3.955   -14.386 1.00 45.89  ? 398 TYR B CD2 1 
ATOM   4233 C  CE1 . TYR B 2 224 ? -25.881 1.897   -12.950 1.00 48.48  ? 398 TYR B CE1 1 
ATOM   4234 C  CE2 . TYR B 2 224 ? -24.679 3.960   -13.003 1.00 46.08  ? 398 TYR B CE2 1 
ATOM   4235 C  CZ  . TYR B 2 224 ? -25.249 2.929   -12.281 1.00 46.73  ? 398 TYR B CZ  1 
ATOM   4236 O  OH  . TYR B 2 224 ? -25.176 2.913   -10.911 1.00 52.75  ? 398 TYR B OH  1 
ATOM   4237 N  N   . LEU B 2 225 ? -28.506 3.321   -17.661 1.00 54.52  ? 399 LEU B N   1 
ATOM   4238 C  CA  . LEU B 2 225 ? -29.897 3.726   -17.466 1.00 56.36  ? 399 LEU B CA  1 
ATOM   4239 C  C   . LEU B 2 225 ? -30.857 2.569   -17.768 1.00 52.70  ? 399 LEU B C   1 
ATOM   4240 O  O   . LEU B 2 225 ? -31.758 2.312   -16.979 1.00 47.16  ? 399 LEU B O   1 
ATOM   4241 C  CB  . LEU B 2 225 ? -30.184 4.979   -18.309 1.00 55.07  ? 399 LEU B CB  1 
ATOM   4242 C  CG  . LEU B 2 225 ? -29.631 6.284   -17.724 1.00 55.49  ? 399 LEU B CG  1 
ATOM   4243 C  CD1 . LEU B 2 225 ? -29.788 7.452   -18.689 1.00 56.28  ? 399 LEU B CD1 1 
ATOM   4244 C  CD2 . LEU B 2 225 ? -30.298 6.618   -16.394 1.00 55.88  ? 399 LEU B CD2 1 
ATOM   4245 N  N   . LYS B 2 226 ? -30.611 1.810   -18.843 1.00 55.52  ? 400 LYS B N   1 
ATOM   4246 C  CA  . LYS B 2 226 ? -31.549 0.795   -19.315 1.00 59.79  ? 400 LYS B CA  1 
ATOM   4247 C  C   . LYS B 2 226 ? -31.169 -0.623  -18.858 1.00 56.15  ? 400 LYS B C   1 
ATOM   4248 O  O   . LYS B 2 226 ? -31.763 -1.590  -19.325 1.00 54.40  ? 400 LYS B O   1 
ATOM   4249 C  CB  . LYS B 2 226 ? -31.653 0.926   -20.841 1.00 66.23  ? 400 LYS B CB  1 
ATOM   4250 C  CG  . LYS B 2 226 ? -31.945 2.346   -21.325 1.00 73.82  ? 400 LYS B CG  1 
ATOM   4251 C  CD  . LYS B 2 226 ? -32.735 2.440   -22.618 1.00 84.56  ? 400 LYS B CD  1 
ATOM   4252 C  CE  . LYS B 2 226 ? -32.078 1.729   -23.782 1.00 89.28  ? 400 LYS B CE  1 
ATOM   4253 N  NZ  . LYS B 2 226 ? -30.776 2.340   -24.136 1.00 90.71  ? 400 LYS B NZ  1 
ATOM   4254 N  N   . ALA B 2 227 ? -30.222 -0.757  -17.915 1.00 57.26  ? 401 ALA B N   1 
ATOM   4255 C  CA  . ALA B 2 227 ? -29.681 -2.051  -17.508 1.00 53.05  ? 401 ALA B CA  1 
ATOM   4256 C  C   . ALA B 2 227 ? -30.760 -2.925  -16.872 1.00 52.48  ? 401 ALA B C   1 
ATOM   4257 O  O   . ALA B 2 227 ? -30.799 -4.128  -17.122 1.00 53.88  ? 401 ALA B O   1 
ATOM   4258 C  CB  . ALA B 2 227 ? -28.512 -1.867  -16.563 1.00 49.32  ? 401 ALA B CB  1 
ATOM   4259 N  N   . PRO B 2 228 ? -31.647 -2.376  -16.008 1.00 58.93  ? 402 PRO B N   1 
ATOM   4260 C  CA  . PRO B 2 228 ? -32.756 -3.161  -15.454 1.00 59.47  ? 402 PRO B CA  1 
ATOM   4261 C  C   . PRO B 2 228 ? -33.707 -3.745  -16.504 1.00 58.02  ? 402 PRO B C   1 
ATOM   4262 O  O   . PRO B 2 228 ? -34.353 -4.740  -16.218 1.00 58.71  ? 402 PRO B O   1 
ATOM   4263 C  CB  . PRO B 2 228 ? -33.489 -2.161  -14.544 1.00 62.20  ? 402 PRO B CB  1 
ATOM   4264 C  CG  . PRO B 2 228 ? -32.433 -1.117  -14.205 1.00 63.46  ? 402 PRO B CG  1 
ATOM   4265 C  CD  . PRO B 2 228 ? -31.624 -0.997  -15.482 1.00 62.95  ? 402 PRO B CD  1 
ATOM   4266 N  N   . GLN B 2 229 ? -33.737 -3.164  -17.717 1.00 58.90  ? 403 GLN B N   1 
ATOM   4267 C  CA  . GLN B 2 229 ? -34.651 -3.535  -18.796 1.00 60.98  ? 403 GLN B CA  1 
ATOM   4268 C  C   . GLN B 2 229 ? -34.017 -4.581  -19.722 1.00 62.95  ? 403 GLN B C   1 
ATOM   4269 O  O   . GLN B 2 229 ? -34.734 -5.309  -20.414 1.00 57.23  ? 403 GLN B O   1 
ATOM   4270 C  CB  . GLN B 2 229 ? -35.033 -2.298  -19.626 1.00 66.20  ? 403 GLN B CB  1 
ATOM   4271 C  CG  . GLN B 2 229 ? -35.515 -1.119  -18.790 1.00 71.68  ? 403 GLN B CG  1 
ATOM   4272 C  CD  . GLN B 2 229 ? -35.823 0.124   -19.592 1.00 79.26  ? 403 GLN B CD  1 
ATOM   4273 O  OE1 . GLN B 2 229 ? -36.580 0.087   -20.560 1.00 72.20  ? 403 GLN B OE1 1 
ATOM   4274 N  NE2 . GLN B 2 229 ? -35.267 1.249   -19.163 1.00 83.45  ? 403 GLN B NE2 1 
ATOM   4275 N  N   . HIS B 2 230 ? -32.675 -4.646  -19.738 1.00 60.70  ? 404 HIS B N   1 
ATOM   4276 C  CA  . HIS B 2 230 ? -31.932 -5.500  -20.661 1.00 54.11  ? 404 HIS B CA  1 
ATOM   4277 C  C   . HIS B 2 230 ? -32.328 -6.969  -20.473 1.00 50.94  ? 404 HIS B C   1 
ATOM   4278 O  O   . HIS B 2 230 ? -32.477 -7.442  -19.343 1.00 48.98  ? 404 HIS B O   1 
ATOM   4279 C  CB  . HIS B 2 230 ? -30.417 -5.285  -20.492 1.00 57.80  ? 404 HIS B CB  1 
ATOM   4280 C  CG  . HIS B 2 230 ? -29.581 -5.746  -21.642 1.00 56.39  ? 404 HIS B CG  1 
ATOM   4281 N  ND1 . HIS B 2 230 ? -29.410 -7.083  -21.942 1.00 50.54  ? 404 HIS B ND1 1 
ATOM   4282 C  CD2 . HIS B 2 230 ? -28.869 -5.054  -22.559 1.00 51.60  ? 404 HIS B CD2 1 
ATOM   4283 C  CE1 . HIS B 2 230 ? -28.639 -7.190  -23.022 1.00 52.74  ? 404 HIS B CE1 1 
ATOM   4284 N  NE2 . HIS B 2 230 ? -28.292 -5.969  -23.406 1.00 51.13  ? 404 HIS B NE2 1 
ATOM   4285 N  N   . ALA B 2 231 ? -32.483 -7.676  -21.605 1.00 52.65  ? 405 ALA B N   1 
ATOM   4286 C  CA  . ALA B 2 231 ? -32.798 -9.102  -21.644 1.00 55.78  ? 405 ALA B CA  1 
ATOM   4287 C  C   . ALA B 2 231 ? -31.858 -9.906  -20.730 1.00 54.51  ? 405 ALA B C   1 
ATOM   4288 O  O   . ALA B 2 231 ? -32.317 -10.685 -19.889 1.00 56.19  ? 405 ALA B O   1 
ATOM   4289 C  CB  . ALA B 2 231 ? -32.744 -9.581  -23.078 1.00 56.89  ? 405 ALA B CB  1 
ATOM   4290 N  N   . GLN B 2 232 ? -30.544 -9.674  -20.871 1.00 53.89  ? 406 GLN B N   1 
ATOM   4291 C  CA  . GLN B 2 232 ? -29.496 -10.370 -20.119 1.00 49.64  ? 406 GLN B CA  1 
ATOM   4292 C  C   . GLN B 2 232 ? -29.291 -9.674  -18.771 1.00 45.87  ? 406 GLN B C   1 
ATOM   4293 O  O   . GLN B 2 232 ? -29.129 -8.449  -18.721 1.00 45.42  ? 406 GLN B O   1 
ATOM   4294 C  CB  . GLN B 2 232 ? -28.204 -10.390 -20.950 1.00 52.69  ? 406 GLN B CB  1 
ATOM   4295 C  CG  . GLN B 2 232 ? -28.176 -11.407 -22.095 1.00 51.48  ? 406 GLN B CG  1 
ATOM   4296 C  CD  . GLN B 2 232 ? -29.204 -11.188 -23.177 1.00 52.06  ? 406 GLN B CD  1 
ATOM   4297 O  OE1 . GLN B 2 232 ? -29.224 -10.162 -23.861 1.00 55.65  ? 406 GLN B OE1 1 
ATOM   4298 N  NE2 . GLN B 2 232 ? -30.063 -12.181 -23.339 1.00 43.49  ? 406 GLN B NE2 1 
ATOM   4299 N  N   . GLN B 2 233 ? -29.313 -10.451 -17.676 1.00 46.57  ? 407 GLN B N   1 
ATOM   4300 C  CA  . GLN B 2 233 ? -29.336 -9.886  -16.330 1.00 44.82  ? 407 GLN B CA  1 
ATOM   4301 C  C   . GLN B 2 233 ? -28.278 -10.502 -15.415 1.00 45.81  ? 407 GLN B C   1 
ATOM   4302 O  O   . GLN B 2 233 ? -28.208 -10.083 -14.258 1.00 52.76  ? 407 GLN B O   1 
ATOM   4303 C  CB  . GLN B 2 233 ? -30.722 -10.071 -15.702 1.00 44.16  ? 407 GLN B CB  1 
ATOM   4304 C  CG  . GLN B 2 233 ? -31.785 -9.152  -16.292 1.00 44.94  ? 407 GLN B CG  1 
ATOM   4305 C  CD  . GLN B 2 233 ? -31.589 -7.703  -15.921 1.00 45.90  ? 407 GLN B CD  1 
ATOM   4306 O  OE1 . GLN B 2 233 ? -31.370 -7.373  -14.755 1.00 46.10  ? 407 GLN B OE1 1 
ATOM   4307 N  NE2 . GLN B 2 233 ? -31.682 -6.825  -16.910 1.00 43.60  ? 407 GLN B NE2 1 
ATOM   4308 N  N   . SER B 2 234 ? -27.449 -11.439 -15.923 1.00 42.25  ? 408 SER B N   1 
ATOM   4309 C  CA  . SER B 2 234 ? -26.496 -12.191 -15.106 1.00 42.32  ? 408 SER B CA  1 
ATOM   4310 C  C   . SER B 2 234 ? -25.500 -11.264 -14.418 1.00 41.98  ? 408 SER B C   1 
ATOM   4311 O  O   . SER B 2 234 ? -25.031 -11.599 -13.344 1.00 43.09  ? 408 SER B O   1 
ATOM   4312 C  CB  . SER B 2 234 ? -25.722 -13.212 -15.894 1.00 44.62  ? 408 SER B CB  1 
ATOM   4313 O  OG  . SER B 2 234 ? -26.547 -14.277 -16.334 1.00 45.36  ? 408 SER B OG  1 
ATOM   4314 N  N   . ILE B 2 235 ? -25.179 -10.128 -15.054 1.00 42.00  ? 409 ILE B N   1 
ATOM   4315 C  CA  . ILE B 2 235 ? -24.203 -9.176  -14.542 1.00 42.58  ? 409 ILE B CA  1 
ATOM   4316 C  C   . ILE B 2 235 ? -24.821 -8.305  -13.452 1.00 39.61  ? 409 ILE B C   1 
ATOM   4317 O  O   . ILE B 2 235 ? -24.194 -8.106  -12.418 1.00 44.57  ? 409 ILE B O   1 
ATOM   4318 C  CB  . ILE B 2 235 ? -23.599 -8.336  -15.687 1.00 43.01  ? 409 ILE B CB  1 
ATOM   4319 C  CG1 . ILE B 2 235 ? -22.813 -9.208  -16.668 1.00 42.93  ? 409 ILE B CG1 1 
ATOM   4320 C  CG2 . ILE B 2 235 ? -22.744 -7.203  -15.145 1.00 43.82  ? 409 ILE B CG2 1 
ATOM   4321 C  CD1 . ILE B 2 235 ? -22.270 -8.457  -17.854 1.00 42.83  ? 409 ILE B CD1 1 
ATOM   4322 N  N   . ARG B 2 236 ? -26.022 -7.763  -13.683 1.00 43.34  ? 410 ARG B N   1 
ATOM   4323 C  CA  . ARG B 2 236 ? -26.771 -7.080  -12.624 1.00 44.19  ? 410 ARG B CA  1 
ATOM   4324 C  C   . ARG B 2 236 ? -26.969 -8.001  -11.417 1.00 43.08  ? 410 ARG B C   1 
ATOM   4325 O  O   . ARG B 2 236 ? -26.804 -7.560  -10.280 1.00 43.74  ? 410 ARG B O   1 
ATOM   4326 C  CB  . ARG B 2 236 ? -28.123 -6.566  -13.124 1.00 47.05  ? 410 ARG B CB  1 
ATOM   4327 C  CG  . ARG B 2 236 ? -28.065 -5.176  -13.737 1.00 50.50  ? 410 ARG B CG  1 
ATOM   4328 C  CD  . ARG B 2 236 ? -29.439 -4.627  -14.079 1.00 56.61  ? 410 ARG B CD  1 
ATOM   4329 N  NE  . ARG B 2 236 ? -30.081 -3.990  -12.933 1.00 59.72  ? 410 ARG B NE  1 
ATOM   4330 C  CZ  . ARG B 2 236 ? -30.998 -4.555  -12.153 1.00 62.72  ? 410 ARG B CZ  1 
ATOM   4331 N  NH1 . ARG B 2 236 ? -31.517 -3.860  -11.156 1.00 64.25  ? 410 ARG B NH1 1 
ATOM   4332 N  NH2 . ARG B 2 236 ? -31.384 -5.807  -12.352 1.00 64.73  ? 410 ARG B NH2 1 
ATOM   4333 N  N   . GLU B 2 237 ? -27.282 -9.283  -11.673 1.00 44.71  ? 411 GLU B N   1 
ATOM   4334 C  CA  . GLU B 2 237 ? -27.468 -10.274 -10.615 1.00 50.17  ? 411 GLU B CA  1 
ATOM   4335 C  C   . GLU B 2 237 ? -26.171 -10.474 -9.828  1.00 54.42  ? 411 GLU B C   1 
ATOM   4336 O  O   . GLU B 2 237 ? -26.180 -10.488 -8.592  1.00 54.52  ? 411 GLU B O   1 
ATOM   4337 C  CB  . GLU B 2 237 ? -27.980 -11.613 -11.168 1.00 53.01  ? 411 GLU B CB  1 
ATOM   4338 C  CG  . GLU B 2 237 ? -29.482 -11.643 -11.448 1.00 60.37  ? 411 GLU B CG  1 
ATOM   4339 C  CD  . GLU B 2 237 ? -30.338 -10.686 -10.625 1.00 67.41  ? 411 GLU B CD  1 
ATOM   4340 O  OE1 . GLU B 2 237 ? -30.583 -10.974 -9.424  1.00 61.81  ? 411 GLU B OE1 1 
ATOM   4341 O  OE2 . GLU B 2 237 ? -30.736 -9.627  -11.176 1.00 70.17  ? 411 GLU B OE2 1 
ATOM   4342 N  N   . LYS B 2 238 ? -25.061 -10.633 -10.556 1.00 50.79  ? 412 LYS B N   1 
ATOM   4343 C  CA  . LYS B 2 238 ? -23.766 -10.904 -9.954  1.00 47.76  ? 412 LYS B CA  1 
ATOM   4344 C  C   . LYS B 2 238 ? -23.380 -9.784  -8.988  1.00 47.62  ? 412 LYS B C   1 
ATOM   4345 O  O   . LYS B 2 238 ? -22.933 -10.061 -7.884  1.00 46.14  ? 412 LYS B O   1 
ATOM   4346 C  CB  . LYS B 2 238 ? -22.737 -11.077 -11.068 1.00 43.70  ? 412 LYS B CB  1 
ATOM   4347 C  CG  . LYS B 2 238 ? -21.286 -10.964 -10.649 1.00 44.74  ? 412 LYS B CG  1 
ATOM   4348 C  CD  . LYS B 2 238 ? -20.414 -11.280 -11.824 1.00 47.04  ? 412 LYS B CD  1 
ATOM   4349 C  CE  . LYS B 2 238 ? -18.927 -11.111 -11.635 1.00 46.54  ? 412 LYS B CE  1 
ATOM   4350 N  NZ  . LYS B 2 238 ? -18.241 -11.627 -12.847 1.00 52.47  ? 412 LYS B NZ  1 
ATOM   4351 N  N   . TYR B 2 239 ? -23.597 -8.531  -9.407  1.00 48.55  ? 413 TYR B N   1 
ATOM   4352 C  CA  . TYR B 2 239 ? -23.163 -7.344  -8.683  1.00 48.75  ? 413 TYR B CA  1 
ATOM   4353 C  C   . TYR B 2 239 ? -24.216 -6.863  -7.675  1.00 53.83  ? 413 TYR B C   1 
ATOM   4354 O  O   . TYR B 2 239 ? -24.179 -5.706  -7.254  1.00 56.89  ? 413 TYR B O   1 
ATOM   4355 C  CB  . TYR B 2 239 ? -22.782 -6.258  -9.696  1.00 46.37  ? 413 TYR B CB  1 
ATOM   4356 C  CG  . TYR B 2 239 ? -21.415 -6.441  -10.305 1.00 43.04  ? 413 TYR B CG  1 
ATOM   4357 C  CD1 . TYR B 2 239 ? -21.219 -7.284  -11.385 1.00 45.23  ? 413 TYR B CD1 1 
ATOM   4358 C  CD2 . TYR B 2 239 ? -20.307 -5.798  -9.779  1.00 43.72  ? 413 TYR B CD2 1 
ATOM   4359 C  CE1 . TYR B 2 239 ? -19.964 -7.461  -11.942 1.00 50.23  ? 413 TYR B CE1 1 
ATOM   4360 C  CE2 . TYR B 2 239 ? -19.045 -5.962  -10.321 1.00 45.10  ? 413 TYR B CE2 1 
ATOM   4361 C  CZ  . TYR B 2 239 ? -18.872 -6.798  -11.412 1.00 48.63  ? 413 TYR B CZ  1 
ATOM   4362 O  OH  . TYR B 2 239 ? -17.633 -6.979  -11.966 1.00 50.53  ? 413 TYR B OH  1 
ATOM   4363 N  N   . LYS B 2 240 ? -25.161 -7.741  -7.305  1.00 57.38  ? 414 LYS B N   1 
ATOM   4364 C  CA  . LYS B 2 240 ? -26.004 -7.570  -6.126  1.00 60.42  ? 414 LYS B CA  1 
ATOM   4365 C  C   . LYS B 2 240 ? -25.295 -8.118  -4.880  1.00 59.51  ? 414 LYS B C   1 
ATOM   4366 O  O   . LYS B 2 240 ? -25.441 -7.553  -3.801  1.00 64.31  ? 414 LYS B O   1 
ATOM   4367 C  CB  . LYS B 2 240 ? -27.369 -8.251  -6.313  1.00 66.63  ? 414 LYS B CB  1 
ATOM   4368 C  CG  . LYS B 2 240 ? -28.386 -7.485  -7.157  1.00 72.11  ? 414 LYS B CG  1 
ATOM   4369 C  CD  . LYS B 2 240 ? -29.723 -8.208  -7.341  1.00 77.67  ? 414 LYS B CD  1 
ATOM   4370 C  CE  . LYS B 2 240 ? -30.773 -7.377  -8.056  1.00 78.29  ? 414 LYS B CE  1 
ATOM   4371 N  NZ  . LYS B 2 240 ? -31.819 -8.220  -8.680  1.00 74.29  ? 414 LYS B NZ  1 
ATOM   4372 N  N   A ASN B 2 241 ? -24.523 -9.211  -5.045  0.50 58.75  ? 415 ASN B N   1 
ATOM   4373 N  N   B ASN B 2 241 ? -24.542 -9.208  -5.038  0.50 59.40  ? 415 ASN B N   1 
ATOM   4374 C  CA  A ASN B 2 241 ? -23.830 -9.910  -3.959  0.50 62.49  ? 415 ASN B CA  1 
ATOM   4375 C  CA  B ASN B 2 241 ? -23.933 -9.902  -3.913  0.50 63.61  ? 415 ASN B CA  1 
ATOM   4376 C  C   A ASN B 2 241 ? -23.096 -8.898  -3.074  0.50 61.92  ? 415 ASN B C   1 
ATOM   4377 C  C   B ASN B 2 241 ? -23.096 -8.920  -3.083  0.50 62.64  ? 415 ASN B C   1 
ATOM   4378 O  O   A ASN B 2 241 ? -22.775 -7.790  -3.513  0.50 53.26  ? 415 ASN B O   1 
ATOM   4379 O  O   B ASN B 2 241 ? -22.721 -7.845  -3.559  0.50 54.15  ? 415 ASN B O   1 
ATOM   4380 C  CB  A ASN B 2 241 ? -22.862 -10.987 -4.492  0.50 63.06  ? 415 ASN B CB  1 
ATOM   4381 C  CB  B ASN B 2 241 ? -23.161 -11.135 -4.405  0.50 64.87  ? 415 ASN B CB  1 
ATOM   4382 C  CG  A ASN B 2 241 ? -22.365 -11.997 -3.466  0.50 64.48  ? 415 ASN B CG  1 
ATOM   4383 C  CG  B ASN B 2 241 ? -24.043 -12.124 -5.143  0.50 66.39  ? 415 ASN B CG  1 
ATOM   4384 O  OD1 A ASN B 2 241 ? -21.677 -11.651 -2.505  0.50 57.06  ? 415 ASN B OD1 1 
ATOM   4385 O  OD1 B ASN B 2 241 ? -25.165 -12.398 -4.722  0.50 59.57  ? 415 ASN B OD1 1 
ATOM   4386 N  ND2 A ASN B 2 241 ? -22.656 -13.269 -3.693  0.50 65.39  ? 415 ASN B ND2 1 
ATOM   4387 N  ND2 B ASN B 2 241 ? -23.550 -12.657 -6.250  0.50 72.16  ? 415 ASN B ND2 1 
ATOM   4388 N  N   . SER B 2 242 ? -22.837 -9.304  -1.823  1.00 64.78  ? 416 SER B N   1 
ATOM   4389 C  CA  . SER B 2 242 ? -22.039 -8.527  -0.882  1.00 67.51  ? 416 SER B CA  1 
ATOM   4390 C  C   . SER B 2 242 ? -20.607 -8.349  -1.399  1.00 61.66  ? 416 SER B C   1 
ATOM   4391 O  O   . SER B 2 242 ? -19.968 -7.345  -1.085  1.00 55.83  ? 416 SER B O   1 
ATOM   4392 C  CB  . SER B 2 242 ? -22.053 -9.166  0.510   1.00 74.50  ? 416 SER B CB  1 
ATOM   4393 O  OG  . SER B 2 242 ? -21.122 -10.245 0.618   1.00 68.78  ? 416 SER B OG  1 
ATOM   4394 N  N   . LYS B 2 243 ? -20.094 -9.323  -2.174  1.00 62.24  ? 417 LYS B N   1 
ATOM   4395 C  CA  . LYS B 2 243 ? -18.721 -9.254  -2.674  1.00 64.92  ? 417 LYS B CA  1 
ATOM   4396 C  C   . LYS B 2 243 ? -18.483 -7.940  -3.437  1.00 59.21  ? 417 LYS B C   1 
ATOM   4397 O  O   . LYS B 2 243 ? -17.385 -7.401  -3.358  1.00 62.69  ? 417 LYS B O   1 
ATOM   4398 C  CB  . LYS B 2 243 ? -18.347 -10.462 -3.549  1.00 67.81  ? 417 LYS B CB  1 
ATOM   4399 C  CG  . LYS B 2 243 ? -16.939 -10.393 -4.143  1.00 71.08  ? 417 LYS B CG  1 
ATOM   4400 C  CD  . LYS B 2 243 ? -16.583 -11.460 -5.171  1.00 81.66  ? 417 LYS B CD  1 
ATOM   4401 C  CE  . LYS B 2 243 ? -15.727 -12.591 -4.633  1.00 86.95  ? 417 LYS B CE  1 
ATOM   4402 N  NZ  . LYS B 2 243 ? -14.878 -13.194 -5.691  1.00 85.97  ? 417 LYS B NZ  1 
ATOM   4403 N  N   . TYR B 2 244 ? -19.496 -7.430  -4.167  1.00 53.39  ? 418 TYR B N   1 
ATOM   4404 C  CA  . TYR B 2 244 ? -19.377 -6.216  -4.980  1.00 54.69  ? 418 TYR B CA  1 
ATOM   4405 C  C   . TYR B 2 244 ? -20.209 -5.064  -4.407  1.00 55.24  ? 418 TYR B C   1 
ATOM   4406 O  O   . TYR B 2 244 ? -20.503 -4.115  -5.129  1.00 54.49  ? 418 TYR B O   1 
ATOM   4407 C  CB  . TYR B 2 244 ? -19.765 -6.485  -6.442  1.00 52.67  ? 418 TYR B CB  1 
ATOM   4408 C  CG  . TYR B 2 244 ? -18.965 -7.592  -7.085  1.00 51.53  ? 418 TYR B CG  1 
ATOM   4409 C  CD1 . TYR B 2 244 ? -17.636 -7.412  -7.436  1.00 52.19  ? 418 TYR B CD1 1 
ATOM   4410 C  CD2 . TYR B 2 244 ? -19.511 -8.855  -7.258  1.00 55.54  ? 418 TYR B CD2 1 
ATOM   4411 C  CE1 . TYR B 2 244 ? -16.879 -8.441  -7.976  1.00 53.93  ? 418 TYR B CE1 1 
ATOM   4412 C  CE2 . TYR B 2 244 ? -18.772 -9.894  -7.802  1.00 55.61  ? 418 TYR B CE2 1 
ATOM   4413 C  CZ  . TYR B 2 244 ? -17.455 -9.685  -8.170  1.00 56.61  ? 418 TYR B CZ  1 
ATOM   4414 O  OH  . TYR B 2 244 ? -16.745 -10.724 -8.720  1.00 61.42  ? 418 TYR B OH  1 
ATOM   4415 N  N   . HIS B 2 245 ? -20.571 -5.133  -3.117  1.00 54.79  ? 419 HIS B N   1 
ATOM   4416 C  CA  . HIS B 2 245 ? -21.151 -4.012  -2.378  1.00 55.46  ? 419 HIS B CA  1 
ATOM   4417 C  C   . HIS B 2 245 ? -22.514 -3.584  -2.932  1.00 52.60  ? 419 HIS B C   1 
ATOM   4418 O  O   . HIS B 2 245 ? -22.895 -2.426  -2.775  1.00 56.80  ? 419 HIS B O   1 
ATOM   4419 C  CB  . HIS B 2 245 ? -20.181 -2.819  -2.336  1.00 56.18  ? 419 HIS B CB  1 
ATOM   4420 C  CG  . HIS B 2 245 ? -18.794 -3.192  -1.930  1.00 61.99  ? 419 HIS B CG  1 
ATOM   4421 N  ND1 . HIS B 2 245 ? -17.793 -3.363  -2.861  1.00 71.51  ? 419 HIS B ND1 1 
ATOM   4422 C  CD2 . HIS B 2 245 ? -18.240 -3.466  -0.740  1.00 64.33  ? 419 HIS B CD2 1 
ATOM   4423 C  CE1 . HIS B 2 245 ? -16.669 -3.709  -2.244  1.00 73.42  ? 419 HIS B CE1 1 
ATOM   4424 N  NE2 . HIS B 2 245 ? -16.917 -3.776  -0.956  1.00 68.71  ? 419 HIS B NE2 1 
ATOM   4425 N  N   . GLY B 2 246 ? -23.238 -4.514  -3.576  1.00 52.49  ? 420 GLY B N   1 
ATOM   4426 C  CA  . GLY B 2 246 ? -24.570 -4.277  -4.125  1.00 51.80  ? 420 GLY B CA  1 
ATOM   4427 C  C   . GLY B 2 246 ? -24.661 -3.076  -5.075  1.00 57.33  ? 420 GLY B C   1 
ATOM   4428 O  O   . GLY B 2 246 ? -25.747 -2.510  -5.254  1.00 57.57  ? 420 GLY B O   1 
ATOM   4429 N  N   . VAL B 2 247 ? -23.543 -2.728  -5.735  1.00 52.49  ? 421 VAL B N   1 
ATOM   4430 C  CA  . VAL B 2 247 ? -23.482 -1.561  -6.609  1.00 50.55  ? 421 VAL B CA  1 
ATOM   4431 C  C   . VAL B 2 247 ? -24.522 -1.646  -7.736  1.00 49.46  ? 421 VAL B C   1 
ATOM   4432 O  O   . VAL B 2 247 ? -24.933 -0.608  -8.251  1.00 48.28  ? 421 VAL B O   1 
ATOM   4433 C  CB  . VAL B 2 247 ? -22.068 -1.339  -7.183  1.00 49.81  ? 421 VAL B CB  1 
ATOM   4434 C  CG1 . VAL B 2 247 ? -21.073 -0.942  -6.103  1.00 48.14  ? 421 VAL B CG1 1 
ATOM   4435 C  CG2 . VAL B 2 247 ? -21.586 -2.549  -7.967  1.00 51.33  ? 421 VAL B CG2 1 
ATOM   4436 N  N   . SER B 2 248 ? -24.946 -2.856  -8.145  1.00 50.97  ? 422 SER B N   1 
ATOM   4437 C  CA  . SER B 2 248 ? -25.905 -2.984  -9.241  1.00 51.74  ? 422 SER B CA  1 
ATOM   4438 C  C   . SER B 2 248 ? -27.264 -2.380  -8.854  1.00 54.38  ? 422 SER B C   1 
ATOM   4439 O  O   . SER B 2 248 ? -28.073 -2.121  -9.742  1.00 58.74  ? 422 SER B O   1 
ATOM   4440 C  CB  . SER B 2 248 ? -26.030 -4.418  -9.758  1.00 50.45  ? 422 SER B CB  1 
ATOM   4441 O  OG  . SER B 2 248 ? -26.559 -5.310  -8.784  1.00 53.25  ? 422 SER B OG  1 
ATOM   4442 N  N   . LEU B 2 249 ? -27.482 -2.111  -7.552  1.00 60.81  ? 423 LEU B N   1 
ATOM   4443 C  CA  . LEU B 2 249 ? -28.728 -1.560  -7.012  1.00 66.62  ? 423 LEU B CA  1 
ATOM   4444 C  C   . LEU B 2 249 ? -28.714 -0.027  -6.921  1.00 69.41  ? 423 LEU B C   1 
ATOM   4445 O  O   . LEU B 2 249 ? -29.771 0.580   -6.740  1.00 71.95  ? 423 LEU B O   1 
ATOM   4446 C  CB  . LEU B 2 249 ? -28.981 -2.181  -5.631  1.00 65.14  ? 423 LEU B CB  1 
ATOM   4447 C  CG  . LEU B 2 249 ? -29.262 -3.685  -5.643  1.00 68.02  ? 423 LEU B CG  1 
ATOM   4448 C  CD1 . LEU B 2 249 ? -29.183 -4.268  -4.240  1.00 64.92  ? 423 LEU B CD1 1 
ATOM   4449 C  CD2 . LEU B 2 249 ? -30.615 -3.993  -6.287  1.00 66.57  ? 423 LEU B CD2 1 
ATOM   4450 N  N   . LEU B 2 250 ? -27.542 0.614   -7.038  1.00 65.27  ? 424 LEU B N   1 
ATOM   4451 C  CA  . LEU B 2 250 ? -27.477 2.071   -7.046  1.00 67.28  ? 424 LEU B CA  1 
ATOM   4452 C  C   . LEU B 2 250 ? -28.312 2.616   -8.204  1.00 69.23  ? 424 LEU B C   1 
ATOM   4453 O  O   . LEU B 2 250 ? -28.342 2.026   -9.284  1.00 74.31  ? 424 LEU B O   1 
ATOM   4454 C  CB  . LEU B 2 250 ? -26.020 2.537   -7.162  1.00 66.05  ? 424 LEU B CB  1 
ATOM   4455 C  CG  . LEU B 2 250 ? -25.129 2.246   -5.955  1.00 69.14  ? 424 LEU B CG  1 
ATOM   4456 C  CD1 . LEU B 2 250 ? -23.709 2.709   -6.213  1.00 70.86  ? 424 LEU B CD1 1 
ATOM   4457 C  CD2 . LEU B 2 250 ? -25.659 2.902   -4.690  1.00 75.58  ? 424 LEU B CD2 1 
ATOM   4458 N  N   . ASN B 2 251 ? -29.003 3.736   -7.944  1.00 79.32  ? 425 ASN B N   1 
ATOM   4459 C  CA  . ASN B 2 251 ? -29.670 4.526   -8.971  1.00 82.35  ? 425 ASN B CA  1 
ATOM   4460 C  C   . ASN B 2 251 ? -28.615 5.318   -9.739  1.00 73.41  ? 425 ASN B C   1 
ATOM   4461 O  O   . ASN B 2 251 ? -27.780 5.994   -9.142  1.00 70.02  ? 425 ASN B O   1 
ATOM   4462 C  CB  . ASN B 2 251 ? -30.760 5.439   -8.392  1.00 84.23  ? 425 ASN B CB  1 
ATOM   4463 C  CG  . ASN B 2 251 ? -32.069 4.712   -8.172  1.00 85.85  ? 425 ASN B CG  1 
ATOM   4464 O  OD1 . ASN B 2 251 ? -32.350 4.251   -7.069  1.00 74.97  ? 425 ASN B OD1 1 
ATOM   4465 N  ND2 . ASN B 2 251 ? -32.859 4.570   -9.226  1.00 93.60  ? 425 ASN B ND2 1 
ATOM   4466 N  N   . PRO B 2 252 ? -28.595 5.225   -11.086 1.00 66.13  ? 426 PRO B N   1 
ATOM   4467 C  CA  . PRO B 2 252 ? -27.670 6.014   -11.890 1.00 63.69  ? 426 PRO B CA  1 
ATOM   4468 C  C   . PRO B 2 252 ? -28.093 7.473   -11.864 1.00 68.89  ? 426 PRO B C   1 
ATOM   4469 O  O   . PRO B 2 252 ? -29.211 7.777   -11.456 1.00 76.10  ? 426 PRO B O   1 
ATOM   4470 C  CB  . PRO B 2 252 ? -27.793 5.437   -13.309 1.00 65.54  ? 426 PRO B CB  1 
ATOM   4471 C  CG  . PRO B 2 252 ? -29.141 4.737   -13.331 1.00 68.57  ? 426 PRO B CG  1 
ATOM   4472 C  CD  . PRO B 2 252 ? -29.449 4.343   -11.900 1.00 69.80  ? 426 PRO B CD  1 
ATOM   4473 N  N   . PRO B 2 253 ? -27.218 8.410   -12.289 1.00 73.88  ? 427 PRO B N   1 
ATOM   4474 C  CA  . PRO B 2 253 ? -27.593 9.817   -12.388 1.00 75.87  ? 427 PRO B CA  1 
ATOM   4475 C  C   . PRO B 2 253 ? -28.355 10.060  -13.688 1.00 81.87  ? 427 PRO B C   1 
ATOM   4476 O  O   . PRO B 2 253 ? -28.049 9.447   -14.708 1.00 75.48  ? 427 PRO B O   1 
ATOM   4477 C  CB  . PRO B 2 253 ? -26.239 10.535  -12.364 1.00 73.71  ? 427 PRO B CB  1 
ATOM   4478 C  CG  . PRO B 2 253 ? -25.293 9.550   -13.029 1.00 72.04  ? 427 PRO B CG  1 
ATOM   4479 C  CD  . PRO B 2 253 ? -25.822 8.170   -12.690 1.00 69.73  ? 427 PRO B CD  1 
ATOM   4480 N  N   . GLU B 2 254 ? -29.363 10.938  -13.627 1.00 92.27  ? 428 GLU B N   1 
ATOM   4481 C  CA  . GLU B 2 254 ? -30.130 11.334  -14.799 1.00 93.01  ? 428 GLU B CA  1 
ATOM   4482 C  C   . GLU B 2 254 ? -29.259 12.215  -15.696 1.00 87.52  ? 428 GLU B C   1 
ATOM   4483 O  O   . GLU B 2 254 ? -29.211 11.999  -16.903 1.00 76.73  ? 428 GLU B O   1 
ATOM   4484 C  CB  . GLU B 2 254 ? -31.406 12.080  -14.396 1.00 101.61 ? 428 GLU B CB  1 
ATOM   4485 C  CG  . GLU B 2 254 ? -32.450 11.218  -13.706 1.00 106.84 ? 428 GLU B CG  1 
ATOM   4486 C  CD  . GLU B 2 254 ? -33.815 11.882  -13.609 1.00 112.71 ? 428 GLU B CD  1 
ATOM   4487 O  OE1 . GLU B 2 254 ? -33.871 13.058  -13.177 1.00 105.51 ? 428 GLU B OE1 1 
ATOM   4488 O  OE2 . GLU B 2 254 ? -34.816 11.228  -13.968 1.00 115.33 ? 428 GLU B OE2 1 
ATOM   4489 N  N   . THR B 2 255 ? -28.580 13.205  -15.096 1.00 88.43  ? 429 THR B N   1 
ATOM   4490 C  CA  . THR B 2 255 ? -27.758 14.170  -15.821 1.00 91.44  ? 429 THR B CA  1 
ATOM   4491 C  C   . THR B 2 255 ? -26.282 13.883  -15.543 1.00 84.23  ? 429 THR B C   1 
ATOM   4492 O  O   . THR B 2 255 ? -25.859 13.874  -14.387 1.00 81.70  ? 429 THR B O   1 
ATOM   4493 C  CB  . THR B 2 255 ? -28.130 15.617  -15.445 1.00 101.09 ? 429 THR B CB  1 
ATOM   4494 O  OG1 . THR B 2 255 ? -29.506 15.818  -15.765 1.00 103.20 ? 429 THR B OG1 1 
ATOM   4495 C  CG2 . THR B 2 255 ? -27.310 16.675  -16.156 1.00 101.85 ? 429 THR B CG2 1 
ATOM   4496 N  N   . LEU B 2 256 ? -25.512 13.648  -16.616 1.00 83.78  ? 430 LEU B N   1 
ATOM   4497 C  CA  . LEU B 2 256 ? -24.062 13.514  -16.530 1.00 86.16  ? 430 LEU B CA  1 
ATOM   4498 C  C   . LEU B 2 256 ? -23.427 14.863  -16.200 1.00 91.57  ? 430 LEU B C   1 
ATOM   4499 O  O   . LEU B 2 256 ? -22.600 14.927  -15.293 1.00 96.91  ? 430 LEU B O   1 
ATOM   4500 C  CB  . LEU B 2 256 ? -23.488 12.938  -17.830 1.00 79.22  ? 430 LEU B CB  1 
ATOM   4501 C  CG  . LEU B 2 256 ? -23.553 11.419  -17.958 1.00 76.01  ? 430 LEU B CG  1 
ATOM   4502 C  CD1 . LEU B 2 256 ? -22.655 10.942  -19.089 1.00 75.36  ? 430 LEU B CD1 1 
ATOM   4503 C  CD2 . LEU B 2 256 ? -23.178 10.747  -16.641 1.00 74.02  ? 430 LEU B CD2 1 
ATOM   4504 N  N   . ASN B 2 257 ? -23.798 15.929  -16.925 1.00 92.54  ? 431 ASN B N   1 
ATOM   4505 C  CA  . ASN B 2 257 ? -23.343 17.262  -16.554 1.00 101.63 ? 431 ASN B CA  1 
ATOM   4506 C  C   . ASN B 2 257 ? -21.808 17.232  -16.549 1.00 97.40  ? 431 ASN B C   1 
ATOM   4507 O  O   . ASN B 2 257 ? -21.175 17.552  -15.547 1.00 92.26  ? 431 ASN B O   1 
ATOM   4508 C  CB  . ASN B 2 257 ? -23.999 17.680  -15.223 1.00 109.03 ? 431 ASN B CB  1 
ATOM   4509 C  CG  . ASN B 2 257 ? -23.667 19.075  -14.740 1.00 106.61 ? 431 ASN B CG  1 
ATOM   4510 O  OD1 . ASN B 2 257 ? -24.461 19.998  -14.911 1.00 117.45 ? 431 ASN B OD1 1 
ATOM   4511 N  ND2 . ASN B 2 257 ? -22.516 19.227  -14.105 1.00 100.55 ? 431 ASN B ND2 1 
ATOM   4512 N  N   . LEU B 2 258 ? -21.217 16.791  -17.671 1.00 98.72  ? 432 LEU B N   1 
ATOM   4513 C  CA  . LEU B 2 258 ? -19.770 16.662  -17.841 1.00 98.14  ? 432 LEU B CA  1 
ATOM   4514 C  C   . LEU B 2 258 ? -19.059 17.963  -17.437 1.00 104.37 ? 432 LEU B C   1 
ATOM   4515 O  O   . LEU B 2 258 ? -18.535 17.990  -16.305 1.00 111.25 ? 432 LEU B O   1 
ATOM   4516 C  CB  . LEU B 2 258 ? -19.443 16.307  -19.302 1.00 89.38  ? 432 LEU B CB  1 
ATOM   4517 C  CG  . LEU B 2 258 ? -19.991 14.979  -19.829 1.00 82.94  ? 432 LEU B CG  1 
ATOM   4518 C  CD1 . LEU B 2 258 ? -19.089 14.419  -20.912 1.00 80.24  ? 432 LEU B CD1 1 
ATOM   4519 C  CD2 . LEU B 2 258 ? -20.150 13.954  -18.721 1.00 85.80  ? 432 LEU B CD2 1 
ATOM   4520 O  OXT . LEU B 2 258 ? -19.029 18.899  -18.276 1.00 99.27  ? 432 LEU B OXT 1 
HETATM 4521 C  C1  . YNK C 3 .   ? 23.954  -28.704 -21.677 1.00 55.92  ? 301 YNK A C1  1 
HETATM 4522 C  C2  . YNK C 3 .   ? 23.662  -27.662 -22.751 1.00 52.98  ? 301 YNK A C2  1 
HETATM 4523 C  C3  . YNK C 3 .   ? 24.886  -26.772 -22.925 1.00 52.06  ? 301 YNK A C3  1 
HETATM 4524 C  C5  . YNK C 3 .   ? 22.816  -27.530 -25.103 1.00 52.48  ? 301 YNK A C5  1 
HETATM 4525 C  C6  . YNK C 3 .   ? 21.613  -26.824 -24.608 1.00 46.49  ? 301 YNK A C6  1 
HETATM 4526 C  C7  . YNK C 3 .   ? 21.950  -25.994 -23.369 1.00 49.99  ? 301 YNK A C7  1 
HETATM 4527 C  C10 . YNK C 3 .   ? 19.797  -25.435 -25.703 1.00 42.47  ? 301 YNK A C10 1 
HETATM 4528 C  C12 . YNK C 3 .   ? 18.232  -24.095 -26.636 1.00 43.35  ? 301 YNK A C12 1 
HETATM 4529 C  C13 . YNK C 3 .   ? 17.273  -24.501 -25.707 1.00 41.97  ? 301 YNK A C13 1 
HETATM 4530 C  C14 . YNK C 3 .   ? 17.679  -25.439 -24.772 1.00 42.20  ? 301 YNK A C14 1 
HETATM 4531 C  C16 . YNK C 3 .   ? 16.829  -26.000 -23.640 1.00 43.82  ? 301 YNK A C16 1 
HETATM 4532 N  N18 . YNK C 3 .   ? 15.383  -26.126 -21.994 1.00 47.73  ? 301 YNK A N18 1 
HETATM 4533 C  C19 . YNK C 3 .   ? 16.038  -27.301 -22.024 1.00 50.04  ? 301 YNK A C19 1 
HETATM 4534 C  C21 . YNK C 3 .   ? 16.692  -29.530 -21.405 1.00 51.61  ? 301 YNK A C21 1 
HETATM 4535 C  C22 . YNK C 3 .   ? 16.541  -30.771 -20.543 1.00 51.90  ? 301 YNK A C22 1 
HETATM 4536 C  C24 . YNK C 3 .   ? 17.647  -29.498 -22.444 1.00 52.64  ? 301 YNK A C24 1 
HETATM 4537 C  C25 . YNK C 3 .   ? 17.802  -28.375 -23.263 1.00 47.30  ? 301 YNK A C25 1 
HETATM 4538 C  C26 . YNK C 3 .   ? 16.968  -27.257 -23.040 1.00 48.00  ? 301 YNK A C26 1 
HETATM 4539 C  C31 . YNK C 3 .   ? 15.861  -23.913 -25.778 1.00 45.88  ? 301 YNK A C31 1 
HETATM 4540 C  C4  . YNK C 3 .   ? 23.388  -28.408 -24.061 1.00 52.60  ? 301 YNK A C4  1 
HETATM 4541 N  N8  . YNK C 3 .   ? 22.510  -26.842 -22.299 1.00 49.13  ? 301 YNK A N8  1 
HETATM 4542 N  N9  . YNK C 3 .   ? 21.155  -25.923 -25.673 1.00 41.70  ? 301 YNK A N9  1 
HETATM 4543 N  N11 . YNK C 3 .   ? 19.486  -24.559 -26.622 1.00 42.92  ? 301 YNK A N11 1 
HETATM 4544 N  N15 . YNK C 3 .   ? 18.928  -25.845 -24.794 1.00 39.38  ? 301 YNK A N15 1 
HETATM 4545 C  C17 . YNK C 3 .   ? 15.846  -25.340 -22.942 1.00 49.51  ? 301 YNK A C17 1 
HETATM 4546 C  C20 . YNK C 3 .   ? 15.867  -28.445 -21.197 1.00 56.22  ? 301 YNK A C20 1 
HETATM 4547 N  N23 . YNK C 3 .   ? 16.398  -31.675 -19.881 1.00 59.63  ? 301 YNK A N23 1 
HETATM 4548 P  P27 . YNK C 3 .   ? 14.589  -28.391 -19.833 1.00 69.60  ? 301 YNK A P27 1 
HETATM 4549 O  O28 . YNK C 3 .   ? 14.605  -29.635 -19.077 1.00 72.58  ? 301 YNK A O28 1 
HETATM 4550 C  C29 . YNK C 3 .   ? 15.217  -27.068 -18.679 1.00 66.72  ? 301 YNK A C29 1 
HETATM 4551 C  C30 . YNK C 3 .   ? 12.903  -28.115 -20.577 1.00 70.68  ? 301 YNK A C30 1 
HETATM 4552 F  F32 . YNK C 3 .   ? 14.897  -24.852 -25.669 1.00 47.39  ? 301 YNK A F32 1 
HETATM 4553 F  F33 . YNK C 3 .   ? 15.610  -22.968 -24.829 1.00 44.68  ? 301 YNK A F33 1 
HETATM 4554 F  F34 . YNK C 3 .   ? 15.758  -23.290 -26.964 1.00 47.45  ? 301 YNK A F34 1 
HETATM 4555 C  C1  . SGM D 4 .   ? -1.378  -9.811  -29.685 1.00 109.67 ? 501 SGM B C1  1 
HETATM 4556 C  C2  . SGM D 4 .   ? -1.023  -9.210  -31.028 1.00 102.95 ? 501 SGM B C2  1 
HETATM 4557 O  O2  . SGM D 4 .   ? -1.816  -9.802  -32.054 1.00 101.44 ? 501 SGM B O2  1 
HETATM 4558 C  C3  . SGM D 4 .   ? 0.441   -9.399  -31.365 1.00 102.77 ? 501 SGM B C3  1 
HETATM 4559 O  O3  . SGM D 4 .   ? 0.909   -8.373  -32.234 1.00 101.97 ? 501 SGM B O3  1 
HETATM 4560 S  S1  . SGM D 4 .   ? -3.152  -9.938  -29.327 1.00 108.94 ? 501 SGM B S1  1 
HETATM 4561 NA NA  . NA  E 5 .   ? -0.573  2.610   -12.587 1.00 87.37  ? 502 NA  B NA  1 
HETATM 4562 NA NA  . NA  F 5 .   ? -25.151 -11.266 -38.695 1.00 66.40  ? 503 NA  B NA  1 
HETATM 4563 O  O   . HOH G 6 .   ? 11.001  -5.080  -9.189  1.00 43.37  ? 401 HOH A O   1 
HETATM 4564 O  O   . HOH G 6 .   ? 32.126  -5.976  -18.324 1.00 45.59  ? 402 HOH A O   1 
HETATM 4565 O  O   . HOH G 6 .   ? -1.441  -22.396 -12.977 1.00 43.52  ? 403 HOH A O   1 
HETATM 4566 O  O   . HOH G 6 .   ? 12.737  -16.243 -6.117  1.00 36.70  ? 404 HOH A O   1 
HETATM 4567 O  O   . HOH G 6 .   ? 0.838   -12.682 -5.902  1.00 44.57  ? 405 HOH A O   1 
HETATM 4568 O  O   . HOH G 6 .   ? 24.549  -22.876 2.818   1.00 46.67  ? 406 HOH A O   1 
HETATM 4569 O  O   . HOH G 6 .   ? 8.263   -22.595 -0.367  1.00 52.39  ? 407 HOH A O   1 
HETATM 4570 O  O   . HOH G 6 .   ? 23.251  -19.342 -5.888  1.00 37.55  ? 408 HOH A O   1 
HETATM 4571 O  O   . HOH G 6 .   ? 23.887  5.144   -13.463 1.00 58.87  ? 409 HOH A O   1 
HETATM 4572 O  O   . HOH G 6 .   ? 15.778  -21.777 -41.385 1.00 52.08  ? 410 HOH A O   1 
HETATM 4573 O  O   . HOH G 6 .   ? 12.335  -5.853  -11.681 1.00 41.48  ? 411 HOH A O   1 
HETATM 4574 O  O   . HOH G 6 .   ? 8.101   -21.406 17.408  1.00 56.58  ? 412 HOH A O   1 
HETATM 4575 O  O   . HOH G 6 .   ? 14.539  -21.593 -10.723 1.00 45.09  ? 413 HOH A O   1 
HETATM 4576 O  O   . HOH G 6 .   ? 17.279  -12.792 -28.763 1.00 48.46  ? 414 HOH A O   1 
HETATM 4577 O  O   . HOH G 6 .   ? 12.951  -22.026 -23.587 1.00 55.72  ? 415 HOH A O   1 
HETATM 4578 O  O   . HOH G 6 .   ? 15.752  -3.789  -20.870 1.00 42.51  ? 416 HOH A O   1 
HETATM 4579 O  O   . HOH G 6 .   ? -0.235  -12.842 -26.603 1.00 62.15  ? 417 HOH A O   1 
HETATM 4580 O  O   . HOH G 6 .   ? 10.616  -4.228  -5.305  1.00 45.86  ? 418 HOH A O   1 
HETATM 4581 O  O   . HOH G 6 .   ? 15.625  -32.819 -17.443 1.00 56.86  ? 419 HOH A O   1 
HETATM 4582 O  O   . HOH G 6 .   ? 3.310   -20.883 -15.937 1.00 43.50  ? 420 HOH A O   1 
HETATM 4583 O  O   . HOH G 6 .   ? 13.475  -12.696 -28.052 1.00 36.89  ? 421 HOH A O   1 
HETATM 4584 O  O   . HOH G 6 .   ? 25.473  -4.951  5.531   1.00 55.18  ? 422 HOH A O   1 
HETATM 4585 O  O   . HOH G 6 .   ? 21.802  -25.043 -9.367  1.00 50.42  ? 423 HOH A O   1 
HETATM 4586 O  O   . HOH G 6 .   ? 9.284   -19.752 -16.473 1.00 42.80  ? 424 HOH A O   1 
HETATM 4587 O  O   . HOH G 6 .   ? 11.028  -14.627 -27.934 1.00 48.66  ? 425 HOH A O   1 
HETATM 4588 O  O   . HOH G 6 .   ? 16.883  -18.937 -2.115  1.00 39.63  ? 426 HOH A O   1 
HETATM 4589 O  O   . HOH G 6 .   ? 12.557  -5.830  -7.014  1.00 39.09  ? 427 HOH A O   1 
HETATM 4590 O  O   . HOH G 6 .   ? 21.418  -20.465 -4.157  1.00 37.49  ? 428 HOH A O   1 
HETATM 4591 O  O   . HOH G 6 .   ? 21.602  -11.311 -28.568 1.00 53.57  ? 429 HOH A O   1 
HETATM 4592 O  O   . HOH G 6 .   ? 13.072  -16.710 -10.904 1.00 40.96  ? 430 HOH A O   1 
HETATM 4593 O  O   . HOH G 6 .   ? 27.475  -24.131 -1.863  1.00 55.26  ? 431 HOH A O   1 
HETATM 4594 O  O   . HOH G 6 .   ? 38.677  -19.873 -17.362 1.00 58.35  ? 432 HOH A O   1 
HETATM 4595 O  O   . HOH G 6 .   ? 28.384  -23.672 -9.290  1.00 60.87  ? 433 HOH A O   1 
HETATM 4596 O  O   . HOH G 6 .   ? -3.192  -25.354 -14.826 1.00 39.11  ? 434 HOH A O   1 
HETATM 4597 O  O   . HOH G 6 .   ? 2.043   -4.498  -10.501 1.00 51.39  ? 435 HOH A O   1 
HETATM 4598 O  O   . HOH G 6 .   ? 20.837  -25.067 -13.066 1.00 47.35  ? 436 HOH A O   1 
HETATM 4599 O  O   . HOH G 6 .   ? 12.797  -26.918 -6.077  1.00 49.89  ? 437 HOH A O   1 
HETATM 4600 O  O   . HOH G 6 .   ? 33.796  -4.301  -16.944 1.00 51.80  ? 438 HOH A O   1 
HETATM 4601 O  O   . HOH G 6 .   ? -5.960  -15.751 -7.904  1.00 52.71  ? 439 HOH A O   1 
HETATM 4602 O  O   . HOH G 6 .   ? 9.425   -15.428 -30.602 1.00 57.16  ? 440 HOH A O   1 
HETATM 4603 O  O   . HOH G 6 .   ? 26.996  -25.533 -4.712  1.00 59.18  ? 441 HOH A O   1 
HETATM 4604 O  O   . HOH G 6 .   ? 9.051   -29.263 -47.453 1.00 51.73  ? 442 HOH A O   1 
HETATM 4605 O  O   . HOH G 6 .   ? 14.617  -0.335  -7.150  1.00 39.29  ? 443 HOH A O   1 
HETATM 4606 O  O   . HOH G 6 .   ? 25.591  0.875   -0.829  1.00 58.30  ? 444 HOH A O   1 
HETATM 4607 O  O   . HOH G 6 .   ? 35.875  -13.191 -10.527 1.00 55.71  ? 445 HOH A O   1 
HETATM 4608 O  O   . HOH G 6 .   ? 17.495  -7.025  4.105   1.00 42.90  ? 446 HOH A O   1 
HETATM 4609 O  O   . HOH G 6 .   ? 5.625   -4.770  -9.938  1.00 53.68  ? 447 HOH A O   1 
HETATM 4610 O  O   . HOH G 6 .   ? 24.909  -20.893 -30.322 1.00 54.25  ? 448 HOH A O   1 
HETATM 4611 O  O   . HOH G 6 .   ? 7.665   -7.182  -5.800  1.00 48.34  ? 449 HOH A O   1 
HETATM 4612 O  O   . HOH G 6 .   ? 23.180  2.834   -4.702  1.00 52.02  ? 450 HOH A O   1 
HETATM 4613 O  O   . HOH G 6 .   ? 27.477  4.775   -13.037 1.00 59.82  ? 451 HOH A O   1 
HETATM 4614 O  O   . HOH G 6 .   ? 11.996  -41.736 -29.997 1.00 56.58  ? 452 HOH A O   1 
HETATM 4615 O  O   . HOH H 6 .   ? -25.993 -1.212  -23.686 1.00 47.78  ? 601 HOH B O   1 
HETATM 4616 O  O   . HOH H 6 .   ? -20.756 -34.329 -23.674 1.00 60.44  ? 602 HOH B O   1 
HETATM 4617 O  O   . HOH H 6 .   ? -32.476 -8.400  -12.447 1.00 64.17  ? 603 HOH B O   1 
HETATM 4618 O  O   . HOH H 6 .   ? -4.299  2.632   -27.055 1.00 39.62  ? 604 HOH B O   1 
HETATM 4619 O  O   . HOH H 6 .   ? 11.929  -2.041  -6.436  1.00 48.65  ? 605 HOH B O   1 
HETATM 4620 O  O   . HOH H 6 .   ? -28.111 -22.312 -38.294 1.00 54.88  ? 606 HOH B O   1 
HETATM 4621 O  O   . HOH H 6 .   ? -20.246 13.985  -15.745 1.00 54.26  ? 607 HOH B O   1 
HETATM 4622 O  O   . HOH H 6 .   ? -6.801  -8.402  -33.643 1.00 56.14  ? 608 HOH B O   1 
HETATM 4623 O  O   . HOH H 6 .   ? -22.432 -16.817 -38.885 1.00 52.33  ? 609 HOH B O   1 
HETATM 4624 O  O   . HOH H 6 .   ? -18.758 -14.172 -13.738 1.00 43.05  ? 610 HOH B O   1 
HETATM 4625 O  O   . HOH H 6 .   ? -6.991  5.935   -27.647 1.00 46.45  ? 611 HOH B O   1 
HETATM 4626 O  O   . HOH H 6 .   ? -24.472 -22.605 -29.798 1.00 42.14  ? 612 HOH B O   1 
HETATM 4627 O  O   . HOH H 6 .   ? -11.582 3.773   -28.754 1.00 51.09  ? 613 HOH B O   1 
HETATM 4628 O  O   . HOH H 6 .   ? -28.535 -1.801  -12.342 1.00 50.67  ? 614 HOH B O   1 
HETATM 4629 O  O   . HOH H 6 .   ? -23.376 -8.319  -28.513 1.00 31.65  ? 615 HOH B O   1 
HETATM 4630 O  O   . HOH H 6 .   ? -6.780  -29.202 -27.544 1.00 55.62  ? 616 HOH B O   1 
HETATM 4631 O  O   . HOH H 6 .   ? -24.960 -4.958  -29.942 1.00 67.26  ? 617 HOH B O   1 
HETATM 4632 O  O   . HOH H 6 .   ? -2.052  -11.042 -34.423 1.00 54.85  ? 618 HOH B O   1 
HETATM 4633 O  O   . HOH H 6 .   ? -29.862 12.684  -11.633 1.00 61.27  ? 619 HOH B O   1 
HETATM 4634 O  O   . HOH H 6 .   ? -12.004 -8.023  -23.534 1.00 48.70  ? 620 HOH B O   1 
HETATM 4635 O  O   . HOH H 6 .   ? -26.803 -7.823  -16.275 1.00 47.08  ? 621 HOH B O   1 
HETATM 4636 O  O   . HOH H 6 .   ? -8.004  -20.202 -10.021 1.00 52.00  ? 622 HOH B O   1 
HETATM 4637 O  O   . HOH H 6 .   ? -27.631 -16.086 -21.406 1.00 54.03  ? 623 HOH B O   1 
HETATM 4638 O  O   . HOH H 6 .   ? -4.298  9.282   -25.398 1.00 47.83  ? 624 HOH B O   1 
HETATM 4639 O  O   . HOH H 6 .   ? -5.196  4.659   -20.833 1.00 33.69  ? 625 HOH B O   1 
HETATM 4640 O  O   . HOH H 6 .   ? -25.420 -4.079  -21.346 1.00 64.65  ? 626 HOH B O   1 
HETATM 4641 O  O   . HOH H 6 .   ? -18.046 -34.330 -18.896 1.00 52.95  ? 627 HOH B O   1 
HETATM 4642 O  O   . HOH H 6 .   ? -6.772  -17.822 -10.190 1.00 44.38  ? 628 HOH B O   1 
HETATM 4643 O  O   . HOH H 6 .   ? -20.208 -20.518 -7.166  1.00 58.71  ? 629 HOH B O   1 
HETATM 4644 O  O   . HOH H 6 .   ? -3.540  -10.390 -20.899 1.00 44.00  ? 630 HOH B O   1 
HETATM 4645 O  O   . HOH H 6 .   ? -26.486 -24.298 -36.333 1.00 58.85  ? 631 HOH B O   1 
HETATM 4646 O  O   . HOH H 6 .   ? -28.529 -1.647  -21.182 1.00 52.59  ? 632 HOH B O   1 
HETATM 4647 O  O   . HOH H 6 .   ? -0.399  -15.809 -17.527 1.00 51.90  ? 633 HOH B O   1 
HETATM 4648 O  O   . HOH H 6 .   ? -29.059 0.417   -13.550 1.00 47.51  ? 634 HOH B O   1 
HETATM 4649 O  O   . HOH H 6 .   ? -17.604 -36.322 -23.571 1.00 45.05  ? 635 HOH B O   1 
HETATM 4650 O  O   . HOH H 6 .   ? -8.325  -27.728 -17.876 1.00 57.28  ? 636 HOH B O   1 
HETATM 4651 O  O   . HOH H 6 .   ? -12.290 -5.987  -21.889 1.00 42.99  ? 637 HOH B O   1 
HETATM 4652 O  O   . HOH H 6 .   ? -25.719 -9.477  -18.397 1.00 53.05  ? 638 HOH B O   1 
HETATM 4653 O  O   . HOH H 6 .   ? -25.620 -24.524 -28.445 1.00 40.64  ? 639 HOH B O   1 
HETATM 4654 O  O   . HOH H 6 .   ? -26.160 -26.676 -30.171 1.00 52.91  ? 640 HOH B O   1 
HETATM 4655 O  O   . HOH H 6 .   ? 8.062   4.691   -17.030 1.00 55.60  ? 641 HOH B O   1 
HETATM 4656 O  O   . HOH H 6 .   ? -26.862 -8.141  -35.204 1.00 55.12  ? 642 HOH B O   1 
HETATM 4657 O  O   . HOH H 6 .   ? -26.614 -7.108  -19.890 1.00 48.61  ? 643 HOH B O   1 
HETATM 4658 O  O   . HOH H 6 .   ? -28.142 -5.585  -17.693 1.00 50.49  ? 644 HOH B O   1 
HETATM 4659 O  O   . HOH H 6 .   ? -22.962 -26.065 -11.741 1.00 57.00  ? 645 HOH B O   1 
HETATM 4660 O  O   . HOH H 6 .   ? -3.481  -9.672  -15.563 1.00 51.06  ? 646 HOH B O   1 
HETATM 4661 O  O   . HOH H 6 .   ? -21.477 12.948  -28.433 1.00 63.45  ? 647 HOH B O   1 
HETATM 4662 O  O   . HOH H 6 .   ? -27.955 -5.060  -31.482 1.00 51.79  ? 648 HOH B O   1 
HETATM 4663 O  O   . HOH H 6 .   ? -25.417 -27.758 -16.144 1.00 62.68  ? 649 HOH B O   1 
HETATM 4664 O  O   . HOH H 6 .   ? -26.509 -18.172 -28.372 1.00 50.13  ? 650 HOH B O   1 
HETATM 4665 O  O   . HOH H 6 .   ? -5.987  10.467  -27.015 1.00 51.28  ? 651 HOH B O   1 
HETATM 4666 O  O   . HOH H 6 .   ? -27.410 -3.741  -19.827 1.00 56.82  ? 652 HOH B O   1 
HETATM 4667 O  O   . HOH H 6 .   ? -30.532 -23.348 -37.994 1.00 57.78  ? 653 HOH B O   1 
# 
